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GBG13_MOUSE
ID   GBG13_MOUSE             Reviewed;          67 AA.
AC   Q9JMF3;
DT   31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 156.
DE   RecName: Full=Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-13;
DE   Flags: Precursor;
GN   Name=Gng13;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6J;
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;
RX   PubMed=10679242; DOI=10.1006/bbrc.2000.2170;
RA   Inoue S., Sano H., Ohta M.;
RT   "Growth suppression of Escherichia coli by induction of expression of
RT   mammalian genes with transmembrane or ATPase domains.";
RL   Biochem. Biophys. Res. Commun. 268:553-561(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
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   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
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   -!- 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; AY029485; AAK40268.1; -; mRNA.
DR   EMBL; AB030194; BAA92757.1; -; mRNA.
DR   EMBL; AK018778; BAB31403.1; -; mRNA.
DR   EMBL; BC048431; AAH48431.1; -; mRNA.
DR   EMBL; BC059712; AAH59712.1; -; mRNA.
DR   CCDS; CCDS37503.1; -.
DR   RefSeq; NP_071867.1; NM_022422.5.
DR   RefSeq; XP_006524842.1; XM_006524779.3.
DR   AlphaFoldDB; Q9JMF3; -.
DR   SMR; Q9JMF3; -.
DR   BioGRID; 211062; 1.
DR   DIP; DIP-46321N; -.
DR   IntAct; Q9JMF3; 2.
DR   STRING; 10090.ENSMUSP00000131648; -.
DR   iPTMnet; Q9JMF3; -.
DR   PhosphoSitePlus; Q9JMF3; -.
DR   MaxQB; Q9JMF3; -.
DR   PaxDb; Q9JMF3; -.
DR   PeptideAtlas; Q9JMF3; -.
DR   PRIDE; Q9JMF3; -.
DR   ProteomicsDB; 268848; -.
DR   Antibodypedia; 52208; 56 antibodies from 18 providers.
DR   DNASU; 64337; -.
DR   Ensembl; ENSMUST00000115108; ENSMUSP00000110760; ENSMUSG00000025739.
DR   Ensembl; ENSMUST00000172002; ENSMUSP00000131648; ENSMUSG00000025739.
DR   GeneID; 64337; -.
DR   KEGG; mmu:64337; -.
DR   UCSC; uc008bbi.2; mouse.
DR   CTD; 51764; -.
DR   MGI; MGI:1925616; Gng13.
DR   VEuPathDB; HostDB:ENSMUSG00000025739; -.
DR   eggNOG; KOG4119; Eukaryota.
DR   GeneTree; ENSGT00530000064157; -.
DR   HOGENOM; CLU_168377_1_1_1; -.
DR   InParanoid; Q9JMF3; -.
DR   OMA; MDEWELP; -.
DR   OrthoDB; 1597581at2759; -.
DR   PhylomeDB; Q9JMF3; -.
DR   TreeFam; TF319909; -.
DR   Reactome; R-MMU-1296041; Activation of G protein gated Potassium channels.
DR   Reactome; R-MMU-202040; G-protein activation.
DR   Reactome; R-MMU-381676; Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
DR   Reactome; R-MMU-381753; Olfactory Signaling Pathway.
DR   Reactome; R-MMU-381771; Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1).
DR   Reactome; R-MMU-392170; ADP signalling through P2Y purinoceptor 12.
DR   Reactome; R-MMU-392451; G beta:gamma signalling through PI3Kgamma.
DR   Reactome; R-MMU-392851; Prostacyclin signalling through prostacyclin receptor.
DR   Reactome; R-MMU-400042; Adrenaline,noradrenaline inhibits insulin secretion.
DR   Reactome; R-MMU-4086398; Ca2+ pathway.
DR   Reactome; R-MMU-416476; G alpha (q) signalling events.
DR   Reactome; R-MMU-416482; G alpha (12/13) signalling events.
DR   Reactome; R-MMU-418217; G beta:gamma signalling through PLC beta.
DR   Reactome; R-MMU-418555; G alpha (s) signalling events.
DR   Reactome; R-MMU-418592; ADP signalling through P2Y purinoceptor 1.
DR   Reactome; R-MMU-418594; G alpha (i) signalling events.
DR   Reactome; R-MMU-418597; G alpha (z) signalling events.
DR   Reactome; R-MMU-420092; Glucagon-type ligand receptors.
DR   Reactome; R-MMU-428930; Thromboxane signalling through TP receptor.
DR   Reactome; R-MMU-432040; Vasopressin regulates renal water homeostasis via Aquaporins.
DR   Reactome; R-MMU-456926; Thrombin signalling through proteinase activated receptors (PARs).
DR   Reactome; R-MMU-500657; Presynaptic function of Kainate receptors.
DR   Reactome; R-MMU-6814122; Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.
DR   Reactome; R-MMU-8964315; G beta:gamma signalling through BTK.
DR   Reactome; R-MMU-8964616; G beta:gamma signalling through CDC42.
DR   Reactome; R-MMU-9009391; Extra-nuclear estrogen signaling.
DR   Reactome; R-MMU-9634597; GPER1 signaling.
DR   Reactome; R-MMU-9717207; Sensory perception of sweet, bitter, and umami (glutamate) taste.
DR   Reactome; R-MMU-997272; Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits.
DR   BioGRID-ORCS; 64337; 1 hit in 70 CRISPR screens.
DR   PRO; PR:Q9JMF3; -.
DR   Proteomes; UP000000589; Chromosome 17.
DR   RNAct; Q9JMF3; protein.
DR   Bgee; ENSMUSG00000025739; Expressed in olfactory epithelium and 117 other tissues.
DR   Genevisible; Q9JMF3; MM.
DR   GO; GO:0030425; C:dendrite; IDA:MGI.
DR   GO; GO:0005834; C:heterotrimeric G-protein complex; IPI:MGI.
DR   GO; GO:0016020; C:membrane; TAS:MGI.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0031681; F:G-protein beta-subunit binding; ISS:CAFA.
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; IDA:MGI.
DR   GO; GO:0050909; P:sensory perception of taste; IDA:MGI.
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   PANTHER; PTHR15936; PTHR15936; 1.
DR   Pfam; PF00631; G-gamma; 1.
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_0000012673"
FT   PROPEP          65..67
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000012674"
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;  7979 MW;  1FB8D74EB5CE50F5 CRC64;
     MEEWDVPQMK KEVESLKYQL AFKREMSSKT IPELLKWIED GIPKDPFLNP DLMKNNPWVE
     KAKCTIL
 
 
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