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P59768 (GBG2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 118. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2
Alternative name(s):
G gamma-I
Gene names
Name:GNG2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length71 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction By similarity.

Subunit structure

G proteins are composed of 3 units, alpha, beta and gamma By similarity. The heterodimer formed by GNB1 and GNG2 interacts with PTH1R (via C-terminus).

Subcellular location

Cell membrane; Lipid-anchor; Cytoplasmic side Potential.

Tissue specificity

Expressed in fetal tissues, including testis, adrenal gland, brain, white blood cells and brain. Ref.1

Sequence similarities

Belongs to the G protein gamma family.

Ontologies

Keywords
   Cellular componentCell membrane
Membrane
   Molecular functionTransducer
   PTMAcetylation
Lipoprotein
Methylation
Prenylation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processadenylate cyclase-activating dopamine receptor signaling pathway

Inferred from sequence or structural similarity. Source: BHF-UCL

blood coagulation

Traceable author statement. Source: Reactome

cell proliferation

Inferred from electronic annotation. Source: Ensembl

cellular response to catecholamine stimulus

Inferred from sequence or structural similarity. Source: BHF-UCL

cellular response to glucagon stimulus

Traceable author statement. Source: Reactome

cellular response to prostaglandin E stimulus

Inferred from sequence or structural similarity. Source: BHF-UCL

energy reserve metabolic process

Traceable author statement. Source: Reactome

platelet activation

Traceable author statement. Source: Reactome

small molecule metabolic process

Traceable author statement. Source: Reactome

synaptic transmission

Traceable author statement. Source: Reactome

   Cellular_componentextracellular vesicular exosome

Inferred from direct assay PubMed 20458337PubMed 23376485. Source: UniProt

heterotrimeric G-protein complex

Inferred from sequence or structural similarity. Source: BHF-UCL

membrane

Inferred from sequence or structural similarity. Source: BHF-UCL

plasma membrane

Traceable author statement. Source: Reactome

   Molecular_functionG-protein beta-subunit binding

Inferred from physical interaction PubMed 12606627. Source: UniProt

signal transducer activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.6
Chain2 – 6867Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2
PRO_0000012611
Propeptide69 – 713Removed in mature form By similarity
PRO_0000012612

Amino acid modifications

Modified residue21N-acetylalanine Ref.6 Ref.7
Modified residue681Cysteine methyl ester By similarity
Lipidation681S-geranylgeranyl cysteine By similarity

Secondary structure

............. 71
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P59768 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: EDB74E4135E7A37A

FASTA717,850
        10         20         30         40         50         60 
MASNNTASIA QARKLVEQLK MEANIDRIKV SKAAADLMAY CEAHAKEDPL LTPVPASENP 

        70 
FREKKFFCAI L 

« Hide

References

« Hide 'large scale' references
[1]"Cloning, characterization, and mapping of the gene encoding the human G protein gamma 2 subunit."
Modarressi M.H., Taylor K.E., Wolfe J.
Biochem. Biophys. Res. Commun. 272:610-615(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
[2]"cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org)."
Puhl H.L. III, Ikeda S.R., Aronstam R.S.
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Lymph node.
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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].
Tissue: Brain and Skin.
[6]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[7]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]"Structure of the parathyroid hormone receptor C terminus bound to the G-protein dimer Gbeta1gamma2."
Johnston C.A., Kimple A.J., Giguere P.M., Siderovski D.P.
Structure 16:1086-1094(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEXES WITH GNB1 AND PTH1R.
[9]Erratum
Johnston C.A., Kimple A.J., Giguere P.M., Siderovski D.P.
Structure 19:1200-1200(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: RETRACTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF493870 mRNA. Translation: AAM12584.1.
AL832878 mRNA. Translation: CAI46198.1.
CH471078 Genomic DNA. Translation: EAW65663.1.
BC020774 mRNA. Translation: AAH20774.1.
BC060856 mRNA. Translation: AAH60856.1.
CCDSCCDS32082.1.
PIRGNG2. JC7290.
RefSeqNP_001230702.1. NM_001243773.1.
NP_001230703.1. NM_001243774.1.
NP_444292.1. NM_053064.4.
XP_006720236.1. XM_006720173.1.
UniGeneHs.187772.
Hs.709082.
Hs.723399.
Hs.741081.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4KFMX-ray3.45G1-68[»]
ProteinModelPortalP59768.
SMRP59768. Positions 8-64.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119933. 18 interactions.
DIPDIP-33949N.
IntActP59768. 2 interactions.
MINTMINT-8189453.
STRING9606.ENSP00000334448.

Chemistry

DrugBankDB01159. Halothane.

PTM databases

PhosphoSiteP59768.

Polymorphism databases

DMDM32699499.

Proteomic databases

MaxQBP59768.
PaxDbP59768.
PeptideAtlasP59768.
PRIDEP59768.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000335281; ENSP00000334448; ENSG00000186469.
ENST00000554736; ENSP00000452014; ENSG00000186469.
ENST00000555472; ENSP00000451102; ENSG00000186469.
ENST00000556752; ENSP00000451576; ENSG00000186469.
ENST00000556766; ENSP00000451231; ENSG00000186469.
GeneID54331.
KEGGhsa:54331.
UCSCuc001wzi.3. human.

Organism-specific databases

CTD54331.
GeneCardsGC14P052327.
HGNCHGNC:4404. GNG2.
HPACAB018380.
HPA003534.
MIM606981. gene.
neXtProtNX_P59768.
PharmGKBPA28784.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG298292.
HOVERGENHBG014983.
InParanoidP59768.
KOK07826.
PhylomeDBP59768.
TreeFamTF319909.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_111217. Metabolism.
REACT_13685. Neuronal System.
REACT_15518. Transmembrane transport of small molecules.
REACT_604. Hemostasis.
SignaLinkP59768.

Gene expression databases

ArrayExpressP59768.
BgeeP59768.
CleanExHS_GNG2.
GenevestigatorP59768.

Family and domain databases

Gene3D4.10.260.10. 1 hit.
InterProIPR015898. G-protein_gamma-like_dom.
IPR001770. Gprotein-gamma.
[Graphical view]
PANTHERPTHR13809. PTHR13809. 1 hit.
PfamPF00631. G-gamma. 1 hit.
[Graphical view]
PRINTSPR00321. GPROTEING.
SMARTSM00224. GGL. 1 hit.
[Graphical view]
SUPFAMSSF48670. SSF48670. 1 hit.
PROSITEPS50058. G_PROTEIN_GAMMA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP59768.
GeneWikiGNG2.
GenomeRNAi54331.
NextBio56571.
PROP59768.
SOURCESearch...

Entry information

Entry nameGBG2_HUMAN
AccessionPrimary (citable) accession number: P59768
Secondary accession number(s): Q5JPE2, Q6P9A9
Entry history
Integrated into UniProtKB/Swiss-Prot: July 11, 2003
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 118 of the entry and version 2 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM