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P25092

- GUC2C_HUMAN

UniProt

P25092 - GUC2C_HUMAN

Protein

Heat-stable enterotoxin receptor

Gene

GUCY2C

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 153 (01 Oct 2014)
      Sequence version 2 (02 Nov 2010)
      Previous versions | rss
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    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

    1. ATP binding Source: InterPro
    2. GTP binding Source: UniProtKB-KW
    3. guanylate cyclase activity Source: ProtInc
    4. protein binding Source: UniProtKB
    5. protein kinase activity Source: InterPro
    6. toxic substance binding Source: Ensembl

    GO - Biological processi

    1. intracellular signal transduction Source: InterPro
    2. receptor guanylyl cyclase signaling pathway Source: ProtInc
    3. regulation of cell proliferation Source: Ensembl
    4. response to toxic substance Source: Ensembl

    Keywords - Molecular functioni

    Lyase, Receptor

    Keywords - Biological processi

    cGMP biosynthesis

    Keywords - Ligandi

    GTP-binding, Nucleotide-binding

    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: 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.

    GO - Cellular componenti

    1. endoplasmic reticulum membrane Source: UniProtKB-SubCell
    2. integral component of membrane Source: UniProtKB-KW
    3. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Endoplasmic reticulum, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Diarrhea 6 (DIAR6) [MIM:614616]: A relatively mild, early-onset chronic diarrhea that may be associated with increased susceptibility to inflammatory bowel disease, small bowel obstruction, and esophagitis.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    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) [MIM:614665]: A 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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    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.

    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.
    GenevestigatoriP25092.

    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 491-772, 815-1001.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

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

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei431 – 45424HelicalSequence AnalysisAdd
    BLAST

    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.
    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.
    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

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    MKTLLLDLAL WSLLFQPGWL SFSSQVSQNC HNGSYEISVL MMGNSAFAEP     50
    LKNLEDAVNE GLEIVRGRLQ NAGLNVTVNA TFMYSDGLIH NSGDCRSSTC 100
    EGLDLLRKIS NAQRMGCVLI GPSCTYSTFQ MYLDTELSYP MISAGSFGLS 150
    CDYKETLTRL MSPARKLMYF LVNFWKTNDL PFKTYSWSTS YVYKNGTETE 200
    DCFWYLNALE ASVSYFSHEL GFKVVLRQDK EFQDILMDHN RKSNVIIMCG 250
    GPEFLYKLKG DRAVAEDIVI ILVDLFNDQY FEDNVTAPDY MKNVLVLTLS 300
    PGNSLLNSSF SRNLSPTKRD FALAYLNGIL LFGHMLKIFL ENGENITTPK 350
    FAHAFRNLTF EGYDGPVTLD DWGDVDSTMV LLYTSVDTKK YKVLLTYDTH 400
    VNKTYPVDMS PTFTWKNSKL PNDITGRGPQ ILMIAVFTLT GAVVLLLLVA 450
    LLMLRKYRKD YELRQKKWSH IPPENIFPLE TNETNHVSLK IDDDKRRDTI 500
    QRLRQCKYDK KRVILKDLKH NDGNFTEKQK IELNKLLQID YYNLTKFYGT 550
    VKLDTMIFGV IEYCERGSLR EVLNDTISYP DGTFMDWEFK ISVLYDIAKG 600
    MSYLHSSKTE VHGRLKSTNC VVDSRMVVKI TDFGCNSILP PKKDLWTAPE 650
    HLRQANISQK GDVYSYGIIA QEIILRKETF YTLSCRDRNE KIFRVENSNG 700
    MKPFRPDLFL ETAEEKELEV YLLVKNCWEE DPEKRPDFKK IETTLAKIFG 750
    LFHDQKNESY MDTLIRRLQL YSRNLEHLVE ERTQLYKAER DRADRLNFML 800
    LPRLVVKSLK EKGFVEPELY EEVTIYFSDI VGFTTICKYS TPMEVVDMLN 850
    DIYKSFDHIV DHHDVYKVET IGDAYMVASG LPKRNGNRHA IDIAKMALEI 900
    LSFMGTFELE HLPGLPIWIR IGVHSGPCAA GVVGIKMPRY CLFGDTVNTA 950
    SRMESTGLPL RIHVSGSTIA ILKRTECQFL YEVRGETYLK GRGNETTYWL 1000
    TGMKDQKFNL PTPPTVENQQ RLQAEFSDMI ANSLQKRQAA GIRSQKPRRV 1050
    ASYKKGTLEY LQLNTTDKES TYF 1073
    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:
    EMBL
    GenBank
    DDBJ
    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.

    Polymorphism databases

    DMDMi311033390.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS8664.1.
    PIRi A40940. OYHUHX.
    RefSeqi NP_004954.2. NM_004963.3.
    UniGenei Hs.524278.

    3D structure databases

    ProteinModelPortali P25092.
    SMRi P25092. Positions 491-772, 815-1001.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109239. 1 interaction.
    IntActi P25092. 3 interactions.
    MINTi MINT-261763.
    STRINGi 9606.ENSP00000261170.

    Chemistry

    ChEMBLi CHEMBL1795197.
    GuidetoPHARMACOLOGYi 1750.

    PTM databases

    PhosphoSitei P25092.

    Polymorphism databases

    DMDMi 311033390.

    Proteomic databases

    PaxDbi P25092.
    PRIDEi P25092.

    Protocols and materials databases

    DNASUi 2984.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000261170 ; ENSP00000261170 ; ENSG00000070019 .
    GeneIDi 2984.
    KEGGi hsa:2984.
    UCSCi uc001rcd.3. human.

    Organism-specific databases

    CTDi 2984.
    GeneCardsi GC12M014765.
    H-InvDB HIX0036867.
    HGNCi HGNC:4688. GUCY2C.
    HPAi HPA037655.
    MIMi 601330. gene.
    614616. phenotype.
    614665. phenotype.
    neXtProti NX_P25092.
    Orphaneti 314373. Chronic diarrhea due to guanylate cyclase 2C overactivity.
    314376. Intestinal obstruction in the newborn due to guanylate cyclase 2C deficiency.
    PharmGKBi PA29069.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000112833.
    HOVERGENi HBG106967.
    InParanoidi P25092.
    KOi K12320.
    OMAi APDYMKN.
    OrthoDBi EOG72VH58.
    PhylomeDBi P25092.

    Miscellaneous databases

    GeneWikii Guanylate_cyclase_2C.
    GenomeRNAii 2984.
    NextBioi 11836.
    PROi P25092.
    SOURCEi Search...

    Gene expression databases

    Bgeei P25092.
    CleanExi HS_GUCY2C.
    HS_STAR.
    Genevestigatori P25092.

    Family and domain databases

    Gene3Di 3.30.70.1230. 1 hit.
    InterProi IPR001054. A/G_cyclase.
    IPR018297. A/G_cyclase_CS.
    IPR001828. ANF_lig-bd_rcpt.
    IPR011009. Kinase-like_dom.
    IPR028082. Peripla_BP_I.
    IPR000719. Prot_kinase_dom.
    IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
    [Graphical view ]
    Pfami PF01094. ANF_receptor. 1 hit.
    PF00211. Guanylate_cyc. 1 hit.
    PF07714. Pkinase_Tyr. 1 hit.
    [Graphical view ]
    SMARTi SM00044. CYCc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53822. SSF53822. 1 hit.
    SSF55073. SSF55073. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEi PS00452. GUANYLATE_CYCLASE_1. 1 hit.
    PS50125. GUANYLATE_CYCLASE_2. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 153 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3