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GBG10_HUMAN
ID   GBG10_HUMAN             Reviewed;          68 AA.
AC   P50151; Q3B7K2; Q4VC27;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 199.
DE   RecName: Full=Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-10;
DE   Flags: Precursor;
GN   Name=GNG10; Synonyms=GNGT10;
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], AND ISOPRENYLATION AT CYS-65.
RX   PubMed=7665596; DOI=10.1074/jbc.270.37.21765;
RA   Ray K., Kunsch C., Bonner L.M., Robishaw J.D.;
RT   "Isolation of cDNA clones encoding eight different human G protein gamma
RT   subunits, including three novel forms designated the gamma 4, gamma 10, and
RT   gamma 11 subunits.";
RL   J. Biol. Chem. 270:21765-21771(1995).
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 sequenced by
RT   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 GENOMIC DNA].
RX   PubMed=15164053; DOI=10.1038/nature02465;
RA   Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA   Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA   Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA   Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA   Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA   Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA   Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA   Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA   Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA   Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA   Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA   Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA   Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA   Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA   Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA   Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA   Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA   Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA   McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA   Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA   Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA   Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA   Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA   West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA   Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA   Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA   Dunham I.;
RT   "DNA sequence and analysis of human chromosome 9.";
RL   Nature 429:369-374(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain, and Lung;
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   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).
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. Interacts with beta-1 and beta-2, but not with beta-3.
CC   -!- SUBUNIT: G proteins are composed of 3 units, alpha, beta and gamma.
CC   -!- INTERACTION:
CC       P50151; P08779: KRT16; NbExp=3; IntAct=EBI-10211741, EBI-356410;
CC       P50151; Q15323: KRT31; NbExp=3; IntAct=EBI-10211741, EBI-948001;
CC       P50151; O76011: KRT34; NbExp=3; IntAct=EBI-10211741, EBI-1047093;
CC       P50151; O76015: KRT38; NbExp=6; IntAct=EBI-10211741, EBI-1047263;
CC       P50151; P15884: TCF4; NbExp=3; IntAct=EBI-10211741, EBI-533224;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC       {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Abundantly and ubiquitously expressed.
CC   -!- SIMILARITY: Belongs to the G protein gamma family. {ECO:0000305}.
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DR   EMBL; U31383; AAC50205.1; -; mRNA.
DR   EMBL; AF493877; AAM12591.1; -; mRNA.
DR   EMBL; AL135787; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC010384; AAH10384.1; -; mRNA.
DR   EMBL; BC015206; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; BC016319; AAH16319.1; -; mRNA.
DR   EMBL; BC072671; AAH72671.1; -; mRNA.
DR   EMBL; BC107574; AAI07575.1; -; mRNA.
DR   CCDS; CCDS35107.1; -.
DR   PIR; I39158; I39158.
DR   RefSeq; NP_001017998.1; NM_001017998.3.
DR   RefSeq; NP_001185593.1; NM_001198664.1.
DR   AlphaFoldDB; P50151; -.
DR   SMR; P50151; -.
DR   BioGRID; 109052; 45.
DR   CORUM; P50151; -.
DR   IntAct; P50151; 11.
DR   STRING; 9606.ENSP00000363411; -.
DR   iPTMnet; P50151; -.
DR   PhosphoSitePlus; P50151; -.
DR   BioMuta; GNG10; -.
DR   DMDM; 1730222; -.
DR   EPD; P50151; -.
DR   jPOST; P50151; -.
DR   MassIVE; P50151; -.
DR   MaxQB; P50151; -.
DR   PaxDb; P50151; -.
DR   PeptideAtlas; P50151; -.
DR   PRIDE; P50151; -.
DR   ProteomicsDB; 56200; -.
DR   Antibodypedia; 76916; 59 antibodies from 13 providers.
DR   DNASU; 2790; -.
DR   Ensembl; ENST00000374293.5; ENSP00000363411.3; ENSG00000242616.4.
DR   GeneID; 2790; -.
DR   KEGG; hsa:2790; -.
DR   MANE-Select; ENST00000374293.5; ENSP00000363411.3; NM_001017998.4; NP_001017998.1.
DR   UCSC; uc004bfp.4; human.
DR   CTD; 2790; -.
DR   GeneCards; GNG10; -.
DR   HGNC; HGNC:4402; GNG10.
DR   HPA; ENSG00000242616; Low tissue specificity.
DR   MIM; 604389; gene.
DR   neXtProt; NX_P50151; -.
DR   OpenTargets; ENSG00000242616; -.
DR   PharmGKB; PA28781; -.
DR   VEuPathDB; HostDB:ENSG00000242616; -.
DR   eggNOG; KOG4119; Eukaryota.
DR   GeneTree; ENSGT01050000244858; -.
DR   HOGENOM; CLU_168377_3_0_1; -.
DR   InParanoid; P50151; -.
DR   OMA; REPRSCN; -.
DR   OrthoDB; 1581168at2759; -.
DR   PhylomeDB; P50151; -.
DR   TreeFam; TF319909; -.
DR   PathwayCommons; P50151; -.
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; P50151; -.
DR   BioGRID-ORCS; 2790; 10 hits in 1006 CRISPR screens.
DR   ChiTaRS; GNG10; human.
DR   GenomeRNAi; 2790; -.
DR   Pharos; P50151; Tdark.
DR   PRO; PR:P50151; -.
DR   Proteomes; UP000005640; Chromosome 9.
DR   RNAct; P50151; protein.
DR   Bgee; ENSG00000242616; Expressed in monocyte and 98 other tissues.
DR   ExpressionAtlas; P50151; baseline and differential.
DR   Genevisible; P50151; HS.
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:0003924; F:GTPase activity; TAS:ProtInc.
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   Prenylation; Reference proteome; Transducer.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   CHAIN           2..65
FT                   /note="Guanine nucleotide-binding protein G(I)/G(S)/G(O)
FT                   subunit gamma-10"
FT                   /id="PRO_0000012655"
FT   PROPEP          66..68
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000012656"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   MOD_RES         65
FT                   /note="Cysteine methyl ester"
FT                   /evidence="ECO:0000250"
FT   LIPID           65
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000269|PubMed:7665596"
SQ   SEQUENCE   68 AA;  7205 MW;  E3EC3CEA0EB0BD5A CRC64;
     MSSGASASAL QRLVEQLKLE AGVERIKVSQ AAAELQQYCM QNACKDALLV GVPAGSNPFR
     EPRSCALL
 
 
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