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Protein

Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2

Gene

GNG2

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.

GO - Molecular functioni

  • G-protein beta-subunit binding Source: UniProtKB
  • GTPase activity Source: MGI
  • signal transducer activity Source: UniProtKB-KW

GO - Biological processi

  • adenylate cyclase-activating dopamine receptor signaling pathway Source: BHF-UCL
  • cell proliferation Source: Ensembl
  • cellular response to catecholamine stimulus Source: BHF-UCL
  • cellular response to prostaglandin E stimulus Source: BHF-UCL
  • G-protein coupled receptor signaling pathway Source: MGI
  • metabolic process Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Transducer

Enzyme and pathway databases

ReactomeiREACT_271820. Thrombin signalling through proteinase activated receptors (PARs).
REACT_273525. ADP signalling through P2Y purinoceptor 1.
REACT_275792. Activation of G protein gated Potassium channels.
REACT_277683. G beta:gamma signalling through PLC beta.
REACT_287476. G alpha (q) signalling events.
REACT_288300. ADP signalling through P2Y purinoceptor 12.
REACT_292261. Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits.
REACT_301171. G beta:gamma signalling through PI3Kgamma.
REACT_308557. Adrenaline,noradrenaline inhibits insulin secretion.
REACT_310840. G alpha (z) signalling events.
REACT_320823. Prostacyclin signalling through prostacyclin receptor.
REACT_324896. G alpha (12/13) signalling events.
REACT_330097. G alpha (s) signalling events.
REACT_335730. Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
REACT_337905. Vasopressin regulates renal water homeostasis via Aquaporins.
REACT_338486. G alpha (i) signalling events.
REACT_338991. Presynaptic function of Kainate receptors.
REACT_340577. Glucagon signaling in metabolic regulation.
REACT_342659. Ca2+ pathway.
REACT_344180. G-protein activation.
REACT_347133. Thromboxane signalling through TP receptor.
REACT_347702. Glucagon-type ligand receptors.

Names & Taxonomyi

Protein namesi
Recommended name:
Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2
Alternative name(s):
G gamma-I
Gene namesi
Name:GNG2
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136 Componenti: Chromosome 10

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: Ensembl
  • heterotrimeric G-protein complex Source: BHF-UCL
  • membrane Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 6867Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2PRO_0000012609Add
BLAST
Propeptidei69 – 713Removed in mature formPRO_0000012610

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei68 – 681Cysteine methyl ester1 Publication
Lipidationi68 – 681S-geranylgeranyl cysteine3 Publications

Keywords - PTMi

Acetylation, Lipoprotein, Methylation, Prenylation

Proteomic databases

PRIDEiP63212.

Expressioni

Tissue specificityi

Adrenal gland and brain.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

DIPiDIP-586N.
IntActiP63212. 1 interaction.
STRINGi9913.ENSBTAP00000003959.

Structurei

Secondary structure

1
71
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi9 – 2315Combined sources
Helixi30 – 4314Combined sources
Helixi45 – 473Combined sources
Turni49 – 513Combined sources
Helixi56 – 583Combined sources
Turni60 – 634Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GG2X-ray2.40G1-71[»]
1GP2X-ray2.30G1-71[»]
1OMWX-ray2.50G1-68[»]
1XHMX-ray2.70B1-71[»]
2BCJX-ray3.06G1-71[»]
3AH8X-ray2.90G1-71[»]
3CIKX-ray2.75G1-68[»]
3KRWX-ray2.90G1-68[»]
3KRXX-ray3.10G1-68[»]
3PSCX-ray2.67G1-68[»]
3PVUX-ray2.48G1-68[»]
3PVWX-ray2.49G1-68[»]
3SN6X-ray3.20G1-68[»]
3UZSX-ray4.52G1-67[»]
3V5WX-ray2.07G1-71[»]
4MK0X-ray2.40G6-64[»]
4PNKX-ray2.56G1-71[»]
ProteinModelPortaliP63212.
SMRiP63212. Positions 8-64.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP63212.

Family & Domainsi

Sequence similaritiesi

Belongs to the G protein gamma family.Curated

Phylogenomic databases

eggNOGiNOG298292.
GeneTreeiENSGT00760000119218.
HOVERGENiHBG014983.
InParanoidiP63212.
KOiK07826.
OMAiAPMASNN.
OrthoDBiEOG7H1JP7.
TreeFamiTF319909.

Family and domain databases

Gene3Di4.10.260.10. 1 hit.
InterProiIPR015898. G-protein_gamma-like_dom.
IPR001770. Gprotein-gamma.
[Graphical view]
PANTHERiPTHR13809. PTHR13809. 1 hit.
PfamiPF00631. G-gamma. 1 hit.
[Graphical view]
PRINTSiPR00321. GPROTEING.
SMARTiSM00224. GGL. 1 hit.
[Graphical view]
SUPFAMiSSF48670. SSF48670. 1 hit.
PROSITEiPS50058. G_PROTEIN_GAMMA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P63212-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASNNTASIA QARKLVEQLK MEANIDRIKV SKAAADLMAY CEAHAKEDPL
60 70
LTPVPASENP FREKKFFCAI L
Length:71
Mass (Da):7,850
Last modified:January 23, 2007 - v2
Checksum:iEDB74E4135E7A37A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J05071 mRNA. Translation: AAA30541.1.
M37183 mRNA. Translation: AAA30555.1.
BC112789 mRNA. Translation: AAI12790.1.
PIRiB34228. RGBOG2.
RefSeqiNP_776497.1. NM_174072.4.
XP_005211711.1. XM_005211654.2.
XP_010807541.1. XM_010809239.1.
UniGeneiBt.4586.
Bt.90717.

Genome annotation databases

EnsembliENSBTAT00000003959; ENSBTAP00000003959; ENSBTAG00000003043.
GeneIDi281203.
KEGGibta:281203.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J05071 mRNA. Translation: AAA30541.1.
M37183 mRNA. Translation: AAA30555.1.
BC112789 mRNA. Translation: AAI12790.1.
PIRiB34228. RGBOG2.
RefSeqiNP_776497.1. NM_174072.4.
XP_005211711.1. XM_005211654.2.
XP_010807541.1. XM_010809239.1.
UniGeneiBt.4586.
Bt.90717.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GG2X-ray2.40G1-71[»]
1GP2X-ray2.30G1-71[»]
1OMWX-ray2.50G1-68[»]
1XHMX-ray2.70B1-71[»]
2BCJX-ray3.06G1-71[»]
3AH8X-ray2.90G1-71[»]
3CIKX-ray2.75G1-68[»]
3KRWX-ray2.90G1-68[»]
3KRXX-ray3.10G1-68[»]
3PSCX-ray2.67G1-68[»]
3PVUX-ray2.48G1-68[»]
3PVWX-ray2.49G1-68[»]
3SN6X-ray3.20G1-68[»]
3UZSX-ray4.52G1-67[»]
3V5WX-ray2.07G1-71[»]
4MK0X-ray2.40G6-64[»]
4PNKX-ray2.56G1-71[»]
ProteinModelPortaliP63212.
SMRiP63212. Positions 8-64.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-586N.
IntActiP63212. 1 interaction.
STRINGi9913.ENSBTAP00000003959.

Proteomic databases

PRIDEiP63212.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000003959; ENSBTAP00000003959; ENSBTAG00000003043.
GeneIDi281203.
KEGGibta:281203.

Organism-specific databases

CTDi54331.

Phylogenomic databases

eggNOGiNOG298292.
GeneTreeiENSGT00760000119218.
HOVERGENiHBG014983.
InParanoidiP63212.
KOiK07826.
OMAiAPMASNN.
OrthoDBiEOG7H1JP7.
TreeFamiTF319909.

Enzyme and pathway databases

ReactomeiREACT_271820. Thrombin signalling through proteinase activated receptors (PARs).
REACT_273525. ADP signalling through P2Y purinoceptor 1.
REACT_275792. Activation of G protein gated Potassium channels.
REACT_277683. G beta:gamma signalling through PLC beta.
REACT_287476. G alpha (q) signalling events.
REACT_288300. ADP signalling through P2Y purinoceptor 12.
REACT_292261. Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits.
REACT_301171. G beta:gamma signalling through PI3Kgamma.
REACT_308557. Adrenaline,noradrenaline inhibits insulin secretion.
REACT_310840. G alpha (z) signalling events.
REACT_320823. Prostacyclin signalling through prostacyclin receptor.
REACT_324896. G alpha (12/13) signalling events.
REACT_330097. G alpha (s) signalling events.
REACT_335730. Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
REACT_337905. Vasopressin regulates renal water homeostasis via Aquaporins.
REACT_338486. G alpha (i) signalling events.
REACT_338991. Presynaptic function of Kainate receptors.
REACT_340577. Glucagon signaling in metabolic regulation.
REACT_342659. Ca2+ pathway.
REACT_344180. G-protein activation.
REACT_347133. Thromboxane signalling through TP receptor.
REACT_347702. Glucagon-type ligand receptors.

Miscellaneous databases

EvolutionaryTraceiP63212.
NextBioi20805259.

Family and domain databases

Gene3Di4.10.260.10. 1 hit.
InterProiIPR015898. G-protein_gamma-like_dom.
IPR001770. Gprotein-gamma.
[Graphical view]
PANTHERiPTHR13809. PTHR13809. 1 hit.
PfamiPF00631. G-gamma. 1 hit.
[Graphical view]
PRINTSiPR00321. GPROTEING.
SMARTiSM00224. GGL. 1 hit.
[Graphical view]
SUPFAMiSSF48670. SSF48670. 1 hit.
PROSITEiPS50058. G_PROTEIN_GAMMA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Existence of two gamma subunits of the G proteins in brain."
    Robishaw J.D., Kalman V.K., Moomaw C.R., Slaughter C.A.
    J. Biol. Chem. 264:15758-15761(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 14-62.
    Tissue: Adrenal gland and Brain.
  2. "A G protein gamma subunit shares homology with ras proteins."
    Gautam N., Baetscher M., Aebersold R., Simon M.I.
    Science 244:971-974(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. NIH - Mammalian Gene Collection (MGC) project
    Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Hereford.
    Tissue: Kidney.
  4. "Determination of the complete covalent structure of the gamma 2 subunit of bovine brain G proteins by mass spectrometry."
    Wilcox M.D., Schey K.L., Busman M., Hildebrandt J.D.
    Biochem. Biophys. Res. Commun. 212:367-374(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-71, ACETYLATION AT ALA-2, ISOPRENYLATION AT CYS-68.
    Tissue: Brain.
  5. "Identification of a novel gamma-subunit from bovine brain GTP binding regulatory proteins (Gi/o)."
    Sohma H., Hashimoto H., Hiraike N., Ohguro H., Akino T.
    Biochem. Biophys. Res. Commun. 190:849-856(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-64.
    Tissue: Brain.
  6. "Gamma-subunits of G proteins, but not their alpha- or beta-subunits, are polyisoprenylated. Studies on post-translational modifications using in vitro translation with rabbit reticulocyte lysates."
    Sanford J., Codina J., Birnbaumer L.
    J. Biol. Chem. 266:9570-9579(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: ISOPRENYLATION AT CYS-68, METHYLATION AT CYS-68.
  7. "The structure of the G protein heterotrimer Gi alpha 1 beta 1 gamma 2."
    Wall M.A., Coleman D.E., Lee E., Iniguez-Lluhi J.A., Posner B.A., Gilman A.G., Sprang S.R.
    Cell 83:1047-1058(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF HETEROTRIMER.
  8. "Keeping G proteins at bay: a complex between G protein-coupled receptor kinase 2 and Gbetagamma."
    Lodowski D.T., Pitcher J.A., Capel W.D., Lefkowitz R.J., Tesmer J.J.
    Science 300:1256-1262(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-68 IN COMPLEX WITH GNB1 AND ADRBK1, SUBCELLULAR LOCATION, ISOPRENYLATION AT CYS-68.

Entry informationi

Entry nameiGBG2_BOVIN
AccessioniPrimary (citable) accession number: P63212
Secondary accession number(s): P16874
, Q2KI31, Q61013, Q9TS47
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 27, 2004
Last sequence update: January 23, 2007
Last modified: June 24, 2015
This is version 103 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.