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Q03431

- PTH1R_HUMAN

UniProt

Q03431 - PTH1R_HUMAN

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Protein

Parathyroid hormone/parathyroid hormone-related peptide receptor

Gene

PTH1R

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

This is a receptor for parathyroid hormone and for parathyroid hormone-related peptide. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase and also a phosphatidylinositol-calcium second messenger system.2 Publications

GO - Molecular functioni

  1. parathyroid hormone receptor activity Source: UniProtKB
  2. peptide hormone binding Source: UniProtKB
  3. protein self-association Source: UniProtKB

GO - Biological processi

  1. adenylate cyclase-activating G-protein coupled receptor signaling pathway Source: BHF-UCL
  2. adenylate cyclase-modulating G-protein coupled receptor signaling pathway Source: UniProtKB
  3. aging Source: Ensembl
  4. bone mineralization Source: Ensembl
  5. bone resorption Source: Ensembl
  6. cell maturation Source: Ensembl
  7. chondrocyte differentiation Source: Ensembl
  8. G-protein coupled receptor signaling pathway Source: ProtInc
  9. G-protein coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger Source: ProtInc
  10. negative regulation of cell proliferation Source: Ensembl
  11. osteoblast development Source: Ensembl
  12. phospholipase C-activating G-protein coupled receptor signaling pathway Source: BHF-UCL
  13. positive regulation of cell proliferation Source: Ensembl
  14. positive regulation of cytosolic calcium ion concentration Source: Ensembl
  15. positive regulation of inositol phosphate biosynthetic process Source: BHF-UCL
  16. skeletal system development Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

G-protein coupled receptor, Receptor, Transducer

Enzyme and pathway databases

ReactomeiREACT_18372. Class B/2 (Secretin family receptors).
REACT_19327. G alpha (s) signalling events.
SignaLinkiQ03431.

Protein family/group databases

TCDBi9.A.14.4.11. the g-protein-coupled receptor (gpcr) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Parathyroid hormone/parathyroid hormone-related peptide receptor
Alternative name(s):
PTH/PTHrP type I receptor
Short name:
PTH/PTHr receptor
Parathyroid hormone 1 receptor
Short name:
PTH1 receptor
Gene namesi
Name:PTH1R
Synonyms:PTHR, PTHR1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:9608. PTH1R.

Subcellular locationi

Cell membrane 1 Publication; Multi-pass membrane protein 1 Publication

GO - Cellular componenti

  1. apical plasma membrane Source: BHF-UCL
  2. basolateral plasma membrane Source: BHF-UCL
  3. brush border membrane Source: Ensembl
  4. cytoplasm Source: ProtInc
  5. extracellular vesicular exosome Source: UniProt
  6. integral component of plasma membrane Source: UniProtKB
  7. nucleus Source: ProtInc
  8. plasma membrane Source: Reactome
  9. receptor complex Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Involvement in diseasei

Jansen metaphyseal chondrodysplasia (JMC) [MIM:156400]: Rare autosomal dominant disorder characterized by a short-limbed dwarfism associated with hypercalcemia and normal or low serum concentrations of the two parathyroid hormones.4 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti223 – 2231H → R in JMC; constitutively activated. 2 Publications
VAR_003582
Natural varianti410 – 4101T → P in JMC; constitutively activated. 1 Publication
VAR_003583
Natural varianti410 – 4101T → R in JMC; leads to agonist-independent cAMP formation which is less pronounced than that observed with the Pro-410 mutant. 1 Publication
VAR_038811
Natural varianti458 – 4581I → R in JMC. 1 Publication
VAR_016064
Chondrodysplasia Blomstrand type (BOCD) [MIM:215045]: Severe skeletal dysplasia.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti132 – 1321P → L in BOCD. 1 Publication
VAR_016062
Enchondromatosis multiple (ENCHOM) [MIM:166000]: A condition characterized by multiple formation of enchondromas, benign neoplasms derived from mesodermal cells that form cartilage. Enchondromas remain within the substance of a cartilage or bone. Clinical problems caused by enchondromas include skeletal deformity and the potential for malignant change to osteosarcoma.1 Publication
Note: The disease may be caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti150 – 1501R → C in ENCHOM; Ollier type; unknown pathological significance. 1 Publication
Corresponds to variant rs121434601 [ dbSNP | Ensembl ].
VAR_016063
Eiken skeletal dysplasia (EISD) [MIM:600002]: A rare skeletal dysplasia characterized by severely retarded ossification, principally of the epiphyses, pelvis, hands and feet, as well as by abnormal modeling of the bones in hands and feet, abnormal persistence of cartilage in the pelvis and mild growth retardation.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Primary failure of tooth eruption (PFE) [MIM:125350]: Rare condition that has high penetrance and variable expressivity and in which tooth retention occurs without evidence of any obvious mechanical interference. Instead, malfunction of the eruptive mechanism itself appears to cause nonankylosed permanent teeth to fail to erupt, although the eruption pathway has been cleared by bone resorption.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi135 – 1351I → K: Abolishes hormone binding and homodimerization. 1 Publication
Mutagenesisi137 – 1371D → A: Abolishes hormone binding. No effect on homodimerization. 1 Publication
Mutagenesisi474 – 4741W → A: Strongly reduced interaction with G protein subunits GNB1 and GNG2; when associated with A-477. 1 Publication
Mutagenesisi477 – 4771W → A: Strongly reduced interaction with G protein subunits GNB1 and GNG2; when associated with A-474. 1 Publication

Keywords - Diseasei

Disease mutation, Dwarfism

Organism-specific databases

MIMi125350. phenotype.
156400. phenotype.
166000. phenotype.
215045. phenotype.
600002. phenotype.
Orphaneti50945. Chondrodysplasia, Blomstrand type.
1077. Dental ankylosis.
79106. Eiken syndrome.
296. Enchondromatosis.
33067. Metaphyseal chondrodysplasia, Jansen type.
PharmGKBiPA33953.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2626Sequence AnalysisAdd
BLAST
Chaini27 – 593567Parathyroid hormone/parathyroid hormone-related peptide receptorPRO_0000012845Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi48 ↔ 117
Disulfide bondi108 ↔ 148
Disulfide bondi131 ↔ 170
Glycosylationi151 – 1511N-linked (GlcNAc...)Sequence Analysis
Glycosylationi161 – 1611N-linked (GlcNAc...)Sequence Analysis
Glycosylationi166 – 1661N-linked (GlcNAc...)Sequence Analysis
Glycosylationi176 – 1761N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ03431.
PRIDEiQ03431.

2D gel databases

REPRODUCTION-2DPAGEQ03431.

PTM databases

PhosphoSiteiQ03431.

Miscellaneous databases

PMAP-CutDBQ03431.

Expressioni

Tissue specificityi

Expressed in most tissues. Most abundant in kidney, bone and liver.

Gene expression databases

BgeeiQ03431.
CleanExiHS_PTH1R.
ExpressionAtlasiQ03431. baseline and differential.
GenevestigatoriQ03431.

Organism-specific databases

HPAiCAB016053.
HPA007978.

Interactioni

Subunit structurei

Interacts (via N-terminal extracellular domain) with PTHLH and PTH. Homodimer in the absence of bound ligand. Peptide hormone binding leads to dissociation of the homodimer. Interacts (via C-terminus) with the heterodimer formed by GNG2 and GNB1.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CTNNB1P352224EBI-2860297,EBI-491549

Protein-protein interaction databases

BioGridi111717. 50 interactions.
IntActiQ03431. 2 interactions.
MINTiMINT-258057.
STRINGi9606.ENSP00000321999.

Structurei

Secondary structure

1
593
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi34 – 5522
Beta strandi126 – 1305
Beta strandi143 – 1486
Beta strandi152 – 1543
Beta strandi160 – 1634
Turni168 – 1736
Helixi180 – 1856
Helixi188 – 1969

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BL1NMR-A168-197[»]
1ET2model-S168-469[»]
1ET3model-S168-469[»]
3C4MX-ray1.95A/B29-187[»]
3H3GX-ray1.94A29-187[»]
3KJ5X-ray3.00C474-481[»]
3L2JX-ray3.24A/B29-187[»]
ProteinModelPortaliQ03431.
SMRiQ03431. Positions 24-469.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ03431.

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini27 – 188162ExtracellularSequence AnalysisAdd
BLAST
Topological domaini213 – 2197CytoplasmicSequence Analysis
Topological domaini240 – 28243ExtracellularSequence AnalysisAdd
BLAST
Topological domaini307 – 32014CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini343 – 36119ExtracellularSequence AnalysisAdd
BLAST
Topological domaini383 – 40927CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini429 – 44012ExtracellularSequence AnalysisAdd
BLAST
Topological domaini464 – 593130CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei189 – 21224Helical; Name=1Sequence AnalysisAdd
BLAST
Transmembranei220 – 23920Helical; Name=2Sequence AnalysisAdd
BLAST
Transmembranei283 – 30624Helical; Name=3Sequence AnalysisAdd
BLAST
Transmembranei321 – 34222Helical; Name=4Sequence AnalysisAdd
BLAST
Transmembranei362 – 38221Helical; Name=5Sequence AnalysisAdd
BLAST
Transmembranei410 – 42819Helical; Name=6Sequence AnalysisAdd
BLAST
Transmembranei441 – 46323Helical; Name=7Sequence AnalysisAdd
BLAST

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi474 – 4774Important for interaction with G proteins

Sequence similaritiesi

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG293423.
GeneTreeiENSGT00760000118800.
HOGENOMiHOG000008248.
HOVERGENiHBG008318.
InParanoidiQ03431.
KOiK04585.
OMAiWIIQVPI.
OrthoDBiEOG7TF78W.
PhylomeDBiQ03431.
TreeFamiTF315710.

Family and domain databases

InterProiIPR017981. GPCR_2-like.
IPR001879. GPCR_2_extracellular_dom.
IPR002170. GPCR_2_parathyroid_rcpt.
IPR000832. GPCR_2_secretin-like.
IPR017983. GPCR_2_secretin-like_CS.
[Graphical view]
PANTHERiPTHR12011:SF24. PTHR12011:SF24. 1 hit.
PfamiPF00002. 7tm_2. 1 hit.
PF02793. HRM. 1 hit.
[Graphical view]
PRINTSiPR00249. GPCRSECRETIN.
PR00393. PTRHORMONER.
SMARTiSM00008. HormR. 1 hit.
[Graphical view]
PROSITEiPS00649. G_PROTEIN_RECEP_F2_1. 1 hit.
PS00650. G_PROTEIN_RECEP_F2_2. 1 hit.
PS50227. G_PROTEIN_RECEP_F2_3. 1 hit.
PS50261. G_PROTEIN_RECEP_F2_4. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q03431-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGTARIAPGL ALLLCCPVLS SAYALVDADD VMTKEEQIFL LHRAQAQCEK
60 70 80 90 100
RLKEVLQRPA SIMESDKGWT SASTSGKPRK DKASGKLYPE SEEDKEAPTG
110 120 130 140 150
SRYRGRPCLP EWDHILCWPL GAPGEVVAVP CPDYIYDFNH KGHAYRRCDR
160 170 180 190 200
NGSWELVPGH NRTWANYSEC VKFLTNETRE REVFDRLGMI YTVGYSVSLA
210 220 230 240 250
SLTVAVLILA YFRRLHCTRN YIHMHLFLSF MLRAVSIFVK DAVLYSGATL
260 270 280 290 300
DEAERLTEEE LRAIAQAPPP PATAAAGYAG CRVAVTFFLY FLATNYYWIL
310 320 330 340 350
VEGLYLHSLI FMAFFSEKKY LWGFTVFGWG LPAVFVAVWV SVRATLANTG
360 370 380 390 400
CWDLSSGNKK WIIQVPILAS IVLNFILFIN IVRVLATKLR ETNAGRCDTR
410 420 430 440 450
QQYRKLLKST LVLMPLFGVH YIVFMATPYT EVSGTLWQVQ MHYEMLFNSF
460 470 480 490 500
QGFFVAIIYC FCNGEVQAEI KKSWSRWTLA LDFKRKARSG SSSYSYGPMV
510 520 530 540 550
SHTSVTNVGP RVGLGLPLSP RLLPTATTNG HPQLPGHAKP GTPALETLET
560 570 580 590
TPPAMAAPKD DGFLNGSCSG LDEEASGPER PPALLQEEWE TVM
Length:593
Mass (Da):66,361
Last modified:October 1, 1993 - v1
Checksum:iDA1400640A6C7F2B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti471 – 4711K → N(PubMed:8397094)Curated
Sequence conflicti473 – 4731S → C(PubMed:8397094)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti132 – 1321P → L in BOCD. 1 Publication
VAR_016062
Natural varianti150 – 1501R → C in ENCHOM; Ollier type; unknown pathological significance. 1 Publication
Corresponds to variant rs121434601 [ dbSNP | Ensembl ].
VAR_016063
Natural varianti223 – 2231H → R in JMC; constitutively activated. 2 Publications
VAR_003582
Natural varianti410 – 4101T → P in JMC; constitutively activated. 1 Publication
VAR_003583
Natural varianti410 – 4101T → R in JMC; leads to agonist-independent cAMP formation which is less pronounced than that observed with the Pro-410 mutant. 1 Publication
VAR_038811
Natural varianti458 – 4581I → R in JMC. 1 Publication
VAR_016064

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L04308 mRNA. Translation: AAA36525.1.
X68596 mRNA. Translation: CAA48589.1.
U22409
, U22401, U22402, U22403, U22404, U22405, U22406, U22407, U22408 Genomic DNA. Translation: AAB60657.1.
U17418 mRNA. Translation: AAA56774.1.
AY449732 mRNA. Translation: AAR18076.1.
BC112221 mRNA. Translation: AAI12222.1.
BC112247 mRNA. Translation: AAI12248.1.
CCDSiCCDS2747.1.
PIRiI38139. A49191.
RefSeqiNP_000307.1. NM_000316.2.
NP_001171673.1. NM_001184744.1.
XP_005265399.1. XM_005265342.1.
UniGeneiHs.1019.

Genome annotation databases

EnsembliENST00000313049; ENSP00000321999; ENSG00000160801.
ENST00000418619; ENSP00000411424; ENSG00000160801.
ENST00000430002; ENSP00000413774; ENSG00000160801.
ENST00000449590; ENSP00000402723; ENSG00000160801.
GeneIDi5745.
KEGGihsa:5745.
UCSCiuc003cqm.3. human.

Polymorphism databases

DMDMi417555.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L04308 mRNA. Translation: AAA36525.1 .
X68596 mRNA. Translation: CAA48589.1 .
U22409
, U22401 , U22402 , U22403 , U22404 , U22405 , U22406 , U22407 , U22408 Genomic DNA. Translation: AAB60657.1 .
U17418 mRNA. Translation: AAA56774.1 .
AY449732 mRNA. Translation: AAR18076.1 .
BC112221 mRNA. Translation: AAI12222.1 .
BC112247 mRNA. Translation: AAI12248.1 .
CCDSi CCDS2747.1.
PIRi I38139. A49191.
RefSeqi NP_000307.1. NM_000316.2.
NP_001171673.1. NM_001184744.1.
XP_005265399.1. XM_005265342.1.
UniGenei Hs.1019.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1BL1 NMR - A 168-197 [» ]
1ET2 model - S 168-469 [» ]
1ET3 model - S 168-469 [» ]
3C4M X-ray 1.95 A/B 29-187 [» ]
3H3G X-ray 1.94 A 29-187 [» ]
3KJ5 X-ray 3.00 C 474-481 [» ]
3L2J X-ray 3.24 A/B 29-187 [» ]
ProteinModelPortali Q03431.
SMRi Q03431. Positions 24-469.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111717. 50 interactions.
IntActi Q03431. 2 interactions.
MINTi MINT-258057.
STRINGi 9606.ENSP00000321999.

Chemistry

BindingDBi Q03431.
ChEMBLi CHEMBL1793.
DrugBanki DB05829. Preotact.
DB06285. Teriparatide.
GuidetoPHARMACOLOGYi 331.

Protein family/group databases

TCDBi 9.A.14.4.11. the g-protein-coupled receptor (gpcr) family.
GPCRDBi Search...

PTM databases

PhosphoSitei Q03431.

Polymorphism databases

DMDMi 417555.

2D gel databases

REPRODUCTION-2DPAGE Q03431.

Proteomic databases

PaxDbi Q03431.
PRIDEi Q03431.

Protocols and materials databases

DNASUi 5745.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000313049 ; ENSP00000321999 ; ENSG00000160801 .
ENST00000418619 ; ENSP00000411424 ; ENSG00000160801 .
ENST00000430002 ; ENSP00000413774 ; ENSG00000160801 .
ENST00000449590 ; ENSP00000402723 ; ENSG00000160801 .
GeneIDi 5745.
KEGGi hsa:5745.
UCSCi uc003cqm.3. human.

Organism-specific databases

CTDi 5745.
GeneCardsi GC03P046919.
HGNCi HGNC:9608. PTH1R.
HPAi CAB016053.
HPA007978.
MIMi 125350. phenotype.
156400. phenotype.
166000. phenotype.
168468. gene.
215045. phenotype.
600002. phenotype.
neXtProti NX_Q03431.
Orphaneti 50945. Chondrodysplasia, Blomstrand type.
1077. Dental ankylosis.
79106. Eiken syndrome.
296. Enchondromatosis.
33067. Metaphyseal chondrodysplasia, Jansen type.
PharmGKBi PA33953.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG293423.
GeneTreei ENSGT00760000118800.
HOGENOMi HOG000008248.
HOVERGENi HBG008318.
InParanoidi Q03431.
KOi K04585.
OMAi WIIQVPI.
OrthoDBi EOG7TF78W.
PhylomeDBi Q03431.
TreeFami TF315710.

Enzyme and pathway databases

Reactomei REACT_18372. Class B/2 (Secretin family receptors).
REACT_19327. G alpha (s) signalling events.
SignaLinki Q03431.

Miscellaneous databases

EvolutionaryTracei Q03431.
GeneWikii Parathyroid_hormone_1_receptor.
GenomeRNAii 5745.
NextBioi 22372.
PMAP-CutDB Q03431.
PROi Q03431.
SOURCEi Search...

Gene expression databases

Bgeei Q03431.
CleanExi HS_PTH1R.
ExpressionAtlasi Q03431. baseline and differential.
Genevestigatori Q03431.

Family and domain databases

InterProi IPR017981. GPCR_2-like.
IPR001879. GPCR_2_extracellular_dom.
IPR002170. GPCR_2_parathyroid_rcpt.
IPR000832. GPCR_2_secretin-like.
IPR017983. GPCR_2_secretin-like_CS.
[Graphical view ]
PANTHERi PTHR12011:SF24. PTHR12011:SF24. 1 hit.
Pfami PF00002. 7tm_2. 1 hit.
PF02793. HRM. 1 hit.
[Graphical view ]
PRINTSi PR00249. GPCRSECRETIN.
PR00393. PTRHORMONER.
SMARTi SM00008. HormR. 1 hit.
[Graphical view ]
PROSITEi PS00649. G_PROTEIN_RECEP_F2_1. 1 hit.
PS00650. G_PROTEIN_RECEP_F2_2. 1 hit.
PS50227. G_PROTEIN_RECEP_F2_3. 1 hit.
PS50261. G_PROTEIN_RECEP_F2_4. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Identical complementary deoxyribonucleic acids encode a human renal and bone parathyroid hormone (PTH)/PTH-related peptide receptor."
    Schipani E., Karga H., Karaplis A.C., Potts J.T. Jr., Kronenberg H.M., Abou-Samra A.-B., Segre G.V., Jueppner H.
    Endocrinology 132:2157-2165(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Kidney.
  2. "Cloning and functional expression of a human parathyroid hormone receptor."
    Schneider H., Feyen J.-H., Rao Movva N.
    Eur. J. Pharmacol. 246:149-155(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Kidney.
  3. "Pseudohypoparathyroidism type Ib is not caused by mutations in the coding exons of the human parathyroid hormone (PTH)/PTH-related peptide receptor gene."
    Schipani E., Weinstein L.S., Bergwitz C., Iida-Klein A., Kong X.F., Stuhrmann M., Kruse K., Whyte M.P., Murray T., Schmidtke J., Dop C., Brickman A.S., Crawford J.D., Potts J.T. Jr., Kronenberg H.M., Abou-Samra A.-B., Segre G.V., Jueppner H.
    J. Clin. Endocrinol. Metab. 80:1611-1621(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "Characterization of cDNA and genomic DNA encoding the human PTH/PTHrP receptor."
    Levine M.A.
    Submitted (NOV-1994) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Kidney.
  5. "Isolation of cDNA coding for parathyroid hormone receptor 1 (PTHR1)."
    King M.M., Aronstam R.S., Sharma S.V.
    Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Lung.
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Cerebellum.
  7. "The N-terminal fragment of human parathyroid hormone receptor 1 constitutes a hormone binding domain and reveals a distinct disulfide pattern."
    Grauschopf U., Lilie H., Honold K., Wozny M., Reusch D., Esswein A., Schafer W., Rucknagel K.P., Rudolph R.
    Biochemistry 39:8878-8887(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISULFIDE BONDS IN EXTRACELLULAR DOMAIN.
  8. "Binding domain of human parathyroid hormone receptor: from conformation to function."
    Pellegrini M., Bisello A., Rosenblatt M., Chorev M., Mierke D.F.
    Biochemistry 37:12737-12743(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 168-198.
  9. "Molecular recognition of parathyroid hormone by its G protein-coupled receptor."
    Pioszak A.A., Xu H.E.
    Proc. Natl. Acad. Sci. U.S.A. 105:5034-5039(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 29-187 IN COMPLEX WITH PTH, DISULFIDE BONDS.
  10. "Structure of the parathyroid hormone receptor C terminus bound to the G-protein dimer Gbeta1gamma2."
    Johnston C.A., Kimple A.J., Giguere P.M., Siderovski D.P.
    Structure 16:1086-1094(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 474-481 IN COMPLEX WITH GNG2 AND GNB1, FUNCTION, SUBUNIT, MUTAGENESIS OF TRP-474 AND TRP-477.
  11. "Structural basis for parathyroid hormone-related protein binding to the parathyroid hormone receptor and design of conformation-selective peptides."
    Pioszak A.A., Parker N.R., Gardella T.J., Xu H.E.
    J. Biol. Chem. 284:28382-28391(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS) OF 29-187 IN COMPLEX WITH PTHLH, DISULFIDE BONDS.
  12. "Dimeric arrangement of the parathyroid hormone receptor and a structural mechanism for ligand-induced dissociation."
    Pioszak A.A., Harikumar K.G., Parker N.R., Miller L.J., Xu H.E.
    J. Biol. Chem. 285:12435-12444(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.24 ANGSTROMS) OF 29-187, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, MUTAGENESIS OF ILE-135 AND ASP-137.
  13. "A constitutively active mutant PTH-PTHrP receptor in Jansen-type metaphyseal chondrodysplasia."
    Schipani E., Kruse K., Jueppner H.
    Science 268:98-100(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT JMC ARG-223.
  14. "Constitutively activated receptors for parathyroid hormone and parathyroid hormone-related peptide in Jansen's metaphyseal chondrodysplasia."
    Schipani E., Langman C.B., Parfitt A.M., Jensen G.S., Kikuchi S., Kooh S.W., Cole W.G., Jueppner H.
    N. Engl. J. Med. 335:708-714(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS JMC ARG-223 AND PRO-410.
  15. "Constitutive activation of the cyclic adenosine 3',5'-monophosphate signaling pathway by parathyroid hormone (PTH)/PTH-related peptide receptors mutated at the two loci for Jansen's metaphyseal chondrodysplasia."
    Schipani E., Jensen G.S., Pincus J., Nissenson R.A., Gardella T.J., Jueppner H.
    Mol. Endocrinol. 11:851-858(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF VARIANTS JMC ARG-223 AND PRO-410.
  16. "A homozygous inactivating mutation in the parathyroid hormone/parathyroid hormone-related peptide receptor causing Blomstrand chondrodysplasia."
    Zhang P., Jobert A.-S., Couvineau A., Silve C.
    J. Clin. Endocrinol. Metab. 83:3365-3368(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT BOCD LEU-132.
  17. "A novel parathyroid hormone (PTH)/PTH-related peptide receptor mutation in Jansen's metaphyseal chondrodysplasia."
    Schipani E., Langman C.B., Hunzelman J., Le Merrer M., Loke K.Y., Dillon M.J., Silve C., Jueppner H.
    J. Clin. Endocrinol. Metab. 84:3052-3057(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT JMC ARG-458.
  18. Cited for: VARIANT ENCHOM CYS-150.
  19. "Enchondromatosis (Ollier disease, Maffucci syndrome) is not caused by the PTHR1 mutation p.R150C."
    Rozeman L.B., Sangiorgi L., Briaire-de Bruijn I.H., Mainil-Varlet P., Bertoni F., Cleton-Jansen A.-M., Hogendoorn P.C.W., Bovee J.V.M.G.
    Hum. Mutat. 24:466-473(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISCUSSION OF THE ASSOCIATION OF CYS-150 WITH ENCHOM.
  20. "A form of Jansen's metaphyseal chondrodysplasia with limited metabolic and skeletal abnormalities is caused by a novel activating parathyroid hormone (PTH)/PTH-related peptide receptor mutation."
    Bastepe M., Raas-Rothschild A., Silver J., Weissman I., Wientroub S., Jueppner H., Gillis D.
    J. Clin. Endocrinol. Metab. 89:3595-3600(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT JMC ARG-410, CHARACTERIZATION OF VARIANT JMC ARG-410.
  21. "Recessive mutations in PTHR1 cause contrasting skeletal dysplasias in Eiken and Blomstrand syndromes."
    Duchatelet S., Ostergaard E., Cortes D., Lemainque A., Julier C.
    Hum. Mol. Genet. 14:1-5(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN EISD.
  22. "PTHR1 loss-of-function mutations in familial, nonsyndromic primary failure of tooth eruption."
    Decker E., Stellzig-Eisenhauer A., Fiebig B.S., Rau C., Kress W., Saar K., Rueschendorf F., Hubner N., Grimm T., Weber B.H.F.
    Am. J. Hum. Genet. 83:781-786(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN PRIMARY FAILURE OF TOOTH ERUPTION.

Entry informationi

Entry nameiPTH1R_HUMAN
AccessioniPrimary (citable) accession number: Q03431
Secondary accession number(s): Q2M1U3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: October 29, 2014
This is version 155 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. 7-transmembrane G-linked receptors
    List of 7-transmembrane G-linked receptor entries
  2. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3