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P63212 (GBG2_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

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.

Subunit structure

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.

Subcellular location

Cell membrane; Lipid-anchor; Cytoplasmic side Potential.

Tissue specificity

Adrenal gland and brain.

Sequence similarities

Belongs to the G protein gamma family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.4 Ref.5
Chain2 – 6867Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2
PRO_0000012609
Propeptide69 – 713Removed in mature form
PRO_0000012610

Amino acid modifications

Modified residue21N-acetylalanine Ref.4
Modified residue681Cysteine methyl ester
Lipidation681S-geranylgeranyl cysteine Ref.4 Ref.6

Secondary structure

............. 71
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P63212 [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]"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.
[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J05071 mRNA. Translation: AAA30541.1.
M37183 mRNA. Translation: AAA30555.1.
BC112789 mRNA. Translation: AAI12790.1.
PIRRGBOG2. B34228.
RefSeqNP_776497.1. NM_174072.4.
XP_005211711.1. XM_005211654.1.
UniGeneBt.4586.
Bt.90717.

3D structure databases

PDBe
RCSB PDB
PDBj
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-ray4.52G1-68[»]
3V5WX-ray2.07G1-71[»]
4MK0X-ray2.40G6-64[»]
ProteinModelPortalP63212.
SMRP63212. Positions 8-64.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-586N.
IntActP63212. 1 interaction.

Proteomic databases

PRIDEP63212.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000003959; ENSBTAP00000003959; ENSBTAG00000003043.
GeneID281203.
KEGGbta:281203.

Organism-specific databases

CTD54331.

Phylogenomic databases

eggNOGNOG298292.
GeneTreeENSGT00740000115378.
HOVERGENHBG014983.
InParanoidP63212.
KOK07826.
OMASYCEAHA.
OrthoDBEOG7H1JP7.
TreeFamTF319909.

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

EvolutionaryTraceP63212.
NextBio20805259.

Entry information

Entry nameGBG2_BOVIN
AccessionPrimary (citable) accession number: P63212
Secondary accession number(s): P16874 expand/collapse secondary AC list , Q2KI31, Q61013, Q9TS47
Entry history
Integrated into UniProtKB/Swiss-Prot: September 27, 2004
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 91 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references