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P32745

- SSR3_HUMAN

UniProt

P32745 - SSR3_HUMAN

Protein

Somatostatin receptor type 3

Gene

SSTR3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 142 (01 Oct 2014)
      Sequence version 1 (01 Oct 1993)
      Previous versions | rss
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    Functioni

    Receptor for somatostatin-14 and -28. This receptor is coupled via pertussis toxin sensitive G proteins to inhibition of adenylyl cyclase.1 Publication

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. somatostatin receptor activity Source: ProtInc

    GO - Biological processi

    1. cell-cell signaling Source: ProtInc
    2. cellular response to estradiol stimulus Source: Ensembl
    3. cellular response to glucocorticoid stimulus Source: Ensembl
    4. cerebellum development Source: Ensembl
    5. forebrain development Source: Ensembl
    6. G-protein coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger Source: ProtInc
    7. hormone-mediated apoptotic signaling pathway Source: ProtInc
    8. negative regulation of cell proliferation Source: ProtInc
    9. response to starvation Source: Ensembl
    10. somatostatin signaling pathway Source: GOC
    11. spermatogenesis Source: Ensembl

    Keywords - Molecular functioni

    G-protein coupled receptor, Receptor, Transducer

    Enzyme and pathway databases

    ReactomeiREACT_14819. Peptide ligand-binding receptors.
    REACT_19231. G alpha (i) signalling events.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Somatostatin receptor type 3
    Short name:
    SS-3-R
    Short name:
    SS3-R
    Short name:
    SS3R
    Alternative name(s):
    SSR-28
    Gene namesi
    Name:SSTR3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 22

    Organism-specific databases

    HGNCiHGNC:11332. SSTR3.

    Subcellular locationi

    Cell membrane By similarity; Multi-pass membrane protein By similarity
    Note: Internalized into endoplasmic vesicles upon somatostatin-stimulation.By similarity

    GO - Cellular componenti

    1. ciliary membrane Source: Ensembl
    2. cytoplasm Source: Ensembl
    3. integral component of plasma membrane Source: ProtInc
    4. nonmotile primary cilium Source: BHF-UCL
    5. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA36156.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 418418Somatostatin receptor type 3PRO_0000070124Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi17 – 171N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi30 – 301N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi116 ↔ 191PROSITE-ProRule annotation
    Modified residuei348 – 3481PhosphothreonineBy similarity

    Post-translational modificationi

    Phosphorylated. Phosphorylation increases upon somatostatin binding By similarity.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    PaxDbiP32745.
    PRIDEiP32745.

    PTM databases

    PhosphoSiteiP32745.

    Expressioni

    Tissue specificityi

    Brain, pituitary and pancreas.1 Publication

    Gene expression databases

    ArrayExpressiP32745.
    BgeeiP32745.
    CleanExiHS_SSTR3.
    GenevestigatoriP32745.

    Organism-specific databases

    HPAiCAB022647.

    Interactioni

    Subunit structurei

    Homodimer and heterodimer with SSTR2. Heterodimerization with SSTR2 inactivates SSTR3 receptor function By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    MPDZO759705EBI-6266935,EBI-821405
    MpdzO551642EBI-6266935,EBI-7401093From a different organism.
    SSTR2P308743EBI-6266935,EBI-6266898

    Protein-protein interaction databases

    BioGridi112631. 13 interactions.
    IntActiP32745. 9 interactions.
    MINTiMINT-6800539.
    STRINGi9606.ENSP00000330138.

    Structurei

    3D structure databases

    ProteinModelPortaliP32745.
    SMRiP32745. Positions 37-325.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 4343ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini70 – 7910CytoplasmicSequence Analysis
    Topological domaini102 – 11615ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini139 – 16123CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini182 – 20524ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini232 – 25726CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini280 – 29314ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini317 – 418102CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei44 – 6926Helical; Name=1Sequence AnalysisAdd
    BLAST
    Transmembranei80 – 10122Helical; Name=2Sequence AnalysisAdd
    BLAST
    Transmembranei117 – 13822Helical; Name=3Sequence AnalysisAdd
    BLAST
    Transmembranei162 – 18120Helical; Name=4Sequence AnalysisAdd
    BLAST
    Transmembranei206 – 23126Helical; Name=5Sequence AnalysisAdd
    BLAST
    Transmembranei258 – 27922Helical; Name=6Sequence AnalysisAdd
    BLAST
    Transmembranei294 – 31623Helical; Name=7Sequence AnalysisAdd
    BLAST

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi346 – 36015Glu-rich (acidic)Add
    BLAST

    Sequence similaritiesi

    Belongs to the G-protein coupled receptor 1 family.PROSITE-ProRule annotation

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG274661.
    HOGENOMiHOG000230485.
    HOVERGENiHBG106919.
    InParanoidiP32745.
    KOiK04219.
    OMAiNASSAWP.
    OrthoDBiEOG7BKCVQ.
    PhylomeDBiP32745.
    TreeFamiTF315737.

    Family and domain databases

    Gene3Di1.20.1070.10. 1 hit.
    InterProiIPR000276. GPCR_Rhodpsn.
    IPR017452. GPCR_Rhodpsn_7TM.
    IPR000586. Somatstn_rcpt.
    IPR001856. Somatstn_rcpt_3.
    [Graphical view]
    PfamiPF00001. 7tm_1. 1 hit.
    [Graphical view]
    PRINTSiPR00237. GPCRRHODOPSN.
    PR00246. SOMATOSTATNR.
    PR00589. SOMATOSTTN3R.
    PROSITEiPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
    PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P32745-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDMLHPSSVS TTSEPENASS AWPPDATLGN VSAGPSPAGL AVSGVLIPLV    50
    YLVVCVVGLL GNSLVIYVVL RHTASPSVTN VYILNLALAD ELFMLGLPFL 100
    AAQNALSYWP FGSLMCRLVM AVDGINQFTS IFCLTVMSVD RYLAVVHPTR 150
    SARWRTAPVA RTVSAAVWVA SAVVVLPVVV FSGVPRGMST CHMQWPEPAA 200
    AWRAGFIIYT AALGFFGPLL VICLCYLLIV VKVRSAGRRV WAPSCQRRRR 250
    SERRVTRMVV AVVALFVLCW MPFYVLNIVN VVCPLPEEPA FFGLYFLVVA 300
    LPYANSCANP ILYGFLSYRF KQGFRRVLLR PSRRVRSQEP TVGPPEKTEE 350
    EDEEEEDGEE SREGGKGKEM NGRVSQITQP GTSGQERPPS RVASKEQQLL 400
    PQEASTGEKS STMRISYL 418
    Length:418
    Mass (Da):45,847
    Last modified:October 1, 1993 - v1
    Checksum:i1227095F801190C4
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti33 – 331A → V.
    Corresponds to variant rs4988466 [ dbSNP | Ensembl ].
    VAR_029219
    Natural varianti37 – 371P → L.
    Corresponds to variant rs34943557 [ dbSNP | Ensembl ].
    VAR_049440
    Natural varianti251 – 2511S → F.
    Corresponds to variant rs6413537 [ dbSNP | Ensembl ].
    VAR_020072
    Natural varianti336 – 3361R → C.
    Corresponds to variant rs4988469 [ dbSNP | Ensembl ].
    VAR_029220
    Natural varianti411 – 4111S → T.
    Corresponds to variant rs229568 [ dbSNP | Ensembl ].
    VAR_011853
    Natural varianti414 – 4141R → H.
    Corresponds to variant rs4988471 [ dbSNP | Ensembl ].
    VAR_029221

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M96738 Genomic DNA. Translation: AAA60592.1.
    AY277678 Genomic DNA. Translation: AAP32288.1.
    AY322541 Genomic DNA. Translation: AAP84354.1.
    CR456585 mRNA. Translation: CAG30471.1.
    AK291165 mRNA. Translation: BAF83854.1.
    Z82188 Genomic DNA. Translation: CAB45263.1.
    BC096829 mRNA. Translation: AAH96829.1.
    CCDSiCCDS13944.1.
    PIRiA46226.
    RefSeqiNP_001042.1. NM_001051.4.
    NP_001265616.1. NM_001278687.2.
    XP_005261778.1. XM_005261721.2.
    XP_006724374.1. XM_006724311.1.
    UniGeneiHs.225995.
    Hs.255208.

    Genome annotation databases

    GeneIDi6753.
    KEGGihsa:6753.
    UCSCiuc003ara.3. human.

    Polymorphism databases

    DMDMi417815.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M96738 Genomic DNA. Translation: AAA60592.1 .
    AY277678 Genomic DNA. Translation: AAP32288.1 .
    AY322541 Genomic DNA. Translation: AAP84354.1 .
    CR456585 mRNA. Translation: CAG30471.1 .
    AK291165 mRNA. Translation: BAF83854.1 .
    Z82188 Genomic DNA. Translation: CAB45263.1 .
    BC096829 mRNA. Translation: AAH96829.1 .
    CCDSi CCDS13944.1.
    PIRi A46226.
    RefSeqi NP_001042.1. NM_001051.4.
    NP_001265616.1. NM_001278687.2.
    XP_005261778.1. XM_005261721.2.
    XP_006724374.1. XM_006724311.1.
    UniGenei Hs.225995.
    Hs.255208.

    3D structure databases

    ProteinModelPortali P32745.
    SMRi P32745. Positions 37-325.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112631. 13 interactions.
    IntActi P32745. 9 interactions.
    MINTi MINT-6800539.
    STRINGi 9606.ENSP00000330138.

    Chemistry

    BindingDBi P32745.
    ChEMBLi CHEMBL2028.
    GuidetoPHARMACOLOGYi 357.

    Protein family/group databases

    GPCRDBi Search...

    PTM databases

    PhosphoSitei P32745.

    Polymorphism databases

    DMDMi 417815.

    Proteomic databases

    PaxDbi P32745.
    PRIDEi P32745.

    Protocols and materials databases

    DNASUi 6753.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 6753.
    KEGGi hsa:6753.
    UCSCi uc003ara.3. human.

    Organism-specific databases

    CTDi 6753.
    GeneCardsi GC22M037600.
    HGNCi HGNC:11332. SSTR3.
    HPAi CAB022647.
    MIMi 182453. gene.
    neXtProti NX_P32745.
    PharmGKBi PA36156.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG274661.
    HOGENOMi HOG000230485.
    HOVERGENi HBG106919.
    InParanoidi P32745.
    KOi K04219.
    OMAi NASSAWP.
    OrthoDBi EOG7BKCVQ.
    PhylomeDBi P32745.
    TreeFami TF315737.

    Enzyme and pathway databases

    Reactomei REACT_14819. Peptide ligand-binding receptors.
    REACT_19231. G alpha (i) signalling events.

    Miscellaneous databases

    GeneWikii Somatostatin_receptor_3.
    GenomeRNAii 6753.
    NextBioi 26344.
    PROi P32745.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P32745.
    Bgeei P32745.
    CleanExi HS_SSTR3.
    Genevestigatori P32745.

    Family and domain databases

    Gene3Di 1.20.1070.10. 1 hit.
    InterProi IPR000276. GPCR_Rhodpsn.
    IPR017452. GPCR_Rhodpsn_7TM.
    IPR000586. Somatstn_rcpt.
    IPR001856. Somatstn_rcpt_3.
    [Graphical view ]
    Pfami PF00001. 7tm_1. 1 hit.
    [Graphical view ]
    PRINTSi PR00237. GPCRRHODOPSN.
    PR00246. SOMATOSTATNR.
    PR00589. SOMATOSTTN3R.
    PROSITEi PS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
    PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Somatostatin receptors, an expanding gene family: cloning and functional characterization of human SSTR3, a protein coupled to adenylyl cyclase."
      Yamada Y., Reisine T., Law S.F., Ihara Y., Kubota A., Kagimoto S., Seino M., Seino Y., Bell G.I., Seino S.
      Mol. Endocrinol. 6:2136-2142(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, TISSUE SPECIFICITY.
    2. "A human somatostatin receptor (SSTR3), located on chromosome 22, displays preferential affinity for somatostatin-14 like peptides."
      Corness J.D., Demchyshyn L.L., Seeman P., van Tol H.H.M., Srikant C.B., Kent G., Patel Y.C., Niznik H.B.
      FEBS Lett. 321:279-284(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "The human somatostatin receptor subtype 3 contains an upstream exon in the 5'-untranslated region: functional promoter studies."
      Rasch A.C., Boehnke C., Petersenn S.
      Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org)."
      Kopatz S.A., Aronstam R.S., Sharma S.V.
      Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    6. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    7. "The DNA sequence of human chromosome 22."
      Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
      , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
      Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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].

    Entry informationi

    Entry nameiSSR3_HUMAN
    AccessioniPrimary (citable) accession number: P32745
    Secondary accession number(s): A8K550, Q53ZR7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1993
    Last sequence update: October 1, 1993
    Last modified: October 1, 2014
    This is version 142 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

    Complete proteome, Reference proteome

    Documents

    1. 7-transmembrane G-linked receptors
      List of 7-transmembrane G-linked receptor entries
    2. Human chromosome 22
      Human chromosome 22: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3