PP1RB_PANTR
ID PP1RB_PANTR Reviewed; 126 AA.
AC Q7YR30;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=E3 ubiquitin-protein ligase PPP1R11;
DE EC=2.3.2.27;
DE AltName: Full=Protein phosphatase 1 regulatory subunit 11;
GN Name=PPP1R11;
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12799463; DOI=10.1073/pnas.1230533100;
RA Anzai T., Shiina T., Kimura N., Yanagiya K., Kohara S., Shigenari A.,
RA Yamagata T., Kulski J.K., Naruse T.K., Fujimori Y., Fukuzumi Y.,
RA Yamazaki M., Tashiro H., Iwamoto C., Umehara Y., Imanishi T., Meyer A.,
RA Ikeo K., Gojobori T., Bahram S., Inoko H.;
RT "Comparative sequencing of human and chimpanzee MHC class I regions unveils
RT insertions/deletions as the major path to genomic divergence.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7708-7713(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16702430; DOI=10.1534/genetics.106.057034;
RA Shiina T., Ota M., Shimizu S., Katsuyama Y., Hashimoto N., Takasu M.,
RA Anzai T., Kulski J.K., Kikkawa E., Naruse T., Kimura N., Yanagiya K.,
RA Watanabe A., Hosomichi K., Kohara S., Iwamoto C., Umehara Y., Meyer A.,
RA Wanner V., Sano K., Macquin C., Ikeo K., Tokunaga K., Gojobori T.,
RA Inoko H., Bahram S.;
RT "Rapid evolution of major histocompatibility complex class I genes in
RT primates generates new disease alleles in humans via hitchhiking
RT diversity.";
RL Genetics 173:1555-1570(2006).
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. Inhibitor of protein phosphatase 1.
CC {ECO:0000250|UniProtKB:O60927}.
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; Evidence={ECO:0000250|UniProtKB:O60927};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with TLR2 and UBE2D2.
CC {ECO:0000250|UniProtKB:Q8K1L5}.
CC -!- PTM: Auto-ubiquitinated. {ECO:0000250|UniProtKB:O60927}.
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DR EMBL; BA000041; BAC78187.1; -; Genomic_DNA.
DR EMBL; AB210195; BAE92810.1; -; Genomic_DNA.
DR EMBL; AB210196; BAE92813.1; -; Genomic_DNA.
DR RefSeq; NP_001065285.1; NM_001071817.1.
DR AlphaFoldDB; Q7YR30; -.
DR STRING; 9598.ENSPTRP00000030557; -.
DR PaxDb; Q7YR30; -.
DR Ensembl; ENSPTRT00000109690; ENSPTRP00000084274; ENSPTRG00000042828.
DR GeneID; 742158; -.
DR KEGG; ptr:742158; -.
DR CTD; 6992; -.
DR VGNC; VGNC:11182; PPP1R11.
DR eggNOG; KOG4102; Eukaryota.
DR GeneTree; ENSGT00390000001153; -.
DR HOGENOM; CLU_098333_6_2_1; -.
DR InParanoid; Q7YR30; -.
DR OMA; CILGHSR; -.
DR OrthoDB; 1599272at2759; -.
DR TreeFam; TF352541; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000002277; Chromosome 6.
DR Bgee; ENSPTRG00000042828; Expressed in Brodmann (1909) area 10 and 21 other tissues.
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; ISS: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; ISS:UniProtKB.
DR InterPro; IPR011107; PPI_Ypi1.
DR PANTHER; PTHR20835; PTHR20835; 1.
DR Pfam; PF07491; PPI_Ypi1; 1.
PE 3: Inferred from homology;
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:0000250|UniProtKB:O60927"
FT CHAIN 2..126
FT /note="E3 ubiquitin-protein ligase PPP1R11"
FT /id="PRO_0000239622"
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:0000250|UniProtKB:O60927"
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:0000250|UniProtKB:O60927"
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:0000250|UniProtKB:O60927"
FT MOD_RES 73
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60927"
FT MOD_RES 74
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60927"
FT MOD_RES 75
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O60927"
FT MOD_RES 77
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60927"
FT MOD_RES 109
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O60927"
SQ SEQUENCE 126 AA; 13953 MW; D6788A5AAC073549 CRC64;
MAEAGAGLSE TVTETTVTVT TEPENRSLTI KLRKRKPEKK VEWTSDTVDN EHMGRRSSKC
CCIYEKPRAF GESSTESDEE EEEGCGHTHC VRGHRKGRRR ATLGPTPTTP PQPPDPSQPP
PGPMQH
