RBCC

Full text data of GNG2

GNG2 [Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2 (G gamma-I; Flags: Precursor)

UniProt P59768
ID GBG2_HUMAN Reviewed; 71 AA.
AC P59768; Q5JPE2; Q6P9A9;
DT 11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 2.
DT 22-JAN-2014, entry version 113.
DE RecName: Full=Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2;
DE AltName: Full=G gamma-I;
DE Flags: Precursor;
GN Name=GNG2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=10833460; DOI=10.1006/bbrc.2000.2832;
RA Modarressi M.H., Taylor K.E., Wolfe J.;
RT "Cloning, characterization, and mapping of the gene encoding the human
RT G protein gamma 2 subunit.";
RL Biochem. Biophys. Res. Commun. 272:610-615(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
RT "cDNA clones of human proteins involved in signal transduction
RT sequenced by the Guthrie cDNA resource center (www.cdna.org).";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lymph node;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEXES WITH GNB1 AND
RP PTH1R.
RX PubMed=18611381; DOI=10.1016/j.str.2008.04.010;
RA Johnston C.A., Kimple A.J., Giguere P.M., Siderovski D.P.;
RT "Structure of the parathyroid hormone receptor C terminus bound to the
RT G-protein dimer Gbeta1gamma2.";
RL Structure 16:1086-1094(2008).
RN [9]
RP ERRATUM, AND RETRACTION.
RX PubMed=21827955; DOI=10.1016/j.str.2011.07.010;
RA Johnston C.A., Kimple A.J., Giguere P.M., Siderovski D.P.;
RL Structure 19:1200-1200(2011).
CC -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are
CC involved as a modulator or transducer in various transmembrane
CC signaling systems. The beta and gamma chains are required for the
CC GTPase activity, for replacement of GDP by GTP, and for G protein-
CC effector interaction (By similarity).
CC -!- SUBUNIT: G proteins are composed of 3 units, alpha, beta and gamma
CC (By similarity). The heterodimer formed by GNB1 and GNG2 interacts
CC with PTH1R (via C-terminus).
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic
CC side (Potential).
CC -!- TISSUE SPECIFICITY: Expressed in fetal tissues, including testis,
CC adrenal gland, brain, white blood cells and brain.
CC -!- SIMILARITY: Belongs to the G protein gamma family.
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DR EMBL; AF493870; AAM12584.1; -; mRNA.
DR EMBL; AL832878; CAI46198.1; -; mRNA.
DR EMBL; CH471078; EAW65663.1; -; Genomic_DNA.
DR EMBL; BC020774; AAH20774.1; -; mRNA.
DR EMBL; BC060856; AAH60856.1; -; mRNA.
DR PIR; JC7290; GNG2.
DR RefSeq; NP_001230702.1; NM_001243773.1.
DR RefSeq; NP_001230703.1; NM_001243774.1.
DR RefSeq; NP_444292.1; NM_053064.4.
DR UniGene; Hs.187772; -.
DR UniGene; Hs.709082; -.
DR UniGene; Hs.723399; -.
DR UniGene; Hs.741081; -.
DR PDB; 4KFM; X-ray; 3.45 A; G=1-68.
DR PDBsum; 4KFM; -.
DR ProteinModelPortal; P59768; -.
DR SMR; P59768; 8-64.
DR DIP; DIP-33949N; -.
DR IntAct; P59768; 2.
DR MINT; MINT-8189453; -.
DR STRING; 9606.ENSP00000334448; -.
DR DrugBank; DB01159; Halothane.
DR PhosphoSite; P59768; -.
DR DMDM; 32699499; -.
DR PaxDb; P59768; -.
DR PeptideAtlas; P59768; -.
DR PRIDE; P59768; -.
DR Ensembl; ENST00000335281; ENSP00000334448; ENSG00000186469.
DR Ensembl; ENST00000554736; ENSP00000452014; ENSG00000186469.
DR Ensembl; ENST00000555472; ENSP00000451102; ENSG00000186469.
DR Ensembl; ENST00000556752; ENSP00000451576; ENSG00000186469.
DR Ensembl; ENST00000556766; ENSP00000451231; ENSG00000186469.
DR GeneID; 54331; -.
DR KEGG; hsa:54331; -.
DR UCSC; uc001wzi.3; human.
DR CTD; 54331; -.
DR GeneCards; GC14P052327; -.
DR HGNC; HGNC:4404; GNG2.
DR HPA; CAB018380; -.
DR HPA; HPA003534; -.
DR MIM; 606981; gene.
DR neXtProt; NX_P59768; -.
DR PharmGKB; PA28784; -.
DR eggNOG; NOG298292; -.
DR HOVERGEN; HBG014983; -.
DR InParanoid; P59768; -.
DR KO; K07826; -.
DR PhylomeDB; P59768; -.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_111217; Metabolism.
DR Reactome; REACT_13685; Neuronal System.
DR Reactome; REACT_15518; Transmembrane transport of small molecules.
DR Reactome; REACT_604; Hemostasis.
DR SignaLink; P59768; -.
DR EvolutionaryTrace; P59768; -.
DR GeneWiki; GNG2; -.
DR GenomeRNAi; 54331; -.
DR NextBio; 56571; -.
DR PRO; PR:P59768; -.
DR ArrayExpress; P59768; -.
DR Bgee; P59768; -.
DR CleanEx; HS_GNG2; -.
DR Genevestigator; P59768; -.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; ISS:BHF-UCL.
DR GO; GO:0004871; F:signal transducer activity; IEA:UniProtKB-KW.
DR GO; GO:0007191; P:adenylate cyclase-activating dopamine receptor signaling pathway; ISS:BHF-UCL.
DR GO; GO:0008283; P:cell proliferation; IEA:Ensembl.
DR GO; GO:0071870; P:cellular response to catecholamine stimulus; ISS:BHF-UCL.
DR GO; GO:0071377; P:cellular response to glucagon stimulus; TAS:Reactome.
DR GO; GO:0071380; P:cellular response to prostaglandin E stimulus; ISS:BHF-UCL.
DR GO; GO:0006112; P:energy reserve metabolic process; TAS:Reactome.
DR GO; GO:0030168; P:platelet activation; TAS:Reactome.
DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome.
DR GO; GO:0007268; P:synaptic transmission; TAS:Reactome.
DR Gene3D; 4.10.260.10; -; 1.
DR InterPro; IPR015898; G-protein_gamma-like_dom.
DR InterPro; IPR001770; Gprotein-gamma.
DR PANTHER; PTHR13809; PTHR13809; 1.
DR Pfam; PF00631; G-gamma; 1.
DR PRINTS; PR00321; GPROTEING.
DR SMART; SM00224; GGL; 1.
DR SUPFAM; SSF48670; SSF48670; 1.
DR PROSITE; PS50058; G_PROTEIN_GAMMA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cell membrane; Complete proteome;
KW Lipoprotein; Membrane; Methylation; Prenylation; Reference proteome;
KW Transducer.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 68 Guanine nucleotide-binding protein
FT G(I)/G(S)/G(O) subunit gamma-2.
FT /FTId=PRO_0000012611.
FT PROPEP 69 71 Removed in mature form (By similarity).
FT /FTId=PRO_0000012612.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 68 68 Cysteine methyl ester (By similarity).
FT LIPID 68 68 S-geranylgeranyl cysteine (By
FT similarity).
FT HELIX 9 23
FT HELIX 30 44
FT HELIX 45 47
FT TURN 49 51
FT TURN 56 58
FT STRAND 60 62
FT TURN 63 66
SQ SEQUENCE 71 AA; 7850 MW; EDB74E4135E7A37A CRC64;
MASNNTASIA QARKLVEQLK MEANIDRIKV SKAAADLMAY CEAHAKEDPL LTPVPASENP
FREKKFFCAI L
//

MIM 606981
*RECORD*
*FIELD* NO
606981
*FIELD* TI
*606981 GUANINE NUCLEOTIDE-BINDING PROTEIN, GAMMA-2; GNG2
;;G PROTEIN GAMMA-2 SUBUNIT;;
read moreGUANINE NUCLEOTIDE-BINDING PROTEIN G(I)/G(O)
*FIELD* TX

DESCRIPTION

Heterotrimeric G proteins play vital roles in cellular responses to
external signals. The specificity of a G protein-receptor interaction is
primarily mediated by the gamma subunit.

CLONING

Modarressi et al. (2000) identified GNG2 by differential display RT-PCR
of normal testis RNA and RNA from the testis of infertile and
azoospermic patients. The full-length cDNA, obtained by 5-prime RACE,
encodes a deduced 71-amino acid protein that is 100% homologous with the
bovine, mouse, and rat GNG2 proteins. RT-PCR revealed expression in
adult testis, adrenals, brain, white blood cells, and lung, but no or
undetectable expression in testis from infertile or azoospermic
patients, or in adult liver, muscle, or prostate. PCR of fetal tissues
revealed highest expression in sternum and brain, intermediate
expression in limbs, stomach, intestine, and kidney, and lowest
expression in testis, heart, spleen, and lung. High expression was also
found in tumor tissues from thyroid and parotid glands, in a squamous
cell carcinoma, and in a lymphoid cell line, with little detected in
granulation tissue.

Yu et al. (2001) independently cloned human GNG2 from a 22-week fetal
liver cDNA library.

GENE FUNCTION

Modarressi et al. (2000) determined that the GNG2 gene contains 3 exons.

Wolfe et al. (2003) demonstrated that inhibition of the alpha-1H
(Ca(v)3.2) (CACNA1H; 607904), but not alpha-1G (Ca(v)3.1) (CACNA1G;
604065), low voltage-activated calcium channels is mediated selectively
by G protein beta-2-gamma-2 subunits (GNB2, 139390, and GNG2) that bind
to the intracellular loop connecting channel transmembrane domains II
and III. This region of the alpha-1H channel is crucial for inhibition,
because its replacement abrogates inhibition and its transfer to
nonmodulated alpha-1G channels confers beta-2-gamma-2-dependent
inhibition. Beta-gamma reduces channel activity independent of voltage,
a mechanism distinct from the established beta-gamma-dependent
inhibition of non-L-type high voltage-activated channels of the Ca(v)2
family. Wolfe et al. (2003) concluded that their studies identified the
alpha-1H channel as a new effector for G protein beta-gamma subunits,
and highlight the selective signaling roles available for particular
beta-gamma combinations.

MAPPING

By PCR amplification of a panel of human and rodent cell hybrids and by
FISH, Modarressi et al. (2000) mapped the GNG2 gene to chromosome 14q21.
The mouse Gng2 gene maps to chromosome 14 (Downes et al., 1999).

*FIELD* RF
1. Downes, G. B.; Gilbert, D. J.; Copeland, N. G.; Gautam, N.; Jenkins,
N. A.: Chromosomal mapping of five mouse G protein gamma subunits. Genomics 57:
173-176, 1999.

2. Modarressi, M. H.; Taylor, K. E.; Wolfe, J.: Cloning, characterization,
and mapping of the gene encoding the human G protein gamma-2 subunit. Biochem.
Biophys. Res. Commun. 272: 610-615, 2000.

3. Wolfe, J. T.; Wang, H.; Howard, J.; Garrison, J. C.; Barrett, P.
Q.: T-type calcium channel regulation by specific G-protein beta-gamma
subunits. Nature 424: 209-213, 2003.

4. Yu, Y.; Zhang, C.; Zhou, G.; Wu, S.; Qu, X.; Wei, H.; Xing, G.;
Dong, C.; Zhai, Y.; Wan, J.; Ouyang, S.; Li, L.; Zhang, S.; Zhou,
K.; Zhang, Y.; Wu, C.; He, F.: Gene expression profiling in human
fetal liver and identification of tissue- and developmental-stage-specific
genes through compiled expression profiles and efficient cloning of
full-length cDNAs. Genome Res. 11: 1392-1403, 2001.

*FIELD* CN
Ada Hamosh - updated: 8/4/2003

*FIELD* CD
Patricia A. Hartz: 5/23/2002

*FIELD* ED
wwang: 06/15/2009
cwells: 11/7/2003
alopez: 8/6/2003
terry: 8/4/2003
carol: 7/9/2002
carol: 5/23/2002

RBCC Red Blood Cell Collection

Full text data of GNG2