PP1RA_MOUSE
ID PP1RA_MOUSE Reviewed; 888 AA.
AC Q80W00; B1B179; Q811B6; Q8C6T7; Q8K2U8;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Serine/threonine-protein phosphatase 1 regulatory subunit 10;
DE AltName: Full=MHC class I region proline-rich protein CAT53;
GN Name=Ppp1r10; Synonyms=Cat53, Pnuts;
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 [MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Raha-Chowdhury R., Andrews S.R., Gruen J.R., Weissman S.M.;
RT "Genes from major histocompatibility complex (MHC) class I region from HLA-
RT C to HLA-A.";
RL Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and Mammary cancer;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-273.
RC STRAIN=C57BL/6J; TISSUE=Lung;
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, 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 [6]
RP IDENTIFICATION IN THE PTW/PP1 PHOSPHATASE COMPLEX, FUNCTION, SUBCELLULAR
RP LOCATION, INTERACTION WITH PPP1CA; TOX4 AND WDR82, AND MUTAGENESIS OF
RP TRP-401.
RX PubMed=20516061; DOI=10.1074/jbc.m110.109801;
RA Lee J.H., You J., Dobrota E., Skalnik D.G.;
RT "Identification and characterization of a novel human PP1 phosphatase
RT complex.";
RL J. Biol. Chem. 285:24466-24476(2010).
RN [7]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-693 AND ARG-737, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Scaffold protein which mediates the formation of the PTW/PP1
CC phosphatase complex by providing a binding platform to each component
CC of the complex. The PTW/PP1 phosphatase complex plays a role in the
CC control of chromatin structure and cell cycle progression during the
CC transition from mitosis into interphase. Mediates interaction of WDR82
CC and PPP1CA. Inhibitor of PPP1CA and PPP1CC phosphatase activities. Has
CC inhibitory activity on PPP1CA only when phosphorylated. Binds to mRNA,
CC single-stranded DNA (ssDNA), poly(A) and poly(G) homopolymers.
CC {ECO:0000269|PubMed:20516061}.
CC -!- SUBUNIT: Component of the PTW/PP1 phosphatase complex, composed of
CC PPP1R10/PNUTS, TOX4, WDR82, and PPP1CA or PPP1CB or PPP1CC. Interacts
CC with PPP1CC (By similarity). Interacts with PPP1CA, WDR82 and TOX4.
CC {ECO:0000250, ECO:0000269|PubMed:20516061}.
CC -!- INTERACTION:
CC Q80W00; Q15554: TERF2; Xeno; NbExp=3; IntAct=EBI-2553719, EBI-706637;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00649}.
CC Note=Found in discrete nucleoplasmic bodies and within nucleoli (By
CC similarity). Associates with chromatin during interphase, excluded from
CC condensed chromosomes during early mitosis and is reloaded onto
CC chromosomes at the late telophase. {ECO:0000250,
CC ECO:0000269|PubMed:20516061}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q80W00-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q80W00-2; Sequence=VSP_013155;
CC -!- PTM: Phosphorylated on Thr-398 by PKA within the region necessary for
CC interaction with PPP1CA. {ECO:0000250}.
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DR EMBL; AJ504718; CAD44294.1; -; mRNA.
DR EMBL; CR974451; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC029765; AAH29765.1; -; mRNA.
DR EMBL; BC052059; AAH52059.1; -; mRNA.
DR EMBL; AK053183; BAC35301.1; -; mRNA.
DR CCDS; CCDS50098.1; -. [Q80W00-1]
DR RefSeq; NP_001157290.1; NM_001163818.1. [Q80W00-1]
DR RefSeq; XP_006524679.1; XM_006524616.2. [Q80W00-1]
DR RefSeq; XP_006524680.1; XM_006524617.2. [Q80W00-1]
DR RefSeq; XP_006524681.1; XM_006524618.1.
DR RefSeq; XP_006524682.1; XM_006524619.2. [Q80W00-1]
DR AlphaFoldDB; Q80W00; -.
DR BMRB; Q80W00; -.
DR SMR; Q80W00; -.
DR BioGRID; 206343; 12.
DR DIP; DIP-48511N; -.
DR IntAct; Q80W00; 10.
DR STRING; 10090.ENSMUSP00000084461; -.
DR iPTMnet; Q80W00; -.
DR PhosphoSitePlus; Q80W00; -.
DR EPD; Q80W00; -.
DR jPOST; Q80W00; -.
DR MaxQB; Q80W00; -.
DR PaxDb; Q80W00; -.
DR PeptideAtlas; Q80W00; -.
DR PRIDE; Q80W00; -.
DR ProteomicsDB; 291775; -. [Q80W00-1]
DR ProteomicsDB; 291776; -. [Q80W00-2]
DR Antibodypedia; 26382; 145 antibodies from 30 providers.
DR DNASU; 52040; -.
DR Ensembl; ENSMUST00000087210; ENSMUSP00000084460; ENSMUSG00000039220. [Q80W00-1]
DR Ensembl; ENSMUST00000087211; ENSMUSP00000084461; ENSMUSG00000039220. [Q80W00-1]
DR GeneID; 52040; -.
DR KEGG; mmu:52040; -.
DR UCSC; uc033hdm.1; mouse. [Q80W00-1]
DR CTD; 5514; -.
DR MGI; MGI:1289273; Ppp1r10.
DR VEuPathDB; HostDB:ENSMUSG00000039220; -.
DR eggNOG; ENOG502QQ2I; Eukaryota.
DR GeneTree; ENSGT00940000159263; -.
DR HOGENOM; CLU_019410_0_0_1; -.
DR InParanoid; Q80W00; -.
DR OMA; MGKNCKY; -.
DR OrthoDB; 999354at2759; -.
DR PhylomeDB; Q80W00; -.
DR TreeFam; TF105541; -.
DR BioGRID-ORCS; 52040; 27 hits in 77 CRISPR screens.
DR ChiTaRS; Ppp1r10; mouse.
DR PRO; PR:Q80W00; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q80W00; protein.
DR Bgee; ENSMUSG00000039220; Expressed in primary oocyte and 66 other tissues.
DR ExpressionAtlas; Q80W00; baseline and differential.
DR Genevisible; Q80W00; MM.
DR GO; GO:0000785; C:chromatin; IDA:UniProtKB.
DR GO; GO:0000781; C:chromosome, telomeric region; ISO:MGI.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0072357; C:PTW/PP1 phosphatase complex; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008157; F:protein phosphatase 1 binding; ISO:MGI.
DR GO; GO:0004864; F:protein phosphatase inhibitor activity; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0010667; P:negative regulation of cardiac muscle cell apoptotic process; ISO:MGI.
DR GO; GO:1904290; P:negative regulation of mitotic DNA damage checkpoint; ISO:MGI.
DR GO; GO:0032206; P:positive regulation of telomere maintenance; ISO:MGI.
DR Gene3D; 1.20.930.10; -; 1.
DR InterPro; IPR003617; TFIIS/CRSP70_N_sub.
DR InterPro; IPR035441; TFIIS/LEDGF_dom_sf.
DR InterPro; IPR017923; TFIIS_N.
DR InterPro; IPR000571; Znf_CCCH.
DR InterPro; IPR036855; Znf_CCCH_sf.
DR Pfam; PF08711; Med26; 1.
DR Pfam; PF00642; zf-CCCH; 1.
DR SMART; SM00509; TFS2N; 1.
DR SMART; SM00356; ZnF_C3H1; 1.
DR SUPFAM; SSF47676; SSF47676; 1.
DR SUPFAM; SSF90229; SSF90229; 1.
DR PROSITE; PS51319; TFIIS_N; 1.
DR PROSITE; PS50103; ZF_C3H1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; DNA-binding; Isopeptide bond; Metal-binding;
KW Methylation; Nucleus; Phosphoprotein; Protein phosphatase inhibitor;
KW Reference proteome; RNA-binding; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..888
FT /note="Serine/threonine-protein phosphatase 1 regulatory
FT subunit 10"
FT /id="PRO_0000071512"
FT DOMAIN 73..147
FT /note="TFIIS N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00649"
FT ZN_FING 854..882
FT /note="C3H1-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT REGION 1..348
FT /note="Interaction with TOX4"
FT /evidence="ECO:0000269|PubMed:20516061"
FT REGION 147..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 247..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 306..400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 382..450
FT /note="Essential for PPP1CA inhibition"
FT /evidence="ECO:0000250"
FT REGION 388..417
FT /note="Necessary for interaction with PPP1CA"
FT /evidence="ECO:0000269|PubMed:20516061"
FT REGION 393..408
FT /note="Necessary for interaction with PPP1CC"
FT /evidence="ECO:0000250"
FT REGION 418..619
FT /note="Interaction with WDR82"
FT /evidence="ECO:0000269|PubMed:20516061"
FT REGION 534..853
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 420..423
FT /note="PP1-binding motif"
FT COMPBIAS 151..200
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 320..335
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 336..359
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 584..600
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 627..677
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 800..851
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 313
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96QC0"
FT MOD_RES 382
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96QC0"
FT MOD_RES 398
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O55000"
FT MOD_RES 545
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96QC0"
FT MOD_RES 591
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96QC0"
FT MOD_RES 665
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q96QC0"
FT MOD_RES 693
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 737
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT CROSSLNK 179
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96QC0"
FT CROSSLNK 262
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96QC0"
FT VAR_SEQ 756..769
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_013155"
FT MUTAGEN 401
FT /note="W->A: Loss of interaction with PPP1CA but no effect
FT on interaction with TOX4 or WDR82. Cell cycle arrest at
FT mitosis and cell death. Exhibits normal association with
FT chromosomes but shows defects in the process of chromosome
FT decondensation at late telophase."
FT /evidence="ECO:0000269|PubMed:20516061"
FT CONFLICT 30
FT /note="G -> A (in Ref. 1; CAD44294)"
FT /evidence="ECO:0000305"
FT CONFLICT 85
FT /note="T -> N (in Ref. 1; CAD44294)"
FT /evidence="ECO:0000305"
FT CONFLICT 171
FT /note="P -> H (in Ref. 1; CAD44294)"
FT /evidence="ECO:0000305"
FT CONFLICT 239
FT /note="K -> N (in Ref. 1; CAD44294)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 888 AA; 94372 MW; F32889274EF3632D CRC64;
MGSGPIDPKE LLKGLDSFLT RDGEVKSVDG ISKIFSLMKE ARKMVSRCTY LNIILQTRAP
EVLVKFIDVG GYKLLNNWLT YSKTTNNIPL LQQILLTLQH LPLTVDHLKQ NNTAKLVKQL
SKSSEDEELR KLASVLVSDW MAVIRSQSST QPAEKDKKKR KEEGKSRTTL PERPLTEVKA
ETRAEEAPEK KKEKPKSLRT TAPSHAKFRS TGLELDTPSL VPVKKNSSTV VVSDKYNLKP
IPLKRQSATA APGDAAPPAE KKYKPLNTAP NTTKEIKVKI IPPQPMEGLG FLDALNSAPV
PGIKIKKKKK VLSPTAAKPS PFEGKTSTEQ STAKPSSPEP APPAEPMDTD RPGTPVPPVE
VPELMDAASS EPGALDAKPV DSPGDPNQLT RKGRKRKTVT WPEEGKLREY FYFELDETER
VNVNKIKDFG EAAKREILSD RHAFETARRL SHDNMEEKVP WVCPRPLVLP SPLVIPGSNS
QERYIQAERE KGILQELFLN KESPHEPDPE PYEPIPPKLI PLDEECAMDE TPYVETLEPG
GSGGSPDGAG GSKLPPVLAN LMGSMGAGKS PQGPGGGGIN VQEILTSIMG SPNSHPSEEL
LKQPDYSDKL KQMLVPHGLL GPGPVANGFP PGGPGGPKGM QHFPPGPGGP MPGPHGGPGG
PVGPRLLGPP PPSRGGDPFW DGPGDPMRGG PMRGGPGPAP GPYHRGRGGR GGNEPPPPPP
FRGARGGRSG GGPPNGRGGP GGGGMVGGGG HRPHEGPGGS MGSGHRSHDG PGGNMGSGHR
SHDGPGGNMG GSGGHRSHEG PGHGGPHGHR PHDVPSHRGH DHRGPPPHEH RGHDGHGGGG
HRGHDGGHSH GGDMSNRPVC RHFMMKGNCR YENNCAFYHP GVNGPPLP
