PP1RA_PANTR
ID PP1RA_PANTR Reviewed; 940 AA.
AC Q7YR38; Q1XHY0;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 118.
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=Protein FB19;
GN Name=PPP1R10; Synonyms=CAT53, FB19;
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12799463; DOI=10.1073/pnas.1230533100;
RA Anzai T., Shiina T., Kimura N., Yanagiya K., Kohara S., Shigenari A.,
RA Yamagata T., Kulski J.K., Naruse T.K., Fujimori Y., Fukuzumi Y.,
RA Yamazaki M., Tashiro H., Iwamoto C., Umehara Y., Imanishi T., Meyer A.,
RA Ikeo K., Gojobori T., Bahram S., Inoko H.;
RT "Comparative sequencing of human and chimpanzee MHC class I regions unveils
RT insertions/deletions as the major path to genomic divergence.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7708-7713(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16702430; DOI=10.1534/genetics.106.057034;
RA Shiina T., Ota M., Shimizu S., Katsuyama Y., Hashimoto N., Takasu M.,
RA Anzai T., Kulski J.K., Kikkawa E., Naruse T., Kimura N., Yanagiya K.,
RA Watanabe A., Hosomichi K., Kohara S., Iwamoto C., Umehara Y., Meyer A.,
RA Wanner V., Sano K., Macquin C., Ikeo K., Tokunaga K., Gojobori T.,
RA Inoko H., Bahram S.;
RT "Rapid evolution of major histocompatibility complex class I genes in
RT primates generates new disease alleles in humans via hitchhiking
RT diversity.";
RL Genetics 173:1555-1570(2006).
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}.
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00649}.
CC Note=Found in discrete nucleoplasmic bodies and within nucleoli.
CC Associates with chromatin during interphase, excluded from condensed
CC chromosomes during early mitosis and is reloaded onto chromosomes at
CC the late telophase (By similarity). {ECO:0000250}.
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; BA000041; BAC78178.1; -; Genomic_DNA.
DR EMBL; AB210175; BAE92788.1; -; Genomic_DNA.
DR EMBL; AB210176; BAE92790.1; -; Genomic_DNA.
DR RefSeq; NP_001038965.1; NM_001045500.1.
DR RefSeq; XP_009449100.1; XM_009450825.2.
DR AlphaFoldDB; Q7YR38; -.
DR BMRB; Q7YR38; -.
DR SMR; Q7YR38; -.
DR STRING; 9598.ENSPTRP00000030588; -.
DR PaxDb; Q7YR38; -.
DR Ensembl; ENSPTRT00000033108; ENSPTRP00000030588; ENSPTRG00000017931.
DR GeneID; 462544; -.
DR KEGG; ptr:462544; -.
DR CTD; 5514; -.
DR VGNC; VGNC:11180; PPP1R10.
DR eggNOG; ENOG502QQ2I; Eukaryota.
DR GeneTree; ENSGT00940000159263; -.
DR HOGENOM; CLU_019410_0_0_1; -.
DR InParanoid; Q7YR38; -.
DR OMA; MGKNCKY; -.
DR OrthoDB; 999354at2759; -.
DR TreeFam; TF105541; -.
DR Proteomes; UP000002277; Chromosome 6.
DR Bgee; ENSPTRG00000017931; Expressed in lung and 21 other tissues.
DR GO; GO:0000785; C:chromatin; ISS:UniProtKB.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:Ensembl.
DR GO; GO:0016604; C:nuclear body; IBA:GO_Central.
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; IEA:UniProtKB-KW.
DR GO; GO:0010667; P:negative regulation of cardiac muscle cell apoptotic process; IEA:Ensembl.
DR GO; GO:1904290; P:negative regulation of mitotic DNA damage checkpoint; IBA:GO_Central.
DR GO; GO:0032206; P:positive regulation of telomere maintenance; IBA:GO_Central.
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 3: Inferred from homology;
KW DNA-binding; Isopeptide bond; Metal-binding; Methylation; Nucleus;
KW Phosphoprotein; Protein phosphatase inhibitor; Reference proteome;
KW RNA-binding; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..940
FT /note="Serine/threonine-protein phosphatase 1 regulatory
FT subunit 10"
FT /id="PRO_0000071513"
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 357..433
FT /note="Necessary for interaction with PPP1CA"
FT /evidence="ECO:0000250"
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:0000250"
FT REGION 418..619
FT /note="Interaction with WDR82"
FT /evidence="ECO:0000250"
FT REGION 534..557
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:0000250|UniProtKB:Q96QC0"
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="Phosphoserine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:Q96QC0"
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:0000250|UniProtKB:Q96QC0"
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: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"
SQ SEQUENCE 940 AA; 99127 MW; 0751F06D27F42E60 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 APPSEAMEAD RPGTPVPPVE
VPELMDTASL EPGALDAKPV ESPGDPNQLT RKGRKRKSVT WPEEGKLREY FYFELDETER
VNVNKIKDFG EAAKREILSD RHAFETARRL SHDNMEEKVP WVCPRPLVLP SPLVTPGSNS
QERYIQAERE KGILQELFLN KESPHEPDPE PYEPIPPKLI PLDEECSMDE TPYVETLEPG
GSGGSPDGAG GSKLPPVLAN LMGSMGAGKG PQGPGAGGIN VQEILTSIMG SPNSHPSEEL
LKQPDYSDKI KQMLVPHGLL GPGPIANGFP PGGPGGPKGM QHFPPGPGGP MPGPHGGPGG
PVGPRLLGPP PPPRGGDPFW DGPGDPMRGG PMRGGPGPGP GPYHRGRGGR GGNEPPPPPP
PFRGARGGRS GGGPPNGRGG PGGGMVGGGG HRPHEGPGGG MGNNSGHRPH EGPGGGMGSG
HRPHEGPAGS MGGGGGHRPH EGPGGGISGG SGHRPHEGPG GGMGAGGGHR PHEGPGGSMG
GSGGHRPHEG PGHGGPHGHR PHDVPGHRGH DHRGPPPHEH RGHDGPGHGG GGHRGHDGGH
SHGGDMSNRP VCRHFMMKGN CRYENNCAFY HPGVNGPPLP
