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Protein

Heat-stable enterotoxin receptor

Gene

GUCY2C

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

Functioni

Receptor for the E.coli heat-stable enterotoxin (E.coli enterotoxin markedly stimulates the accumulation of cGMP in mammalian cells expressing GC-C). Also activated by the endogenous peptides guanylin and uroguanylin.

Catalytic activityi

GTP = 3',5'-cyclic GMP + diphosphate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei357 – 3571Not glycosylated

GO - Molecular functioni

  • ATP binding Source: InterPro
  • GTP binding Source: UniProtKB-KW
  • guanylate cyclase activity Source: ProtInc
  • protein kinase activity Source: InterPro
  • toxic substance binding Source: Ensembl

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase, Receptor

Keywords - Biological processi

cGMP biosynthesis

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi4.6.1.2. 2681.

Names & Taxonomyi

Protein namesi
Recommended name:
Heat-stable enterotoxin receptor (EC:4.6.1.2)
Short name:
STA receptor
Short name:
hSTAR
Alternative name(s):
Guanylyl cyclase C
Short name:
GC-C
Intestinal guanylate cyclase
Gene namesi
Name:GUCY2C
Synonyms:GUC2C, STAR
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:4688. GUCY2C.

Subcellular locationi

  • Cell membrane 1 Publication; Single-pass type I membrane protein 1 Publication
  • Endoplasmic reticulum membrane 1 Publication; Single-pass type I membrane protein 1 Publication

  • Note: The 145 kDa plasma membrane form of GC-C contains sialic acid and galactose residues, while a differencially glycosylated 130 Kda form is a high mannose form that is resident in the endoplasmic reticulum and may serve as the precursor for the cell surface form.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini24 – 430407ExtracellularSequence AnalysisAdd
BLAST
Transmembranei431 – 45424HelicalSequence AnalysisAdd
BLAST
Topological domaini455 – 1073619CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Endoplasmic reticulum, Membrane

Pathology & Biotechi

Involvement in diseasei

Diarrhea 6 (DIAR6)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA relatively mild, early-onset chronic diarrhea that may be associated with increased susceptibility to inflammatory bowel disease, small bowel obstruction, and esophagitis.

See also OMIM:614616
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti840 – 8401S → I in DIAR6; activating mutation; exposure of the mutant receptor to its ligands results in markedly increased production of cyclic guanosine monophosphate. 1 Publication
VAR_067724
Meconium ileus (MECIL)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA condition characterized by a intestinal obstruction due to inspissated meconium in the distal ileum and cecum, which develops in utero and presents shortly after birth as a failure to pass meconium. Meconium ileus is a known clinical manifestation of cystic fibrosis.

See also OMIM:614665
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti387 – 3871D → G in MECIL; activation of guanylate cyclase activity is 60% lower than in wild-type. 1 Publication
VAR_068174

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi614616. phenotype.
614665. phenotype.
Orphaneti314373. Chronic diarrhea due to guanylate cyclase 2C overactivity.
314376. Intestinal obstruction in the newborn due to guanylate cyclase 2C deficiency.
PharmGKBiPA29069.

Chemistry

DrugBankiDB08890. Linaclotide.

Polymorphism and mutation databases

BioMutaiGUCY2C.
DMDMi311033390.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323Sequence AnalysisAdd
BLAST
Chaini24 – 10731050Heat-stable enterotoxin receptorPRO_0000012376Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi32 – 321N-linked (GlcNAc...)1 Publication
Glycosylationi75 – 751N-linked (GlcNAc...)1 Publication
Glycosylationi79 – 791N-linked (GlcNAc...)1 Publication
Glycosylationi195 – 1951N-linked (GlcNAc...)1 Publication
Glycosylationi284 – 2841N-linked (GlcNAc...)1 Publication
Glycosylationi307 – 3071N-linked (GlcNAc...)1 Publication
Glycosylationi345 – 3451N-linked (GlcNAc...)1 Publication
Glycosylationi402 – 4021N-linked (GlcNAc...)1 Publication

Post-translational modificationi

Glycosylation at Asn-75 and/or Asn-79 is required for interaction with VIP36 while glycosylation at Asn-345 and Asn-402 modulates ligand-mediated GC-C activation.1 Publication

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiP25092.
PRIDEiP25092.

PTM databases

PhosphoSiteiP25092.

Expressioni

Gene expression databases

BgeeiP25092.
CleanExiHS_GUCY2C.
HS_STAR.
GenevisibleiP25092. HS.

Organism-specific databases

HPAiHPA037655.

Interactioni

Subunit structurei

Homotrimer. Interacts via its C-terminal region with PDZK2. Interacts with the lectin chaperone VIP36.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
PDZD3Q86UT5-24EBI-2816795,EBI-8299496

Protein-protein interaction databases

BioGridi109239. 1 interaction.
IntActiP25092. 3 interactions.
MINTiMINT-261763.
STRINGi9606.ENSP00000261170.

Structurei

3D structure databases

ProteinModelPortaliP25092.
SMRiP25092. Positions 490-773, 815-1001.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini489 – 749261Protein kinasePROSITE-ProRule annotationAdd
BLAST
Domaini824 – 954131Guanylate cyclasePROSITE-ProRule annotationAdd
BLAST

Domaini

The protein kinase domain is predicted to be catalytically inactive.

Sequence similaritiesi

Belongs to the adenylyl cyclase class-4/guanylyl cyclase family.PROSITE-ProRule annotation
Contains 1 guanylate cyclase domain.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118959.
HOGENOMiHOG000112833.
HOVERGENiHBG106967.
InParanoidiP25092.
KOiK12320.
OMAiAPDYMKN.
OrthoDBiEOG72VH58.
PhylomeDBiP25092.

Family and domain databases

Gene3Di3.30.70.1230. 1 hit.
InterProiIPR001054. A/G_cyclase.
IPR018297. A/G_cyclase_CS.
IPR001828. ANF_lig-bd_rcpt.
IPR011009. Kinase-like_dom.
IPR029787. Nucleotide_cyclase.
IPR028082. Peripla_BP_I.
IPR000719. Prot_kinase_dom.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
[Graphical view]
PfamiPF01094. ANF_receptor. 1 hit.
PF00211. Guanylate_cyc. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
SMARTiSM00044. CYCc. 1 hit.
[Graphical view]
SUPFAMiSSF53822. SSF53822. 1 hit.
SSF55073. SSF55073. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS00452. GUANYLATE_CYCLASE_1. 1 hit.
PS50125. GUANYLATE_CYCLASE_2. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P25092-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKTLLLDLAL WSLLFQPGWL SFSSQVSQNC HNGSYEISVL MMGNSAFAEP
60 70 80 90 100
LKNLEDAVNE GLEIVRGRLQ NAGLNVTVNA TFMYSDGLIH NSGDCRSSTC
110 120 130 140 150
EGLDLLRKIS NAQRMGCVLI GPSCTYSTFQ MYLDTELSYP MISAGSFGLS
160 170 180 190 200
CDYKETLTRL MSPARKLMYF LVNFWKTNDL PFKTYSWSTS YVYKNGTETE
210 220 230 240 250
DCFWYLNALE ASVSYFSHEL GFKVVLRQDK EFQDILMDHN RKSNVIIMCG
260 270 280 290 300
GPEFLYKLKG DRAVAEDIVI ILVDLFNDQY FEDNVTAPDY MKNVLVLTLS
310 320 330 340 350
PGNSLLNSSF SRNLSPTKRD FALAYLNGIL LFGHMLKIFL ENGENITTPK
360 370 380 390 400
FAHAFRNLTF EGYDGPVTLD DWGDVDSTMV LLYTSVDTKK YKVLLTYDTH
410 420 430 440 450
VNKTYPVDMS PTFTWKNSKL PNDITGRGPQ ILMIAVFTLT GAVVLLLLVA
460 470 480 490 500
LLMLRKYRKD YELRQKKWSH IPPENIFPLE TNETNHVSLK IDDDKRRDTI
510 520 530 540 550
QRLRQCKYDK KRVILKDLKH NDGNFTEKQK IELNKLLQID YYNLTKFYGT
560 570 580 590 600
VKLDTMIFGV IEYCERGSLR EVLNDTISYP DGTFMDWEFK ISVLYDIAKG
610 620 630 640 650
MSYLHSSKTE VHGRLKSTNC VVDSRMVVKI TDFGCNSILP PKKDLWTAPE
660 670 680 690 700
HLRQANISQK GDVYSYGIIA QEIILRKETF YTLSCRDRNE KIFRVENSNG
710 720 730 740 750
MKPFRPDLFL ETAEEKELEV YLLVKNCWEE DPEKRPDFKK IETTLAKIFG
760 770 780 790 800
LFHDQKNESY MDTLIRRLQL YSRNLEHLVE ERTQLYKAER DRADRLNFML
810 820 830 840 850
LPRLVVKSLK EKGFVEPELY EEVTIYFSDI VGFTTICKYS TPMEVVDMLN
860 870 880 890 900
DIYKSFDHIV DHHDVYKVET IGDAYMVASG LPKRNGNRHA IDIAKMALEI
910 920 930 940 950
LSFMGTFELE HLPGLPIWIR IGVHSGPCAA GVVGIKMPRY CLFGDTVNTA
960 970 980 990 1000
SRMESTGLPL RIHVSGSTIA ILKRTECQFL YEVRGETYLK GRGNETTYWL
1010 1020 1030 1040 1050
TGMKDQKFNL PTPPTVENQQ RLQAEFSDMI ANSLQKRQAA GIRSQKPRRV
1060 1070
ASYKKGTLEY LQLNTTDKES TYF
Length:1,073
Mass (Da):123,403
Last modified:November 2, 2010 - v2
Checksum:i486A4DE6F9097E22
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti322 – 3221A → R in AAB19934 (PubMed:1718270).Curated
Sequence conflicti331 – 3311L → V in AAB19934 (PubMed:1718270).Curated
Sequence conflicti509 – 5091D → V in AAB19934 (PubMed:1718270).Curated
Sequence conflicti543 – 5431N → T in AAB19934 (PubMed:1718270).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti30 – 301C → R.1 Publication
Corresponds to variant rs56142849 [ dbSNP | Ensembl ].
VAR_042221
Natural varianti61 – 611G → R in a metastatic melanoma sample; somatic mutation. 1 Publication
VAR_042222
Natural varianti114 – 1141R → Q.1 Publication
Corresponds to variant rs56275235 [ dbSNP | Ensembl ].
VAR_042223
Natural varianti281 – 2811F → L.5 Publications
Corresponds to variant rs1420635 [ dbSNP | Ensembl ].
VAR_049253
Natural varianti387 – 3871D → G in MECIL; activation of guanylate cyclase activity is 60% lower than in wild-type. 1 Publication
VAR_068174
Natural varianti464 – 4641R → L.1 Publication
Corresponds to variant rs55684775 [ dbSNP | Ensembl ].
VAR_042224
Natural varianti610 – 6101E → K.1 Publication
Corresponds to variant rs55897626 [ dbSNP | Ensembl ].
VAR_042225
Natural varianti840 – 8401S → I in DIAR6; activating mutation; exposure of the mutant receptor to its ligands results in markedly increased production of cyclic guanosine monophosphate. 1 Publication
VAR_067724
Natural varianti859 – 8591I → V.1 Publication
Corresponds to variant rs34890806 [ dbSNP | Ensembl ].
VAR_042226
Natural varianti1045 – 10451Q → R.1 Publication
Corresponds to variant rs35617837 [ dbSNP | Ensembl ].
VAR_042227
Natural varianti1072 – 10721Y → C.1 Publication
Corresponds to variant rs35179392 [ dbSNP | Ensembl ].
VAR_042228

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S57551 mRNA. Translation: AAB19934.2.
M73489 mRNA. Translation: AAA36655.1.
AC007545 Genomic DNA. No translation available.
AC010168 Genomic DNA. No translation available.
CH471094 Genomic DNA. Translation: EAW96324.1.
BC136544 mRNA. Translation: AAI36545.1.
BC136545 mRNA. Translation: AAI36546.1.
U20230 Genomic DNA. Translation: AAC50381.1.
CCDSiCCDS8664.1.
PIRiA40940. OYHUHX.
RefSeqiNP_004954.2. NM_004963.3.
UniGeneiHs.524278.

Genome annotation databases

EnsembliENST00000261170; ENSP00000261170; ENSG00000070019.
GeneIDi2984.
KEGGihsa:2984.
UCSCiuc001rcd.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S57551 mRNA. Translation: AAB19934.2.
M73489 mRNA. Translation: AAA36655.1.
AC007545 Genomic DNA. No translation available.
AC010168 Genomic DNA. No translation available.
CH471094 Genomic DNA. Translation: EAW96324.1.
BC136544 mRNA. Translation: AAI36545.1.
BC136545 mRNA. Translation: AAI36546.1.
U20230 Genomic DNA. Translation: AAC50381.1.
CCDSiCCDS8664.1.
PIRiA40940. OYHUHX.
RefSeqiNP_004954.2. NM_004963.3.
UniGeneiHs.524278.

3D structure databases

ProteinModelPortaliP25092.
SMRiP25092. Positions 490-773, 815-1001.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109239. 1 interaction.
IntActiP25092. 3 interactions.
MINTiMINT-261763.
STRINGi9606.ENSP00000261170.

Chemistry

ChEMBLiCHEMBL1795197.
DrugBankiDB08890. Linaclotide.
GuidetoPHARMACOLOGYi1750.

PTM databases

PhosphoSiteiP25092.

Polymorphism and mutation databases

BioMutaiGUCY2C.
DMDMi311033390.

Proteomic databases

PaxDbiP25092.
PRIDEiP25092.

Protocols and materials databases

DNASUi2984.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000261170; ENSP00000261170; ENSG00000070019.
GeneIDi2984.
KEGGihsa:2984.
UCSCiuc001rcd.3. human.

Organism-specific databases

CTDi2984.
GeneCardsiGC12M014765.
H-InvDBHIX0036867.
HGNCiHGNC:4688. GUCY2C.
HPAiHPA037655.
MIMi601330. gene.
614616. phenotype.
614665. phenotype.
neXtProtiNX_P25092.
Orphaneti314373. Chronic diarrhea due to guanylate cyclase 2C overactivity.
314376. Intestinal obstruction in the newborn due to guanylate cyclase 2C deficiency.
PharmGKBiPA29069.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118959.
HOGENOMiHOG000112833.
HOVERGENiHBG106967.
InParanoidiP25092.
KOiK12320.
OMAiAPDYMKN.
OrthoDBiEOG72VH58.
PhylomeDBiP25092.

Enzyme and pathway databases

BRENDAi4.6.1.2. 2681.

Miscellaneous databases

GeneWikiiGuanylate_cyclase_2C.
GenomeRNAii2984.
NextBioi11836.
PROiP25092.
SOURCEiSearch...

Gene expression databases

BgeeiP25092.
CleanExiHS_GUCY2C.
HS_STAR.
GenevisibleiP25092. HS.

Family and domain databases

Gene3Di3.30.70.1230. 1 hit.
InterProiIPR001054. A/G_cyclase.
IPR018297. A/G_cyclase_CS.
IPR001828. ANF_lig-bd_rcpt.
IPR011009. Kinase-like_dom.
IPR029787. Nucleotide_cyclase.
IPR028082. Peripla_BP_I.
IPR000719. Prot_kinase_dom.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
[Graphical view]
PfamiPF01094. ANF_receptor. 1 hit.
PF00211. Guanylate_cyc. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
SMARTiSM00044. CYCc. 1 hit.
[Graphical view]
SUPFAMiSSF53822. SSF53822. 1 hit.
SSF55073. SSF55073. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS00452. GUANYLATE_CYCLASE_1. 1 hit.
PS50125. GUANYLATE_CYCLASE_2. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and expression of a guanylate cyclase-coupled heat stable enterotoxin receptor cDNA from a human colonic cell line."
    Singh S., Singh G., Heim J.-M., Gerzer R.
    Biochem. Biophys. Res. Commun. 179:1455-1463(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT LEU-281.
  2. "Primary structure and functional expression of the human receptor for Escherichia coli heat-stable enterotoxin."
    de Sauvage F.J., Camerato T.R., Goeddel D.V.
    J. Biol. Chem. 266:17912-17918(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT LEU-281.
  3. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT LEU-281.
  5. "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], VARIANT LEU-281.
  6. "Cell line-specific transcriptional activation of the promoter of the human guanylyl cyclase C/heat-stable enterotoxin receptor gene."
    Mann E.A., Jump M.L., Giannella R.A.
    Biochim. Biophys. Acta 1305:7-10(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-72.
    Tissue: Placenta.
  7. "Comparison of receptors for Escherichia coli heat-stable enterotoxin: novel receptor present in IEC-6 cells."
    Mann E.A., Cohen M.B., Giannella R.A.
    Am. J. Physiol. 264:G172-G178(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 24-1073, VARIANT LEU-281.
    Tissue: Colon carcinoma.
  8. "Biochemical characterization of the intracellular domain of the human guanylyl cyclase C receptor provides evidence for a catalytically active homotrimer."
    Vijayachandra K., Guruprasad M., Bhandari R., Manjunath U.H., Somesh B.P., Srinivasan N., Suguna K., Visweswariah S.S.
    Biochemistry 39:16075-16083(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  9. "A novel PDZ protein regulates the activity of guanylyl cyclase C, the heat-stable enterotoxin receptor."
    Scott R.O., Thelin W.R., Milgram S.L.
    J. Biol. Chem. 277:22934-22941(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PDZK2.
  10. "Site-specific N-linked glycosylation of receptor guanylyl cyclase C regulates ligand binding, ligand-mediated activation and interaction with vesicular integral membrane protein 36, VIP36."
    Arshad N., Ballal S., Visweswariah S.S.
    J. Biol. Chem. 288:3907-3917(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION AT ASN-32; ASN-75; ASN-79; ASN-195; ASN-284; ASN-307; ASN-345 AND ASN-402, ABSENCE OF GLYCOSYLATION AT ASN-357, INTERACTION WITH VIP36, SUBCELLULAR LOCATION.
  11. "Meconium ileus caused by mutations in GUCY2C, encoding the CFTR-activating guanylate cyclase 2C."
    Romi H., Cohen I., Landau D., Alkrinawi S., Yerushalmi B., Hershkovitz R., Newman-Heiman N., Cutting G.R., Ofir R., Sivan S., Birk O.S.
    Am. J. Hum. Genet. 90:893-899(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT MECIL GLY-387, CHARACTERIZATION OF VARIANT MECIL GLY-387.
  12. Cited for: VARIANT DIAR6 ILE-840, CHARACTERIZATION OF VARIANT DIAR6 ILE-840.
  13. "Patterns of somatic mutation in human cancer genomes."
    Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
    , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
    Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS [LARGE SCALE ANALYSIS] ARG-30; ARG-61; GLN-114; LEU-464; LYS-610; VAL-859; ARG-1045 AND CYS-1072.

Entry informationi

Entry nameiGUC2C_HUMAN
AccessioniPrimary (citable) accession number: P25092
Secondary accession number(s): B2RMY6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: November 2, 2010
Last modified: June 24, 2015
This is version 159 of the entry and version 2 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.