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Protein

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

Gene

Gng2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript 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

GO - Biological processi

  • cell proliferation Source: MGI
  • G-protein coupled receptor signaling pathway Source: MGI
  • metabolic process Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Transducer

Enzyme and pathway databases

ReactomeiREACT_272374. Adrenaline,noradrenaline inhibits insulin secretion.
REACT_275222. Thrombin signalling through proteinase activated receptors (PARs).
REACT_286837. Vasopressin regulates renal water homeostasis via Aquaporins.
REACT_291272. G beta:gamma signalling through PI3Kgamma.
REACT_293887. Prostacyclin signalling through prostacyclin receptor.
REACT_296380. G alpha (z) signalling events.
REACT_297430. Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
REACT_299052. G alpha (12/13) signalling events.
REACT_303206. G-protein activation.
REACT_308732. Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits.
REACT_313192. G alpha (s) signalling events.
REACT_326624. Presynaptic function of Kainate receptors.
REACT_330925. ADP signalling through P2Y purinoceptor 12.
REACT_331048. G alpha (i) signalling events.
REACT_331940. Ca2+ pathway.
REACT_334244. ADP signalling through P2Y purinoceptor 1.
REACT_336725. Thromboxane signalling through TP receptor.
REACT_339334. Activation of G protein gated Potassium channels.
REACT_339920. Glucagon-type ligand receptors.
REACT_345203. Glucagon signaling in metabolic regulation.
REACT_347934. G alpha (q) signalling events.
REACT_351801. G beta:gamma signalling through PLC beta.

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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 14

Organism-specific databases

MGIiMGI:102705. Gng2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 6867Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2PRO_0000012613Add
BLAST
Propeptidei69 – 713Removed in mature formPRO_0000012614

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei68 – 681Cysteine methyl esterBy similarity
Lipidationi68 – 681S-geranylgeranyl cysteineBy similarity

Keywords - PTMi

Acetylation, Lipoprotein, Methylation, Prenylation

Proteomic databases

MaxQBiP63213.
PaxDbiP63213.
PRIDEiP63213.

PTM databases

PhosphoSiteiP63213.

Expressioni

Tissue specificityi

Adrenal gland and brain.

Gene expression databases

BgeeiP63213.
GenevestigatoriP63213.

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

BioGridi199986. 5 interactions.
IntActiP63213. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliP63213.
SMRiP63213. Positions 8-64.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the G protein gamma family.Curated

Phylogenomic databases

eggNOGiNOG298292.
GeneTreeiENSGT00760000119218.
HOVERGENiHBG014983.
InParanoidiP63213.
KOiK07826.
OMAiAPMASNN.
OrthoDBiEOG7H1JP7.
PhylomeDBiP63213.
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.

P63213-1 [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
AF098489, AF098488 Genomic DNA. Translation: AAD16272.1.
AK003588 mRNA. Translation: BAB22878.1.
AK012405 mRNA. Translation: BAB28219.1.
AK036138 mRNA. Translation: BAC29316.1.
AK075698 mRNA. Translation: BAC35896.1.
AK158697 mRNA. Translation: BAE34615.1.
AK160396 mRNA. Translation: BAE35765.1.
BC021599 mRNA. Translation: AAH21599.1.
U38496 mRNA. Translation: AAB01727.1.
CCDSiCCDS26840.1.
PIRiD36204.
RefSeqiNP_001033726.1. NM_001038637.1.
NP_001272837.1. NM_001285908.1.
NP_001272838.1. NM_001285909.1.
NP_001272839.1. NM_001285910.1.
NP_001272840.1. NM_001285911.1.
NP_034445.1. NM_010315.4.
UniGeneiMm.41737.

Genome annotation databases

EnsembliENSMUST00000055100; ENSMUSP00000055256; ENSMUSG00000043004.
ENSMUST00000159028; ENSMUSP00000125141; ENSMUSG00000043004.
ENSMUST00000159073; ENSMUSP00000125000; ENSMUSG00000043004.
ENSMUST00000160013; ENSMUSP00000125697; ENSMUSG00000043004.
ENSMUST00000161247; ENSMUSP00000124725; ENSMUSG00000043004.
ENSMUST00000162425; ENSMUSP00000124153; ENSMUSG00000043004.
GeneIDi14702.
KEGGimmu:14702.
UCSCiuc007siw.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF098489, AF098488 Genomic DNA. Translation: AAD16272.1.
AK003588 mRNA. Translation: BAB22878.1.
AK012405 mRNA. Translation: BAB28219.1.
AK036138 mRNA. Translation: BAC29316.1.
AK075698 mRNA. Translation: BAC35896.1.
AK158697 mRNA. Translation: BAE34615.1.
AK160396 mRNA. Translation: BAE35765.1.
BC021599 mRNA. Translation: AAH21599.1.
U38496 mRNA. Translation: AAB01727.1.
CCDSiCCDS26840.1.
PIRiD36204.
RefSeqiNP_001033726.1. NM_001038637.1.
NP_001272837.1. NM_001285908.1.
NP_001272838.1. NM_001285909.1.
NP_001272839.1. NM_001285910.1.
NP_001272840.1. NM_001285911.1.
NP_034445.1. NM_010315.4.
UniGeneiMm.41737.

3D structure databases

ProteinModelPortaliP63213.
SMRiP63213. Positions 8-64.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi199986. 5 interactions.
IntActiP63213. 1 interaction.

PTM databases

PhosphoSiteiP63213.

Proteomic databases

MaxQBiP63213.
PaxDbiP63213.
PRIDEiP63213.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000055100; ENSMUSP00000055256; ENSMUSG00000043004.
ENSMUST00000159028; ENSMUSP00000125141; ENSMUSG00000043004.
ENSMUST00000159073; ENSMUSP00000125000; ENSMUSG00000043004.
ENSMUST00000160013; ENSMUSP00000125697; ENSMUSG00000043004.
ENSMUST00000161247; ENSMUSP00000124725; ENSMUSG00000043004.
ENSMUST00000162425; ENSMUSP00000124153; ENSMUSG00000043004.
GeneIDi14702.
KEGGimmu:14702.
UCSCiuc007siw.1. mouse.

Organism-specific databases

CTDi54331.
MGIiMGI:102705. Gng2.

Phylogenomic databases

eggNOGiNOG298292.
GeneTreeiENSGT00760000119218.
HOVERGENiHBG014983.
InParanoidiP63213.
KOiK07826.
OMAiAPMASNN.
OrthoDBiEOG7H1JP7.
PhylomeDBiP63213.
TreeFamiTF319909.

Enzyme and pathway databases

ReactomeiREACT_272374. Adrenaline,noradrenaline inhibits insulin secretion.
REACT_275222. Thrombin signalling through proteinase activated receptors (PARs).
REACT_286837. Vasopressin regulates renal water homeostasis via Aquaporins.
REACT_291272. G beta:gamma signalling through PI3Kgamma.
REACT_293887. Prostacyclin signalling through prostacyclin receptor.
REACT_296380. G alpha (z) signalling events.
REACT_297430. Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
REACT_299052. G alpha (12/13) signalling events.
REACT_303206. G-protein activation.
REACT_308732. Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits.
REACT_313192. G alpha (s) signalling events.
REACT_326624. Presynaptic function of Kainate receptors.
REACT_330925. ADP signalling through P2Y purinoceptor 12.
REACT_331048. G alpha (i) signalling events.
REACT_331940. Ca2+ pathway.
REACT_334244. ADP signalling through P2Y purinoceptor 1.
REACT_336725. Thromboxane signalling through TP receptor.
REACT_339334. Activation of G protein gated Potassium channels.
REACT_339920. Glucagon-type ligand receptors.
REACT_345203. Glucagon signaling in metabolic regulation.
REACT_347934. G alpha (q) signalling events.
REACT_351801. G beta:gamma signalling through PLC beta.

Miscellaneous databases

NextBioi286671.
PROiP63213.
SOURCEiSearch...

Gene expression databases

BgeeiP63213.
GenevestigatoriP63213.

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. "Chromosomal mapping of five mouse G protein gamma subunits."
    Downes G.B., Gilbert D.J., Copeland N.G., Gautam N., Jenkins N.A.
    Genomics 57:173-176(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Cerebellum and Embryo.
  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: Mammary tumor.
  4. "G protein gene expression during mouse oocyte growth and maturation, and preimplantation embryo development."
    Williams C.J., Schultz R.M., Kopf G.S.
    Mol. Reprod. Dev. 44:315-323(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 18-52.
    Strain: CF-1 / Harlan.
    Tissue: Embryo.

Entry informationi

Entry nameiGBG2_MOUSE
AccessioniPrimary (citable) accession number: P63213
Secondary accession number(s): P16874
, Q3TYE8, Q61013, Q9TS47
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 27, 2004
Last sequence update: January 23, 2007
Last modified: May 27, 2015
This is version 98 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

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  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.