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

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P63212 (GBG2_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 82. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

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

Alternative name(s):
G gamma-I

Gene names

Name:

GNG2

Organism

Bos taurus (Bovine) [Reference proteome]

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	71 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Cellular component	Cell membrane Membrane
Molecular function	Transducer
PTM	Acetylation Lipoprotein Methylation Phosphoprotein Prenylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	adenylate cyclase-activating dopamine receptor signaling pathway Inferred from direct assay PubMed 18403039. Source: BHF-UCL cell proliferation Inferred from electronic annotation. Source: Compara cellular response to catecholamine stimulus Inferred from direct assay PubMed 18403039. Source: BHF-UCL cellular response to prostaglandin E stimulus Inferred from direct assay PubMed 18403039. Source: BHF-UCL
Cellular_component	heterotrimeric G-protein complex Inferred from direct assay PubMed 18403039. Source: BHF-UCL
Molecular_function	GTPase activity Inferred from direct assay PubMed 2122451. Source: MGI signal transducer activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.4 Ref.5

Chain

2 – 68

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

PRO_0000012609

Propeptide

69 – 71

Removed in mature form

PRO_0000012610

Amino acid modifications

Modified residue

N-acetylalanine Ref.4

Modified residue

Phosphothreonine By similarity

Modified residue

Cysteine methyl ester

Lipidation

S-geranylgeranyl cysteine Ref.4 Ref.6

Secondary structure

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P63212 [UniParc].

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

7,850

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

        70 
FREKKFFCAI L

« Hide

References

	« Hide 'large scale' referencesShow '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.

IPI

IPI00706808.

PIR

RGBOG2. B34228.

RefSeq

NP_776497.1. NM_174072.4.

UniGene

Bt.4586.
Bt.90717.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1GG2	X-ray	2.40	G	1-71	[»]
1GP2	X-ray	2.30	G	1-71	[»]
1OMW	X-ray	2.50	G	1-68	[»]
1XHM	X-ray	2.70	B	1-71	[»]
2BCJ	X-ray	3.06	G	1-71	[»]
3AH8	X-ray	2.90	G	1-71	[»]
3CIK	X-ray	2.75	G	1-68	[»]
3KRW	X-ray	2.90	G	1-68	[»]
3KRX	X-ray	3.10	G	1-68	[»]
3PSC	X-ray	2.67	G	1-68	[»]
3PVU	X-ray	2.48	G	1-68	[»]
3PVW	X-ray	2.49	G	1-68	[»]
3SN6	X-ray	3.20	G	1-68	[»]
3UZS	X-ray	4.52	G	1-68	[»]
3V5W	X-ray	2.07	G	1-71	[»]

ProteinModelPortal

P63212.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-586N.

IntAct

P63212. 1 interaction.

Proteomic databases

PRIDE

P63212.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSBTAT00000003959; ENSBTAP00000003959; ENSBTAG00000003043.

GeneID

281203.

KEGG

bta:281203.

Organism-specific databases

CTD

54331.

Phylogenomic databases

eggNOG

NOG298292.

GeneTree

ENSGT00550000074352.

HOVERGEN

HBG014983.

InParanoid

P63212.

K07826.

OMA

SYCEAHA.

OrthoDB

EOG47WNQC.

Family and domain databases

Gene3D

4.10.260.10. 1 hit.

InterPro

IPR015898. G-protein_gamma-like_dom.
IPR001770. Gprotein-gamma.
[Graphical view]

PANTHER

PTHR13809. PTHR13809. 1 hit.

Pfam

PF00631. G-gamma. 1 hit.
[Graphical view]

PRINTS

PR00321. GPROTEING.

SMART

SM00224. GGL. 1 hit.
[Graphical view]

SUPFAM

SSF48670. G-protein_gamma-like. 1 hit.

PROSITE

PS50058. G_PROTEIN_GAMMA. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P63212.

NextBio

20805259.

Entry information

Entry name

GBG2_BOVIN

Accession

Primary (citable) accession number: P63212
Secondary accession number(s): P16874

Q9TS47

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 27, 2004
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 82 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Amino acid modifications

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Other

Entry information

Relevant documents