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PP13G_HUMAN
ID   PP13G_HUMAN             Reviewed;         358 AA.
AC   B7ZBB8;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Protein phosphatase 1 regulatory subunit 3G;
GN   Name=PPP1R3G;
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 [LARGE SCALE GENOMIC DNA].
RX   PubMed=14574404; DOI=10.1038/nature02055;
RA   Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA   Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA   Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA   Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA   Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA   Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA   Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA   Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA   Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA   French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA   Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA   Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA   Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA   Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA   Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA   Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA   Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA   Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA   Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA   Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA   Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA   Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA   Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA   Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA   West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA   Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA   Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA   Rogers J., Beck S.;
RT   "The DNA sequence and analysis of human chromosome 6.";
RL   Nature 425:805-811(2003).
RN   [2]
RP   IDENTIFICATION.
RX   PubMed=11948623; DOI=10.1002/bies.10069;
RA   Ceulemans H., Stalmans W., Bollen M.;
RT   "Regulator-driven functional diversification of protein phosphatase-1 in
RT   eukaryotic evolution.";
RL   Bioessays 24:371-381(2002).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86, 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).
CC   -!- FUNCTION: Glycogen-targeting subunit for protein phosphatase 1 (PP1).
CC       Involved in the regulation of hepatic glycogenesis in a manner coupled
CC       to the fasting-feeding cycle and distinct from other glycogen-targeting
CC       subunits (By similarity). {ECO:0000250}.
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DR   EMBL; AL035653; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS47366.1; -.
DR   RefSeq; NP_001138587.1; NM_001145115.2.
DR   AlphaFoldDB; B7ZBB8; -.
DR   SMR; B7ZBB8; -.
DR   BioGRID; 572922; 1.
DR   IntAct; B7ZBB8; 1.
DR   STRING; 9606.ENSP00000393832; -.
DR   iPTMnet; B7ZBB8; -.
DR   PhosphoSitePlus; B7ZBB8; -.
DR   BioMuta; PPP1R3G; -.
DR   jPOST; B7ZBB8; -.
DR   MassIVE; B7ZBB8; -.
DR   PaxDb; B7ZBB8; -.
DR   PeptideAtlas; B7ZBB8; -.
DR   PRIDE; B7ZBB8; -.
DR   ProteomicsDB; 7109; -.
DR   Antibodypedia; 58036; 58 antibodies from 12 providers.
DR   DNASU; 648791; -.
DR   Ensembl; ENST00000405617.4; ENSP00000393832.2; ENSG00000219607.4.
DR   GeneID; 648791; -.
DR   KEGG; hsa:648791; -.
DR   MANE-Select; ENST00000405617.4; ENSP00000393832.2; NM_001145115.3; NP_001138587.1.
DR   UCSC; uc011dia.2; human.
DR   CTD; 648791; -.
DR   DisGeNET; 648791; -.
DR   GeneCards; PPP1R3G; -.
DR   HGNC; HGNC:14945; PPP1R3G.
DR   HPA; ENSG00000219607; Tissue enhanced (heart muscle, liver).
DR   MIM; 619541; gene.
DR   neXtProt; NX_B7ZBB8; -.
DR   OpenTargets; ENSG00000219607; -.
DR   PharmGKB; PA33657; -.
DR   VEuPathDB; HostDB:ENSG00000219607; -.
DR   eggNOG; KOG3986; Eukaryota.
DR   GeneTree; ENSGT00940000163747; -.
DR   HOGENOM; CLU_040215_1_0_1; -.
DR   InParanoid; B7ZBB8; -.
DR   OMA; GAECFHF; -.
DR   OrthoDB; 1232750at2759; -.
DR   PhylomeDB; B7ZBB8; -.
DR   TreeFam; TF105537; -.
DR   PathwayCommons; B7ZBB8; -.
DR   SignaLink; B7ZBB8; -.
DR   BioGRID-ORCS; 648791; 9 hits in 1067 CRISPR screens.
DR   GenomeRNAi; 648791; -.
DR   Pharos; B7ZBB8; Tbio.
DR   PRO; PR:B7ZBB8; -.
DR   Proteomes; UP000005640; Chromosome 6.
DR   RNAct; B7ZBB8; protein.
DR   Bgee; ENSG00000219607; Expressed in apex of heart and 88 other tissues.
DR   GO; GO:0000164; C:protein phosphatase type 1 complex; IBA:GO_Central.
DR   GO; GO:2001069; F:glycogen binding; IBA:GO_Central.
DR   GO; GO:0008157; F:protein phosphatase 1 binding; IBA:GO_Central.
DR   GO; GO:0042593; P:glucose homeostasis; IEA:Ensembl.
DR   GO; GO:0005978; P:glycogen biosynthetic process; IEA:Ensembl.
DR   GO; GO:2000467; P:positive regulation of glycogen (starch) synthase activity; IEA:Ensembl.
DR   GO; GO:0045725; P:positive regulation of glycogen biosynthetic process; IEA:Ensembl.
DR   GO; GO:0005979; P:regulation of glycogen biosynthetic process; IBA:GO_Central.
DR   Gene3D; 2.60.40.2440; -; 1.
DR   InterPro; IPR005036; CBM21_dom.
DR   InterPro; IPR038175; CBM21_dom_sf.
DR   Pfam; PF03370; CBM_21; 1.
DR   PROSITE; PS51159; CBM21; 1.
PE   1: Evidence at protein level;
KW   Phosphoprotein; Reference proteome.
FT   CHAIN           1..358
FT                   /note="Protein phosphatase 1 regulatory subunit 3G"
FT                   /id="PRO_0000394965"
FT   DOMAIN          210..350
FT                   /note="CBM21"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00491"
FT   REGION          1..71
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          270..295
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         86
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   VARIANT         280
FT                   /note="P -> Q (in dbSNP:rs436556)"
FT                   /id="VAR_063262"
SQ   SEQUENCE   358 AA;  38019 MW;  8976D05A4FA43F1F CRC64;
     MEPIGARLSL EAPGPAPFRE APPAEELPAP VVPCVQGGGD GGGASETPSP DAQLGDRPLS
     PKEEAAPQEQ EELLECRRRC RARSFSLPAD PILQAAKFLQ QQQQQAVALG GEGAEDAQLG
     PGGCCAKCKK RVQFADTLGL SLASVKHFSE AEEPQVPPAV LSRLRSFPMR AEDLEQLGGL
     LAAAAVAAPL SAPPSRLRPL FQLPGPSAAA ERLQRQRVCL ERVQCSTASG AEVKGSGRVL
     SCPGPRAVTV RYTFTEWRSF LDVPAELQPE PLEPQQPEAP SGASEPGSGD AKKEPGAECF
     HFSLCLPPGL QPEDEEDADE RGVAVHFAVC YRCAQGEYWD NNAGANYTLR YARPADAL
 
 
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