GBG13_HUMAN
ID GBG13_HUMAN Reviewed; 67 AA.
AC Q9P2W3; B2R5C8; Q52LX0; Q9UJJ3;
DT 31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-13;
DE Flags: Precursor;
GN Name=GNG13;
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 [MRNA].
RX PubMed=10570481; DOI=10.1038/15981;
RA Huang L., Shanker Y.G., Dubauskaite J., Zheng J.Z., Yan W., Rosenzweig S.,
RA Spielman A.I., Max M., Margolskee R.F.;
RT "Ggamma13 colocalizes with gustducin in taste receptor cells and mediates
RT IP3 responses to bitter denatonium.";
RL Nat. Neurosci. 2:1055-1062(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RA Inoue S., Sano H., Ohta M.;
RT "E.coli toxicity assay: a novel expression screening method for isolation
RT of mammalian genes with membrane-associated domains or ATP binding/ATPase
RT domains.";
RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cerebellum;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11157797; DOI=10.1093/hmg/10.4.339;
RA Daniels R.J., Peden J.F., Lloyd C., Horsley S.W., Clark K., Tufarelli C.,
RA Kearney L., Buckle V.J., Doggett N.A., Flint J., Higgs D.R.;
RT "Sequence, structure and pathology of the fully annotated terminal 2 Mb of
RT the short arm of human chromosome 16.";
RL Hum. Mol. Genet. 10:339-352(2001).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [7]
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).
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 Q9P2W3; Q9P2A4: ABI3; NbExp=3; IntAct=EBI-11427343, EBI-742038;
CC Q9P2W3; Q6UY14-3: ADAMTSL4; NbExp=3; IntAct=EBI-11427343, EBI-10173507;
CC Q9P2W3; Q5H9J7: BEX5; NbExp=3; IntAct=EBI-11427343, EBI-10243741;
CC Q9P2W3; Q8TD31-3: CCHCR1; NbExp=3; IntAct=EBI-11427343, EBI-10175300;
CC Q9P2W3; P78358: CTAG1B; NbExp=3; IntAct=EBI-11427343, EBI-1188472;
CC Q9P2W3; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-11427343, EBI-3867333;
CC Q9P2W3; Q9NRI5-2: DISC1; NbExp=3; IntAct=EBI-11427343, EBI-11988027;
CC Q9P2W3; Q9Y6C2-2: EMILIN1; NbExp=3; IntAct=EBI-11427343, EBI-11748557;
CC Q9P2W3; Q9C0B1-2: FTO; NbExp=3; IntAct=EBI-11427343, EBI-18138793;
CC Q9P2W3; O76003: GLRX3; NbExp=3; IntAct=EBI-11427343, EBI-374781;
CC Q9P2W3; Q68CZ6: HAUS3; NbExp=3; IntAct=EBI-11427343, EBI-2558217;
CC Q9P2W3; P31260-2: HOXA10; NbExp=3; IntAct=EBI-11427343, EBI-12896693;
CC Q9P2W3; Q7Z3Y8: KRT27; NbExp=3; IntAct=EBI-11427343, EBI-3044087;
CC Q9P2W3; O76011: KRT34; NbExp=3; IntAct=EBI-11427343, EBI-1047093;
CC Q9P2W3; O76014: KRT37; NbExp=3; IntAct=EBI-11427343, EBI-1045716;
CC Q9P2W3; O76015: KRT38; NbExp=3; IntAct=EBI-11427343, EBI-1047263;
CC Q9P2W3; Q9BYQ4: KRTAP9-2; NbExp=3; IntAct=EBI-11427343, EBI-1044640;
CC Q9P2W3; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-11427343, EBI-16439278;
CC Q9P2W3; Q02548: PAX5; NbExp=3; IntAct=EBI-11427343, EBI-296331;
CC Q9P2W3; Q9NRY7: PLSCR2; NbExp=3; IntAct=EBI-11427343, EBI-3937430;
CC Q9P2W3; A6NK89: RASSF10; NbExp=3; IntAct=EBI-11427343, EBI-6912267;
CC Q9P2W3; Q9NS64: RPRM; NbExp=3; IntAct=EBI-11427343, EBI-1052363;
CC Q9P2W3; Q2I0M5: RSPO4; NbExp=3; IntAct=EBI-11427343, EBI-12821217;
CC Q9P2W3; Q15562-2: TEAD2; NbExp=3; IntAct=EBI-11427343, EBI-9370956;
CC Q9P2W3; Q96N21: TEPSIN; NbExp=3; IntAct=EBI-11427343, EBI-11139477;
CC Q9P2W3; Q9BYV2: TRIM54; NbExp=3; IntAct=EBI-11427343, EBI-2130429;
CC Q9P2W3; Q9BRT2: UQCC2; NbExp=3; IntAct=EBI-11427343, EBI-1054584;
CC Q9P2W3; Q6GMQ7: VPS16; NbExp=3; IntAct=EBI-11427343, EBI-17974829;
CC Q9P2W3; Q9Y3C0: WASHC3; NbExp=3; IntAct=EBI-11427343, EBI-712969;
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY029486; AAK40269.1; -; mRNA.
DR EMBL; AB030207; BAA92768.1; -; mRNA.
DR EMBL; AF493880; AAM12594.1; -; mRNA.
DR EMBL; AK312139; BAG35075.1; -; mRNA.
DR EMBL; AE006465; AAK61257.1; -; Genomic_DNA.
DR EMBL; AL031033; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC093760; AAH93760.1; -; mRNA.
DR EMBL; BC095525; AAH95525.1; -; mRNA.
DR CCDS; CCDS10427.1; -.
DR RefSeq; NP_057625.1; NM_016541.2.
DR AlphaFoldDB; Q9P2W3; -.
DR SMR; Q9P2W3; -.
DR BioGRID; 119721; 35.
DR CORUM; Q9P2W3; -.
DR IntAct; Q9P2W3; 29.
DR STRING; 9606.ENSP00000248150; -.
DR iPTMnet; Q9P2W3; -.
DR PhosphoSitePlus; Q9P2W3; -.
DR BioMuta; GNG13; -.
DR DMDM; 20138402; -.
DR MassIVE; Q9P2W3; -.
DR PaxDb; Q9P2W3; -.
DR PeptideAtlas; Q9P2W3; -.
DR PRIDE; Q9P2W3; -.
DR ProteomicsDB; 83903; -.
DR Antibodypedia; 52208; 56 antibodies from 18 providers.
DR DNASU; 51764; -.
DR Ensembl; ENST00000248150.5; ENSP00000248150.4; ENSG00000127588.5.
DR GeneID; 51764; -.
DR KEGG; hsa:51764; -.
DR MANE-Select; ENST00000248150.5; ENSP00000248150.4; NM_016541.3; NP_057625.1.
DR UCSC; uc002ckh.4; human.
DR CTD; 51764; -.
DR DisGeNET; 51764; -.
DR GeneCards; GNG13; -.
DR HGNC; HGNC:14131; GNG13.
DR HPA; ENSG00000127588; Group enriched (brain, retina).
DR MIM; 607298; gene.
DR neXtProt; NX_Q9P2W3; -.
DR OpenTargets; ENSG00000127588; -.
DR PharmGKB; PA28783; -.
DR VEuPathDB; HostDB:ENSG00000127588; -.
DR eggNOG; KOG4119; Eukaryota.
DR GeneTree; ENSGT00530000064157; -.
DR HOGENOM; CLU_168377_1_1_1; -.
DR InParanoid; Q9P2W3; -.
DR OMA; MDEWELP; -.
DR OrthoDB; 1597581at2759; -.
DR PhylomeDB; Q9P2W3; -.
DR TreeFam; TF319909; -.
DR PathwayCommons; Q9P2W3; -.
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-381753; Olfactory Signaling Pathway.
DR Reactome; R-HSA-381771; Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1).
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-9717207; Sensory perception of sweet, bitter, and umami (glutamate) taste.
DR Reactome; R-HSA-997272; Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits.
DR SignaLink; Q9P2W3; -.
DR BioGRID-ORCS; 51764; 28 hits in 1058 CRISPR screens.
DR GeneWiki; GNG13; -.
DR GenomeRNAi; 51764; -.
DR Pharos; Q9P2W3; Tbio.
DR PRO; PR:Q9P2W3; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q9P2W3; protein.
DR Bgee; ENSG00000127588; Expressed in right hemisphere of cerebellum and 68 other tissues.
DR Genevisible; Q9P2W3; HS.
DR GO; GO:0030425; C:dendrite; IEA:Ensembl.
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; IPI:UniProtKB.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0050909; P:sensory perception of taste; IEA:Ensembl.
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; IPR039227; GNG13.
DR InterPro; IPR001770; Gprotein-gamma.
DR PANTHER; PTHR15936; PTHR15936; 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 Cell membrane; Lipoprotein; Membrane; Methylation; Prenylation;
KW Reference proteome; Transducer.
FT CHAIN 1..64
FT /note="Guanine nucleotide-binding protein G(I)/G(S)/G(O)
FT subunit gamma-13"
FT /id="PRO_0000012671"
FT PROPEP 65..67
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000012672"
FT MOD_RES 64
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 64
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 67 AA; 7949 MW; 080E0C34A8F70327 CRC64;
MEEWDVPQMK KEVESLKYQL AFQREMASKT IPELLKWIED GIPKDPFLNP DLMKNNPWVE
KGKCTIL
