PP1RB_XENTR
ID PP1RB_XENTR Reviewed; 119 AA.
AC Q6GLB0;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 68.
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; ORFNames=TEgg002a15.1;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Egg;
RG Sanger Xenopus tropicalis EST/cDNA project;
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Atypical E3 ubiquitin-protein ligase which ubiquitinates TLR2
CC at 'Lys-754' leading to its degradation by the proteasome. Inhibitor of
CC protein phosphatase 1. {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.
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DR EMBL; CR760958; CAJ82067.1; -; mRNA.
DR EMBL; BC074590; AAH74590.1; -; mRNA.
DR RefSeq; NP_001004815.1; NM_001004815.1.
DR AlphaFoldDB; Q6GLB0; -.
DR STRING; 8364.ENSXETP00000007163; -.
DR PaxDb; Q6GLB0; -.
DR DNASU; 448065; -.
DR GeneID; 448065; -.
DR KEGG; xtr:448065; -.
DR CTD; 6992; -.
DR Xenbase; XB-GENE-999517; ppp1r11.
DR eggNOG; KOG4102; Eukaryota.
DR InParanoid; Q6GLB0; -.
DR OrthoDB; 1599272at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000008143; Chromosome 8.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000035391; Expressed in brain and 16 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 Protein phosphatase inhibitor; Reference proteome; Transferase;
KW Ubl conjugation pathway.
FT CHAIN 1..119
FT /note="E3 ubiquitin-protein ligase PPP1R11"
FT /id="PRO_0000239626"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 55..65
FT /note="Atypical RING finger domain 1"
FT /evidence="ECO:0000250|UniProtKB:O60927"
FT REGION 87..96
FT /note="Atypical RING finger domain 2"
FT /evidence="ECO:0000250|UniProtKB:O60927"
FT REGION 96..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..112
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 119 AA; 12988 MW; 2A9650DEDC2FA0D2 CRC64;
MAESSGPTAG GGATSSTVTT ESDTQPEHRS LTLKLRKRKP DKKVEWTCDT VDNENLGRRS
SKCCCIYEKP RPFGESSSES EDEDDCCESA HCIRGHKKAT SGSKETPSSH HDKTGSMQH
