PP1RB_MOUSE
ID PP1RB_MOUSE Reviewed; 131 AA.
AC Q8K1L5; Q9DB02;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 25-MAY-2022, entry version 115.
DE RecName: Full=E3 ubiquitin-protein ligase PPP1R11 {ECO:0000303|PubMed:27805901};
DE EC=2.3.2.27;
DE AltName: Full=Protein phosphatase 1 regulatory subunit 11;
DE AltName: Full=T-complex testis expressed protein 5;
DE Short=Tctex-5;
GN Name=Ppp1r11; Synonyms=Tctex5;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=NOD; TISSUE=Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N-3; TISSUE=Mammary tumor;
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 [3]
RP TISSUE SPECIFICITY.
RX PubMed=1718647; DOI=10.1002/dvg.1020120409;
RA Ha H., Howard C.A., Yeom Y.I., Abe K., Uehara H., Artzt K., Bennett D.;
RT "Several testis-expressed genes in the mouse T-complex have expression
RT differences between wild-type and t-mutant mice.";
RL Dev. Genet. 12:318-332(1991).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79; THR-80 AND SER-82, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Liver, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP FUNCTION, AND INTERACTION WITH TLR2 AND UBE2D2.
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 (By similarity). {ECO:0000250|UniProtKB:O60927,
CC ECO:0000269|PubMed:27805901}.
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 {ECO:0000250|UniProtKB:O60927}.
CC -!- SUBUNIT: Interacts with TLR2 and UBE2D2. {ECO:0000269|PubMed:27805901}.
CC -!- TISSUE SPECIFICITY: Expressed in testis with high level during
CC spermatogenesis. {ECO:0000269|PubMed:1718647}.
CC -!- PTM: Auto-ubiquitinated. {ECO:0000250|UniProtKB:O60927}.
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DR EMBL; AK005379; BAB23986.1; -; mRNA.
DR EMBL; AK089107; BAC40754.1; -; mRNA.
DR EMBL; AK170104; BAE41566.1; -; mRNA.
DR EMBL; BC027737; AAH27737.1; -; mRNA.
DR CCDS; CCDS28729.1; -.
DR RefSeq; NP_083908.1; NM_029632.3.
DR AlphaFoldDB; Q8K1L5; -.
DR BioGRID; 218153; 9.
DR STRING; 10090.ENSMUSP00000047202; -.
DR iPTMnet; Q8K1L5; -.
DR PhosphoSitePlus; Q8K1L5; -.
DR EPD; Q8K1L5; -.
DR MaxQB; Q8K1L5; -.
DR PaxDb; Q8K1L5; -.
DR PeptideAtlas; Q8K1L5; -.
DR PRIDE; Q8K1L5; -.
DR ProteomicsDB; 291777; -.
DR DNASU; 76497; -.
DR GeneID; 76497; -.
DR KEGG; mmu:76497; -.
DR CTD; 6992; -.
DR MGI; MGI:1923747; Ppp1r11.
DR eggNOG; KOG4102; Eukaryota.
DR InParanoid; Q8K1L5; -.
DR OrthoDB; 1599272at2759; -.
DR PhylomeDB; Q8K1L5; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 76497; 20 hits in 74 CRISPR screens.
DR ChiTaRS; Ppp1r11; mouse.
DR PRO; PR:Q8K1L5; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q8K1L5; protein.
DR GO; GO:0005737; C:cytoplasm; IDA: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:0004864; F:protein phosphatase inhibitor activity; IDA:UniProtKB.
DR GO; GO:0004865; F:protein serine/threonine phosphatase inhibitor activity; IBA:GO_Central.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISO:MGI.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IMP:UniProtKB.
DR GO; GO:0001818; P:negative regulation of cytokine production; IMP: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 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:0000250|UniProtKB:O60927"
FT CHAIN 2..131
FT /note="E3 ubiquitin-protein ligase PPP1R11"
FT /id="PRO_0000239621"
FT REGION 1..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 57..67
FT /note="Atypical RING finger domain 1"
FT /evidence="ECO:0000250|UniProtKB:O60927"
FT REGION 90..99
FT /note="Atypical RING finger domain 2"
FT /evidence="ECO:0000250|UniProtKB:O60927"
FT COMPBIAS 8..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..67
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..131
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 78
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60927"
FT MOD_RES 79
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 80
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 82
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 114
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O60927"
FT CONFLICT 34
FT /note="I -> T (in Ref. 1; BAB23986)"
FT /evidence="ECO:0000305"
FT CONFLICT 123
FT /note="Q -> K (in Ref. 1; BAB23986)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 131 AA; 14544 MW; 533FCEC7128FA14C CRC64;
MAETGAGISE TVTETTVTET TVTETTEPEN QSLIMKLRKR KPEKKVEWSS DTVDNEHMGR
RSSKCCCIYE KPRAFGESST ESDEDEEEGC SHKHCVRGHR KGRRPTTPAP TPTTPPQPPD
PSQPPPGPMQ H
