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P22466 (GALA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 135. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Galanin peptides

Cleaved into the following 2 chains:

  1. Galanin
  2. Galanin message-associated peptide
    Short name=GMAP
Gene names
Name:GAL
Synonyms:GAL1, GALN, GLNN
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length123 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Contracts smooth muscle of the gastrointestinal and genitourinary tract, regulates growth hormone release, modulates insulin release, and may be involved in the control of adrenal secretion.

Subcellular location

Secreted.

Sequence similarities

Belongs to the galanin family.

Ontologies

Keywords
   Cellular componentSecreted
   Coding sequence diversityPolymorphism
   DomainSignal
   Molecular functionHormone
Neuropeptide
   PTMCleavage on pair of basic residues
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcAMP-mediated signaling

Inferred from direct assay PubMed 17982695. Source: UniProt

feeding behavior

Inferred from electronic annotation. Source: Ensembl

inflammatory response

Inferred from electronic annotation. Source: Ensembl

insulin secretion

Non-traceable author statement Ref.2. Source: UniProtKB

negative regulation of lymphocyte proliferation

Inferred from electronic annotation. Source: Ensembl

negative regulation of root hair elongation

Inferred from direct assay PubMed 22329353. Source: UniProt

nervous system development

Inferred from electronic annotation. Source: Ensembl

neuropeptide signaling pathway

Inferred from electronic annotation. Source: UniProtKB-KW

positive regulation of apoptotic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of catagen

Inferred from direct assay PubMed 22329353. Source: UniProt

positive regulation of cortisol secretion

Inferred from direct assay PubMed 17982695. Source: UniProt

positive regulation of large conductance calcium-activated potassium channel activity

Inferred from direct assay PubMed 24602615. Source: UniProt

protein kinase A signaling

Inferred from direct assay PubMed 17982695. Source: UniProt

regulation of glucocorticoid metabolic process

Inferred from electronic annotation. Source: Ensembl

response to drug

Inferred from electronic annotation. Source: Ensembl

response to estrogen

Inferred from electronic annotation. Source: Ensembl

response to insulin

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentGolgi apparatus

Inferred from electronic annotation. Source: Ensembl

extracellular region

Traceable author statement. Source: Reactome

extracellular space

Inferred from direct assay PubMed 9402244. Source: UniProt

neuronal cell body

Inferred from direct assay PubMed 23415787. Source: UniProt

secretory granule

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionneuropeptide hormone activity

Non-traceable author statement Ref.5. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 23597562. Source: IntAct

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Potential
Propeptide20 – 3011
PRO_0000010448
Peptide33 – 6230Galanin Ref.4 Ref.5
PRO_0000010449
Peptide65 – 12359Galanin message-associated peptide
PRO_0000010450

Amino acid modifications

Modified residue1171Phosphoserine Ref.6 Ref.9

Natural variations

Natural variant161A → V.
Corresponds to variant rs34725707 [ dbSNP | Ensembl ].
VAR_049121

Sequences

Sequence LengthMass (Da)Tools
P22466 [UniParc].

Last modified November 1, 1997. Version 3.
Checksum: 48D2170AF1248E6D

FASTA12313,302
        10         20         30         40         50         60 
MARGSALLLA SLLLAAALSA SAGLWSPAKE KRGWTLNSAG YLLGPHAVGN HRSFSDKNGL 

        70         80         90        100        110        120 
TSKRELRPED DMKPGSFDRS IPENNIMRTI IEFLSFLHLK EAGALDRLLD LPAAASSEDI 


ERS 

« Hide

References

« Hide 'large scale' references
[1]"Genomic organization and localization of the gene encoding human preprogalanin."
Evans H., Baumgartner M., Shine J., Herzog H.
Genomics 18:473-477(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-45.
Tissue: Blood.
[2]"Sequence of human galanin and its inhibition of glucose-stimulated insulin secretion from RIN cells."
McKnight G.L., Karlsen A.E., Kowalyk S., Mathewes S.L., Sheppard P.O., O'Hara P.J., Taborsky G.L.
Diabetes 41:82-87(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 16-123.
[3]"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].
Tissue: Cervix.
[4]"Human galanin: primary structure and identification of two molecular forms."
Bersani M., Johnsen A.H., Hoejrup P., Dunning B.E., Andreasen J.J., Holst J.J.
FEBS Lett. 283:189-194(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 33-62.
[5]"Isolation and primary structure of pituitary human galanin, a 30-residue nonamidated neuropeptide."
Schmidt W.E., Kratzin H., Eckart K., Drevs D., Mundkowski G., Clemens A., Katsoulis S., Schaefer H., Gallwitz B., Creutzfeldt W.
Proc. Natl. Acad. Sci. U.S.A. 88:11435-11439(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 33-62, SYNTHESIS.
Tissue: Pituitary.
[6]"Identification and characterization of phosphorylated proteins in the human pituitary."
Giorgianni F., Beranova-Giorgianni S., Desiderio D.M.
Proteomics 4:587-598(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-117.
Tissue: Pituitary.
[7]"Phosphoproteomic analysis of the human pituitary."
Beranova-Giorgianni S., Zhao Y., Desiderio D.M., Giorgianni F.
Pituitary 9:109-120(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Pituitary.
[8]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-117, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L11144 Genomic DNA. Translation: AAA18248.1.
M77140 mRNA. Translation: AAA60178.1.
BC030241 mRNA. Translation: AAH30241.1.
CCDSCCDS8183.1.
PIRRHHUN. A49353.
RefSeqNP_057057.2. NM_015973.3.
UniGeneHs.278959.

3D structure databases

ProteinModelPortalP22466.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119273. 1 interaction.
IntActP22466. 3 interactions.
MINTMINT-7232142.
STRING9606.ENSP00000265643.

Chemistry

BindingDBP22466.

PTM databases

PhosphoSiteP22466.

Polymorphism databases

DMDM2506449.

Proteomic databases

MaxQBP22466.
PaxDbP22466.
PRIDEP22466.

Protocols and materials databases

DNASU51083.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000265643; ENSP00000265643; ENSG00000069482.
GeneID51083.
KEGGhsa:51083.
UCSCuc001oob.3. human.

Organism-specific databases

CTD51083.
GeneCardsGC11P068451.
HGNCHGNC:4114. GAL.
HPACAB000462.
HPA049864.
MIM137035. gene.
neXtProtNX_P22466.
PharmGKBPA28529.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG44932.
HOGENOMHOG000112690.
HOVERGENHBG005799.
InParanoidP22466.
KOK05244.
OMAGICESAA.
OrthoDBEOG79SF01.
PhylomeDBP22466.
TreeFamTF335850.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.

Gene expression databases

BgeeP22466.
CleanExHS_GAL.
GenevestigatorP22466.

Family and domain databases

InterProIPR008174. Galanin.
IPR008175. Galanin_pre.
IPR013068. GMAP.
[Graphical view]
PfamPF01296. Galanin. 1 hit.
PF06540. GMAP. 1 hit.
[Graphical view]
PRINTSPR00273. GALANIN.
ProDomPD005962. Galanin. 1 hit.
PD012185. GMAP. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00071. Galanin. 1 hit.
[Graphical view]
PROSITEPS00861. GALANIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSGAL. human.
GeneWikiGalanin.
GenomeRNAi51083.
NextBio53733.
PROP22466.
SOURCESearch...

Entry information

Entry nameGALA_HUMAN
AccessionPrimary (citable) accession number: P22466
Secondary accession number(s): Q14413
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: November 1, 1997
Last modified: July 9, 2014
This is version 135 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM