UniProtKB - P41180 (CASR_HUMAN)
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- BLAST>sp|P41180|CASR_HUMAN Extracellular calcium-sensing receptor OS=Homo sapiens GN=CASR PE=1 SV=3 MAFYSCCWVLLALTWHTSAYGPDQRAQKKGDIILGGLFPIHFGVAAKDQDLKSRPESVEC IRYNFRGFRWLQAMIFAIEEINSSPALLPNLTLGYRIFDTCNTVSKALEATLSFVAQNKI DSLNLDEFCNCSEHIPSTIAVVGATGSGVSTAVANLLGLFYIPQVSYASSSRLLSNKNQF KSFLRTIPNDEHQATAMADIIEYFRWNWVGTIAADDDYGRPGIEKFREEAEERDICIDFS ELISQYSDEEEIQHVVEVIQNSTAKVIVVFSSGPDLEPLIKEIVRRNITGKIWLASEAWA SSSLIAMPQYFHVVGGTIGFALKAGQIPGFREFLKKVHPRKSVHNGFAKEFWEETFNCHL QEGAKGPLPVDTFLRGHEESGDRFSNSSTAFRPLCTGDENISSVETPYIDYTHLRISYNV YLAVYSIAHALQDIYTCLPGRGLFTNGSCADIKKVEAWQVLKHLRHLNFTNNMGEQVTFD ECGDLVGNYSIINWHLSPEDGSIVFKEVGYYNVYAKKGERLFINEEKILWSGFSREVPFS NCSRDCLAGTRKGIIEGEPTCCFECVECPDGEYSDETDASACNKCPDDFWSNENHTSCIA KEIEFLSWTEPFGIALTLFAVLGIFLTAFVLGVFIKFRNTPIVKATNRELSYLLLFSLLC CFSSSLFFIGEPQDWTCRLRQPAFGISFVLCISCILVKTNRVLLVFEAKIPTSFHRKWWG LNLQFLLVFLCTFMQIVICVIWLYTAPPSSYRNQELEDEIIFITCHEGSLMALGFLIGYT CLLAAICFFFAFKSRKLPENFNEAKFITFSMLIFFIVWISFIPAYASTYGKFVSAVEVIA ILAASFGLLACIFFNKIYIILFKPSRNTIEEVRCSTAAHAFKVAARATLRRSNVSRKRSS SLGGSTGSTPSSSISSKSNSEDPFPQPERQKQQQPLALTQQEQQQQPLTLPQQQRSQQQP RCKQKVIFGSGTVTFSLSFDEPQKNAMAHRNSTHQNSLEAQKSSDTLTRHEPLLPLQCGE TDLDLTVQETGLQGPVGGDQRPEVEDPEELSPALVVSSSQSFVISGGGSTVTENVVNS
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Protein
Extracellular calcium-sensing receptor
Gene
CASR
Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:
Annotation score:5 out of 5
<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>Select a section on the left to see content.
<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni
G-protein-coupled receptor that senses changes in the extracellular concentration of calcium ions and plays a key role in maintaining calcium homeostasis (PubMed:7759551, PubMed:8702647, PubMed:8636323, PubMed:8878438, PubMed:17555508, PubMed:19789209, PubMed:21566075, PubMed:22114145, PubMed:23966241, PubMed:25292184, PubMed:25104082, PubMed:26386835, PubMed:25766501, PubMed:22789683). Senses fluctuations in the circulating calcium concentration and modulates the production of parathyroid hormone (PTH) in parathyroid glands (By similarity). The activity of this receptor is mediated by a G-protein that activates a phosphatidylinositol-calcium second messenger system (PubMed:7759551). The G-protein-coupled receptor activity is activated by a co-agonist mechanism: aromatic amino acids, such as Trp or Phe, act concertedly with divalent cations, such as calcium or magnesium, to achieve full receptor activation (PubMed:27434672, PubMed:27386547).By similarity
<p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More…</a></p> Manual assertion inferred from sequence similarity toi
16 Publications<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
- Ref.2"Molecular cloning and functional expression of human parathyroid calcium receptor cDNAs."
Garrett J.E., Capuano I.V., Hammerland L.G., Hung B.C., Brown E.M., Hebert S.C., Nemeth E.F., Fuller F.
J. Biol. Chem. 270:12919-12925(1995) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, VARIANT GLY-990. - Ref.13"Structural mechanism of ligand activation in human calcium-sensing receptor."
Geng Y., Mosyak L., Kurinov I., Zuo H., Sturchler E., Cheng T.C., Subramanyam P., Brown A.P., Brennan S.C., Mun H.C., Bush M., Chen Y., Nguyen T.X., Cao B., Chang D.D., Quick M., Conigrave A.D., Colecraft H.M., McDonald P., Fan Q.R.
Elife 5:0-0(2016) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 20-607 IN COMPLEX WITH CALCIUM; ANION AND TRYPTOPHAN, FUNCTION, ENZYME REGULATION, DOMAIN, DISULFIDE BONDS, GLYCOSYLATION AT ASN-261; ASN-287; ASN-446; ASN-468; ASN-488; ASN-541 AND ASN-594, MUTAGENESIS OF ARG-69; ASN-102; THR-145; SER-147; SER-170; TYR-218; SER-417 AND TRP-458, CHARACTERIZATION OF VARIANTS NSHPT ILE-100; LEU-227 AND LYS-551, CHARACTERIZATION OF VARIANTS HHC1 HIS-66; MET-81; PRO-159; GLY-172; GLY-215; LYS-297 AND GLU-557. - Ref.14"Structural basis for regulation of human calcium-sensing receptor by magnesium ions and an unexpected tryptophan derivative co-agonist."
Zhang C., Zhang T., Zou J., Miller C.L., Gorkhali R., Yang J.Y., Schilmiller A., Wang S., Huang K., Brown E.M., Moremen K.W., Hu J., Yang J.J.
Sci. Adv. 2:E1600241-E1600241(2016) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 20-541 IN COMPLEX WITH MAGNESIUM AND TRYPTOPHAN, FUNCTION, ENZYME REGULATION, DOMAIN, DISULFIDE BONDS, MUTAGENESIS OF GLU-297. - Ref.21"Expression and characterization of inactivating and activating mutations in the human Ca2+o-sensing receptor."
Bai M., Quinn S., Trivedi S., Kifor O., Pearce S.H.S., Pollak M.R., Krapcho K., Hebert S.C., Brown E.M.
J. Biol. Chem. 271:19537-19545(1996) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS HHC1 MET-62; CYS-66; MET-138; GLU-143; GLN-185; LYS-297 AND TRP-795, VARIANT HYPOC1 ALA-127, FUNCTION, SUBCELLULAR LOCATION, GLYCOSYLATION, CHARACTERIZATION OF VARIANTS HHC1 MET-62; CYS-66; MET-138; GLU-143; GLN-185; LYS-297 AND TRP-795, CHARACTERIZATION OF VARIANT HYPOC1 ALA-127. - Ref.22"Clustered inactivating mutations and benign polymorphisms of the calcium receptor gene in familial benign hypocalciuric hypercalcemia suggest receptor functional domains."
Heath H. III, Odelberg S., Jackson C.E., Teh B.T., Hayward N., Larsson C., Buist N.R., Krapcho K.J., Hung B.C., Capuano I.V., Garrett J.E., Leppert M.F.
J. Clin. Endocrinol. Metab. 81:1312-1317(1996) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS HHC1 PRO-53; LEU-55; GLN-185; GLY-215; TYR-657 AND ARG-748, VARIANTS SER-986; GLY-990 AND GLN-1011, CHARACTERIZATION OF VARIANTS HHC1 PRO-53; LEU-55 AND GLY-215. - Ref.23"Functional characterization of calcium-sensing receptor mutations expressed in human embryonic kidney cells."
Pearce S.H.S., Bai M., Quinn S.J., Kifor O., Brown E.M., Thakker R.V.
J. Clin. Invest. 98:1860-1866(1996) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS HHC1 LEU-55; ASP-178; SER-221 AND ILE-817, VARIANTS HYPOC1 LEU-128; MET-151 AND LYS-191, VARIANT NSHPT LEU-227, CHARACTERIZATION OF VARIANTS HHC1 LEU-55; ASP-178; SER-221 AND ILE-817, FUNCTION, CHARACTERIZATION OF VARIANTS HYPOC1 LEU-128; MET-151 AND LYS-191, CHARACTERIZATION OF VARIANT NSHPT LEU-227. - Ref.50"Neonatal severe hyperparathyroidism associated with a novel de novo heterozygous R551K inactivating mutation and a heterozygous A986S polymorphism of the calcium-sensing receptor gene."
Toke J., Czirjak G., Patocs A., Enyedi B., Gergics P., Csakvary V., Enyedi P., Toth M.
Clin. Endocrinol. (Oxf.) 67:385-392(2007) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT NSHPT LYS-551, VARIANT SER-986, FUNCTION, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANT NSHPT LYS-551. - Ref.53"A novel loss-of-function mutation, Gln459Arg, of the calcium-sensing receptor gene associated with apparent autosomal recessive inheritance of familial hypocalciuric hypercalcemia."
Lietman S.A., Tenenbaum-Rakover Y., Jap T.S., Yi-Chi W., De-Ming Y., Ding C., Kussiny N., Levine M.A.
J. Clin. Endocrinol. Metab. 94:4372-4379(2009) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT HHC1 ARG-459, VARIANTS SER-986 AND GLN-1011, FUNCTION, CHARACTERIZATION OF VARIANT HHC1 ARG-459. - Ref.56"A novel mutation in the calcium-sensing receptor in a French family with familial hypocalciuric hypercalcaemia."
Al-Salameh A., Cetani F., Pardi E., Vulpoi C., Pierre P., de Calan L., Guyetant S., Jeunemaitre X., Lecomte P.
Eur. J. Endocrinol. 165:359-363(2011) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT HHC1 ILE-550, FUNCTION, CHARACTERIZATION OF VARIANT HHC1 ILE-550. - Ref.57"Agonist-driven maturation and plasma membrane insertion of calcium-sensing receptors dynamically control signal amplitude."
Grant M.P., Stepanchick A., Cavanaugh A., Breitwieser G.E.
Sci. Signal. 4:RA78-RA78(2011) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS HHC1 PRO-159 AND TRP-795, FUNCTION, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANTS HHC1 PRO-159 AND TRP-795. - Ref.59"Loss-of-function and gain-of-function mutations of calcium-sensing receptor: functional analysis and the effect of allosteric modulators NPS R-568 and NPS 2143."
Nakamura A., Hotsubo T., Kobayashi K., Mochizuki H., Ishizu K., Tajima T.
J. Clin. Endocrinol. Metab. 98:E1692-E1701(2013) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS HHC1 THR-110 AND GLY-172, VARIANTS HYPOC1 CYS-122; HIS-569 AND THR-839, FUNCTION, CHARACTERIZATION OF VARIANTS HHC1 THR-110 AND GLY-172, CHARACTERIZATION OF VARIANTS HYPOC1 CYS-122; HIS-569 AND THR-839. - Ref.61"A novel mutation in calcium-sensing receptor gene associated to hypercalcemia and hypercalciuria."
Mastromatteo E., Lamacchia O., Campo M.R., Conserva A., Baorda F., Cinque L., Guarnieri V., Scillitani A., Cignarelli M.
BMC Endocr. Disord. 14:81-81(2014) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT HHC1 MET-972, FUNCTION, CHARACTERIZATION OF VARIANT HHC1 MET-972. - Ref.62"Calcium-sensing-related gene mutations in hypercalcaemic hypocalciuric patients as differential diagnosis from primary hyperparathyroidism: detection of two novel inactivating mutations in an Italian population."
Stratta P., Merlotti G., Musetti C., Quaglia M., Pagani A., Izzo C., Radin E., Airoldi A., Baorda F., Palladino T., Leone M.P., Guarnieri V.
Nephrol. Dial. Transplant. 29:1902-1909(2014) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS HHC1 VAL-707 AND SER-774, FUNCTION, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANTS HHC1 VAL-707 AND SER-774. - Ref.63"Identification and functional analysis of a novel CaSR mutation in a family with familial hypocalciuric hypercalcemia."
Kim E.S., Kim S.Y., Lee J.Y., Han J.H., Sohn T.S., Son H.S., Moon S.D.
J. Bone Miner. Metab. 34:662-667(2016) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT HHC1 TRP-571, FUNCTION, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANT HHC1 TRP-571. - Ref.64"Novel activating mutation of human calcium-sensing receptor in a family with autosomal dominant hypocalcaemia."
Baran N., ter Braak M., Saffrich R., Woelfle J., Schmitz U.
Mol. Cell. Endocrinol. 407:18-25(2015) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT HYPOC1 LEU-136, FUNCTION, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANT HYPOC1 LEU-136. - Ref.65"CASR gene activating mutations in two families with autosomal dominant hypocalcemia."
Guarnieri V., Valentina D'Elia A., Baorda F., Pazienza V., Benegiamo G., Stanziale P., Copetti M., Battista C., Grimaldi F., Damante G., Pellegrini F., D'Agruma L., Zelante L., Carella M., Scillitani A.
Mol. Genet. Metab. 107:548-552(2012) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS HYPOC1 LEU-221; ARG-681 AND GLN-727, FUNCTION, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANTS HYPOC1 ARG-681 AND GLN-727.
<p>This subsection of the ‘Function’ section describes an enzyme regulatory mechanism and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/enzyme_regulation' target='_top'>More...</a></p>Enzyme regulationi
In resting state, adopts an open conformation, anion-binding promoting the inactive configuration (PubMed:27434672). Upon aromatic amino acid-binding, the groove in the extracellular venus flytrap module is closed, thereby inducing the formation of a novel homodimer interface between subunits (PubMed:27434672, PubMed:27386547). Calcium ions stabilize the active state by enhancing homodimer interactions between membrane-proximal domains to fully activate the receptor (PubMed:27434672, PubMed:27386547). Activated by AMG 416, a D-amino acid-containing peptide agonist that is being evaluated for the treatment of secondary hyperparathyroidism in chronic kidney disease patients receiving hemodialysis (PubMed:26290606). AMG 416 agonist acts by forming a disulfide bond with Cys-482 (PubMed:26290606).3 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
- Ref.12"Critical cysteine residues in both the calcium-sensing receptor and the allosteric activator AMG 416 underlie the mechanism of action."
Alexander S.T., Hunter T., Walter S., Dong J., Maclean D., Baruch A., Subramanian R., Tomlinson J.
Mol. Pharmacol. 88:853-865(2015) [PubMed] [Europe PMC] [Abstract]Cited for: ENZYME REGULATION, MUTAGENESIS OF CYS-482. - Ref.13"Structural mechanism of ligand activation in human calcium-sensing receptor."
Geng Y., Mosyak L., Kurinov I., Zuo H., Sturchler E., Cheng T.C., Subramanyam P., Brown A.P., Brennan S.C., Mun H.C., Bush M., Chen Y., Nguyen T.X., Cao B., Chang D.D., Quick M., Conigrave A.D., Colecraft H.M., McDonald P., Fan Q.R.
Elife 5:0-0(2016) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 20-607 IN COMPLEX WITH CALCIUM; ANION AND TRYPTOPHAN, FUNCTION, ENZYME REGULATION, DOMAIN, DISULFIDE BONDS, GLYCOSYLATION AT ASN-261; ASN-287; ASN-446; ASN-468; ASN-488; ASN-541 AND ASN-594, MUTAGENESIS OF ARG-69; ASN-102; THR-145; SER-147; SER-170; TYR-218; SER-417 AND TRP-458, CHARACTERIZATION OF VARIANTS NSHPT ILE-100; LEU-227 AND LYS-551, CHARACTERIZATION OF VARIANTS HHC1 HIS-66; MET-81; PRO-159; GLY-172; GLY-215; LYS-297 AND GLU-557. - Ref.14"Structural basis for regulation of human calcium-sensing receptor by magnesium ions and an unexpected tryptophan derivative co-agonist."
Zhang C., Zhang T., Zou J., Miller C.L., Gorkhali R., Yang J.Y., Schilmiller A., Wang S., Huang K., Brown E.M., Moremen K.W., Hu J., Yang J.J.
Sci. Adv. 2:E1600241-E1600241(2016) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 20-541 IN COMPLEX WITH MAGNESIUM AND TRYPTOPHAN, FUNCTION, ENZYME REGULATION, DOMAIN, DISULFIDE BONDS, MUTAGENESIS OF GLU-297.
Sites
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi | 81 | Calcium; via carbonyl oxygenCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei 1 Publication<p>Manually curated information which has been inferred by a curator based on his/her scientific knowledge or on the scientific content of an article.</p> <p><a href="/manual/evidences#ECO:0000305">More…</a></p> Manual assertion inferred by curator fromi
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi | 84 | CalciumCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei 1 Publication<p>Manually curated information which has been inferred by a curator based on his/her scientific knowledge or on the scientific content of an article.</p> <p><a href="/manual/evidences#ECO:0000305">More…</a></p> Manual assertion inferred by curator fromi
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi | 87 | Calcium; via carbonyl oxygenCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei 1 Publication<p>Manually curated information which has been inferred by a curator based on his/her scientific knowledge or on the scientific content of an article.</p> <p><a href="/manual/evidences#ECO:0000305">More…</a></p> Manual assertion inferred by curator fromi
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi | 88 | Calcium; via carbonyl oxygenCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei 1 Publication<p>Manually curated information which has been inferred by a curator based on his/her scientific knowledge or on the scientific content of an article.</p> <p><a href="/manual/evidences#ECO:0000305">More…</a></p> Manual assertion inferred by curator fromi
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi | 100 | CalciumCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei 1 Publication<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi | 145 | CalciumCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei 1 Publication<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei | 147 | Aromatic amino acidCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei 2 Publications<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei | 168 | Aromatic amino acid; via carbonyl oxygenCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei 2 Publications<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei | 170 | Aromatic amino acidCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei 2 Publications<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi | 231 | CalciumCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei 1 Publication<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi | 234 | CalciumCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei 1 Publication<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei | 297 | Aromatic amino acidCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei 2 Publications<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei | 482 | Important for ability of agonist AMG 416 to activate G-protein-coupled receptor activity1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi | 557 | Calcium; via carbonyl oxygenCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei 1 Publication<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 |
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- amino acid binding Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- calcium ion binding Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- G-protein coupled receptor activity Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- phosphatidylinositol phospholipase C activity Source: ProtInc <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementi
- protein homodimerization activity Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi
- anatomical structure morphogenesis Source: ProtInc <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementi
- calcium ion import Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- cellular calcium ion homeostasis Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- chemosensory behavior Source: ProtInc <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementi
- detection of calcium ion Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- G-protein coupled receptor signaling pathway Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- ossification Source: ProtInc <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementi
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi
| Molecular function | G-protein coupled receptor, Receptor, Transducer |
| Ligand | Calcium, Metal-binding |
Enzyme and pathway databases
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-416476. G alpha (q) signalling events. R-HSA-418594. G alpha (i) signalling events. R-HSA-420499. Class C/3 (Metabotropic glutamate/pheromone receptors). |
SIGNOR Signaling Network Open Resource More...SIGNORi | P41180. |
Protein family/group databases
Transport Classification Database More...TCDBi | 9.A.14.7.2. the g-protein-coupled receptor (gpcr) family. |
<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi
| <p>This subsection of the ‘Names and Taxonomy’ section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi | Recommended name: Extracellular calcium-sensing receptorCuratedShort name: CaR2 Publications <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More…</a></p> Manual assertion based on opinion ini
Short name: CaSR Short name: hCasR1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More…</a></p> Manual assertion based on opinion ini
Alternative name(s): Parathyroid cell calcium-sensing receptor 11 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More…</a></p> Manual assertion based on opinion ini
Short name: PCaR11 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More…</a></p> Manual assertion based on opinion ini
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| <p>This subsection of the ‘Names and taxonomy’ section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi | Name:CASRImported <p>Manually validated information which has been imported from another database.</p> <p><a href="/manual/evidences#ECO:0000312">More…</a></p> Manual assertion inferred from database entriesi Synonyms:GPRC2A, PCAR11 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More…</a></p> Manual assertion based on opinion ini
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| <p>This subsection of the ‘Names and taxonomy’ section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>Organismi | Homo sapiens (Human) |
| <p>This subsection of the ‘Names and taxonomy’ section shows the unique identifier assigned by the <span class="caps">NCBI</span> to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri | 9606 [NCBI] |
| <p>This subsection of the ‘Names and taxonomy’ section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineagei | cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo |
| <p>This subsection of the “Names and Taxonomy” section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi |
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Organism-specific databases
Human Gene Nomenclature Database More...HGNCi | HGNC:1514. CASR. |
<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi
- Cell membrane 11 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
- Ref.11"Rab1 small GTP-binding protein regulates cell surface trafficking of the human calcium-sensing receptor."
Zhuang X., Adipietro K.A., Datta S., Northup J.K., Ray K.
Endocrinology 151:5114-5123(2010) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, GLYCOSYLATION. - Ref.21"Expression and characterization of inactivating and activating mutations in the human Ca2+o-sensing receptor."
Bai M., Quinn S., Trivedi S., Kifor O., Pearce S.H.S., Pollak M.R., Krapcho K., Hebert S.C., Brown E.M.
J. Biol. Chem. 271:19537-19545(1996) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS HHC1 MET-62; CYS-66; MET-138; GLU-143; GLN-185; LYS-297 AND TRP-795, VARIANT HYPOC1 ALA-127, FUNCTION, SUBCELLULAR LOCATION, GLYCOSYLATION, CHARACTERIZATION OF VARIANTS HHC1 MET-62; CYS-66; MET-138; GLU-143; GLN-185; LYS-297 AND TRP-795, CHARACTERIZATION OF VARIANT HYPOC1 ALA-127. - Ref.45"Functional characterization of calcium-sensing receptor codon 227 mutations presenting as either familial (benign) hypocalciuric hypercalcemia or neonatal hyperparathyroidism."
Wystrychowski A., Pidasheva S., Canaff L., Chudek J., Kokot F., Wiecek A., Hendy G.N.
J. Clin. Endocrinol. Metab. 90:864-870(2005) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT HHC1 GLN-227, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANT NSHPT LEU-227, CHARACTERIZATION OF VARIANT HHC1 GLN-227. - Ref.47"Calcium-sensing receptor dimerizes in the endoplasmic reticulum: biochemical and biophysical characterization of CASR mutants retained intracellularly."
Pidasheva S., Grant M., Canaff L., Ercan O., Kumar U., Hendy G.N.
Hum. Mol. Genet. 15:2200-2209(2006) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS HHC1 CYS-66; HIS-66 AND 583-ASN--SER-1078 DEL, SUBCELLULAR LOCATION, SUBUNIT, GLYCOSYLATION, CHARACTERIZATION OF VARIANTS CYS-66; HIS-66 AND 583-ASN--SER-1078 DEL. - Ref.50"Neonatal severe hyperparathyroidism associated with a novel de novo heterozygous R551K inactivating mutation and a heterozygous A986S polymorphism of the calcium-sensing receptor gene."
Toke J., Czirjak G., Patocs A., Enyedi B., Gergics P., Csakvary V., Enyedi P., Toth M.
Clin. Endocrinol. (Oxf.) 67:385-392(2007) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT NSHPT LYS-551, VARIANT SER-986, FUNCTION, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANT NSHPT LYS-551. - Ref.53"A novel loss-of-function mutation, Gln459Arg, of the calcium-sensing receptor gene associated with apparent autosomal recessive inheritance of familial hypocalciuric hypercalcemia."
Lietman S.A., Tenenbaum-Rakover Y., Jap T.S., Yi-Chi W., De-Ming Y., Ding C., Kussiny N., Levine M.A.
J. Clin. Endocrinol. Metab. 94:4372-4379(2009) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT HHC1 ARG-459, VARIANTS SER-986 AND GLN-1011, FUNCTION, CHARACTERIZATION OF VARIANT HHC1 ARG-459. - Ref.57"Agonist-driven maturation and plasma membrane insertion of calcium-sensing receptors dynamically control signal amplitude."
Grant M.P., Stepanchick A., Cavanaugh A., Breitwieser G.E.
Sci. Signal. 4:RA78-RA78(2011) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS HHC1 PRO-159 AND TRP-795, FUNCTION, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANTS HHC1 PRO-159 AND TRP-795. - Ref.62"Calcium-sensing-related gene mutations in hypercalcaemic hypocalciuric patients as differential diagnosis from primary hyperparathyroidism: detection of two novel inactivating mutations in an Italian population."
Stratta P., Merlotti G., Musetti C., Quaglia M., Pagani A., Izzo C., Radin E., Airoldi A., Baorda F., Palladino T., Leone M.P., Guarnieri V.
Nephrol. Dial. Transplant. 29:1902-1909(2014) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS HHC1 VAL-707 AND SER-774, FUNCTION, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANTS HHC1 VAL-707 AND SER-774. - Ref.63"Identification and functional analysis of a novel CaSR mutation in a family with familial hypocalciuric hypercalcemia."
Kim E.S., Kim S.Y., Lee J.Y., Han J.H., Sohn T.S., Son H.S., Moon S.D.
J. Bone Miner. Metab. 34:662-667(2016) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT HHC1 TRP-571, FUNCTION, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANT HHC1 TRP-571. - Ref.64"Novel activating mutation of human calcium-sensing receptor in a family with autosomal dominant hypocalcaemia."
Baran N., ter Braak M., Saffrich R., Woelfle J., Schmitz U.
Mol. Cell. Endocrinol. 407:18-25(2015) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT HYPOC1 LEU-136, FUNCTION, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANT HYPOC1 LEU-136. - Ref.65"CASR gene activating mutations in two families with autosomal dominant hypocalcemia."
Guarnieri V., Valentina D'Elia A., Baorda F., Pazienza V., Benegiamo G., Stanziale P., Copetti M., Battista C., Grimaldi F., Damante G., Pellegrini F., D'Agruma L., Zelante L., Carella M., Scillitani A.
Mol. Genet. Metab. 107:548-552(2012) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS HYPOC1 LEU-221; ARG-681 AND GLN-727, FUNCTION, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANTS HYPOC1 ARG-681 AND GLN-727.
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
- Ref.11"Rab1 small GTP-binding protein regulates cell surface trafficking of the human calcium-sensing receptor."
Zhuang X., Adipietro K.A., Datta S., Northup J.K., Ray K.
Endocrinology 151:5114-5123(2010) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, GLYCOSYLATION.
Topology
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">‘Subcellular location’</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini | 20 – 612 | ExtracellularSequence analysisAdd BLAST | 593 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">‘Subcellular location’</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei | 613 – 635 | Helical; Name=1Sequence analysisAdd BLAST | 23 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">‘Subcellular location’</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini | 636 – 649 | CytoplasmicSequence analysisAdd BLAST | 14 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">‘Subcellular location’</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei | 650 – 670 | Helical; Name=2Sequence analysisAdd BLAST | 21 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">‘Subcellular location’</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini | 671 – 681 | ExtracellularSequence analysisAdd BLAST | 11 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">‘Subcellular location’</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei | 682 – 700 | Helical; Name=3Sequence analysisAdd BLAST | 19 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">‘Subcellular location’</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini | 701 – 724 | CytoplasmicSequence analysisAdd BLAST | 24 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">‘Subcellular location’</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei | 725 – 745 | Helical; Name=4Sequence analysisAdd BLAST | 21 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">‘Subcellular location’</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini | 746 – 769 | ExtracellularSequence analysisAdd BLAST | 24 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">‘Subcellular location’</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei | 770 – 792 | Helical; Name=5Sequence analysisAdd BLAST | 23 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">‘Subcellular location’</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini | 793 – 805 | CytoplasmicSequence analysisAdd BLAST | 13 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">‘Subcellular location’</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei | 806 – 828 | Helical; Name=6Sequence analysisAdd BLAST | 23 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">‘Subcellular location’</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini | 829 – 836 | ExtracellularSequence analysis | 8 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">‘Subcellular location’</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei | 837 – 862 | Helical; Name=7Sequence analysisAdd BLAST | 26 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">‘Subcellular location’</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini | 863 – 1078 | CytoplasmicSequence analysisAdd BLAST | 216 |
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Cellular componenti
- integral component of plasma membrane Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- plasma membrane Source: Reactome
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Cellular componenti
Cell membrane, Membrane<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi
<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim"><span class="caps">OMIM</span></a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei
Hypocalciuric hypercalcemia, familial 1 (HHC1)26 Publications
<p>Manually curated information for which there is published experimental evidence.</p>
<p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
- Ref.7"Familial hypocalciuric hypercalcemia associated with mutation in the human Ca(2+)-sensing receptor gene."
Aida K., Koishi S., Inoue M., Nakazato M., Tawata M., Onaya T.
J. Clin. Endocrinol. Metab. 80:2594-2598(1995) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-61, VARIANT HHC1 ALA-39. - Ref.13"Structural mechanism of ligand activation in human calcium-sensing receptor."
Geng Y., Mosyak L., Kurinov I., Zuo H., Sturchler E., Cheng T.C., Subramanyam P., Brown A.P., Brennan S.C., Mun H.C., Bush M., Chen Y., Nguyen T.X., Cao B., Chang D.D., Quick M., Conigrave A.D., Colecraft H.M., McDonald P., Fan Q.R.
Elife 5:0-0(2016) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 20-607 IN COMPLEX WITH CALCIUM; ANION AND TRYPTOPHAN, FUNCTION, ENZYME REGULATION, DOMAIN, DISULFIDE BONDS, GLYCOSYLATION AT ASN-261; ASN-287; ASN-446; ASN-468; ASN-488; ASN-541 AND ASN-594, MUTAGENESIS OF ARG-69; ASN-102; THR-145; SER-147; SER-170; TYR-218; SER-417 AND TRP-458, CHARACTERIZATION OF VARIANTS NSHPT ILE-100; LEU-227 AND LYS-551, CHARACTERIZATION OF VARIANTS HHC1 HIS-66; MET-81; PRO-159; GLY-172; GLY-215; LYS-297 AND GLU-557. - Ref.15"Mutations in the human Ca(2+)-sensing receptor gene cause familial hypocalciuric hypercalcemia and neonatal severe hyperparathyroidism."
Pollak M.R., Brown E.M., Chou Y.-H.W., Hebert S.C., Marx S.J., Steinmann B., Levi T., Seidman C.E., Seidman J.G.
Cell 75:1297-1303(1993) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS HHC1 GLN-185; LYS-297 AND TRP-795. - Ref.17"Mutations in the human Ca(2+)-sensing-receptor gene that cause familial hypocalciuric hypercalcemia."
Chou Y.-H.W., Pollak M.R., Brandi M.L., Toss G., Arnqvist H., Atkinson A.B., Papapoulos S.E., Marx S., Brown E.M., Seidman J.G., Seidman C.E.
Am. J. Hum. Genet. 56:1075-1079(1995) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS HHC1 MET-62; CYS-66; MET-138; GLU-143 AND GLN-227. - Ref.21"Expression and characterization of inactivating and activating mutations in the human Ca2+o-sensing receptor."
Bai M., Quinn S., Trivedi S., Kifor O., Pearce S.H.S., Pollak M.R., Krapcho K., Hebert S.C., Brown E.M.
J. Biol. Chem. 271:19537-19545(1996) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS HHC1 MET-62; CYS-66; MET-138; GLU-143; GLN-185; LYS-297 AND TRP-795, VARIANT HYPOC1 ALA-127, FUNCTION, SUBCELLULAR LOCATION, GLYCOSYLATION, CHARACTERIZATION OF VARIANTS HHC1 MET-62; CYS-66; MET-138; GLU-143; GLN-185; LYS-297 AND TRP-795, CHARACTERIZATION OF VARIANT HYPOC1 ALA-127. - Ref.22"Clustered inactivating mutations and benign polymorphisms of the calcium receptor gene in familial benign hypocalciuric hypercalcemia suggest receptor functional domains."
Heath H. III, Odelberg S., Jackson C.E., Teh B.T., Hayward N., Larsson C., Buist N.R., Krapcho K.J., Hung B.C., Capuano I.V., Garrett J.E., Leppert M.F.
J. Clin. Endocrinol. Metab. 81:1312-1317(1996) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS HHC1 PRO-53; LEU-55; GLN-185; GLY-215; TYR-657 AND ARG-748, VARIANTS SER-986; GLY-990 AND GLN-1011, CHARACTERIZATION OF VARIANTS HHC1 PRO-53; LEU-55 AND GLY-215. - Ref.23"Functional characterization of calcium-sensing receptor mutations expressed in human embryonic kidney cells."
Pearce S.H.S., Bai M., Quinn S.J., Kifor O., Brown E.M., Thakker R.V.
J. Clin. Invest. 98:1860-1866(1996) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS HHC1 LEU-55; ASP-178; SER-221 AND ILE-817, VARIANTS HYPOC1 LEU-128; MET-151 AND LYS-191, VARIANT NSHPT LEU-227, CHARACTERIZATION OF VARIANTS HHC1 LEU-55; ASP-178; SER-221 AND ILE-817, FUNCTION, CHARACTERIZATION OF VARIANTS HYPOC1 LEU-128; MET-151 AND LYS-191, CHARACTERIZATION OF VARIANT NSHPT LEU-227. - Ref.24"A novel mutation (L174R) in the Ca2+-sensing receptor gene associated with familial hypocalciuric hypercalcemia."
Ward B.K., Stuckey B.G.A., Gutteridge D.H., Laing N.G., Pullan P.T., Ratajczak T.
Hum. Mutat. 10:233-235(1997) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT HHC1 ARG-174. - Ref.33"A novel mutation in Ca2+-sensing receptor gene in familial hypocalciuric hypercalcemia."
Nakayama T., Minato M., Nakagawa M., Soma M., Tobe H., Aoi N., Kosuge K., Sato M., Ozawa Y., Kanmatsuse K., Kokubun S.
Endocrine 15:277-282(2001) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT HHC1 GLU-557. - Ref.41"Severe hypercalcemia in a 9-year-old Brazilian girl due to a novel inactivating mutation of the calcium-sensing receptor."
Miyashiro K., Kunii I., Manna T.D., de Menezes Filho H.C., Damiani D., Setian N., Hauache O.M.
J. Clin. Endocrinol. Metab. 89:5936-5941(2004) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT HHC1 PRO-13, CHARACTERIZATION OF VARIANT HHC1 PRO-13. - Ref.44"Impaired cotranslational processing of the calcium-sensing receptor due to signal peptide missense mutations in familial hypocalciuric hypercalcemia."
Pidasheva S., Canaff L., Simonds W.F., Marx S.J., Hendy G.N.
Hum. Mol. Genet. 14:1679-1690(2005) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS HHC1 SER-11 AND PRO-13, VARIANT ALA-14, CHARACTERIZATION OF VARIANTS HHC1 SER-11 AND PRO-13, CHARACTERIZATION OF VARIANT ALA-14. - Ref.45"Functional characterization of calcium-sensing receptor codon 227 mutations presenting as either familial (benign) hypocalciuric hypercalcemia or neonatal hyperparathyroidism."
Wystrychowski A., Pidasheva S., Canaff L., Chudek J., Kokot F., Wiecek A., Hendy G.N.
J. Clin. Endocrinol. Metab. 90:864-870(2005) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT HHC1 GLN-227, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANT NSHPT LEU-227, CHARACTERIZATION OF VARIANT HHC1 GLN-227. - Ref.46"Identification of a novel inactivating R465Q mutation of the calcium-sensing receptor."
Leech C., Lohse P., Stanojevic V., Lechner A., Goeke B., Spitzweg C.
Biochem. Biophys. Res. Commun. 342:996-1002(2006) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT HHC1 GLN-465, CHARACTERIZATION OF VARIANT HHC1 GLN-465, VARIANT SER-986. - Ref.47"Calcium-sensing receptor dimerizes in the endoplasmic reticulum: biochemical and biophysical characterization of CASR mutants retained intracellularly."
Pidasheva S., Grant M., Canaff L., Ercan O., Kumar U., Hendy G.N.
Hum. Mol. Genet. 15:2200-2209(2006) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS HHC1 CYS-66; HIS-66 AND 583-ASN--SER-1078 DEL, SUBCELLULAR LOCATION, SUBUNIT, GLYCOSYLATION, CHARACTERIZATION OF VARIANTS CYS-66; HIS-66 AND 583-ASN--SER-1078 DEL. - Ref.49"Identification and functional characterization of a novel mutation in the calcium-sensing receptor gene in familial hypocalciuric hypercalcemia: modulation of clinical severity by vitamin D status."
Zajickova K., Vrbikova J., Canaff L., Pawelek P.D., Goltzman D., Hendy G.N.
J. Clin. Endocrinol. Metab. 92:2616-2623(2007) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT HHC1 CYS-180, CHARACTERIZATION OF VARIANT HHC1 CYS-180. - Ref.51"Molecular genetic analysis of the calcium sensing receptor gene in patients clinically suspected to have familial hypocalciuric hypercalcemia: phenotypic variation and mutation spectrum in a Danish population."
Nissen P.H., Christensen S.E., Heickendorff L., Brixen K., Mosekilde L.
J. Clin. Endocrinol. Metab. 92:4373-4379(2007) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS HHC1 ARG-21; ASN-171; GLN-221; THR-225; PHE-271; ARG-397; ARG-509; ARG-553; VAL-555; TYR-562; PHE-582; TYR-582; ASP-623; ARG-670; PHE-728; ARG-742 AND TRP-886, VARIANTS LYS-250; SER-986; GLY-990 AND GLN-1011. - Ref.53"A novel loss-of-function mutation, Gln459Arg, of the calcium-sensing receptor gene associated with apparent autosomal recessive inheritance of familial hypocalciuric hypercalcemia."
Lietman S.A., Tenenbaum-Rakover Y., Jap T.S., Yi-Chi W., De-Ming Y., Ding C., Kussiny N., Levine M.A.
J. Clin. Endocrinol. Metab. 94:4372-4379(2009) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT HHC1 ARG-459, VARIANTS SER-986 AND GLN-1011, FUNCTION, CHARACTERIZATION OF VARIANT HHC1 ARG-459. - Ref.54"Calcium-sensing receptor mutations and denaturing high performance liquid chromatography."
Cole D.E., Yun F.H., Wong B.Y., Shuen A.Y., Booth R.A., Scillitani A., Pidasheva S., Zhou X., Canaff L., Hendy G.N.
J. Mol. Endocrinol. 42:331-339(2009) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS HHC1 SER-42; LEU-55; HIS-66; MET-81; MET-138; ARG-143; ARG-158; GLY-166; TRP-220; ARG-549; TYR-562; GLY-565; TYR-582; 583-ASN--SER-1078 DEL; TYR-661; HIS-680; ILE-761 DEL AND TRP-795, VARIANTS HYPOC1 LYS-118; PHE-125; ARG-129; LYS-228; LYS-604; ILE-802; SER-830; LEU-832 AND SER-832. - Ref.56"A novel mutation in the calcium-sensing receptor in a French family with familial hypocalciuric hypercalcaemia."
Al-Salameh A., Cetani F., Pardi E., Vulpoi C., Pierre P., de Calan L., Guyetant S., Jeunemaitre X., Lecomte P.
Eur. J. Endocrinol. 165:359-363(2011) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT HHC1 ILE-550, FUNCTION, CHARACTERIZATION OF VARIANT HHC1 ILE-550. - Ref.57"Agonist-driven maturation and plasma membrane insertion of calcium-sensing receptors dynamically control signal amplitude."
Grant M.P., Stepanchick A., Cavanaugh A., Breitwieser G.E.
Sci. Signal. 4:RA78-RA78(2011) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS HHC1 PRO-159 AND TRP-795, FUNCTION, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANTS HHC1 PRO-159 AND TRP-795. - Ref.58"Familial hypocalciuric hypercalcemia: new mutation in the CASR gene converting valine 697 to methionine."
Aparicio Lopez C., Anton-Martin P., Gil-Fournier B., Ramiro-Leon S., Perez-Nanclares G., Perez de Nanclares G., Martinez Menendez B., Castano L.
Eur. J. Pediatr. 171:147-150(2012) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT HHC1 MET-697. - Ref.59"Loss-of-function and gain-of-function mutations of calcium-sensing receptor: functional analysis and the effect of allosteric modulators NPS R-568 and NPS 2143."
Nakamura A., Hotsubo T., Kobayashi K., Mochizuki H., Ishizu K., Tajima T.
J. Clin. Endocrinol. Metab. 98:E1692-E1701(2013) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS HHC1 THR-110 AND GLY-172, VARIANTS HYPOC1 CYS-122; HIS-569 AND THR-839, FUNCTION, CHARACTERIZATION OF VARIANTS HHC1 THR-110 AND GLY-172, CHARACTERIZATION OF VARIANTS HYPOC1 CYS-122; HIS-569 AND THR-839. - Ref.60"Two novel mutations of the calcium-sensing receptor gene affecting the same amino acid position lead to opposite phenotypes and reveal the importance of p.N802 on receptor activity."
Lia-Baldini A.S., Magdelaine C., Nizou A., Airault C., Salles J.P., Moulin P., Delemer B., Aitouares M., Funalot B., Sturtz F., Lienhardt-Roussie A.
Eur. J. Endocrinol. 168:K27-K34(2013) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT HHC1 SER-802, VARIANT HYPOC1 ILE-802. - Ref.61"A novel mutation in calcium-sensing receptor gene associated to hypercalcemia and hypercalciuria."
Mastromatteo E., Lamacchia O., Campo M.R., Conserva A., Baorda F., Cinque L., Guarnieri V., Scillitani A., Cignarelli M.
BMC Endocr. Disord. 14:81-81(2014) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT HHC1 MET-972, FUNCTION, CHARACTERIZATION OF VARIANT HHC1 MET-972. - Ref.62"Calcium-sensing-related gene mutations in hypercalcaemic hypocalciuric patients as differential diagnosis from primary hyperparathyroidism: detection of two novel inactivating mutations in an Italian population."
Stratta P., Merlotti G., Musetti C., Quaglia M., Pagani A., Izzo C., Radin E., Airoldi A., Baorda F., Palladino T., Leone M.P., Guarnieri V.
Nephrol. Dial. Transplant. 29:1902-1909(2014) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS HHC1 VAL-707 AND SER-774, FUNCTION, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANTS HHC1 VAL-707 AND SER-774. - Ref.63"Identification and functional analysis of a novel CaSR mutation in a family with familial hypocalciuric hypercalcemia."
Kim E.S., Kim S.Y., Lee J.Y., Han J.H., Sohn T.S., Son H.S., Moon S.D.
J. Bone Miner. Metab. 34:662-667(2016) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT HHC1 TRP-571, FUNCTION, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANT HHC1 TRP-571.
Ref.7
"Familial hypocalciuric hypercalcemia associated with mutation in the human Ca(2+)-sensing receptor gene."
Aida K., Koishi S., Inoue M., Nakazato M., Tawata M., Onaya T.
J. Clin. Endocrinol. Metab. 80:2594-2598(1995) [PubMed] [Europe PMC] [Abstract]
Aida K., Koishi S., Inoue M., Nakazato M., Tawata M., Onaya T.
J. Clin. Endocrinol. Metab. 80:2594-2598(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-61, VARIANT HHC1 ALA-39.
Ref.13
"Structural mechanism of ligand activation in human calcium-sensing receptor."
Geng Y., Mosyak L., Kurinov I., Zuo H., Sturchler E., Cheng T.C., Subramanyam P., Brown A.P., Brennan S.C., Mun H.C., Bush M., Chen Y., Nguyen T.X., Cao B., Chang D.D., Quick M., Conigrave A.D., Colecraft H.M., McDonald P., Fan Q.R.
Elife 5:0-0(2016) [PubMed] [Europe PMC] [Abstract]
Geng Y., Mosyak L., Kurinov I., Zuo H., Sturchler E., Cheng T.C., Subramanyam P., Brown A.P., Brennan S.C., Mun H.C., Bush M., Chen Y., Nguyen T.X., Cao B., Chang D.D., Quick M., Conigrave A.D., Colecraft H.M., McDonald P., Fan Q.R.
Elife 5:0-0(2016) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 20-607 IN COMPLEX WITH CALCIUM; ANION AND TRYPTOPHAN, FUNCTION, ENZYME REGULATION, DOMAIN, DISULFIDE BONDS, GLYCOSYLATION AT ASN-261; ASN-287; ASN-446; ASN-468; ASN-488; ASN-541 AND ASN-594, MUTAGENESIS OF ARG-69; ASN-102; THR-145; SER-147; SER-170; TYR-218; SER-417 AND TRP-458, CHARACTERIZATION OF VARIANTS NSHPT ILE-100; LEU-227 AND LYS-551, CHARACTERIZATION OF VARIANTS HHC1 HIS-66; MET-81; PRO-159; GLY-172; GLY-215; LYS-297 AND GLU-557.
Ref.15
"Mutations in the human Ca(2+)-sensing receptor gene cause familial hypocalciuric hypercalcemia and neonatal severe hyperparathyroidism."
Pollak M.R., Brown E.M., Chou Y.-H.W., Hebert S.C., Marx S.J., Steinmann B., Levi T., Seidman C.E., Seidman J.G.
Cell 75:1297-1303(1993) [PubMed] [Europe PMC] [Abstract]
Pollak M.R., Brown E.M., Chou Y.-H.W., Hebert S.C., Marx S.J., Steinmann B., Levi T., Seidman C.E., Seidman J.G.
Cell 75:1297-1303(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HHC1 GLN-185; LYS-297 AND TRP-795.
Ref.17
"Mutations in the human Ca(2+)-sensing-receptor gene that cause familial hypocalciuric hypercalcemia."
Chou Y.-H.W., Pollak M.R., Brandi M.L., Toss G., Arnqvist H., Atkinson A.B., Papapoulos S.E., Marx S., Brown E.M., Seidman J.G., Seidman C.E.
Am. J. Hum. Genet. 56:1075-1079(1995) [PubMed] [Europe PMC] [Abstract]
Chou Y.-H.W., Pollak M.R., Brandi M.L., Toss G., Arnqvist H., Atkinson A.B., Papapoulos S.E., Marx S., Brown E.M., Seidman J.G., Seidman C.E.
Am. J. Hum. Genet. 56:1075-1079(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HHC1 MET-62; CYS-66; MET-138; GLU-143 AND GLN-227.
Ref.21
"Expression and characterization of inactivating and activating mutations in the human Ca2+o-sensing receptor."
Bai M., Quinn S., Trivedi S., Kifor O., Pearce S.H.S., Pollak M.R., Krapcho K., Hebert S.C., Brown E.M.
J. Biol. Chem. 271:19537-19545(1996) [PubMed] [Europe PMC] [Abstract]
Bai M., Quinn S., Trivedi S., Kifor O., Pearce S.H.S., Pollak M.R., Krapcho K., Hebert S.C., Brown E.M.
J. Biol. Chem. 271:19537-19545(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HHC1 MET-62; CYS-66; MET-138; GLU-143; GLN-185; LYS-297 AND TRP-795, VARIANT HYPOC1 ALA-127, FUNCTION, SUBCELLULAR LOCATION, GLYCOSYLATION, CHARACTERIZATION OF VARIANTS HHC1 MET-62; CYS-66; MET-138; GLU-143; GLN-185; LYS-297 AND TRP-795, CHARACTERIZATION OF VARIANT HYPOC1 ALA-127.
Ref.22
"Clustered inactivating mutations and benign polymorphisms of the calcium receptor gene in familial benign hypocalciuric hypercalcemia suggest receptor functional domains."
Heath H. III, Odelberg S., Jackson C.E., Teh B.T., Hayward N., Larsson C., Buist N.R., Krapcho K.J., Hung B.C., Capuano I.V., Garrett J.E., Leppert M.F.
J. Clin. Endocrinol. Metab. 81:1312-1317(1996) [PubMed] [Europe PMC] [Abstract]
Heath H. III, Odelberg S., Jackson C.E., Teh B.T., Hayward N., Larsson C., Buist N.R., Krapcho K.J., Hung B.C., Capuano I.V., Garrett J.E., Leppert M.F.
J. Clin. Endocrinol. Metab. 81:1312-1317(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HHC1 PRO-53; LEU-55; GLN-185; GLY-215; TYR-657 AND ARG-748, VARIANTS SER-986; GLY-990 AND GLN-1011, CHARACTERIZATION OF VARIANTS HHC1 PRO-53; LEU-55 AND GLY-215.
Ref.23
"Functional characterization of calcium-sensing receptor mutations expressed in human embryonic kidney cells."
Pearce S.H.S., Bai M., Quinn S.J., Kifor O., Brown E.M., Thakker R.V.
J. Clin. Invest. 98:1860-1866(1996) [PubMed] [Europe PMC] [Abstract]
Pearce S.H.S., Bai M., Quinn S.J., Kifor O., Brown E.M., Thakker R.V.
J. Clin. Invest. 98:1860-1866(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HHC1 LEU-55; ASP-178; SER-221 AND ILE-817, VARIANTS HYPOC1 LEU-128; MET-151 AND LYS-191, VARIANT NSHPT LEU-227, CHARACTERIZATION OF VARIANTS HHC1 LEU-55; ASP-178; SER-221 AND ILE-817, FUNCTION, CHARACTERIZATION OF VARIANTS HYPOC1 LEU-128; MET-151 AND LYS-191, CHARACTERIZATION OF VARIANT NSHPT LEU-227.
Ref.24
"A novel mutation (L174R) in the Ca2+-sensing receptor gene associated with familial hypocalciuric hypercalcemia."
Ward B.K., Stuckey B.G.A., Gutteridge D.H., Laing N.G., Pullan P.T., Ratajczak T.
Hum. Mutat. 10:233-235(1997) [PubMed] [Europe PMC] [Abstract]
Ward B.K., Stuckey B.G.A., Gutteridge D.H., Laing N.G., Pullan P.T., Ratajczak T.
Hum. Mutat. 10:233-235(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HHC1 ARG-174.
Ref.33
"A novel mutation in Ca2+-sensing receptor gene in familial hypocalciuric hypercalcemia."
Nakayama T., Minato M., Nakagawa M., Soma M., Tobe H., Aoi N., Kosuge K., Sato M., Ozawa Y., Kanmatsuse K., Kokubun S.
Endocrine 15:277-282(2001) [PubMed] [Europe PMC] [Abstract]
Nakayama T., Minato M., Nakagawa M., Soma M., Tobe H., Aoi N., Kosuge K., Sato M., Ozawa Y., Kanmatsuse K., Kokubun S.
Endocrine 15:277-282(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HHC1 GLU-557.
Ref.41
"Severe hypercalcemia in a 9-year-old Brazilian girl due to a novel inactivating mutation of the calcium-sensing receptor."
Miyashiro K., Kunii I., Manna T.D., de Menezes Filho H.C., Damiani D., Setian N., Hauache O.M.
J. Clin. Endocrinol. Metab. 89:5936-5941(2004) [PubMed] [Europe PMC] [Abstract]
Miyashiro K., Kunii I., Manna T.D., de Menezes Filho H.C., Damiani D., Setian N., Hauache O.M.
J. Clin. Endocrinol. Metab. 89:5936-5941(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HHC1 PRO-13, CHARACTERIZATION OF VARIANT HHC1 PRO-13.
Ref.44
"Impaired cotranslational processing of the calcium-sensing receptor due to signal peptide missense mutations in familial hypocalciuric hypercalcemia."
Pidasheva S., Canaff L., Simonds W.F., Marx S.J., Hendy G.N.
Hum. Mol. Genet. 14:1679-1690(2005) [PubMed] [Europe PMC] [Abstract]
Pidasheva S., Canaff L., Simonds W.F., Marx S.J., Hendy G.N.
Hum. Mol. Genet. 14:1679-1690(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HHC1 SER-11 AND PRO-13, VARIANT ALA-14, CHARACTERIZATION OF VARIANTS HHC1 SER-11 AND PRO-13, CHARACTERIZATION OF VARIANT ALA-14.
Ref.45
"Functional characterization of calcium-sensing receptor codon 227 mutations presenting as either familial (benign) hypocalciuric hypercalcemia or neonatal hyperparathyroidism."
Wystrychowski A., Pidasheva S., Canaff L., Chudek J., Kokot F., Wiecek A., Hendy G.N.
J. Clin. Endocrinol. Metab. 90:864-870(2005) [PubMed] [Europe PMC] [Abstract]
Wystrychowski A., Pidasheva S., Canaff L., Chudek J., Kokot F., Wiecek A., Hendy G.N.
J. Clin. Endocrinol. Metab. 90:864-870(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HHC1 GLN-227, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANT NSHPT LEU-227, CHARACTERIZATION OF VARIANT HHC1 GLN-227.
Ref.46
"Identification of a novel inactivating R465Q mutation of the calcium-sensing receptor."
Leech C., Lohse P., Stanojevic V., Lechner A., Goeke B., Spitzweg C.
Biochem. Biophys. Res. Commun. 342:996-1002(2006) [PubMed] [Europe PMC] [Abstract]
Leech C., Lohse P., Stanojevic V., Lechner A., Goeke B., Spitzweg C.
Biochem. Biophys. Res. Commun. 342:996-1002(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HHC1 GLN-465, CHARACTERIZATION OF VARIANT HHC1 GLN-465, VARIANT SER-986.
Ref.47
"Calcium-sensing receptor dimerizes in the endoplasmic reticulum: biochemical and biophysical characterization of CASR mutants retained intracellularly."
Pidasheva S., Grant M., Canaff L., Ercan O., Kumar U., Hendy G.N.
Hum. Mol. Genet. 15:2200-2209(2006) [PubMed] [Europe PMC] [Abstract]
Pidasheva S., Grant M., Canaff L., Ercan O., Kumar U., Hendy G.N.
Hum. Mol. Genet. 15:2200-2209(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HHC1 CYS-66; HIS-66 AND 583-ASN--SER-1078 DEL, SUBCELLULAR LOCATION, SUBUNIT, GLYCOSYLATION, CHARACTERIZATION OF VARIANTS CYS-66; HIS-66 AND 583-ASN--SER-1078 DEL.
Ref.49
"Identification and functional characterization of a novel mutation in the calcium-sensing receptor gene in familial hypocalciuric hypercalcemia: modulation of clinical severity by vitamin D status."
Zajickova K., Vrbikova J., Canaff L., Pawelek P.D., Goltzman D., Hendy G.N.
J. Clin. Endocrinol. Metab. 92:2616-2623(2007) [PubMed] [Europe PMC] [Abstract]
Zajickova K., Vrbikova J., Canaff L., Pawelek P.D., Goltzman D., Hendy G.N.
J. Clin. Endocrinol. Metab. 92:2616-2623(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HHC1 CYS-180, CHARACTERIZATION OF VARIANT HHC1 CYS-180.
Ref.51
"Molecular genetic analysis of the calcium sensing receptor gene in patients clinically suspected to have familial hypocalciuric hypercalcemia: phenotypic variation and mutation spectrum in a Danish population."
Nissen P.H., Christensen S.E., Heickendorff L., Brixen K., Mosekilde L.
J. Clin. Endocrinol. Metab. 92:4373-4379(2007) [PubMed] [Europe PMC] [Abstract]
Nissen P.H., Christensen S.E., Heickendorff L., Brixen K., Mosekilde L.
J. Clin. Endocrinol. Metab. 92:4373-4379(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HHC1 ARG-21; ASN-171; GLN-221; THR-225; PHE-271; ARG-397; ARG-509; ARG-553; VAL-555; TYR-562; PHE-582; TYR-582; ASP-623; ARG-670; PHE-728; ARG-742 AND TRP-886, VARIANTS LYS-250; SER-986; GLY-990 AND GLN-1011.
Ref.53
"A novel loss-of-function mutation, Gln459Arg, of the calcium-sensing receptor gene associated with apparent autosomal recessive inheritance of familial hypocalciuric hypercalcemia."
Lietman S.A., Tenenbaum-Rakover Y., Jap T.S., Yi-Chi W., De-Ming Y., Ding C., Kussiny N., Levine M.A.
J. Clin. Endocrinol. Metab. 94:4372-4379(2009) [PubMed] [Europe PMC] [Abstract]
Lietman S.A., Tenenbaum-Rakover Y., Jap T.S., Yi-Chi W., De-Ming Y., Ding C., Kussiny N., Levine M.A.
J. Clin. Endocrinol. Metab. 94:4372-4379(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HHC1 ARG-459, VARIANTS SER-986 AND GLN-1011, FUNCTION, CHARACTERIZATION OF VARIANT HHC1 ARG-459.
Ref.54
"Calcium-sensing receptor mutations and denaturing high performance liquid chromatography."
Cole D.E., Yun F.H., Wong B.Y., Shuen A.Y., Booth R.A., Scillitani A., Pidasheva S., Zhou X., Canaff L., Hendy G.N.
J. Mol. Endocrinol. 42:331-339(2009) [PubMed] [Europe PMC] [Abstract]
Cole D.E., Yun F.H., Wong B.Y., Shuen A.Y., Booth R.A., Scillitani A., Pidasheva S., Zhou X., Canaff L., Hendy G.N.
J. Mol. Endocrinol. 42:331-339(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HHC1 SER-42; LEU-55; HIS-66; MET-81; MET-138; ARG-143; ARG-158; GLY-166; TRP-220; ARG-549; TYR-562; GLY-565; TYR-582; 583-ASN--SER-1078 DEL; TYR-661; HIS-680; ILE-761 DEL AND TRP-795, VARIANTS HYPOC1 LYS-118; PHE-125; ARG-129; LYS-228; LYS-604; ILE-802; SER-830; LEU-832 AND SER-832.
Ref.56
"A novel mutation in the calcium-sensing receptor in a French family with familial hypocalciuric hypercalcaemia."
Al-Salameh A., Cetani F., Pardi E., Vulpoi C., Pierre P., de Calan L., Guyetant S., Jeunemaitre X., Lecomte P.
Eur. J. Endocrinol. 165:359-363(2011) [PubMed] [Europe PMC] [Abstract]
Al-Salameh A., Cetani F., Pardi E., Vulpoi C., Pierre P., de Calan L., Guyetant S., Jeunemaitre X., Lecomte P.
Eur. J. Endocrinol. 165:359-363(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HHC1 ILE-550, FUNCTION, CHARACTERIZATION OF VARIANT HHC1 ILE-550.
Ref.57
"Agonist-driven maturation and plasma membrane insertion of calcium-sensing receptors dynamically control signal amplitude."
Grant M.P., Stepanchick A., Cavanaugh A., Breitwieser G.E.
Sci. Signal. 4:RA78-RA78(2011) [PubMed] [Europe PMC] [Abstract]
Grant M.P., Stepanchick A., Cavanaugh A., Breitwieser G.E.
Sci. Signal. 4:RA78-RA78(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HHC1 PRO-159 AND TRP-795, FUNCTION, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANTS HHC1 PRO-159 AND TRP-795.
Ref.58
"Familial hypocalciuric hypercalcemia: new mutation in the CASR gene converting valine 697 to methionine."
Aparicio Lopez C., Anton-Martin P., Gil-Fournier B., Ramiro-Leon S., Perez-Nanclares G., Perez de Nanclares G., Martinez Menendez B., Castano L.
Eur. J. Pediatr. 171:147-150(2012) [PubMed] [Europe PMC] [Abstract]
Aparicio Lopez C., Anton-Martin P., Gil-Fournier B., Ramiro-Leon S., Perez-Nanclares G., Perez de Nanclares G., Martinez Menendez B., Castano L.
Eur. J. Pediatr. 171:147-150(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HHC1 MET-697.
Ref.59
"Loss-of-function and gain-of-function mutations of calcium-sensing receptor: functional analysis and the effect of allosteric modulators NPS R-568 and NPS 2143."
Nakamura A., Hotsubo T., Kobayashi K., Mochizuki H., Ishizu K., Tajima T.
J. Clin. Endocrinol. Metab. 98:E1692-E1701(2013) [PubMed] [Europe PMC] [Abstract]
Nakamura A., Hotsubo T., Kobayashi K., Mochizuki H., Ishizu K., Tajima T.
J. Clin. Endocrinol. Metab. 98:E1692-E1701(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HHC1 THR-110 AND GLY-172, VARIANTS HYPOC1 CYS-122; HIS-569 AND THR-839, FUNCTION, CHARACTERIZATION OF VARIANTS HHC1 THR-110 AND GLY-172, CHARACTERIZATION OF VARIANTS HYPOC1 CYS-122; HIS-569 AND THR-839.
Ref.60
"Two novel mutations of the calcium-sensing receptor gene affecting the same amino acid position lead to opposite phenotypes and reveal the importance of p.N802 on receptor activity."
Lia-Baldini A.S., Magdelaine C., Nizou A., Airault C., Salles J.P., Moulin P., Delemer B., Aitouares M., Funalot B., Sturtz F., Lienhardt-Roussie A.
Eur. J. Endocrinol. 168:K27-K34(2013) [PubMed] [Europe PMC] [Abstract]
Lia-Baldini A.S., Magdelaine C., Nizou A., Airault C., Salles J.P., Moulin P., Delemer B., Aitouares M., Funalot B., Sturtz F., Lienhardt-Roussie A.
Eur. J. Endocrinol. 168:K27-K34(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HHC1 SER-802, VARIANT HYPOC1 ILE-802.
Ref.61
"A novel mutation in calcium-sensing receptor gene associated to hypercalcemia and hypercalciuria."
Mastromatteo E., Lamacchia O., Campo M.R., Conserva A., Baorda F., Cinque L., Guarnieri V., Scillitani A., Cignarelli M.
BMC Endocr. Disord. 14:81-81(2014) [PubMed] [Europe PMC] [Abstract]
Mastromatteo E., Lamacchia O., Campo M.R., Conserva A., Baorda F., Cinque L., Guarnieri V., Scillitani A., Cignarelli M.
BMC Endocr. Disord. 14:81-81(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HHC1 MET-972, FUNCTION, CHARACTERIZATION OF VARIANT HHC1 MET-972.
Ref.62
"Calcium-sensing-related gene mutations in hypercalcaemic hypocalciuric patients as differential diagnosis from primary hyperparathyroidism: detection of two novel inactivating mutations in an Italian population."
Stratta P., Merlotti G., Musetti C., Quaglia M., Pagani A., Izzo C., Radin E., Airoldi A., Baorda F., Palladino T., Leone M.P., Guarnieri V.
Nephrol. Dial. Transplant. 29:1902-1909(2014) [PubMed] [Europe PMC] [Abstract]
Stratta P., Merlotti G., Musetti C., Quaglia M., Pagani A., Izzo C., Radin E., Airoldi A., Baorda F., Palladino T., Leone M.P., Guarnieri V.
Nephrol. Dial. Transplant. 29:1902-1909(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HHC1 VAL-707 AND SER-774, FUNCTION, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANTS HHC1 VAL-707 AND SER-774.
Ref.63
"Identification and functional analysis of a novel CaSR mutation in a family with familial hypocalciuric hypercalcemia."
Kim E.S., Kim S.Y., Lee J.Y., Han J.H., Sohn T.S., Son H.S., Moon S.D.
J. Bone Miner. Metab. 34:662-667(2016) [PubMed] [Europe PMC] [Abstract]
Kim E.S., Kim S.Y., Lee J.Y., Han J.H., Sohn T.S., Son H.S., Moon S.D.
J. Bone Miner. Metab. 34:662-667(2016) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HHC1 TRP-571, FUNCTION, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANT HHC1 TRP-571.
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of hypocalciuric hypercalcemia, a disorder of mineral homeostasis that is transmitted as an autosomal dominant trait with a high degree of penetrance. It is characterized biochemically by lifelong elevation of serum calcium concentrations and is associated with inappropriately low urinary calcium excretion and a normal or mildly elevated circulating parathyroid hormone level. Hypermagnesemia is typically present. Affected individuals are usually asymptomatic and the disorder is considered benign. However, chondrocalcinosis and pancreatitis occur in some adults.
See also OMIM:145980| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_058046 | 11 | L → S in HHC1; demonstrates reduced intracellular and plasma membrane expression and signaling to the MAPK pathway in response to extracellular calcium relative to wild-type; fails to be inserted in the microsomes and does not undergo proper glycosylation. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_058047 | 13 | L → P in HHC1; has a dose-response curve shifted to the right relative to that of wild-type; demonstrates reduced intracellular and plasma membrane expression and signaling to the MAPK pathway in response to extracellular calcium relative to wild-type; fails to be inserted in the microsomes and does not undergo proper glycosylation. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_058049 | 21 | G → R in HHC1. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_003585 | 39 | P → A in HHC1. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_078139 | 42 | F → S in HHC1. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_078140 | 53 | S → P in HHC1; decreased G-protein coupled receptor signaling pathway. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_078141 | 55 | P → L in HHC1; decreased G-protein coupled receptor signaling pathway. 3 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_003586 | 62 | R → M in HHC1; mild; decreased G-protein coupled receptor signaling pathway. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_003587 | 66 | R → C in HHC1; does not affect homodimerization; impaired N-glycosylation; impaired cell membrane localization; decreased G-protein coupled receptor signaling pathway. 3 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_078142 | 66 | R → H in HHC1; does not affect homodimerization; impaired N-glycosylation; impaired cell membrane localization; decreased G-protein coupled receptor signaling pathway. 3 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_078143 | 81 | I → M in HHC1; decreased G-protein coupled receptor signaling pathway. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_078144 | 110 | A → T in HHC1; decreased G-protein coupled receptor signaling pathway. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_003590 | 138 | T → M in HHC1; decreased G-protein coupled receptor signaling pathway. 3 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_003591 | 143 | G → E in HHC1; decreased G-protein coupled receptor signaling pathway. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_078149 | 143 | G → R in HHC1. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_078150 | 158 | G → R in HHC1. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_078151 | 159 | L → P in HHC1; decreased G-protein coupled receptor signaling pathway. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_078152 | 166 | S → G in HHC1. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_058056 | 171 | S → N in HHC1. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_078153 | 172 | R → G in HHC1; decreased G-protein coupled receptor signaling pathway. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_003592 | 174 | L → R in HHC1. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_078154 | 178 | N → D in HHC1; decreased G-protein coupled receptor signaling pathway. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_058057 | 180 | F → C in HHC1; although the mutant receptor is expressed normally at the cell surface it is unresponsive with respect to intracellular signaling (MAPK activation) to increases in extracellular calcium concentrations. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_003593 | 185 | R → Q in HHC1; decreased G-protein coupled receptor signaling pathway. 3 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_078155 | 215 | D → G in HHC1; decreased G-protein coupled receptor signaling pathway. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_078156 | 220 | R → W in HHC1. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_058059 | 221 | P → Q in HHC1. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_078158 | 221 | P → S in HHC1; decreased G-protein coupled receptor signaling pathway. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_058060 | 225 | K → T in HHC1. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_003595 | 227 | R → Q in HHC1; G-protein coupled receptor signaling pathway; less markedly impaired relative to wild-type than L-227; does not affect cell membrane localization. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_058062 | 271 | S → F in HHC1. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_003596 | 297 | E → K in HHC1; decreased G-protein coupled receptor signaling pathway. 3 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_058063 | 397 | G → R in HHC1. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_078160 | 459 | Q → R in HHC1; decreased G-protein coupled receptor signaling pathway; does not affect cell membrane localization. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_058064 | 465 | R → Q in HHC1; loss-of-function mutation; the quantity of the mutant receptor is higher than that of the wild-type receptor; dose-response curves show that the mutation significantly reduces the sensitivity of the receptor to extracellular calcium concentrations. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_058065 | 509 | G → R in HHC1. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_078161 | 549 | G → R in HHC1. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_078162 | 550 | T → I in HHC1; decreased G-protein coupled receptor signaling pathway. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_058066 | 553 | G → R in HHC1. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_058067 | 555 | I → V in HHC1. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_012649 | 557 | G → E in HHC1; Abolished G-protein coupled receptor activity. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_058068 | 562 | C → Y in HHC1. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_078164 | 565 | C → G in HHC1. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_078166 | 571 | G → W in HHC1; decreased G-protein coupled receptor signaling pathway; does not affect cell membrane localization. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_058069 | 582 | C → F in HHC1. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_003597 | 582 | C → Y in NSHPT and HHC1. 3 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_078167 | 583 – 1078 | Missing in HHC1; impaired homodimerization; impaired cell membrane localization. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 496 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_058072 | 623 | G → D in HHC1. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_078168 | 657 | S → Y in HHC1. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_078169 | 661 | C → Y in HHC1. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_058074 | 670 | G → R in HHC1. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_078170 | 680 | R → H in HHC1. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_065494 | 697 | V → M in HHC1. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_078172 | 707 | E → V in HHC1; decreased protein level. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_058076 | 728 | V → F in HHC1. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_058077 | 742 | W → R in HHC1. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_078173 | 748 | P → R in HHC1. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_078174 | 761 | Missing in HHC1. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_078175 | 774 | G → S in HHC1; decreased G-protein coupled receptor signaling pathway; does not affect cell membrane localization. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_003599 | 795 | R → W in HHC1; decreased G-protein coupled receptor signaling pathway. 4 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_078177 | 802 | N → S in HHC1; decreased G-protein coupled receptor signaling pathway. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_078178 | 817 | V → I in HHC1; decreased G-protein coupled receptor signaling pathway. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_058084 | 886 | R → W in HHC1. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_078183 | 972 | T → M in HHC1; decreased G-protein coupled receptor signaling pathway. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 |
Hyperparathyroidism, neonatal severe (NSHPT)7 Publications
<p>Manually curated information for which there is published experimental evidence.</p>
<p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
- Ref.13"Structural mechanism of ligand activation in human calcium-sensing receptor."
Geng Y., Mosyak L., Kurinov I., Zuo H., Sturchler E., Cheng T.C., Subramanyam P., Brown A.P., Brennan S.C., Mun H.C., Bush M., Chen Y., Nguyen T.X., Cao B., Chang D.D., Quick M., Conigrave A.D., Colecraft H.M., McDonald P., Fan Q.R.
Elife 5:0-0(2016) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 20-607 IN COMPLEX WITH CALCIUM; ANION AND TRYPTOPHAN, FUNCTION, ENZYME REGULATION, DOMAIN, DISULFIDE BONDS, GLYCOSYLATION AT ASN-261; ASN-287; ASN-446; ASN-468; ASN-488; ASN-541 AND ASN-594, MUTAGENESIS OF ARG-69; ASN-102; THR-145; SER-147; SER-170; TYR-218; SER-417 AND TRP-458, CHARACTERIZATION OF VARIANTS NSHPT ILE-100; LEU-227 AND LYS-551, CHARACTERIZATION OF VARIANTS HHC1 HIS-66; MET-81; PRO-159; GLY-172; GLY-215; LYS-297 AND GLU-557. - Ref.18"Calcium-sensing receptor mutations in familial benign hypercalcemia and neonatal hyperparathyroidism."
Pearce S.H.S., Trump D., Wooding C., Besser G.M., Chew S.L., Grant D.B., Heath D.A., Hughes I.A., Paterson C.R., Whyte M.P., Thakker R.V.
J. Clin. Invest. 96:2683-2692(1995) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS NSHPT LEU-227 AND TYR-582. - Ref.23"Functional characterization of calcium-sensing receptor mutations expressed in human embryonic kidney cells."
Pearce S.H.S., Bai M., Quinn S.J., Kifor O., Brown E.M., Thakker R.V.
J. Clin. Invest. 98:1860-1866(1996) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS HHC1 LEU-55; ASP-178; SER-221 AND ILE-817, VARIANTS HYPOC1 LEU-128; MET-151 AND LYS-191, VARIANT NSHPT LEU-227, CHARACTERIZATION OF VARIANTS HHC1 LEU-55; ASP-178; SER-221 AND ILE-817, FUNCTION, CHARACTERIZATION OF VARIANTS HYPOC1 LEU-128; MET-151 AND LYS-191, CHARACTERIZATION OF VARIANT NSHPT LEU-227. - Ref.26"Two novel missense mutations in calcium-sensing receptor gene associated with neonatal severe hyperparathyroidism."
Kobayashi M., Tanaka H., Tsuzuki K., Tsuyuki M., Igaki H., Ichinose Y., Aya K., Nishioka N., Seino Y.
J. Clin. Endocrinol. Metab. 82:2716-2719(1997) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT NSHPT GLU-670. - Ref.42"Genetic testing in familial isolated hyperparathyroidism: unexpected results and their implications."
Warner J., Epstein M., Sweet A., Singh D., Burgess J., Stranks S., Hill P., Perry-Keene D., Learoyd D., Robinson B., Birdsey P., Mackenzie E., Teh B.T., Prins J.B., Cardinal J.
J. Med. Genet. 41:155-160(2004) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS NSHPT ILE-100; LYS-336 DEL; PRO-650 AND MET-689, VARIANTS SER-986; GLY-990 AND GLN-1011. - Ref.45"Functional characterization of calcium-sensing receptor codon 227 mutations presenting as either familial (benign) hypocalciuric hypercalcemia or neonatal hyperparathyroidism."
Wystrychowski A., Pidasheva S., Canaff L., Chudek J., Kokot F., Wiecek A., Hendy G.N.
J. Clin. Endocrinol. Metab. 90:864-870(2005) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT HHC1 GLN-227, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANT NSHPT LEU-227, CHARACTERIZATION OF VARIANT HHC1 GLN-227. - Ref.50"Neonatal severe hyperparathyroidism associated with a novel de novo heterozygous R551K inactivating mutation and a heterozygous A986S polymorphism of the calcium-sensing receptor gene."
Toke J., Czirjak G., Patocs A., Enyedi B., Gergics P., Csakvary V., Enyedi P., Toth M.
Clin. Endocrinol. (Oxf.) 67:385-392(2007) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT NSHPT LYS-551, VARIANT SER-986, FUNCTION, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANT NSHPT LYS-551.
Ref.13
"Structural mechanism of ligand activation in human calcium-sensing receptor."
Geng Y., Mosyak L., Kurinov I., Zuo H., Sturchler E., Cheng T.C., Subramanyam P., Brown A.P., Brennan S.C., Mun H.C., Bush M., Chen Y., Nguyen T.X., Cao B., Chang D.D., Quick M., Conigrave A.D., Colecraft H.M., McDonald P., Fan Q.R.
Elife 5:0-0(2016) [PubMed] [Europe PMC] [Abstract]
Geng Y., Mosyak L., Kurinov I., Zuo H., Sturchler E., Cheng T.C., Subramanyam P., Brown A.P., Brennan S.C., Mun H.C., Bush M., Chen Y., Nguyen T.X., Cao B., Chang D.D., Quick M., Conigrave A.D., Colecraft H.M., McDonald P., Fan Q.R.
Elife 5:0-0(2016) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 20-607 IN COMPLEX WITH CALCIUM; ANION AND TRYPTOPHAN, FUNCTION, ENZYME REGULATION, DOMAIN, DISULFIDE BONDS, GLYCOSYLATION AT ASN-261; ASN-287; ASN-446; ASN-468; ASN-488; ASN-541 AND ASN-594, MUTAGENESIS OF ARG-69; ASN-102; THR-145; SER-147; SER-170; TYR-218; SER-417 AND TRP-458, CHARACTERIZATION OF VARIANTS NSHPT ILE-100; LEU-227 AND LYS-551, CHARACTERIZATION OF VARIANTS HHC1 HIS-66; MET-81; PRO-159; GLY-172; GLY-215; LYS-297 AND GLU-557.
Ref.18
"Calcium-sensing receptor mutations in familial benign hypercalcemia and neonatal hyperparathyroidism."
Pearce S.H.S., Trump D., Wooding C., Besser G.M., Chew S.L., Grant D.B., Heath D.A., Hughes I.A., Paterson C.R., Whyte M.P., Thakker R.V.
J. Clin. Invest. 96:2683-2692(1995) [PubMed] [Europe PMC] [Abstract]
Pearce S.H.S., Trump D., Wooding C., Besser G.M., Chew S.L., Grant D.B., Heath D.A., Hughes I.A., Paterson C.R., Whyte M.P., Thakker R.V.
J. Clin. Invest. 96:2683-2692(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS NSHPT LEU-227 AND TYR-582.
Ref.23
"Functional characterization of calcium-sensing receptor mutations expressed in human embryonic kidney cells."
Pearce S.H.S., Bai M., Quinn S.J., Kifor O., Brown E.M., Thakker R.V.
J. Clin. Invest. 98:1860-1866(1996) [PubMed] [Europe PMC] [Abstract]
Pearce S.H.S., Bai M., Quinn S.J., Kifor O., Brown E.M., Thakker R.V.
J. Clin. Invest. 98:1860-1866(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HHC1 LEU-55; ASP-178; SER-221 AND ILE-817, VARIANTS HYPOC1 LEU-128; MET-151 AND LYS-191, VARIANT NSHPT LEU-227, CHARACTERIZATION OF VARIANTS HHC1 LEU-55; ASP-178; SER-221 AND ILE-817, FUNCTION, CHARACTERIZATION OF VARIANTS HYPOC1 LEU-128; MET-151 AND LYS-191, CHARACTERIZATION OF VARIANT NSHPT LEU-227.
Ref.26
"Two novel missense mutations in calcium-sensing receptor gene associated with neonatal severe hyperparathyroidism."
Kobayashi M., Tanaka H., Tsuzuki K., Tsuyuki M., Igaki H., Ichinose Y., Aya K., Nishioka N., Seino Y.
J. Clin. Endocrinol. Metab. 82:2716-2719(1997) [PubMed] [Europe PMC] [Abstract]
Kobayashi M., Tanaka H., Tsuzuki K., Tsuyuki M., Igaki H., Ichinose Y., Aya K., Nishioka N., Seino Y.
J. Clin. Endocrinol. Metab. 82:2716-2719(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT NSHPT GLU-670.
Ref.42
"Genetic testing in familial isolated hyperparathyroidism: unexpected results and their implications."
Warner J., Epstein M., Sweet A., Singh D., Burgess J., Stranks S., Hill P., Perry-Keene D., Learoyd D., Robinson B., Birdsey P., Mackenzie E., Teh B.T., Prins J.B., Cardinal J.
J. Med. Genet. 41:155-160(2004) [PubMed] [Europe PMC] [Abstract]
Warner J., Epstein M., Sweet A., Singh D., Burgess J., Stranks S., Hill P., Perry-Keene D., Learoyd D., Robinson B., Birdsey P., Mackenzie E., Teh B.T., Prins J.B., Cardinal J.
J. Med. Genet. 41:155-160(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS NSHPT ILE-100; LYS-336 DEL; PRO-650 AND MET-689, VARIANTS SER-986; GLY-990 AND GLN-1011.
Ref.45
"Functional characterization of calcium-sensing receptor codon 227 mutations presenting as either familial (benign) hypocalciuric hypercalcemia or neonatal hyperparathyroidism."
Wystrychowski A., Pidasheva S., Canaff L., Chudek J., Kokot F., Wiecek A., Hendy G.N.
J. Clin. Endocrinol. Metab. 90:864-870(2005) [PubMed] [Europe PMC] [Abstract]
Wystrychowski A., Pidasheva S., Canaff L., Chudek J., Kokot F., Wiecek A., Hendy G.N.
J. Clin. Endocrinol. Metab. 90:864-870(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HHC1 GLN-227, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANT NSHPT LEU-227, CHARACTERIZATION OF VARIANT HHC1 GLN-227.
Ref.50
"Neonatal severe hyperparathyroidism associated with a novel de novo heterozygous R551K inactivating mutation and a heterozygous A986S polymorphism of the calcium-sensing receptor gene."
Toke J., Czirjak G., Patocs A., Enyedi B., Gergics P., Csakvary V., Enyedi P., Toth M.
Clin. Endocrinol. (Oxf.) 67:385-392(2007) [PubMed] [Europe PMC] [Abstract]
Toke J., Czirjak G., Patocs A., Enyedi B., Gergics P., Csakvary V., Enyedi P., Toth M.
Clin. Endocrinol. (Oxf.) 67:385-392(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT NSHPT LYS-551, VARIANT SER-986, FUNCTION, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANT NSHPT LYS-551.
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disorder characterized by severe hypercalcemia, bone demineralization, and failure to thrive usually manifesting in the first 6 months of life. If untreated, NSHPT can be a devastating neurodevelopmental disorder, which in some cases is lethal without parathyroidectomy.
See also OMIM:239200| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_065199 | 100 | T → I in NSHPT; Abolished G-protein coupled receptor activity. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_003594 | 227 | R → L in NSHPT; decreased G-protein coupled receptor signaling pathway; does not affect cell membrane localization. 4 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_065200 | 336 | Missing in NSHPT. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_078163 | 551 | R → K in NSHPT; decreased G-protein coupled receptor signaling pathway; does not affect cell membrane localization. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_003597 | 582 | C → Y in NSHPT and HHC1. 3 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_065202 | 650 | L → P in NSHPT. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_058073 | 670 | G → E in NSHPT. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_065203 | 689 | V → M in NSHPT. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 |
Hypocalcemia, autosomal dominant 1 (HYPOC1)21 Publications
<p>Manually curated information for which there is published experimental evidence.</p>
<p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
- Ref.1"A familial syndrome of hypocalcemia with hypercalciuria due to mutations in the calcium-sensing receptor."
Pearce S.H.S., Williamson C., Kifor O., Bai M., Coulthard M.G., Davies M., Lewis-Barned N., McCredie D., Powell H., Kendall-Taylor P., Brown E.M., Thakker R.V.
N. Engl. J. Med. 335:1115-1122(1996) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS HYPOC1 LYS-118; LEU-128; MET-151; LYS-191 AND SER-612, CHARACTERIZATION OF VARIANTS HYPOC1 LEU-128; MET-151 AND LYS-191. - Ref.16"Autosomal dominant hypocalcaemia caused by a Ca(2+)-sensing receptor gene mutation."
Pollak M.R., Brown E.M., Estep H.L., McLaine P.N., Kifor O., Park J., Hebert S.C., Seidman C.E., Seidman J.G.
Nat. Genet. 8:303-307(1994) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT HYPOC1 ALA-127. - Ref.20"Mutations in the Ca(2+)-sensing receptor gene cause autosomal dominant and sporadic hypoparathyroidism."
Baron J., Winer K.K., Yanovski J.A., Cunningham A.W., Laue L., Zimmerman D., Cutler G.B. Jr.
Hum. Mol. Genet. 5:601-606(1996) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS HYPOC1 THR-116; HIS-681 AND SER-806, VARIANT SER-851. - Ref.21"Expression and characterization of inactivating and activating mutations in the human Ca2+o-sensing receptor."
Bai M., Quinn S., Trivedi S., Kifor O., Pearce S.H.S., Pollak M.R., Krapcho K., Hebert S.C., Brown E.M.
J. Biol. Chem. 271:19537-19545(1996) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS HHC1 MET-62; CYS-66; MET-138; GLU-143; GLN-185; LYS-297 AND TRP-795, VARIANT HYPOC1 ALA-127, FUNCTION, SUBCELLULAR LOCATION, GLYCOSYLATION, CHARACTERIZATION OF VARIANTS HHC1 MET-62; CYS-66; MET-138; GLU-143; GLN-185; LYS-297 AND TRP-795, CHARACTERIZATION OF VARIANT HYPOC1 ALA-127. - Ref.23"Functional characterization of calcium-sensing receptor mutations expressed in human embryonic kidney cells."
Pearce S.H.S., Bai M., Quinn S.J., Kifor O., Brown E.M., Thakker R.V.
J. Clin. Invest. 98:1860-1866(1996) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS HHC1 LEU-55; ASP-178; SER-221 AND ILE-817, VARIANTS HYPOC1 LEU-128; MET-151 AND LYS-191, VARIANT NSHPT LEU-227, CHARACTERIZATION OF VARIANTS HHC1 LEU-55; ASP-178; SER-221 AND ILE-817, FUNCTION, CHARACTERIZATION OF VARIANTS HYPOC1 LEU-128; MET-151 AND LYS-191, CHARACTERIZATION OF VARIANT NSHPT LEU-227. - Ref.25"Sporadic hypoparathyroidism caused by de Novo gain-of-function mutations of the Ca(2+)-sensing receptor."
De Luca F., Ray K., Mancilla E.E., Fan G.-F., Winer K.K., Gore P., Spiegel A.M., Baron J.
J. Clin. Endocrinol. Metab. 82:2710-2715(1997) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS HYPOC1 LYS-118; ARG-773 AND SER-806, CHARACTERIZATION OF VARIANTS HYPOC1 LYS-118; ARG-773 AND SER-806. - Ref.27"Familial hypoparathyroidism: identification of a novel gain of function mutation in transmembrane domain 5 of the calcium-sensing receptor."
Watanabe T., Bai M., Lane C.R., Matsumoto S., Minamitani K., Minagawa M., Niimi H., Brown E.M., Yasuda T.
J. Clin. Endocrinol. Metab. 83:2497-2502(1998) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT HYPOC1 CYS-788, CHARACTERIZATION OF VARIANT HYPOC1 CYS-788. - Ref.29"A novel activating mutation in calcium-sensing receptor gene associated with a family of autosomal dominant hypocalcemia."
Okazaki R., Chikatsu N., Nakatsu M., Takeuchi Y., Ajima M., Miki J., Fujita T., Arai M., Totsuka Y., Tanaka K., Fukumoto S.
J. Clin. Endocrinol. Metab. 84:363-366(1999) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT HYPOC1 ASN-47, CHARACTERIZATION OF VARIANT HYPOC1 ASN-47. - Ref.30"Autosomal dominant hypoparathyroidism associated with short stature and premature osteoarthritis."
Stock J.L., Brown R.S., Baron J., Coderre J.A., Mancilla E., De Luca F., Ray K., Mericq M.V.
J. Clin. Endocrinol. Metab. 84:3036-3040(1999) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT HYPOC1 VAL-616, CHARACTERIZATION OF VARIANT HYPOC1 VAL-616. - Ref.35"A family of autosomal dominant hypocalcemia with a positive correlation between serum calcium and magnesium: identification of a novel gain of function mutation (Ser(820)Phe) in the calcium-sensing receptor."
Nagase T., Murakami T., Tsukada T., Kitamura R., Chikatsu N., Takeo H., Takata N., Yasuda H., Fukumoto S., Tanaka Y., Nagata N., Yamaguchi K., Akatsu T., Yamamoto M.
J. Clin. Endocrinol. Metab. 87:2681-2687(2002) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT HYPOC1 PHE-820, CHARACTERIZATION OF VARIANT HYPOC1 PHE-820, VARIANT GLY-990. - Ref.36"Hydrochlorothiazide effectively reduces urinary calcium excretion in two Japanese patients with gain-of-function mutations of the calcium-sensing receptor gene."
Sato K., Hasegawa Y., Nakae J., Nanao K., Takahashi I., Tajima T., Shinohara N., Fujieda K.
J. Clin. Endocrinol. Metab. 87:3068-3073(2002) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS HYPOC1 PRO-125 AND GLU-843, CHARACTERIZATION OF VARIANTS HYPOC1 PRO-125 AND GLU-843. - Ref.37"Association between activating mutations of calcium-sensing receptor and Bartter's syndrome."
Watanabe S., Fukumoto S., Chang H., Takeuchi Y., Hasegawa Y., Okazaki R., Chikatsu N., Fujita T.
Lancet 360:692-694(2002) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS HYPOC1 TRP-131 AND GLU-843. - Ref.38"Autosomal dominant hypocalcemia: a novel activating mutation (E604K) in the cysteine-rich domain of the calcium-sensing receptor."
Tan Y.M., Cardinal J., Franks A.H., Mun H.-C., Lewis N., Harris L.B., Prins J.B., Conigrave A.D.
J. Clin. Endocrinol. Metab. 88:605-610(2003) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT HYPOC1 LYS-604, CHARACTERIZATION OF VARIANT HYPOC1 LYS-604. - Ref.39"Recurrent familial hypocalcemia due to germline mosaicism for an activating mutation of the calcium-sensing receptor gene."
Hendy G.N., Minutti C., Canaff L., Pidasheva S., Yang B., Nouhi Z., Zimmerman D., Wei C., Cole D.E.C.
J. Clin. Endocrinol. Metab. 88:3674-3681(2003) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT HYPOC1 LEU-788, CHARACTERIZATION OF VARIANT HYPOC1 LEU-788. - Ref.43"A novel mutation (E767K) in the second extracellular loop of the calcium sensing receptor in a family with autosomal dominant hypocalcemia."
Uckun-Kitapci A., Underwood L.E., Zhang J., Moats-Staats B.
Am. J. Med. Genet. A 132:125-129(2005) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT HYPOC1 LYS-767, VARIANT GLY-990. - Ref.48"A hypocalcemic child with a novel activating mutation of the calcium-sensing receptor gene: successful treatment with recombinant human parathyroid hormone."
Mittelman S.D., Hendy G.N., Fefferman R.A., Canaff L., Mosesova I., Cole D.E., Burkett L., Geffner M.E.
J. Clin. Endocrinol. Metab. 91:2474-2479(2006) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT HYPOC1 GLN-727, CHARACTERIZATION OF VARIANT HYPOC1 GLN-727. - Ref.54"Calcium-sensing receptor mutations and denaturing high performance liquid chromatography."
Cole D.E., Yun F.H., Wong B.Y., Shuen A.Y., Booth R.A., Scillitani A., Pidasheva S., Zhou X., Canaff L., Hendy G.N.
J. Mol. Endocrinol. 42:331-339(2009) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS HHC1 SER-42; LEU-55; HIS-66; MET-81; MET-138; ARG-143; ARG-158; GLY-166; TRP-220; ARG-549; TYR-562; GLY-565; TYR-582; 583-ASN--SER-1078 DEL; TYR-661; HIS-680; ILE-761 DEL AND TRP-795, VARIANTS HYPOC1 LYS-118; PHE-125; ARG-129; LYS-228; LYS-604; ILE-802; SER-830; LEU-832 AND SER-832. - Ref.59"Loss-of-function and gain-of-function mutations of calcium-sensing receptor: functional analysis and the effect of allosteric modulators NPS R-568 and NPS 2143."
Nakamura A., Hotsubo T., Kobayashi K., Mochizuki H., Ishizu K., Tajima T.
J. Clin. Endocrinol. Metab. 98:E1692-E1701(2013) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS HHC1 THR-110 AND GLY-172, VARIANTS HYPOC1 CYS-122; HIS-569 AND THR-839, FUNCTION, CHARACTERIZATION OF VARIANTS HHC1 THR-110 AND GLY-172, CHARACTERIZATION OF VARIANTS HYPOC1 CYS-122; HIS-569 AND THR-839. - Ref.60"Two novel mutations of the calcium-sensing receptor gene affecting the same amino acid position lead to opposite phenotypes and reveal the importance of p.N802 on receptor activity."
Lia-Baldini A.S., Magdelaine C., Nizou A., Airault C., Salles J.P., Moulin P., Delemer B., Aitouares M., Funalot B., Sturtz F., Lienhardt-Roussie A.
Eur. J. Endocrinol. 168:K27-K34(2013) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT HHC1 SER-802, VARIANT HYPOC1 ILE-802. - Ref.64"Novel activating mutation of human calcium-sensing receptor in a family with autosomal dominant hypocalcaemia."
Baran N., ter Braak M., Saffrich R., Woelfle J., Schmitz U.
Mol. Cell. Endocrinol. 407:18-25(2015) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT HYPOC1 LEU-136, FUNCTION, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANT HYPOC1 LEU-136. - Ref.65"CASR gene activating mutations in two families with autosomal dominant hypocalcemia."
Guarnieri V., Valentina D'Elia A., Baorda F., Pazienza V., Benegiamo G., Stanziale P., Copetti M., Battista C., Grimaldi F., Damante G., Pellegrini F., D'Agruma L., Zelante L., Carella M., Scillitani A.
Mol. Genet. Metab. 107:548-552(2012) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS HYPOC1 LEU-221; ARG-681 AND GLN-727, FUNCTION, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANTS HYPOC1 ARG-681 AND GLN-727.
Ref.1
"A familial syndrome of hypocalcemia with hypercalciuria due to mutations in the calcium-sensing receptor."
Pearce S.H.S., Williamson C., Kifor O., Bai M., Coulthard M.G., Davies M., Lewis-Barned N., McCredie D., Powell H., Kendall-Taylor P., Brown E.M., Thakker R.V.
N. Engl. J. Med. 335:1115-1122(1996) [PubMed] [Europe PMC] [Abstract]
Pearce S.H.S., Williamson C., Kifor O., Bai M., Coulthard M.G., Davies M., Lewis-Barned N., McCredie D., Powell H., Kendall-Taylor P., Brown E.M., Thakker R.V.
N. Engl. J. Med. 335:1115-1122(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS HYPOC1 LYS-118; LEU-128; MET-151; LYS-191 AND SER-612, CHARACTERIZATION OF VARIANTS HYPOC1 LEU-128; MET-151 AND LYS-191.
Ref.16
"Autosomal dominant hypocalcaemia caused by a Ca(2+)-sensing receptor gene mutation."
Pollak M.R., Brown E.M., Estep H.L., McLaine P.N., Kifor O., Park J., Hebert S.C., Seidman C.E., Seidman J.G.
Nat. Genet. 8:303-307(1994) [PubMed] [Europe PMC] [Abstract]
Pollak M.R., Brown E.M., Estep H.L., McLaine P.N., Kifor O., Park J., Hebert S.C., Seidman C.E., Seidman J.G.
Nat. Genet. 8:303-307(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HYPOC1 ALA-127.
Ref.20
"Mutations in the Ca(2+)-sensing receptor gene cause autosomal dominant and sporadic hypoparathyroidism."
Baron J., Winer K.K., Yanovski J.A., Cunningham A.W., Laue L., Zimmerman D., Cutler G.B. Jr.
Hum. Mol. Genet. 5:601-606(1996) [PubMed] [Europe PMC] [Abstract]
Baron J., Winer K.K., Yanovski J.A., Cunningham A.W., Laue L., Zimmerman D., Cutler G.B. Jr.
Hum. Mol. Genet. 5:601-606(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HYPOC1 THR-116; HIS-681 AND SER-806, VARIANT SER-851.
Ref.21
"Expression and characterization of inactivating and activating mutations in the human Ca2+o-sensing receptor."
Bai M., Quinn S., Trivedi S., Kifor O., Pearce S.H.S., Pollak M.R., Krapcho K., Hebert S.C., Brown E.M.
J. Biol. Chem. 271:19537-19545(1996) [PubMed] [Europe PMC] [Abstract]
Bai M., Quinn S., Trivedi S., Kifor O., Pearce S.H.S., Pollak M.R., Krapcho K., Hebert S.C., Brown E.M.
J. Biol. Chem. 271:19537-19545(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HHC1 MET-62; CYS-66; MET-138; GLU-143; GLN-185; LYS-297 AND TRP-795, VARIANT HYPOC1 ALA-127, FUNCTION, SUBCELLULAR LOCATION, GLYCOSYLATION, CHARACTERIZATION OF VARIANTS HHC1 MET-62; CYS-66; MET-138; GLU-143; GLN-185; LYS-297 AND TRP-795, CHARACTERIZATION OF VARIANT HYPOC1 ALA-127.
Ref.23
"Functional characterization of calcium-sensing receptor mutations expressed in human embryonic kidney cells."
Pearce S.H.S., Bai M., Quinn S.J., Kifor O., Brown E.M., Thakker R.V.
J. Clin. Invest. 98:1860-1866(1996) [PubMed] [Europe PMC] [Abstract]
Pearce S.H.S., Bai M., Quinn S.J., Kifor O., Brown E.M., Thakker R.V.
J. Clin. Invest. 98:1860-1866(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HHC1 LEU-55; ASP-178; SER-221 AND ILE-817, VARIANTS HYPOC1 LEU-128; MET-151 AND LYS-191, VARIANT NSHPT LEU-227, CHARACTERIZATION OF VARIANTS HHC1 LEU-55; ASP-178; SER-221 AND ILE-817, FUNCTION, CHARACTERIZATION OF VARIANTS HYPOC1 LEU-128; MET-151 AND LYS-191, CHARACTERIZATION OF VARIANT NSHPT LEU-227.
Ref.25
"Sporadic hypoparathyroidism caused by de Novo gain-of-function mutations of the Ca(2+)-sensing receptor."
De Luca F., Ray K., Mancilla E.E., Fan G.-F., Winer K.K., Gore P., Spiegel A.M., Baron J.
J. Clin. Endocrinol. Metab. 82:2710-2715(1997) [PubMed] [Europe PMC] [Abstract]
De Luca F., Ray K., Mancilla E.E., Fan G.-F., Winer K.K., Gore P., Spiegel A.M., Baron J.
J. Clin. Endocrinol. Metab. 82:2710-2715(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HYPOC1 LYS-118; ARG-773 AND SER-806, CHARACTERIZATION OF VARIANTS HYPOC1 LYS-118; ARG-773 AND SER-806.
Ref.27
"Familial hypoparathyroidism: identification of a novel gain of function mutation in transmembrane domain 5 of the calcium-sensing receptor."
Watanabe T., Bai M., Lane C.R., Matsumoto S., Minamitani K., Minagawa M., Niimi H., Brown E.M., Yasuda T.
J. Clin. Endocrinol. Metab. 83:2497-2502(1998) [PubMed] [Europe PMC] [Abstract]
Watanabe T., Bai M., Lane C.R., Matsumoto S., Minamitani K., Minagawa M., Niimi H., Brown E.M., Yasuda T.
J. Clin. Endocrinol. Metab. 83:2497-2502(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HYPOC1 CYS-788, CHARACTERIZATION OF VARIANT HYPOC1 CYS-788.
Ref.29
"A novel activating mutation in calcium-sensing receptor gene associated with a family of autosomal dominant hypocalcemia."
Okazaki R., Chikatsu N., Nakatsu M., Takeuchi Y., Ajima M., Miki J., Fujita T., Arai M., Totsuka Y., Tanaka K., Fukumoto S.
J. Clin. Endocrinol. Metab. 84:363-366(1999) [PubMed] [Europe PMC] [Abstract]
Okazaki R., Chikatsu N., Nakatsu M., Takeuchi Y., Ajima M., Miki J., Fujita T., Arai M., Totsuka Y., Tanaka K., Fukumoto S.
J. Clin. Endocrinol. Metab. 84:363-366(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HYPOC1 ASN-47, CHARACTERIZATION OF VARIANT HYPOC1 ASN-47.
Ref.30
"Autosomal dominant hypoparathyroidism associated with short stature and premature osteoarthritis."
Stock J.L., Brown R.S., Baron J., Coderre J.A., Mancilla E., De Luca F., Ray K., Mericq M.V.
J. Clin. Endocrinol. Metab. 84:3036-3040(1999) [PubMed] [Europe PMC] [Abstract]
Stock J.L., Brown R.S., Baron J., Coderre J.A., Mancilla E., De Luca F., Ray K., Mericq M.V.
J. Clin. Endocrinol. Metab. 84:3036-3040(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HYPOC1 VAL-616, CHARACTERIZATION OF VARIANT HYPOC1 VAL-616.
Ref.35
"A family of autosomal dominant hypocalcemia with a positive correlation between serum calcium and magnesium: identification of a novel gain of function mutation (Ser(820)Phe) in the calcium-sensing receptor."
Nagase T., Murakami T., Tsukada T., Kitamura R., Chikatsu N., Takeo H., Takata N., Yasuda H., Fukumoto S., Tanaka Y., Nagata N., Yamaguchi K., Akatsu T., Yamamoto M.
J. Clin. Endocrinol. Metab. 87:2681-2687(2002) [PubMed] [Europe PMC] [Abstract]
Nagase T., Murakami T., Tsukada T., Kitamura R., Chikatsu N., Takeo H., Takata N., Yasuda H., Fukumoto S., Tanaka Y., Nagata N., Yamaguchi K., Akatsu T., Yamamoto M.
J. Clin. Endocrinol. Metab. 87:2681-2687(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HYPOC1 PHE-820, CHARACTERIZATION OF VARIANT HYPOC1 PHE-820, VARIANT GLY-990.
Ref.36
"Hydrochlorothiazide effectively reduces urinary calcium excretion in two Japanese patients with gain-of-function mutations of the calcium-sensing receptor gene."
Sato K., Hasegawa Y., Nakae J., Nanao K., Takahashi I., Tajima T., Shinohara N., Fujieda K.
J. Clin. Endocrinol. Metab. 87:3068-3073(2002) [PubMed] [Europe PMC] [Abstract]
Sato K., Hasegawa Y., Nakae J., Nanao K., Takahashi I., Tajima T., Shinohara N., Fujieda K.
J. Clin. Endocrinol. Metab. 87:3068-3073(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HYPOC1 PRO-125 AND GLU-843, CHARACTERIZATION OF VARIANTS HYPOC1 PRO-125 AND GLU-843.
Ref.37
"Association between activating mutations of calcium-sensing receptor and Bartter's syndrome."
Watanabe S., Fukumoto S., Chang H., Takeuchi Y., Hasegawa Y., Okazaki R., Chikatsu N., Fujita T.
Lancet 360:692-694(2002) [PubMed] [Europe PMC] [Abstract]
Watanabe S., Fukumoto S., Chang H., Takeuchi Y., Hasegawa Y., Okazaki R., Chikatsu N., Fujita T.
Lancet 360:692-694(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HYPOC1 TRP-131 AND GLU-843.
Ref.38
"Autosomal dominant hypocalcemia: a novel activating mutation (E604K) in the cysteine-rich domain of the calcium-sensing receptor."
Tan Y.M., Cardinal J., Franks A.H., Mun H.-C., Lewis N., Harris L.B., Prins J.B., Conigrave A.D.
J. Clin. Endocrinol. Metab. 88:605-610(2003) [PubMed] [Europe PMC] [Abstract]
Tan Y.M., Cardinal J., Franks A.H., Mun H.-C., Lewis N., Harris L.B., Prins J.B., Conigrave A.D.
J. Clin. Endocrinol. Metab. 88:605-610(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HYPOC1 LYS-604, CHARACTERIZATION OF VARIANT HYPOC1 LYS-604.
Ref.39
"Recurrent familial hypocalcemia due to germline mosaicism for an activating mutation of the calcium-sensing receptor gene."
Hendy G.N., Minutti C., Canaff L., Pidasheva S., Yang B., Nouhi Z., Zimmerman D., Wei C., Cole D.E.C.
J. Clin. Endocrinol. Metab. 88:3674-3681(2003) [PubMed] [Europe PMC] [Abstract]
Hendy G.N., Minutti C., Canaff L., Pidasheva S., Yang B., Nouhi Z., Zimmerman D., Wei C., Cole D.E.C.
J. Clin. Endocrinol. Metab. 88:3674-3681(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HYPOC1 LEU-788, CHARACTERIZATION OF VARIANT HYPOC1 LEU-788.
Ref.43
"A novel mutation (E767K) in the second extracellular loop of the calcium sensing receptor in a family with autosomal dominant hypocalcemia."
Uckun-Kitapci A., Underwood L.E., Zhang J., Moats-Staats B.
Am. J. Med. Genet. A 132:125-129(2005) [PubMed] [Europe PMC] [Abstract]
Uckun-Kitapci A., Underwood L.E., Zhang J., Moats-Staats B.
Am. J. Med. Genet. A 132:125-129(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HYPOC1 LYS-767, VARIANT GLY-990.
Ref.48
"A hypocalcemic child with a novel activating mutation of the calcium-sensing receptor gene: successful treatment with recombinant human parathyroid hormone."
Mittelman S.D., Hendy G.N., Fefferman R.A., Canaff L., Mosesova I., Cole D.E., Burkett L., Geffner M.E.
J. Clin. Endocrinol. Metab. 91:2474-2479(2006) [PubMed] [Europe PMC] [Abstract]
Mittelman S.D., Hendy G.N., Fefferman R.A., Canaff L., Mosesova I., Cole D.E., Burkett L., Geffner M.E.
J. Clin. Endocrinol. Metab. 91:2474-2479(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HYPOC1 GLN-727, CHARACTERIZATION OF VARIANT HYPOC1 GLN-727.
Ref.54
"Calcium-sensing receptor mutations and denaturing high performance liquid chromatography."
Cole D.E., Yun F.H., Wong B.Y., Shuen A.Y., Booth R.A., Scillitani A., Pidasheva S., Zhou X., Canaff L., Hendy G.N.
J. Mol. Endocrinol. 42:331-339(2009) [PubMed] [Europe PMC] [Abstract]
Cole D.E., Yun F.H., Wong B.Y., Shuen A.Y., Booth R.A., Scillitani A., Pidasheva S., Zhou X., Canaff L., Hendy G.N.
J. Mol. Endocrinol. 42:331-339(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HHC1 SER-42; LEU-55; HIS-66; MET-81; MET-138; ARG-143; ARG-158; GLY-166; TRP-220; ARG-549; TYR-562; GLY-565; TYR-582; 583-ASN--SER-1078 DEL; TYR-661; HIS-680; ILE-761 DEL AND TRP-795, VARIANTS HYPOC1 LYS-118; PHE-125; ARG-129; LYS-228; LYS-604; ILE-802; SER-830; LEU-832 AND SER-832.
Ref.59
"Loss-of-function and gain-of-function mutations of calcium-sensing receptor: functional analysis and the effect of allosteric modulators NPS R-568 and NPS 2143."
Nakamura A., Hotsubo T., Kobayashi K., Mochizuki H., Ishizu K., Tajima T.
J. Clin. Endocrinol. Metab. 98:E1692-E1701(2013) [PubMed] [Europe PMC] [Abstract]
Nakamura A., Hotsubo T., Kobayashi K., Mochizuki H., Ishizu K., Tajima T.
J. Clin. Endocrinol. Metab. 98:E1692-E1701(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HHC1 THR-110 AND GLY-172, VARIANTS HYPOC1 CYS-122; HIS-569 AND THR-839, FUNCTION, CHARACTERIZATION OF VARIANTS HHC1 THR-110 AND GLY-172, CHARACTERIZATION OF VARIANTS HYPOC1 CYS-122; HIS-569 AND THR-839.
Ref.60
"Two novel mutations of the calcium-sensing receptor gene affecting the same amino acid position lead to opposite phenotypes and reveal the importance of p.N802 on receptor activity."
Lia-Baldini A.S., Magdelaine C., Nizou A., Airault C., Salles J.P., Moulin P., Delemer B., Aitouares M., Funalot B., Sturtz F., Lienhardt-Roussie A.
Eur. J. Endocrinol. 168:K27-K34(2013) [PubMed] [Europe PMC] [Abstract]
Lia-Baldini A.S., Magdelaine C., Nizou A., Airault C., Salles J.P., Moulin P., Delemer B., Aitouares M., Funalot B., Sturtz F., Lienhardt-Roussie A.
Eur. J. Endocrinol. 168:K27-K34(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HHC1 SER-802, VARIANT HYPOC1 ILE-802.
Ref.64
"Novel activating mutation of human calcium-sensing receptor in a family with autosomal dominant hypocalcaemia."
Baran N., ter Braak M., Saffrich R., Woelfle J., Schmitz U.
Mol. Cell. Endocrinol. 407:18-25(2015) [PubMed] [Europe PMC] [Abstract]
Baran N., ter Braak M., Saffrich R., Woelfle J., Schmitz U.
Mol. Cell. Endocrinol. 407:18-25(2015) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HYPOC1 LEU-136, FUNCTION, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANT HYPOC1 LEU-136.
Ref.65
"CASR gene activating mutations in two families with autosomal dominant hypocalcemia."
Guarnieri V., Valentina D'Elia A., Baorda F., Pazienza V., Benegiamo G., Stanziale P., Copetti M., Battista C., Grimaldi F., Damante G., Pellegrini F., D'Agruma L., Zelante L., Carella M., Scillitani A.
Mol. Genet. Metab. 107:548-552(2012) [PubMed] [Europe PMC] [Abstract]
Guarnieri V., Valentina D'Elia A., Baorda F., Pazienza V., Benegiamo G., Stanziale P., Copetti M., Battista C., Grimaldi F., Damante G., Pellegrini F., D'Agruma L., Zelante L., Carella M., Scillitani A.
Mol. Genet. Metab. 107:548-552(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HYPOC1 LEU-221; ARG-681 AND GLN-727, FUNCTION, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANTS HYPOC1 ARG-681 AND GLN-727.
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disorder of mineral homeostasis characterized by blood calcium levels below normal, and low or normal serum parathyroid hormone concentrations. Disease manifestations include mild or asymptomatic hypocalcemia, paresthesias, carpopedal spasm, seizures, hypercalciuria with nephrocalcinosis or kidney stones, and ectopic and basal ganglia calcifications. Few patients manifest hypocalcemia and features of Bartter syndrome, including hypomagnesemia, hypokalemia, metabolic alkalosis, hyperreninemia, and hyperaldosteronemia.
See also OMIM:601198| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_058050 | 47 | K → N in HYPOC1; the EC(50) of the mutant is significantly lower than that of wild-type. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_003588 | 116 | A → T in HYPOC1. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_058051 | 118 | N → K in HYPOC1; the mutation shifts the concentration-response curve to the left and increases maximal activity. 3 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_078145 | 122 | S → C in HYPOC1; increased G-protein coupled receptor signaling pathway. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_078146 | 125 | L → F in HYPOC1. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_058052 | 125 | L → P in HYPOC1; shifts the concentration-response curve of calcium ions to the left. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_003589 | 127 | E → A in HYPOC1; increased G-protein coupled receptor signaling pathway. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_058053 | 128 | F → L in HYPOC1; increased G-protein coupled receptor signaling pathway. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_078147 | 129 | C → R in HYPOC1. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_058054 | 131 | C → W in HYPOC1; associated with clinical features of Bartter syndrome. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_078148 | 136 | P → L in HYPOC1; increased G-protein coupled receptor signaling pathway; does not affect cell membrane localization. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_058055 | 151 | T → M in HYPOC1; increased G-protein coupled receptor signaling pathway. 3 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_058058 | 191 | E → K in HYPOC1; increased G-protein coupled receptor signaling pathway. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_078157 | 221 | P → L in HYPOC1. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_078159 | 228 | E → K in HYPOC1. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_078165 | 569 | P → H in HYPOC1; increased G-protein coupled receptor signaling pathway. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_058070 | 604 | E → K in HYPOC1; there is a significant leftward shift in the concentration response curves for the effects of extracellular calcium on both intracellular calcium mobilization and MAPK activity. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_058071 | 612 | F → S in HYPOC1. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_015414 | 616 | L → V in HYPOC1; does not affect the total accumulation of inositol phosphates as a function of extracellular calcium concentrations in transfected cells. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_003598 | 681 | Q → H in HYPOC1. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_078171 | 681 | Q → R in HYPOC1; increased G-protein coupled receptor signaling pathway; does not affect cell membrane localization. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_058075 | 727 | L → Q in HYPOC1; increased G-protein coupled receptor signaling pathway; does not affect cell membrane localization. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_021019 | 767 | E → K in HYPOC1. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_058078 | 773 | L → R in HYPOC1; the mutation shifts the concentration-response curve to the left and increases maximal activity. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_058079 | 788 | F → C in HYPOC1; leftward shift in the concentration-response curve for the mutant receptor; cells cotransfected with both the wild-type and the mutant receptor show an EC(50) similar to the mutant; a gain-of-function mutation rendering the receptor more sensitive than normal to activation. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_058080 | 788 | F → L in HYPOC1; induces a significant shift to the left relative to the wild-type protein in the MAPK response to increasing extracellular calcium concentrations. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_078176 | 802 | N → I in HYPOC1; increased G-protein coupled receptor signaling pathway. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_003600 | 806 | F → S in HYPOC1; does not produce a significant activating effect; decreased cell surface receptor expression. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_058081 | 820 | S → F in HYPOC1; the concentration-response curve of the mutant receptor is left-shifted and its EC(50) is significantly lower than that of the wild-type. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_078179 | 830 | G → S in HYPOC1. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_078180 | 832 | F → L in HYPOC1. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_078181 | 832 | F → S in HYPOC1. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_078182 | 839 | I → T in HYPOC1; increased G-protein coupled receptor signaling pathway. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_058082 | 843 | A → E in HYPOC1; also in HYPOC1 associated with clinical features of Bartter syndrome; shifts the concentration-response curve of calcium ions to the left. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 |
Epilepsy, idiopathic generalized 8 (EIG8)1 Publication
<p>Manually curated information for which there is published experimental evidence.</p>
<p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
- Ref.52"An idiopathic epilepsy syndrome linked to 3q13.3-q21 and missense mutations in the extracellular calcium sensing receptor gene."
Kapoor A., Satishchandra P., Ratnapriya R., Reddy R., Kadandale J., Shankar S.K., Anand A.
Ann. Neurol. 64:158-167(2008) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS EIG8 ALA-354; VAL-686; GLN-898; VAL-988 AND GLY-988, VARIANTS SER-986 AND GLY-990, TISSUE SPECIFICITY.
Ref.52
"An idiopathic epilepsy syndrome linked to 3q13.3-q21 and missense mutations in the extracellular calcium sensing receptor gene."
Kapoor A., Satishchandra P., Ratnapriya R., Reddy R., Kadandale J., Shankar S.K., Anand A.
Ann. Neurol. 64:158-167(2008) [PubMed] [Europe PMC] [Abstract]
Kapoor A., Satishchandra P., Ratnapriya R., Reddy R., Kadandale J., Shankar S.K., Anand A.
Ann. Neurol. 64:158-167(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS EIG8 ALA-354; VAL-686; GLN-898; VAL-988 AND GLY-988, VARIANTS SER-986 AND GLY-990, TISSUE SPECIFICITY.
Disease susceptibility is associated with variations affecting the gene represented in this entry.
Disease descriptionA disorder characterized by recurring generalized seizures in the absence of detectable brain lesions and/or metabolic abnormalities. Seizure types are variable, but include myoclonic seizures, absence seizures, febrile seizures, complex partial seizures, and generalized tonic-clonic seizures.
See also OMIM:612899| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_060206 | 354 | E → A in EIG8; patients present juvenile myoclonus epilepsy. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_060207 | 686 | I → V in EIG8; patients present juvenile myoclonus epilepsy. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_060208 | 898 | R → Q in EIG8. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_060209 | 988 | A → G in EIG8; patients present juvenile myoclonus epilepsy. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_060210 | 988 | A → V in EIG8; patients present juvenile myoclonus epilepsy. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 |
Mutagenesis
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">‘Pathology and Biotech’</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 69 | R → E: Abolishes G-protein coupled receptor signaling pathway. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">‘Pathology and Biotech’</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 102 | N → I: Abolishes G-protein coupled receptor activity. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">‘Pathology and Biotech’</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 145 | T → A: Abolishes G-protein coupled receptor activity. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">‘Pathology and Biotech’</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 147 | S → A: Nearly abolished G-protein coupled receptor activity. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">‘Pathology and Biotech’</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 170 | S → A: Abolishes G-protein coupled receptor activity. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">‘Pathology and Biotech’</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 218 | Y → S: Abolishes G-protein coupled receptor activity. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">‘Pathology and Biotech’</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 297 | E → I: Abolishes ability to sense calcium or magnesium levels. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">‘Pathology and Biotech’</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 417 | S → L: Abolishes G-protein coupled receptor signaling pathway. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">‘Pathology and Biotech’</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 458 | W → A: Decreased G-protein coupled receptor signaling pathway. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">‘Pathology and Biotech’</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 482 | C → S or Y: Abolishes ability of agonist AMG 416 to activate G-protein-coupled receptor activity. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 |
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Diseasei
Disease mutation, EpilepsyOrganism-specific databases
DisGeNET More...DisGeNETi | 846. |
MalaCards human disease database More...MalaCardsi | CASR. |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 145980. phenotype. 239200. phenotype. 601198. phenotype. 601199. gene+phenotype. 612899. phenotype. |
Open Targets More...OpenTargetsi | ENSG00000036828. |
Orphanet; a database dedicated to information on rare diseases and orphan drugs More...Orphaneti | 428. Autosomal dominant hypocalcemia. 263417. Bartter syndrome with hypocalcemia. 93372. Familial hypocalciuric hypercalcemia type 1. 189466. Familial isolated hypoparathyroidism due to impaired PTH secretion. 417. Neonatal severe primary hyperparathyroidism. |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA26097. |
Chemistry databases
ChEMBL database of bioactive drug-like small molecules More...ChEMBLi | CHEMBL1878. |
Drug and drug target database More...DrugBanki | DB05255. 751689. DB01012. Cinacalcet. DB12865. Etelcalcetide. |
IUPHAR/BPS Guide to PHARMACOLOGY More...GuidetoPHARMACOLOGYi | 54. |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | CASR. |
Domain mapping of disease mutations (DMDM) More...DMDMi | 1168781. |
<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi
Molecule processing
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei | 1 – 19 | Sequence analysisAdd BLAST | 19 | |
| <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000012946 | 20 – 1078 | Extracellular calcium-sensing receptorAdd BLAST | 1059 |
Amino acid modifications
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <span class="caps">PTM</span> / Processing”:/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi | 60 ↔ 101 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei 2 Publications<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| ||
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section"><span class="caps">PTM</span> / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi | 90 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
| <p>This subsection of the <span class="caps">PTM</span> / Processing”:/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi | 129 | Interchain1 Publication <p>Manually curated information which has been inferred by a curator based on his/her scientific knowledge or on the scientific content of an article.</p> <p><a href="/manual/evidences#ECO:0000305">More…</a></p> Manual assertion inferred by curator fromi
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| ||
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section"><span class="caps">PTM</span> / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi | 130 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
| <p>This subsection of the <span class="caps">PTM</span> / Processing”:/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi | 131 | Interchain1 Publication <p>Manually curated information which has been inferred by a curator based on his/her scientific knowledge or on the scientific content of an article.</p> <p><a href="/manual/evidences#ECO:0000305">More…</a></p> Manual assertion inferred by curator fromi
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| ||
| <p>This subsection of the <span class="caps">PTM</span> / Processing”:/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi | 236 ↔ 561 | 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| ||
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section"><span class="caps">PTM</span> / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi | 261 | N-linked (GlcNAc...) asparagineSequence analysis1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section"><span class="caps">PTM</span> / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi | 287 | N-linked (GlcNAc...) asparagineSequence analysis1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <span class="caps">PTM</span> / Processing”:/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi | 358 ↔ 395 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei 2 Publications<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| ||
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section"><span class="caps">PTM</span> / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi | 386 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section"><span class="caps">PTM</span> / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi | 400 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
| <p>This subsection of the <span class="caps">PTM</span> / Processing”:/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi | 437 ↔ 449 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei 2 Publications<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| ||
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section"><span class="caps">PTM</span> / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi | 446 | N-linked (GlcNAc...) asparagineSequence analysis1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section"><span class="caps">PTM</span> / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi | 468 | N-linked (GlcNAc...) asparagineSequence analysis1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section"><span class="caps">PTM</span> / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi | 488 | N-linked (GlcNAc...) asparagineSequence analysis1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section"><span class="caps">PTM</span> / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi | 541 | N-linked (GlcNAc...) asparagineSequence analysis1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <span class="caps">PTM</span> / Processing”:/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi | 542 ↔ 562 | 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| ||
| <p>This subsection of the <span class="caps">PTM</span> / Processing”:/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi | 546 ↔ 565 | 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| ||
| <p>This subsection of the <span class="caps">PTM</span> / Processing”:/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi | 568 ↔ 582 | 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| ||
| <p>This subsection of the <span class="caps">PTM</span> / Processing”:/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi | 585 ↔ 598 | 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| ||
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section"><span class="caps">PTM</span> / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi | 594 | N-linked (GlcNAc...) asparagineSequence analysis1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 920 | PhosphoserineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More…</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 1061 | PhosphoserineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More…</a></p> Manual assertion inferred from sequence similarity toi | 1 |
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section"><span class="caps">PTM</span>/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi
N-glycosylated.5 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
- Ref.9"Calcium-sensing receptor ubiquitination and degradation mediated by the E3 ubiquitin ligase dorfin."
Huang Y., Niwa J., Sobue G., Breitwieser G.E.
J. Biol. Chem. 281:11610-11617(2006) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH VCP AND RNF19A, GLYCOSYLATION, UBIQUITINATION. - Ref.11"Rab1 small GTP-binding protein regulates cell surface trafficking of the human calcium-sensing receptor."
Zhuang X., Adipietro K.A., Datta S., Northup J.K., Ray K.
Endocrinology 151:5114-5123(2010) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, GLYCOSYLATION. - Ref.13"Structural mechanism of ligand activation in human calcium-sensing receptor."
Geng Y., Mosyak L., Kurinov I., Zuo H., Sturchler E., Cheng T.C., Subramanyam P., Brown A.P., Brennan S.C., Mun H.C., Bush M., Chen Y., Nguyen T.X., Cao B., Chang D.D., Quick M., Conigrave A.D., Colecraft H.M., McDonald P., Fan Q.R.
Elife 5:0-0(2016) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 20-607 IN COMPLEX WITH CALCIUM; ANION AND TRYPTOPHAN, FUNCTION, ENZYME REGULATION, DOMAIN, DISULFIDE BONDS, GLYCOSYLATION AT ASN-261; ASN-287; ASN-446; ASN-468; ASN-488; ASN-541 AND ASN-594, MUTAGENESIS OF ARG-69; ASN-102; THR-145; SER-147; SER-170; TYR-218; SER-417 AND TRP-458, CHARACTERIZATION OF VARIANTS NSHPT ILE-100; LEU-227 AND LYS-551, CHARACTERIZATION OF VARIANTS HHC1 HIS-66; MET-81; PRO-159; GLY-172; GLY-215; LYS-297 AND GLU-557. - Ref.21"Expression and characterization of inactivating and activating mutations in the human Ca2+o-sensing receptor."
Bai M., Quinn S., Trivedi S., Kifor O., Pearce S.H.S., Pollak M.R., Krapcho K., Hebert S.C., Brown E.M.
J. Biol. Chem. 271:19537-19545(1996) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS HHC1 MET-62; CYS-66; MET-138; GLU-143; GLN-185; LYS-297 AND TRP-795, VARIANT HYPOC1 ALA-127, FUNCTION, SUBCELLULAR LOCATION, GLYCOSYLATION, CHARACTERIZATION OF VARIANTS HHC1 MET-62; CYS-66; MET-138; GLU-143; GLN-185; LYS-297 AND TRP-795, CHARACTERIZATION OF VARIANT HYPOC1 ALA-127. - Ref.47"Calcium-sensing receptor dimerizes in the endoplasmic reticulum: biochemical and biophysical characterization of CASR mutants retained intracellularly."
Pidasheva S., Grant M., Canaff L., Ercan O., Kumar U., Hendy G.N.
Hum. Mol. Genet. 15:2200-2209(2006) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS HHC1 CYS-66; HIS-66 AND 583-ASN--SER-1078 DEL, SUBCELLULAR LOCATION, SUBUNIT, GLYCOSYLATION, CHARACTERIZATION OF VARIANTS CYS-66; HIS-66 AND 583-ASN--SER-1078 DEL.
Ubiquitinated by RNF19A; which induces proteasomal degradation.1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
- Ref.9"Calcium-sensing receptor ubiquitination and degradation mediated by the E3 ubiquitin ligase dorfin."
Huang Y., Niwa J., Sobue G., Breitwieser G.E.
J. Biol. Chem. 281:11610-11617(2006) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH VCP AND RNF19A, GLYCOSYLATION, UBIQUITINATION.
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - PTMi
Disulfide bond, Glycoprotein, Phosphoprotein, Ubl conjugationProteomic databases
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P41180. |
PeptideAtlas More...PeptideAtlasi | P41180. |
PRoteomics IDEntifications database More...PRIDEi | P41180. |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | P41180. |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | P41180. |
<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni
<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression"><span class="caps">P92958</span></a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression"><span class="caps">Q8TDN4</span></a>, <a href="http://www.uniprot.org/uniprot/O14734#expression"><span class="caps">O14734</span></a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi
Expressed in the temporal lobe, frontal lobe, parietal lobe, hippocampus, and cerebellum. Also found in kidney, lung, liver, heart, skeletal muscle, placenta.1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
- Ref.52"An idiopathic epilepsy syndrome linked to 3q13.3-q21 and missense mutations in the extracellular calcium sensing receptor gene."
Kapoor A., Satishchandra P., Ratnapriya R., Reddy R., Kadandale J., Shankar S.K., Anand A.
Ann. Neurol. 64:158-167(2008) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS EIG8 ALA-354; VAL-686; GLN-898; VAL-988 AND GLY-988, VARIANTS SER-986 AND GLY-990, TISSUE SPECIFICITY.
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000036828. |
CleanEx database of gene expression profiles More...CleanExi | HS_CASR. |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | P41180. baseline and differential. |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | P41180. HS. |
Organism-specific databases
Human Protein Atlas More...HPAi | HPA039686. HPA050335. |
<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni
<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">‘Interaction’</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">‘Function’</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei
Homodimer; disulfide-linked (PubMed:27434672, PubMed:27386547, PubMed:16740594). Interacts with VCP and RNF19A (PubMed:16513638). Interacts with ARRB1 (By similarity).By similarity
<p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More…</a></p> Manual assertion inferred from sequence similarity toi
4 Publications<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
- Ref.9"Calcium-sensing receptor ubiquitination and degradation mediated by the E3 ubiquitin ligase dorfin."
Huang Y., Niwa J., Sobue G., Breitwieser G.E.
J. Biol. Chem. 281:11610-11617(2006) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH VCP AND RNF19A, GLYCOSYLATION, UBIQUITINATION. - Ref.13"Structural mechanism of ligand activation in human calcium-sensing receptor."
Geng Y., Mosyak L., Kurinov I., Zuo H., Sturchler E., Cheng T.C., Subramanyam P., Brown A.P., Brennan S.C., Mun H.C., Bush M., Chen Y., Nguyen T.X., Cao B., Chang D.D., Quick M., Conigrave A.D., Colecraft H.M., McDonald P., Fan Q.R.
Elife 5:0-0(2016) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 20-607 IN COMPLEX WITH CALCIUM; ANION AND TRYPTOPHAN, FUNCTION, ENZYME REGULATION, DOMAIN, DISULFIDE BONDS, GLYCOSYLATION AT ASN-261; ASN-287; ASN-446; ASN-468; ASN-488; ASN-541 AND ASN-594, MUTAGENESIS OF ARG-69; ASN-102; THR-145; SER-147; SER-170; TYR-218; SER-417 AND TRP-458, CHARACTERIZATION OF VARIANTS NSHPT ILE-100; LEU-227 AND LYS-551, CHARACTERIZATION OF VARIANTS HHC1 HIS-66; MET-81; PRO-159; GLY-172; GLY-215; LYS-297 AND GLU-557. - Ref.14"Structural basis for regulation of human calcium-sensing receptor by magnesium ions and an unexpected tryptophan derivative co-agonist."
Zhang C., Zhang T., Zou J., Miller C.L., Gorkhali R., Yang J.Y., Schilmiller A., Wang S., Huang K., Brown E.M., Moremen K.W., Hu J., Yang J.J.
Sci. Adv. 2:E1600241-E1600241(2016) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 20-541 IN COMPLEX WITH MAGNESIUM AND TRYPTOPHAN, FUNCTION, ENZYME REGULATION, DOMAIN, DISULFIDE BONDS, MUTAGENESIS OF GLU-297. - Ref.47"Calcium-sensing receptor dimerizes in the endoplasmic reticulum: biochemical and biophysical characterization of CASR mutants retained intracellularly."
Pidasheva S., Grant M., Canaff L., Ercan O., Kumar U., Hendy G.N.
Hum. Mol. Genet. 15:2200-2209(2006) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS HHC1 CYS-66; HIS-66 AND 583-ASN--SER-1078 DEL, SUBCELLULAR LOCATION, SUBUNIT, GLYCOSYLATION, CHARACTERIZATION OF VARIANTS CYS-66; HIS-66 AND 583-ASN--SER-1078 DEL.
<p>This subsection of the ‘Interaction’ section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi
| With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| TMED2 | Q15363 | 3 | EBI-4400127,EBI-998485 |
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- protein homodimerization activity Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 107296. 9 interactors. |
Database of interacting proteins More...DIPi | DIP-5975N. |
The Eukaryotic Linear Motif resource for Functional Sites in Proteins More...ELMi | P41180. |
Protein interaction database and analysis system More...IntActi | P41180. 1 interactor. |
Molecular INTeraction database More...MINTi | MINT-201342. |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000420194. |
Chemistry databases
BindingDB database of measured binding affinities More...BindingDBi | P41180. |
<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more detailsHide details| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 26 – 28 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 31 – 38 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 40 – 44 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 60 – 63 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 65 – 82 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 18 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 85 – 90 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assert |