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P01350

- GAST_HUMAN

UniProt

P01350 - GAST_HUMAN

Protein

Gastrin

Gene

GAST

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

    Gastrin stimulates the stomach mucosa to produce and secrete hydrochloric acid and the pancreas to secrete its digestive enzymes. It also stimulates smooth muscle contraction and increases blood circulation and water secretion in the stomach and intestine.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei40 – 412Cleavage
    Sitei58 – 592Cleavage
    Sitei75 – 762Cleavage
    Sitei95 – 962Cleavage

    GO - Molecular functioni

    1. hormone activity Source: ProtInc
    2. protein binding Source: IntAct

    GO - Biological processi

    1. G-protein coupled receptor signaling pathway Source: Ensembl
    2. signal transduction Source: ProtInc

    Keywords - Molecular functioni

    Hormone

    Enzyme and pathway databases

    ReactomeiREACT_120966. Gastrin-CREB signalling pathway via PKC and MAPK.
    REACT_18283. G alpha (q) signalling events.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Gastrin
    Cleaved into the following 6 chains:
    Alternative name(s):
    Gastrin component I
    Gastrin-52
    Short name:
    G52
    Alternative name(s):
    Gastrin component II
    Gastrin-34
    Short name:
    G34
    Alternative name(s):
    Gastrin component III
    Gastrin-17
    Short name:
    G17
    Gastrin-14
    Short name:
    G14
    Gastrin-6
    Short name:
    G6
    Gene namesi
    Name:GAST
    Synonyms:GAS
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:4164. GAST.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: Reactome

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi86 – 861A → D: Small increase in ratio of gastrin-17 versus gastrin-34 production. No change in ratio of gastrin-17 versus gastrin-34 production; when associated with F-87. 1 Publication
    Mutagenesisi87 – 871Y → F: Small decrease in ratio of gastrin-17 versus gastrin-34 production. No change in ratio of gastrin-17 versus gastrin-34 production; when associated with D-86. 1 Publication

    Organism-specific databases

    PharmGKBiPA28577.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 21211 PublicationAdd
    BLAST
    Peptidei22 – 9271Gastrin-71PRO_0000010633Add
    BLAST
    Peptidei41 – 9252Gastrin-52PRO_0000010634Add
    BLAST
    Peptidei59 – 9234Big gastrinPRO_0000010635Add
    BLAST
    Peptidei76 – 9217GastrinPRO_0000010636Add
    BLAST
    Peptidei79 – 9214Gastrin-14PRO_0000010637Add
    BLAST
    Peptidei87 – 926Gastrin-6PRO_0000010638
    Propeptidei96 – 1016Removed in mature formPRO_0000010639

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei59 – 591Pyrrolidone carboxylic acid; in form big gastrin1 Publication
    Modified residuei76 – 761Pyrrolidone carboxylic acid; in form gastrin1 Publication
    Modified residuei87 – 871Sulfotyrosine; partial3 Publications
    Modified residuei92 – 921Phenylalanine amide1 Publication
    Modified residuei96 – 961Phosphoserine1 Publication

    Post-translational modificationi

    Two different processing pathways probably exist in antral G-cells. In the dominant pathway progastrin is cleaved at three sites resulting in two major bioactive gastrins, gastrin-34 and gastrin-17. In the putative alternative pathway, progastrin may be processed only at the most C-terminal dibasic site resulting in the synthesis of gastrin-71.
    Sulfation enhances proteolytic processing, and blocks peptide degradation. Levels of sulfation differ between proteolytically-cleaved gastrins. Thus, gastrin-6 is almost 73% sulfated, whereas the larger gastrins are less than 50% sulfated. Sulfation levels are also tissue-specific.3 Publications

    Keywords - PTMi

    Amidation, Cleavage on pair of basic residues, Phosphoprotein, Pyrrolidone carboxylic acid, Sulfation

    Proteomic databases

    PaxDbiP01350.
    PRIDEiP01350.

    PTM databases

    PhosphoSiteiP01350.

    Miscellaneous databases

    PMAP-CutDBP01350.

    Expressioni

    Gene expression databases

    BgeeiP01350.
    CleanExiHS_GAST.
    GenevestigatoriP01350.

    Organism-specific databases

    HPAiCAB000038.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    TFP027875EBI-3436637,EBI-714319

    Protein-protein interaction databases

    BioGridi108796. 1 interaction.
    DIPiDIP-403N.
    IntActiP01350. 2 interactions.
    MINTiMINT-7212817.
    STRINGi9606.ENSP00000331358.

    Structurei

    3D structure databases

    ProteinModelPortaliP01350.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the gastrin/cholecystokinin family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG39909.
    HOGENOMiHOG000073533.
    HOVERGENiHBG097593.
    InParanoidiP01350.
    KOiK13768.
    OMAiGPWVEEE.
    OrthoDBiEOG72ZCH9.
    PhylomeDBiP01350.
    TreeFamiTF336994.

    Family and domain databases

    InterProiIPR001651. Gastrin.
    IPR013152. Gastrin/cholecystokinin_CS.
    [Graphical view]
    PfamiPF00918. Gastrin. 1 hit.
    [Graphical view]
    SMARTiSM00029. GASTRIN. 1 hit.
    [Graphical view]
    PROSITEiPS00259. GASTRIN. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P01350-1 [UniParc]FASTAAdd to Basket

    « Hide

    MQRLCVYVLI FALALAAFSE ASWKPRSQQP DAPLGTGANR DLELPWLEQQ    50
    GPASHHRRQL GPQGPPHLVA DPSKKQGPWL EEEEEAYGWM DFGRRSAEDE 100
    N 101
    Length:101
    Mass (Da):11,394
    Last modified:October 23, 1986 - v1
    Checksum:iA03C847FCFE7216C
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti3 – 31R → P.
    Corresponds to variant rs34309618 [ dbSNP | Ensembl ].
    VAR_049127

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X00183 Genomic DNA. Translation: CAA25005.1.
    X00183 Genomic DNA. Translation: CAA25006.1.
    X00183 Genomic DNA. Translation: CAA25007.1.
    V00511 mRNA. Translation: CAA23769.1.
    M15958 Genomic DNA. Translation: AAA52520.1.
    K01254 Genomic DNA. Translation: AAB59533.1.
    BC069724 mRNA. Translation: AAH69724.1.
    BC069762 mRNA. Translation: AAH69762.1.
    CCDSiCCDS11404.1.
    PIRiA93997. GMHUB.
    RefSeqiNP_000796.1. NM_000805.4.
    UniGeneiHs.2681.

    Genome annotation databases

    EnsembliENST00000329402; ENSP00000331358; ENSG00000184502.
    GeneIDi2520.
    KEGGihsa:2520.
    UCSCiuc002hxl.3. human.

    Polymorphism databases

    DMDMi120952.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    Wikipedia

    Gastrin entry

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X00183 Genomic DNA. Translation: CAA25005.1 .
    X00183 Genomic DNA. Translation: CAA25006.1 .
    X00183 Genomic DNA. Translation: CAA25007.1 .
    V00511 mRNA. Translation: CAA23769.1 .
    M15958 Genomic DNA. Translation: AAA52520.1 .
    K01254 Genomic DNA. Translation: AAB59533.1 .
    BC069724 mRNA. Translation: AAH69724.1 .
    BC069762 mRNA. Translation: AAH69762.1 .
    CCDSi CCDS11404.1.
    PIRi A93997. GMHUB.
    RefSeqi NP_000796.1. NM_000805.4.
    UniGenei Hs.2681.

    3D structure databases

    ProteinModelPortali P01350.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108796. 1 interaction.
    DIPi DIP-403N.
    IntActi P01350. 2 interactions.
    MINTi MINT-7212817.
    STRINGi 9606.ENSP00000331358.

    PTM databases

    PhosphoSitei P01350.

    Polymorphism databases

    DMDMi 120952.

    Proteomic databases

    PaxDbi P01350.
    PRIDEi P01350.

    Protocols and materials databases

    DNASUi 2520.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000329402 ; ENSP00000331358 ; ENSG00000184502 .
    GeneIDi 2520.
    KEGGi hsa:2520.
    UCSCi uc002hxl.3. human.

    Organism-specific databases

    CTDi 2520.
    GeneCardsi GC17P039868.
    HGNCi HGNC:4164. GAST.
    HPAi CAB000038.
    MIMi 137250. gene.
    neXtProti NX_P01350.
    PharmGKBi PA28577.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG39909.
    HOGENOMi HOG000073533.
    HOVERGENi HBG097593.
    InParanoidi P01350.
    KOi K13768.
    OMAi GPWVEEE.
    OrthoDBi EOG72ZCH9.
    PhylomeDBi P01350.
    TreeFami TF336994.

    Enzyme and pathway databases

    Reactomei REACT_120966. Gastrin-CREB signalling pathway via PKC and MAPK.
    REACT_18283. G alpha (q) signalling events.

    Miscellaneous databases

    GeneWikii Gastrin.
    GenomeRNAii 2520.
    NextBioi 9923.
    PMAP-CutDB P01350.
    PROi P01350.
    SOURCEi Search...

    Gene expression databases

    Bgeei P01350.
    CleanExi HS_GAST.
    Genevestigatori P01350.

    Family and domain databases

    InterProi IPR001651. Gastrin.
    IPR013152. Gastrin/cholecystokinin_CS.
    [Graphical view ]
    Pfami PF00918. Gastrin. 1 hit.
    [Graphical view ]
    SMARTi SM00029. GASTRIN. 1 hit.
    [Graphical view ]
    PROSITEi PS00259. GASTRIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Expression of human gastrin gene in normal and gastrinoma tissues."
      Kariya Y., Kato K., Hayashizaki Y., Himeno S., Tarui S., Matsubara K.
      Gene 50:345-352(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Structural analysis of the gene encoding human gastrin: the large intron contains an Alu sequence."
      Ito R., Sato K., Helmer T., Jay G., Agarwal K.L.
      Proc. Natl. Acad. Sci. U.S.A. 81:4662-4666(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "Molecular cloning of human gastrin cDNA: evidence for evolution of gastrin by gene duplication."
      Boel E., Vuust J., Norris F., Norris K., Wind A., Rehfeld J.F., Marcker K.A.
      Proc. Natl. Acad. Sci. U.S.A. 80:2866-2869(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    6. "Molecular cloning of human gastrin precursor cDNA."
      Kato K., Himeno S., Takahashi Y., Wakabayashi T., Tarui S., Matsubara K.
      Gene 26:53-57(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    7. "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].
    8. "Identification of gastrin component I as gastrin-71. The largest possible bioactive progastrin product."
      Rehfeld J.F., Johnsen A.H.
      Eur. J. Biochem. 223:765-773(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 22-101, CHARACTERIZATION OF GASTRIN 71.
      Tissue: Gastric mucosa.
    9. Cited for: PROTEIN SEQUENCE OF 76-92, PYROGLUTAMATE FORMATION AT GLN-76, AMIDATION AT PHE-92.
    10. "Purification and structural determination of urinary NH2-terminal big gastrin fragments."
      Higashimoto Y., Himeno S., Shinomura Y., Nagao K., Tamura T., Tarui S.
      Biochem. Biophys. Res. Commun. 160:1364-1370(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 59-68, PYROGLUTAMATE FORMATION AT GLN-59.
    11. "Aminoacid constitution of two gastrins isolated from Zollinger-Ellison tumour tissue."
      Gregory R.A., Tracy H.J., Agarwal K.L., Grossman M.I.
      Gut 10:603-608(1969) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 76-92.
    12. "The human gastrin precursor. Characterization of phosphorylated forms and fragments."
      Varro A., Desmond H., Pauwels S., Gregory H., Young J., Dockray G.J.
      Biochem. J. 256:951-957(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-96.
    13. "Post-poly(Glu) cleavage and degradation modified by O-sulfated tyrosine: a novel post-translational processing mechanism."
      Rehfeld J.F., Hansen C.P., Johnsen A.H.
      EMBO J. 14:389-396(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEOLYTIC PROCESSING, IDENTIFICATION BY MASS SPECTROMETRY, SULFATION AT TYR-87.
    14. "Tyrosine O-sulfation promotes proteolytic processing of progastrin."
      Bundgaard J.R., Vuust J., Rehfeld J.F.
      EMBO J. 14:3073-3079(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: SULFATION, MUTAGENESIS OF ALA-86 AND TYR-87, PROTEOLYTIC PROCESSING.
    15. "Metabolism and acid secretory effect of sulfated and nonsulfated gastrin-6 in humans."
      Palnaes Hansen C., Stadil F., Rehfeld J.F.
      Am. J. Physiol. 279:G903-G909(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEOLYTIC PROCESSING, SULFATION AT TYR-87.

    Entry informationi

    Entry nameiGAST_HUMAN
    AccessioniPrimary (citable) accession number: P01350
    Secondary accession number(s): P78463, P78464
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: October 23, 1986
    Last modified: October 1, 2014
    This is version 143 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 17
      Human chromosome 17: 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