PP1RA_HUMAN
ID PP1RA_HUMAN Reviewed; 940 AA.
AC Q96QC0; O00405;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Serine/threonine-protein phosphatase 1 regulatory subunit 10;
DE AltName: Full=MHC class I region proline-rich protein CAT53;
DE AltName: Full=PP1-binding protein of 114 kDa;
DE AltName: Full=Phosphatase 1 nuclear targeting subunit;
DE AltName: Full=Protein FB19;
DE AltName: Full=p99;
GN Name=PPP1R10; Synonyms=CAT53, FB19, PNUTS;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=9784381; DOI=10.1006/bbrc.1998.9354;
RA Totaro A., Grifa A., Carella M., Rommens J.M., Valentino M.A., Roetto A.,
RA Zelante L., Gasparini P.;
RT "Cloning of a new gene (FB19) within HLA class I region.";
RL Biochem. Biophys. Res. Commun. 250:555-557(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RA Raha-Chowdhury R., Andrews S.R., Gruen J.R.;
RT "CAT53: a protein phosphatase 1 nuclear targeting subunit encoded in MHC
RT class 1 may take part in memory and learning.";
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Shiina S., Tamiya G., Oka A., Inoko H.;
RT "Homo sapiens 2,229,817bp genomic DNA of 6p21.3 HLA class I region.";
RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Shiina T., Ota M., Katsuyama Y., Hashimoto N., Inoko H.;
RT "Genome diversity in HLA: a new strategy for detection of genetic
RT polymorphisms in expressed genes within the HLA class III and class I
RT regions.";
RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [6]
RP PROTEIN SEQUENCE OF 164-173; 261-270; 410-413; 437-444 AND 483-488,
RP FUNCTION IN PPP1CA AND PPP1CC INHIBITION, INTERACTION WITH PPP1CC,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Cervix carcinoma;
RX PubMed=9450550; DOI=10.1016/s0014-5793(97)01485-3;
RA Kreivi J.P., Trinkle-Mulcahy L., Lyon C.E., Morrice N.A., Cohen P.,
RA Lamond A.I.;
RT "Purification and characterisation of p99, a nuclear modulator of protein
RT phosphatase 1 activity.";
RL FEBS Lett. 420:57-62(1997).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-256, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-313 AND SER-591, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-256; SER-313 AND SER-591, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-313, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-256; SER-313 AND SER-398, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-313; SER-382; SER-545 AND
RP SER-591, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [17]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-665 AND ARG-693, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
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).
RN [18]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-179 AND LYS-262, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
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 (By
CC similarity). {ECO:0000250, ECO:0000269|PubMed:9450550}.
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. Interacts with PPP1CA, WDR82 and TOX4 (By similarity).
CC {ECO:0000250}.
CC -!- INTERACTION:
CC Q96QC0; P62136: PPP1CA; NbExp=4; IntAct=EBI-1210346, EBI-357253;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00649,
CC ECO:0000269|PubMed:9450550}. Note=Found in discrete nucleoplasmic
CC bodies and within nucleoli. Associates with chromatin during
CC interphase, excluded from condensed chromosomes during early mitosis
CC and is reloaded onto chromosomes at the late telophase (By similarity).
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in heart, brain, placenta, lung, liver,
CC skeletal muscle, kidney and pancreas. {ECO:0000269|PubMed:9450550,
CC ECO:0000269|PubMed:9784381}.
CC -!- PTM: Phosphorylated on Ser-398 by PKA within the region necessary for
CC interaction with PPP1CA. {ECO:0000250}.
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DR EMBL; Y13247; CAA73697.1; -; mRNA.
DR EMBL; AJ544537; CAD67521.1; -; mRNA.
DR EMBL; BA000025; BAB63324.1; -; Genomic_DNA.
DR EMBL; AB088097; BAC54929.1; -; Genomic_DNA.
DR EMBL; AL662800; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL662825; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX248507; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS4681.1; -.
DR PIR; JE0291; JE0291.
DR RefSeq; NP_002705.2; NM_002714.3.
DR RefSeq; XP_006715193.1; XM_006715130.2.
DR RefSeq; XP_011513024.1; XM_011514722.1.
DR RefSeq; XP_016866484.1; XM_017010995.1.
DR PDB; 6ZV2; NMR; -; A=1-147.
DR PDBsum; 6ZV2; -.
DR AlphaFoldDB; Q96QC0; -.
DR SMR; Q96QC0; -.
DR BioGRID; 111506; 177.
DR CORUM; Q96QC0; -.
DR DIP; DIP-39343N; -.
DR ELM; Q96QC0; -.
DR IntAct; Q96QC0; 45.
DR MINT; Q96QC0; -.
DR STRING; 9606.ENSP00000365694; -.
DR iPTMnet; Q96QC0; -.
DR PhosphoSitePlus; Q96QC0; -.
DR BioMuta; PPP1R10; -.
DR DMDM; 61214507; -.
DR CPTAC; CPTAC-993; -.
DR EPD; Q96QC0; -.
DR jPOST; Q96QC0; -.
DR MassIVE; Q96QC0; -.
DR MaxQB; Q96QC0; -.
DR PaxDb; Q96QC0; -.
DR PeptideAtlas; Q96QC0; -.
DR PRIDE; Q96QC0; -.
DR ProteomicsDB; 77851; -.
DR TopDownProteomics; Q96QC0; -.
DR Antibodypedia; 26382; 145 antibodies from 30 providers.
DR DNASU; 5514; -.
DR Ensembl; ENST00000376511.7; ENSP00000365694.2; ENSG00000204569.10.
DR Ensembl; ENST00000383586.8; ENSP00000373080.4; ENSG00000206489.9.
DR Ensembl; ENST00000420949.6; ENSP00000413554.2; ENSG00000230995.7.
DR Ensembl; ENST00000424446.6; ENSP00000407181.2; ENSG00000231737.7.
DR Ensembl; ENST00000426299.6; ENSP00000389299.2; ENSG00000235291.7.
DR Ensembl; ENST00000429597.6; ENSP00000407310.2; ENSG00000238104.7.
DR Ensembl; ENST00000449113.6; ENSP00000416060.2; ENSG00000227804.7.
DR GeneID; 5514; -.
DR KEGG; hsa:5514; -.
DR MANE-Select; ENST00000376511.7; ENSP00000365694.2; NM_002714.4; NP_002705.2.
DR UCSC; uc003nqn.3; human.
DR CTD; 5514; -.
DR DisGeNET; 5514; -.
DR GeneCards; PPP1R10; -.
DR HGNC; HGNC:9284; PPP1R10.
DR HPA; ENSG00000204569; Low tissue specificity.
DR MIM; 603771; gene.
DR neXtProt; NX_Q96QC0; -.
DR OpenTargets; ENSG00000204569; -.
DR PharmGKB; PA33612; -.
DR VEuPathDB; HostDB:ENSG00000204569; -.
DR eggNOG; ENOG502QQ2I; Eukaryota.
DR GeneTree; ENSGT00940000159263; -.
DR HOGENOM; CLU_019410_0_0_1; -.
DR InParanoid; Q96QC0; -.
DR OMA; MGKNCKY; -.
DR OrthoDB; 999354at2759; -.
DR PhylomeDB; Q96QC0; -.
DR TreeFam; TF105541; -.
DR PathwayCommons; Q96QC0; -.
DR SignaLink; Q96QC0; -.
DR BioGRID-ORCS; 5514; 693 hits in 1097 CRISPR screens.
DR ChiTaRS; PPP1R10; human.
DR GeneWiki; PPP1R10; -.
DR GenomeRNAi; 5514; -.
DR Pharos; Q96QC0; Tbio.
DR PRO; PR:Q96QC0; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q96QC0; protein.
DR Bgee; ENSG00000204569; Expressed in bone marrow cell and 101 other tissues.
DR ExpressionAtlas; Q96QC0; baseline and differential.
DR Genevisible; Q96QC0; HS.
DR GO; GO:0000785; C:chromatin; ISS:UniProtKB.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; TAS:ProtInc.
DR GO; GO:0072357; C:PTW/PP1 phosphatase complex; ISS: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; IBA:GO_Central.
DR GO; GO:0004864; F:protein phosphatase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0010667; P:negative regulation of cardiac muscle cell apoptotic process; IDA:BHF-UCL.
DR GO; GO:1904290; P:negative regulation of mitotic DNA damage checkpoint; IGI:BHF-UCL.
DR GO; GO:0032206; P:positive regulation of telomere maintenance; IMP:BHF-UCL.
DR GO; GO:0006606; P:protein import into nucleus; TAS:ProtInc.
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 3D-structure; Direct protein sequencing; DNA-binding; Isopeptide bond;
KW Metal-binding; Methylation; Nucleus; Phosphoprotein;
KW Protein phosphatase inhibitor; Reference proteome; RNA-binding;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..940
FT /note="Serine/threonine-protein phosphatase 1 regulatory
FT subunit 10"
FT /id="PRO_0000071510"
FT DOMAIN 73..147
FT /note="TFIIS N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00649"
FT ZN_FING 906..934
FT /note="C3H1-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT REGION 1..348
FT /note="Interaction with TOX4"
FT /evidence="ECO:0000250"
FT REGION 147..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 248..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 304..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:0000250"
FT REGION 393..408
FT /note="Necessary for interaction with PPP1CC"
FT /evidence="ECO:0000269|PubMed:9450550"
FT REGION 418..619
FT /note="Interaction with WDR82"
FT /evidence="ECO:0000250"
FT REGION 533..580
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 617..905
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..334
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 627..679
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 850..903
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 256
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 313
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 382
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 398
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 545
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 591
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569"
FT MOD_RES 665
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 693
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 738
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q80W00"
FT CROSSLNK 179
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 262
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 173
FT /note="R -> P (in dbSNP:rs16897725)"
FT /id="VAR_051747"
FT CONFLICT 225
FT /note="K -> E (in Ref. 1; CAA73697)"
FT /evidence="ECO:0000305"
FT CONFLICT 861
FT /note="P -> L (in Ref. 1; CAA73697)"
FT /evidence="ECO:0000305"
FT CONFLICT 875
FT /note="P -> Q (in Ref. 1; CAA73697)"
FT /evidence="ECO:0000305"
FT HELIX 8..13
FT /evidence="ECO:0007829|PDB:6ZV2"
FT HELIX 14..18
FT /evidence="ECO:0007829|PDB:6ZV2"
FT STRAND 23..25
FT /evidence="ECO:0007829|PDB:6ZV2"
FT HELIX 30..38
FT /evidence="ECO:0007829|PDB:6ZV2"
FT HELIX 44..56
FT /evidence="ECO:0007829|PDB:6ZV2"
FT HELIX 60..68
FT /evidence="ECO:0007829|PDB:6ZV2"
FT HELIX 71..83
FT /evidence="ECO:0007829|PDB:6ZV2"
FT TURN 84..86
FT /evidence="ECO:0007829|PDB:6ZV2"
FT HELIX 88..100
FT /evidence="ECO:0007829|PDB:6ZV2"
FT HELIX 105..110
FT /evidence="ECO:0007829|PDB:6ZV2"
FT HELIX 113..123
FT /evidence="ECO:0007829|PDB:6ZV2"
FT HELIX 127..144
FT /evidence="ECO:0007829|PDB:6ZV2"
SQ SEQUENCE 940 AA; 99058 MW; 49EE42961D734121 CRC64;
MGSGPIDPKE LLKGLDSFLN RDGEVKSVDG ISKIFSLMKE ARKMVSRCTY LNILLQTRSP
EILVKFIDVG GYKLLNNWLT YSKTTNNIPL LQQILLTLQH LPLTVDHLKQ NNTAKLVKQL
SKSSEDEELR KLASVLVSDW MAVIRSQSST QPAEKDKKKR KDEGKSRTTL PERPLTEVKA
ETRAEEAPEK KREKPKSLRT TAPSHAKFRS TGLELETPSL VPVKKNASTV VVSDKYNLKP
IPLKRQSNVA APGDATPPAE KKYKPLNTTP NATKEIKVKI IPPQPMEGLG FLDALNSAPV
PGIKIKKKKK VLSPTAAKPS PFEGKTSTEP STAKPSSPEP APPSEAMDAD RPGTPVPPVE
VPELMDTASL EPGALDAKPV ESPGDPNQLT RKGRKRKSVT WPEEGKLREY FYFELDETER
VNVNKIKDFG EAAKREILSD RHAFETARRL SHDNMEEKVP WVCPRPLVLP SPLVTPGSNS
QERYIQAERE KGILQELFLN KESPHEPDPE PYEPIPPKLI PLDEECSMDE TPYVETLEPG
GSGGSPDGAG GSKLPPVLAN LMGSMGAGKG PQGPGGGGIN VQEILTSIMG SPNSHPSEEL
LKQPDYSDKI KQMLVPHGLL GPGPIANGFP PGGPGGPKGM QHFPPGPGGP MPGPHGGPGG
PVGPRLLGPP PPPRGGDPFW DGPGDPMRGG PMRGGPGPGP GPYHRGRGGR GGNEPPPPPP
PFRGARGGRS GGGPPNGRGG PGGGMVGGGG HRPHEGPGGG MGNSSGHRPH EGPGGGMGSG
HRPHEGPGGS MGGGGGHRPH EGPGGGISGG SGHRPHEGPG GGMGAGGGHR PHEGPGGSMG
GSGGHRPHEG PGHGGPHGHR PHDVPGHRGH DHRGPPPHEH RGHDGPGHGG GGHRGHDGGH
SHGGDMSNRP VCRHFMMKGN CRYENNCAFY HPGVNGPPLP
