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P01350

- GAST_HUMAN

UniProt

P01350 - GAST_HUMAN

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Protein

Gastrin

Gene

GAST

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

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

GO - Biological processi

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

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
Complete GO annotation...

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; partial2 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.
GeneTreeiENSGT00390000014792.
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

        10         20         30         40         50
MQRLCVYVLI FALALAAFSE ASWKPRSQQP DAPLGTGANR DLELPWLEQQ
60 70 80 90 100
GPASHHRRQL GPQGPPHLVA DPSKKQGPWL EEEEEAYGWM DFGRRSAEDE

N
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.
GeneTreei ENSGT00390000014792.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 144 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