ID   PP1RB_DANRE             Reviewed;         122 AA.
AC   Q568K2;
DT   13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 93.
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=zgc:110245;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Ovary;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-20, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RC   TISSUE=Embryo;
RX   PubMed=18307296; DOI=10.1021/pr700667w;
RA   Lemeer S., Pinkse M.W.H., Mohammed S., van Breukelen B., den Hertog J.,
RA   Slijper M., Heck A.J.R.;
RT   "Online automated in vivo zebrafish phosphoproteomics: from large-scale
RT   analysis down to a single embryo.";
RL   J. Proteome Res. 7:1555-1564(2008).
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.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BC092823; AAH92823.1; -; mRNA.
DR   RefSeq; NP_001017627.1; NM_001017627.1.
DR   AlphaFoldDB; Q568K2; -.
DR   STRING; 7955.ENSDARP00000052351; -.
DR   iPTMnet; Q568K2; -.
DR   PaxDb; Q568K2; -.
DR   Ensembl; ENSDART00000052352; ENSDARP00000052351; ENSDARG00000036063.
DR   GeneID; 550290; -.
DR   KEGG; dre:550290; -.
DR   CTD; 6992; -.
DR   ZFIN; ZDB-GENE-050417-99; ppp1r11.
DR   eggNOG; KOG4102; Eukaryota.
DR   GeneTree; ENSGT00390000001153; -.
DR   HOGENOM; CLU_098333_6_2_1; -.
DR   InParanoid; Q568K2; -.
DR   OMA; CILGHSR; -.
DR   OrthoDB; 1599272at2759; -.
DR   PhylomeDB; Q568K2; -.
DR   TreeFam; TF352541; -.
DR   UniPathway; UPA00143; -.
DR   PRO; PR:Q568K2; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 19.
DR   Bgee; ENSDARG00000036063; Expressed in mature ovarian follicle and 26 other tissues.
DR   ExpressionAtlas; Q568K2; baseline and differential.
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   1: Evidence at protein level;
KW   Phosphoprotein; Protein phosphatase inhibitor; Reference proteome;
KW   Transferase; Ubl conjugation pathway.
FT   CHAIN           1..122
FT                   /note="E3 ubiquitin-protein ligase PPP1R11"
FT                   /id="PRO_0000239624"
FT   REGION          1..33
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          72..122
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          88..97
FT                   /note="Atypical RING finger domain 2"
FT                   /evidence="ECO:0000250|UniProtKB:O60927"
FT   COMPBIAS        1..27
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         20
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:18307296"
SQ   SEQUENCE   122 AA;  13106 MW;  9281E79398E495EB CRC64;
     MAEVPGTSSE TITETVQTGT PPPPQQEGRS LTIKLRKRKT EKKVEWSSDT VDNEHLGRRS
     SKCCCIYEKP RQFGESSSES EGDDEEGCGS AHCILGHGRR GHGQREGGGT TVPPSSGGTN
     PH