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Serine/threonine-protein phosphatase 1 regulatory subunit 10 (MHC class I region proline-rich protein CAT53)

 PP1RA_MOUSE             Reviewed;         888 AA.
Q80W00; B1B179; Q811B6; Q8C6T7; Q8K2U8;
15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
01-JUN-2003, sequence version 1.
23-MAY-2018, entry version 135.
RecName: Full=Serine/threonine-protein phosphatase 1 regulatory subunit 10;
AltName: Full=MHC class I region proline-rich protein CAT53;
Name=Ppp1r10; Synonyms=Cat53, Pnuts;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
STRAIN=C57BL/6J; TISSUE=Brain;
Raha-Chowdhury R., Andrews S.R., Gruen J.R., Weissman S.M.;
"Genes from major histocompatibility complex (MHC) class I region from
HLA-C to HLA-A.";
Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and Mammary cancer;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-273.
STRAIN=C57BL/6J; TISSUE=Lung;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Kidney, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[6]
IDENTIFICATION IN THE PTW/PP1 PHOSPHATASE COMPLEX, FUNCTION,
SUBCELLULAR LOCATION, INTERACTION WITH PPP1CA; TOX4 AND WDR82, AND
MUTAGENESIS OF TRP-401.
PubMed=20516061; DOI=10.1074/jbc.M110.109801;
Lee J.H., You J., Dobrota E., Skalnik D.G.;
"Identification and characterization of a novel human PP1 phosphatase
complex.";
J. Biol. Chem. 285:24466-24476(2010).
[7]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-693 AND ARG-737, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, and Embryo;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
-!- FUNCTION: Scaffold protein which mediates the formation of the
PTW/PP1 phosphatase complex by providing a binding platform to
each component of the complex. The PTW/PP1 phosphatase complex
plays a role in the control of chromatin structure and cell cycle
progression during the transition from mitosis into interphase.
Mediates interaction of WDR82 and PPP1CA. Inhibitor of PPP1CA and
PPP1CC phosphatase activities. Has inhibitory activity on PPP1CA
only when phosphorylated. Binds to mRNA, single-stranded DNA
(ssDNA), poly(A) and poly(G) homopolymers.
{ECO:0000269|PubMed:20516061}.
-!- SUBUNIT: Component of the PTW/PP1 phosphatase complex, composed of
PPP1R10/PNUTS, TOX4, WDR82, and PPP1CA or PPP1CB or PPP1CC.
Interacts with PPP1CC (By similarity). Interacts with PPP1CA,
WDR82 and TOX4. {ECO:0000250, ECO:0000269|PubMed:20516061}.
-!- INTERACTION:
Q15554:TERF2 (xeno); NbExp=3; IntAct=EBI-2553719, EBI-706637;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
ProRule:PRU00649}. Note=Found in discrete nucleoplasmic bodies and
within nucleoli (By similarity). Associates with chromatin during
interphase, excluded from condensed chromosomes during early
mitosis and is reloaded onto chromosomes at the late telophase.
{ECO:0000250, ECO:0000269|PubMed:20516061}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q80W00-1; Sequence=Displayed;
Name=2;
IsoId=Q80W00-2; Sequence=VSP_013155;
Note=No experimental confirmation available.;
-!- PTM: Phosphorylated on Thr-398 by PKA within the region necessary
for interaction with PPP1CA. {ECO:0000250}.
-----------------------------------------------------------------------
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EMBL; AJ504718; CAD44294.1; -; mRNA.
EMBL; CR974451; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC029765; AAH29765.1; -; mRNA.
EMBL; BC052059; AAH52059.1; -; mRNA.
EMBL; AK053183; BAC35301.1; -; mRNA.
CCDS; CCDS50098.1; -. [Q80W00-1]
RefSeq; NP_001157290.1; NM_001163818.1. [Q80W00-1]
RefSeq; XP_006524679.1; XM_006524616.2. [Q80W00-1]
RefSeq; XP_006524680.1; XM_006524617.2. [Q80W00-1]
RefSeq; XP_006524681.1; XM_006524618.1.
RefSeq; XP_006524682.1; XM_006524619.2. [Q80W00-1]
UniGene; Mm.29385; -.
ProteinModelPortal; Q80W00; -.
SMR; Q80W00; -.
BioGrid; 206343; 10.
DIP; DIP-48511N; -.
IntAct; Q80W00; 11.
MINT; Q80W00; -.
STRING; 10090.ENSMUSP00000084460; -.
iPTMnet; Q80W00; -.
PhosphoSitePlus; Q80W00; -.
PaxDb; Q80W00; -.
PeptideAtlas; Q80W00; -.
PRIDE; Q80W00; -.
Ensembl; ENSMUST00000087210; ENSMUSP00000084460; ENSMUSG00000039220. [Q80W00-1]
Ensembl; ENSMUST00000087211; ENSMUSP00000084461; ENSMUSG00000039220. [Q80W00-1]
GeneID; 52040; -.
KEGG; mmu:52040; -.
UCSC; uc033hdm.1; mouse. [Q80W00-1]
CTD; 5514; -.
MGI; MGI:1289273; Ppp1r10.
eggNOG; ENOG410IGTC; Eukaryota.
eggNOG; ENOG410XP4M; LUCA.
GeneTree; ENSGT00530000063820; -.
HOGENOM; HOG000049285; -.
HOVERGEN; HBG053646; -.
InParanoid; Q80W00; -.
KO; K17552; -.
OMA; TVTWPEE; -.
OrthoDB; EOG091G07K1; -.
PhylomeDB; Q80W00; -.
TreeFam; TF105541; -.
ChiTaRS; Ppp1r10; mouse.
PRO; PR:Q80W00; -.
Proteomes; UP000000589; Chromosome 17.
Bgee; ENSMUSG00000039220; -.
CleanEx; MM_PPP1R10; -.
ExpressionAtlas; Q80W00; baseline and differential.
Genevisible; Q80W00; MM.
GO; GO:0000785; C:chromatin; IDA:UniProtKB.
GO; GO:0016604; C:nuclear body; ISO:MGI.
GO; GO:0000784; C:nuclear chromosome, telomeric region; IEA:Ensembl.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0072357; C:PTW/PP1 phosphatase complex; IDA:UniProtKB.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004864; F:protein phosphatase inhibitor activity; IEA:UniProtKB-KW.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
GO; GO:0010667; P:negative regulation of cardiac muscle cell apoptotic process; ISO:MGI.
GO; GO:1904290; P:negative regulation of mitotic DNA damage checkpoint; ISO:MGI.
GO; GO:0032206; P:positive regulation of telomere maintenance; ISO:MGI.
Gene3D; 1.20.930.10; -; 1.
InterPro; IPR003617; TFIIS/CRSP70_N_sub.
InterPro; IPR035441; TFIIS/LEDGF_dom_sf.
InterPro; IPR017923; TFIIS_N.
InterPro; IPR000571; Znf_CCCH.
InterPro; IPR036855; Znf_CCCH_sf.
Pfam; PF08711; Med26; 1.
Pfam; PF00642; zf-CCCH; 1.
SMART; SM00509; TFS2N; 1.
SMART; SM00356; ZnF_C3H1; 1.
SUPFAM; SSF47676; SSF47676; 1.
SUPFAM; SSF90229; SSF90229; 1.
PROSITE; PS51319; TFIIS_N; 1.
PROSITE; PS50103; ZF_C3H1; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; DNA-binding; Isopeptide bond;
Metal-binding; Methylation; Nucleus; Phosphoprotein;
Protein phosphatase inhibitor; Reference proteome; RNA-binding;
Ubl conjugation; Zinc; Zinc-finger.
CHAIN 1 888 Serine/threonine-protein phosphatase 1
regulatory subunit 10.
/FTId=PRO_0000071512.
DOMAIN 73 147 TFIIS N-terminal. {ECO:0000255|PROSITE-
ProRule:PRU00649}.
ZN_FING 854 882 C3H1-type. {ECO:0000255|PROSITE-
ProRule:PRU00723}.
REGION 1 348 Interaction with TOX4.
{ECO:0000269|PubMed:20516061}.
REGION 382 450 Essential for PPP1CA inhibition.
{ECO:0000250}.
REGION 388 417 Necessary for interaction with PPP1CA.
{ECO:0000269|PubMed:20516061}.
REGION 393 408 Necessary for interaction with PPP1CC.
{ECO:0000250}.
REGION 418 619 Interaction with WDR82.
{ECO:0000269|PubMed:20516061}.
MOTIF 420 423 PP1-binding motif.
COMPBIAS 304 310 Poly-Lys.
COMPBIAS 540 852 Gly-rich.
MOD_RES 313 313 Phosphoserine.
{ECO:0000250|UniProtKB:Q96QC0}.
MOD_RES 382 382 Phosphoserine.
{ECO:0000250|UniProtKB:Q96QC0}.
MOD_RES 398 398 Phosphothreonine.
{ECO:0000250|UniProtKB:O55000}.
MOD_RES 545 545 Phosphoserine.
{ECO:0000250|UniProtKB:Q96QC0}.
MOD_RES 591 591 Phosphoserine.
{ECO:0000250|UniProtKB:Q96QC0}.
MOD_RES 665 665 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:Q96QC0}.
MOD_RES 693 693 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 737 737 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
CROSSLNK 179 179 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q96QC0}.
CROSSLNK 262 262 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q96QC0}.
VAR_SEQ 756 769 Missing (in isoform 2).
{ECO:0000303|Ref.1}.
/FTId=VSP_013155.
MUTAGEN 401 401 W->A: Loss of interaction with PPP1CA but
no effect on interaction with TOX4 or
WDR82. Cell cycle arrest at mitosis and
cell death. Exhibits normal association
with chromosomes but shows defects in the
process of chromosome decondensation at
late telophase.
{ECO:0000269|PubMed:20516061}.
CONFLICT 30 30 G -> A (in Ref. 1; CAD44294).
{ECO:0000305}.
CONFLICT 85 85 T -> N (in Ref. 1; CAD44294).
{ECO:0000305}.
CONFLICT 171 171 P -> H (in Ref. 1; CAD44294).
{ECO:0000305}.
CONFLICT 239 239 K -> N (in Ref. 1; CAD44294).
{ECO:0000305}.
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


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