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PP1RB_HUMAN
ID   PP1RB_HUMAN             Reviewed;         126 AA.
AC   O60927;
DT   13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 167.
DE   RecName: Full=E3 ubiquitin-protein ligase PPP1R11 {ECO:0000303|PubMed:27805901};
DE            EC=2.3.2.27;
DE   AltName: Full=Hemochromatosis candidate gene V protein;
DE            Short=HCG V;
DE   AltName: Full=Protein phosphatase 1 regulatory subunit 11;
DE   AltName: Full=Protein phosphatase inhibitor 3;
GN   Name=PPP1R11; Synonyms=HCGV, TCTE5;
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 / MRNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Duodenal mucosa;
RX   PubMed=8781118; DOI=10.1007/bf02602777;
RA   Giffon T., Lepourcelet M., Pichon L., Jezequel P., Bouric P., Carn G.,
RA   Pontarotti P., Gall J.-Y., David V.;
RT   "Cloning of a human homologue of the mouse Tctex-5 gene within the MHC
RT   class I region.";
RL   Immunogenetics 44:331-339(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8938444; DOI=10.1006/geno.1996.0566;
RA   Lepourcelet M., Andrieux N., Giffon T., Pichon L., Hampe A., Galibert F.,
RA   Mosser J.;
RT   "Systematic sequencing of the human HLA-A/HLA-F region: establishment of a
RT   cosmid contig and identification of a new gene cluster within 37 kb of
RT   sequence.";
RL   Genomics 37:316-326(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Shiina S., Tamiya G., Oka A., Inoko H.;
RT   "Homo sapiens 2,229,817bp genomic DNA of 6p21.3 HLA class I region.";
RL   Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Peripheral blood leukocyte;
RA   Shiina T., Ota M., Takasu M., Katsuyama Y., Hashimoto N., Tokunaga K.,
RA   Inoko H.;
RT   "Genome diversity in HLA: a new strategy for detection of genetic
RT   polymorphisms in expressed genes within the HLA class III and class I
RT   regions.";
RL   Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
RN   [5]
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   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 14-126, AND FUNCTION.
RC   TISSUE=Brain;
RX   PubMed=9843442; DOI=10.1021/bi981169g;
RA   Zhang J., Zhang L., Zhao S., Lee E.Y.C.;
RT   "Identification and characterization of the human HCG V gene product as a
RT   novel inhibitor of protein phosphatase-1.";
RL   Biochemistry 37:16728-16734(1998).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73; SER-74; THR-75; SER-77
RP   AND THR-109, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   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   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [10]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-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   [11]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [12]
RP   FUNCTION, MUTAGENESIS OF HIS-52; 60-CYS--CYS-62; CYS-85; HIS-87 AND HIS-94,
RP   REGION ZINC-FINGER DOMAIN, AND AUTOUBIQUITINATION.
RX   PubMed=27805901; DOI=10.7554/elife.18496;
RA   McKelvey A.C., Lear T.B., Dunn S.R., Evankovich J., Londino J.D.,
RA   Bednash J.S., Zhang Y., McVerry B.J., Liu Y., Chen B.B.;
RT   "RING finger E3 ligase PPP1R11 regulates TLR2 signaling and innate
RT   immunity.";
RL   Elife 5:0-0(2016).
CC   -!- FUNCTION: Atypical E3 ubiquitin-protein ligase which ubiquitinates TLR2
CC       at 'Lys-754' leading to its degradation by the proteasome. Plays a role
CC       in regulating inflammatory cytokine release and gram-positive bacterial
CC       clearance by functioning, in part, through the ubiquitination and
CC       degradation of TLR2 (PubMed:27805901). Inhibitor of protein phosphatase
CC       1 (PubMed:9843442). {ECO:0000269|PubMed:27805901,
CC       ECO:0000269|PubMed:9843442}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC         [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC         cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC         EC=2.3.2.27;
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Interacts with TLR2 and UBE2D2.
CC       {ECO:0000250|UniProtKB:Q8K1L5}.
CC   -!- INTERACTION:
CC       O60927; P55212: CASP6; NbExp=3; IntAct=EBI-1048104, EBI-718729;
CC       O60927; O94985-2: CLSTN1; NbExp=3; IntAct=EBI-1048104, EBI-16041593;
CC       O60927; P22607: FGFR3; NbExp=3; IntAct=EBI-1048104, EBI-348399;
CC       O60927; Q8IY31-3: IFT20; NbExp=3; IntAct=EBI-1048104, EBI-9091197;
CC       O60927; P13473-2: LAMP2; NbExp=3; IntAct=EBI-1048104, EBI-21591415;
CC       O60927; Q96CV9: OPTN; NbExp=3; IntAct=EBI-1048104, EBI-748974;
CC       O60927; P62140: PPP1CB; NbExp=8; IntAct=EBI-1048104, EBI-352350;
CC       O60927; P36873: PPP1CC; NbExp=6; IntAct=EBI-1048104, EBI-356283;
CC       O60927; P62826: RAN; NbExp=3; IntAct=EBI-1048104, EBI-286642;
CC       O60927; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-1048104, EBI-741480;
CC       O60927; Q8IY57-5: YAF2; NbExp=3; IntAct=EBI-1048104, EBI-12111538;
CC       O60927; P62139: PPP1CA; Xeno; NbExp=2; IntAct=EBI-1048104, EBI-2008988;
CC   -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:8781118}.
CC   -!- PTM: Auto-ubiquitinated. {ECO:0000269|PubMed:27805901}.
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DR   EMBL; X81003; CAC16920.1; -; mRNA.
DR   EMBL; X89902; CAC16919.1; -; Genomic_DNA.
DR   EMBL; U53588; AAC52082.1; -; Genomic_DNA.
DR   EMBL; BA000025; BAB63334.1; -; Genomic_DNA.
DR   EMBL; AB088087; BAC54919.1; -; Genomic_DNA.
DR   EMBL; AB202082; BAE78601.1; -; Genomic_DNA.
DR   EMBL; AL669914; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL671859; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL845439; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC102010; AAI02011.1; -; mRNA.
DR   EMBL; BC102011; AAI02012.1; -; mRNA.
DR   EMBL; BC104750; AAI04751.1; -; mRNA.
DR   CCDS; CCDS4671.1; -.
DR   RefSeq; NP_068778.1; NM_021959.2.
DR   AlphaFoldDB; O60927; -.
DR   BioGRID; 112852; 19.
DR   IntAct; O60927; 18.
DR   MINT; O60927; -.
DR   STRING; 9606.ENSP00000365963; -.
DR   GlyGen; O60927; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; O60927; -.
DR   MetOSite; O60927; -.
DR   PhosphoSitePlus; O60927; -.
DR   BioMuta; PPP1R11; -.
DR   EPD; O60927; -.
DR   jPOST; O60927; -.
DR   MassIVE; O60927; -.
DR   MaxQB; O60927; -.
DR   PaxDb; O60927; -.
DR   PeptideAtlas; O60927; -.
DR   PRIDE; O60927; -.
DR   ProteomicsDB; 49672; -.
DR   TopDownProteomics; O60927; -.
DR   Antibodypedia; 26202; 111 antibodies from 22 providers.
DR   DNASU; 6992; -.
DR   Ensembl; ENST00000376772.8; ENSP00000365963.3; ENSG00000204619.8.
DR   Ensembl; ENST00000383612.8; ENSP00000373107.4; ENSG00000206501.8.
DR   Ensembl; ENST00000431424.6; ENSP00000411038.2; ENSG00000236560.6.
DR   Ensembl; ENST00000431977.6; ENSP00000407981.2; ENSG00000237829.6.
DR   Ensembl; ENST00000436591.6; ENSP00000414808.2; ENSG00000234058.6.
DR   Ensembl; ENST00000437937.6; ENSP00000394056.2; ENSG00000233314.6.
DR   Ensembl; ENST00000448378.6; ENSP00000403557.2; ENSG00000237403.6.
DR   Ensembl; ENST00000452679.6; ENSP00000412297.2; ENSG00000227720.6.
DR   GeneID; 6992; -.
DR   KEGG; hsa:6992; -.
DR   MANE-Select; ENST00000376772.8; ENSP00000365963.3; NM_021959.3; NP_068778.1.
DR   UCSC; uc003npb.4; human.
DR   CTD; 6992; -.
DR   DisGeNET; 6992; -.
DR   GeneCards; PPP1R11; -.
DR   HGNC; HGNC:9285; PPP1R11.
DR   HPA; ENSG00000204619; Low tissue specificity.
DR   MIM; 606670; gene.
DR   neXtProt; NX_O60927; -.
DR   OpenTargets; ENSG00000204619; -.
DR   PharmGKB; PA33614; -.
DR   VEuPathDB; HostDB:ENSG00000204619; -.
DR   eggNOG; KOG4102; Eukaryota.
DR   GeneTree; ENSGT00390000001153; -.
DR   HOGENOM; CLU_098333_6_2_1; -.
DR   InParanoid; O60927; -.
DR   OMA; CILGHSR; -.
DR   OrthoDB; 1599272at2759; -.
DR   PhylomeDB; O60927; -.
DR   TreeFam; TF352541; -.
DR   PathwayCommons; O60927; -.
DR   SignaLink; O60927; -.
DR   UniPathway; UPA00143; -.
DR   BioGRID-ORCS; 6992; 640 hits in 1094 CRISPR screens.
DR   ChiTaRS; PPP1R11; human.
DR   GeneWiki; PPP1R11; -.
DR   GenomeRNAi; 6992; -.
DR   Pharos; O60927; Tbio.
DR   PRO; PR:O60927; -.
DR   Proteomes; UP000005640; Chromosome 6.
DR   RNAct; O60927; protein.
DR   Bgee; ENSG00000204619; Expressed in rectum and 98 other tissues.
DR   ExpressionAtlas; O60927; baseline and differential.
DR   Genevisible; O60927; HS.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0008157; F:protein phosphatase 1 binding; IBA:GO_Central.
DR   GO; GO:0004865; F:protein serine/threonine phosphatase inhibitor activity; IBA:GO_Central.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:UniProtKB.
DR   GO; GO:0050830; P:defense response to Gram-positive bacterium; ISS:UniProtKB.
DR   GO; GO:0001818; P:negative regulation of cytokine production; ISS:UniProtKB.
DR   GO; GO:0032515; P:negative regulation of phosphoprotein phosphatase activity; IBA:GO_Central.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
DR   DisProt; DP00219; -.
DR   InterPro; IPR011107; PPI_Ypi1.
DR   PANTHER; PTHR20835; PTHR20835; 1.
DR   Pfam; PF07491; PPI_Ypi1; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Phosphoprotein; Protein phosphatase inhibitor;
KW   Reference proteome; Transferase; Ubl conjugation; Ubl conjugation pathway.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   CHAIN           2..126
FT                   /note="E3 ubiquitin-protein ligase PPP1R11"
FT                   /id="PRO_0000239619"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          52..62
FT                   /note="Atypical RING finger domain 1"
FT                   /evidence="ECO:0000269|PubMed:27805901"
FT   REGION          70..126
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          85..94
FT                   /note="Atypical RING finger domain 2"
FT                   /evidence="ECO:0000269|PubMed:27805901"
FT   COMPBIAS        9..25
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        106..126
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   MOD_RES         73
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         74
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         75
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         77
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         109
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MUTAGEN         52
FT                   /note="H->A: Loss of function in inducing TLR2
FT                   degradation."
FT                   /evidence="ECO:0000269|PubMed:27805901"
FT   MUTAGEN         60..62
FT                   /note="CCC->SSS: Loss of function in inducing TLR2
FT                   degradation."
FT                   /evidence="ECO:0000269|PubMed:27805901"
FT   MUTAGEN         85
FT                   /note="C->S: Loss of function in inducing TLR2
FT                   degradation."
FT                   /evidence="ECO:0000269|PubMed:27805901"
FT   MUTAGEN         87
FT                   /note="H->A: Loss of function in inducing TLR2
FT                   degradation."
FT                   /evidence="ECO:0000269|PubMed:27805901"
FT   MUTAGEN         89..90
FT                   /note="HC->AS: Loss of function in inducing TLR2
FT                   degradation."
FT                   /evidence="ECO:0000269|PubMed:27805901"
FT   MUTAGEN         94
FT                   /note="H->A: Loss of function in inducing TLR2
FT                   degradation."
FT                   /evidence="ECO:0000269|PubMed:27805901"
SQ   SEQUENCE   126 AA;  13953 MW;  D6788A5AAC073549 CRC64;
     MAEAGAGLSE TVTETTVTVT TEPENRSLTI KLRKRKPEKK VEWTSDTVDN EHMGRRSSKC
     CCIYEKPRAF GESSTESDEE EEEGCGHTHC VRGHRKGRRR ATLGPTPTTP PQPPDPSQPP
     PGPMQH
 
 
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