GBG12_HUMAN
ID GBG12_HUMAN Reviewed; 72 AA.
AC Q9UBI6; Q69YP5; Q9BRV5;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-12;
DE Flags: Precursor;
GN Name=GNG12;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10819326; DOI=10.1093/dnares/7.2.111;
RA Hurowitz E.H., Melnyk J.M., Chen Y.J., Kouros-Mehr H., Simon M.I.,
RA Shizuya H.;
RT "Genomic characterization of the human heterotrimeric G protein alpha,
RT beta, and gamma subunit genes.";
RL DNA Res. 7:111-120(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Yang L., Yu L., Zhao S.Y.;
RT "Cloning and characterizing a novel human cDNA homologous to Bos taurus G-
RT protein gamma-12 subunit mRNA.";
RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Adrenal gland;
RX PubMed=10931946; DOI=10.1073/pnas.160270997;
RA Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
RA Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W.,
RA Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J., Xu S.-H., Gu J.,
RA Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z.,
RA Chen M.-D., Chen J.-L.;
RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis
RT and full-length cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11714923; DOI=10.1110/ps.ps.26401;
RA Cook L.A., Schey K.L., Cleator J.H., Wilcox M.D., Dingus J.,
RA Hildebrandt J.D.;
RT "Identification of a region in G protein gamma subunits conserved across
RT species but hypervariable among subunit isoforms.";
RL Protein Sci. 10:2548-2555(2001).
RN [5]
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 sequenced by
RT the Guthrie cDNA resource center (www.cdna.org).";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Melanoma;
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., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
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., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [13]
RP ISOPRENYLATION AT CYS-69, METHYLATION AT CYS-69, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=24023390; DOI=10.1074/mcp.m113.030114;
RA Catherman A.D., Durbin K.R., Ahlf D.R., Early B.P., Fellers R.T.,
RA Tran J.C., Thomas P.M., Kelleher N.L.;
RT "Large-scale top down proteomics of the human proteome: membrane proteins,
RT mitochondria, and senescence.";
RL Mol. Cell. Proteomics 12:3465-3473(2013).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved
CC as a modulator or transducer in various transmembrane signaling
CC systems. The beta and gamma chains are required for the GTPase
CC activity, for replacement of GDP by GTP, and for G protein-effector
CC interaction.
CC -!- SUBUNIT: G proteins are composed of 3 units, alpha, beta and gamma.
CC -!- INTERACTION:
CC Q9UBI6; Q14192: FHL2; NbExp=11; IntAct=EBI-358636, EBI-701903;
CC Q9UBI6; Q8WUI4-6: HDAC7; NbExp=3; IntAct=EBI-358636, EBI-12094670;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the G protein gamma family. {ECO:0000305}.
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DR EMBL; AF188181; AAF04571.1; -; Genomic_DNA.
DR EMBL; AF123766; AAP97245.1; -; mRNA.
DR EMBL; AF119663; AAF17220.1; -; mRNA.
DR EMBL; AF365871; AAK53385.1; -; mRNA.
DR EMBL; AF493879; AAM12593.1; -; mRNA.
DR EMBL; AK293101; BAF85790.1; -; mRNA.
DR EMBL; AL832431; CAH10645.1; -; mRNA.
DR EMBL; CH471059; EAX06484.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX06485.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX06486.1; -; Genomic_DNA.
DR EMBL; BC005940; AAH05940.1; -; mRNA.
DR CCDS; CCDS30749.1; -.
DR RefSeq; NP_061329.3; NM_018841.5.
DR RefSeq; XP_016857298.1; XM_017001809.1.
DR RefSeq; XP_016857299.1; XM_017001810.1.
DR RefSeq; XP_016857300.1; XM_017001811.1.
DR AlphaFoldDB; Q9UBI6; -.
DR SMR; Q9UBI6; -.
DR BioGRID; 121016; 82.
DR CORUM; Q9UBI6; -.
DR IntAct; Q9UBI6; 33.
DR MINT; Q9UBI6; -.
DR STRING; 9606.ENSP00000360021; -.
DR iPTMnet; Q9UBI6; -.
DR PhosphoSitePlus; Q9UBI6; -.
DR SwissPalm; Q9UBI6; -.
DR BioMuta; GNG12; -.
DR DMDM; 12229817; -.
DR EPD; Q9UBI6; -.
DR jPOST; Q9UBI6; -.
DR MassIVE; Q9UBI6; -.
DR MaxQB; Q9UBI6; -.
DR PaxDb; Q9UBI6; -.
DR PeptideAtlas; Q9UBI6; -.
DR PRIDE; Q9UBI6; -.
DR ProteomicsDB; 83975; -.
DR TopDownProteomics; Q9UBI6; -.
DR Antibodypedia; 33413; 66 antibodies from 21 providers.
DR DNASU; 55970; -.
DR Ensembl; ENST00000370982.4; ENSP00000360021.3; ENSG00000172380.6.
DR GeneID; 55970; -.
DR KEGG; hsa:55970; -.
DR MANE-Select; ENST00000370982.4; ENSP00000360021.3; NM_018841.6; NP_061329.3.
DR UCSC; uc001dea.3; human.
DR CTD; 55970; -.
DR DisGeNET; 55970; -.
DR GeneCards; GNG12; -.
DR HGNC; HGNC:19663; GNG12.
DR HPA; ENSG00000172380; Low tissue specificity.
DR MIM; 615405; gene.
DR neXtProt; NX_Q9UBI6; -.
DR OpenTargets; ENSG00000172380; -.
DR PharmGKB; PA134956700; -.
DR VEuPathDB; HostDB:ENSG00000172380; -.
DR eggNOG; KOG4119; Eukaryota.
DR GeneTree; ENSGT01050000244858; -.
DR HOGENOM; CLU_168377_3_1_1; -.
DR InParanoid; Q9UBI6; -.
DR OMA; MDIMASN; -.
DR OrthoDB; 1581168at2759; -.
DR PhylomeDB; Q9UBI6; -.
DR TreeFam; TF319909; -.
DR PathwayCommons; Q9UBI6; -.
DR Reactome; R-HSA-1296041; Activation of G protein gated Potassium channels.
DR Reactome; R-HSA-163359; Glucagon signaling in metabolic regulation.
DR Reactome; R-HSA-202040; G-protein activation.
DR Reactome; R-HSA-381676; Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
DR Reactome; R-HSA-392170; ADP signalling through P2Y purinoceptor 12.
DR Reactome; R-HSA-392451; G beta:gamma signalling through PI3Kgamma.
DR Reactome; R-HSA-392851; Prostacyclin signalling through prostacyclin receptor.
DR Reactome; R-HSA-400042; Adrenaline,noradrenaline inhibits insulin secretion.
DR Reactome; R-HSA-4086398; Ca2+ pathway.
DR Reactome; R-HSA-416476; G alpha (q) signalling events.
DR Reactome; R-HSA-416482; G alpha (12/13) signalling events.
DR Reactome; R-HSA-418217; G beta:gamma signalling through PLC beta.
DR Reactome; R-HSA-418555; G alpha (s) signalling events.
DR Reactome; R-HSA-418592; ADP signalling through P2Y purinoceptor 1.
DR Reactome; R-HSA-418594; G alpha (i) signalling events.
DR Reactome; R-HSA-418597; G alpha (z) signalling events.
DR Reactome; R-HSA-420092; Glucagon-type ligand receptors.
DR Reactome; R-HSA-428930; Thromboxane signalling through TP receptor.
DR Reactome; R-HSA-432040; Vasopressin regulates renal water homeostasis via Aquaporins.
DR Reactome; R-HSA-456926; Thrombin signalling through proteinase activated receptors (PARs).
DR Reactome; R-HSA-500657; Presynaptic function of Kainate receptors.
DR Reactome; R-HSA-6814122; Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.
DR Reactome; R-HSA-8964315; G beta:gamma signalling through BTK.
DR Reactome; R-HSA-8964616; G beta:gamma signalling through CDC42.
DR Reactome; R-HSA-9009391; Extra-nuclear estrogen signaling.
DR Reactome; R-HSA-9634597; GPER1 signaling.
DR Reactome; R-HSA-9660821; ADORA2B mediated anti-inflammatory cytokines production.
DR Reactome; R-HSA-997272; Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits.
DR SignaLink; Q9UBI6; -.
DR SIGNOR; Q9UBI6; -.
DR BioGRID-ORCS; 55970; 13 hits in 1073 CRISPR screens.
DR ChiTaRS; GNG12; human.
DR GeneWiki; GNG12; -.
DR GenomeRNAi; 55970; -.
DR Pharos; Q9UBI6; Tbio.
DR PRO; PR:Q9UBI6; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9UBI6; protein.
DR Bgee; ENSG00000172380; Expressed in jejunal mucosa and 209 other tissues.
DR Genevisible; Q9UBI6; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0031681; F:G-protein beta-subunit binding; IBA:GO_Central.
DR GO; GO:0030165; F:PDZ domain binding; IDA:MGI.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR CDD; cd00068; GGL; 1.
DR Gene3D; 4.10.260.10; -; 1.
DR InterPro; IPR015898; G-protein_gamma-like_dom.
DR InterPro; IPR036284; GGL_sf.
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 Acetylation; Cell membrane; Lipoprotein; Membrane; Methylation;
KW Phosphoprotein; Prenylation; Reference proteome; Transducer.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..69
FT /note="Guanine nucleotide-binding protein G(I)/G(S)/G(O)
FT subunit gamma-12"
FT /id="PRO_0000012667"
FT PROPEP 70..72
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000012668"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 26
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9DAS9"
FT MOD_RES 42
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9DAS9"
FT MOD_RES 49
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 69
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000269|PubMed:24023390"
FT LIPID 69
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000269|PubMed:24023390"
FT CONFLICT 29
FT /note="R -> G (in Ref. 9; AAH05940)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 72 AA; 8006 MW; A4C489A61697FAA9 CRC64;
MSSKTASTNN IAQARRTVQQ LRLEASIERI KVSKASADLM SYCEEHARSD PLLIGIPTSE
NPFKDKKTCI IL
