PPP1R10
entrez
5514
canonical
uniprot
Q96QC0
canonical
ensembl
ENSG00000204569
resolver
ensembl
ENSG00000206489
resolver
ensembl
ENSG00000227804
resolver
ensembl
ENSG00000230995
resolver
ensembl
ENSG00000231737
resolver
ensembl
ENSG00000235291
resolver
ensembl
ENSG00000238104
resolver
ensp
ENSP00000365694
resolver
ensp
ENSP00000373080
resolver
ensp
ENSP00000389299
resolver
ensp
ENSP00000407181
resolver
ensp
ENSP00000407310
resolver
ensp
ENSP00000413554
resolver
ensp
ENSP00000416060
resolver
ensp
ENSP00000583736
resolver
ensp
ENSP00000583737
resolver
ensp
ENSP00000583738
resolver
ensp
ENSP00000583739
resolver
ensp
ENSP00000583740
resolver
ensp
ENSP00000621390
resolver
enst
ENST00000376511
resolver
enst
ENST00000383586
resolver
enst
ENST00000420949
resolver
enst
ENST00000424446
resolver
enst
ENST00000426299
resolver
enst
ENST00000429597
resolver
enst
ENST00000449113
resolver
enst
ENST00000913677
resolver
enst
ENST00000913678
resolver
enst
ENST00000913679
resolver
enst
ENST00000913680
resolver
enst
ENST00000913681
resolver
enst
ENST00000951331
resolver
genesymbol
PPP1R10
resolver
genesymbol_syn
CAT53
resolver
genesymbol_syn
FB19
resolver
genesymbol_syn
PNUTS
resolver
hgnc
HGNC:9284
resolver
uniprot
A0A1U9X8C5
resolver
uniprot
O00405
resolver
uniprot
Q2L6I0
resolver
uniprot_entry
PP1RA_HUMAN
resolver
uniprot_entry
Q2L6I0_HUMAN
resolver
uniprot_sec
A0A1U9X8C5
resolver
uniprot_sec
O00405
resolver
amino_acid_sequence
MGSGPIDPKELLKGLDSFLNRDGEVKSVDGISKIFSLMKEARKMVSRCTYLNILLQTRSPEILVKFIDVGGYKLLNNWLTYSKTTNNIPLLQQILLTLQHLPLTVDHLKQNNTAKLVKQLSKSSEDEELRKLASVLVSDWMAVIRSQSSTQPAEKDKKKRKDEGKSRTTLPERPLTEVKAETRAEEAPEKKREKPKSLRTTAPSHAKFRSTGLELETPSLVPVKKNASTVVVSDKYNLKPIPLKRQSNVAAPGDATPPAEKKYKPLNTTPNATKEIKVKIIPPQPMEGLGFLDALNSAPVPGIKIKKKKKVLSPTAAKPSPFEGKTSTEPSTAKPSSPEPAPPSEAMDADRPGTPVPPVEVPELMDTASLEPGALDAKPVESPGDPNQLTRKGRKRKSVTWPEEGKLREYFYFELDETERVNVNKIKDFGEAAKREILSDRHAFETARRLSHDNMEEKVPWVCPRPLVLPSPLVTPGSNSQERYIQAEREKGILQELFLNKESPHEPDPEPYEPIPPKLIPLDEECSMDETPYVETLEPGGSGGSPDGAGGSKLPPVLANLMGSMGAGKGPQGPGGGGINVQEILTSIMGSPNSHPSEELLKQPDYSDKIKQMLVPHGLLGPGPIANGFPPGGPGGPKGMQHFPPGPGGPMPGPHGGPGGPVGPRLLGPPPPPRGGDPFWDGPGDPMRGGPMRGGPGPGPGPYHRGRGGRGGNEPPPPPPPFRGARGGRSGGGPPNGRGGPGGGMVGGGGHRPHEGPGGGMGNSSGHRPHEGPGGGMGSGHRPHEGPGGSMGGGGGHRPHEGPGGGISGGSGHRPHEGPGGGMGAGGGHRPHEGPGGSMGGSGGHRPHEGPGHGGPHGHRPHDVPGHRGHDHRGPPPHEHRGHDGPGHGGGGHRGHDGGHSHGGDMSNRPVCRHFMMKGNCRYENNCAFYHPGVNGPPLP
uniprot
proteins
function
FUNCTION: Substrate-recognition component of the PNUTS-PP1 protein phosphatase complex, a protein phosphatase 1 (PP1) complex that promotes RNA polymerase II transcription pause-release, allowing transcription elongation (PubMed:39603239, PubMed:39603240). Promoter-proximal pausing by RNA polymerase II is a transcription halt following transcription initiation but prior to elongation, which acts as a checkpoint to control that transcripts are favorably configured for transcriptional elongation (PubMed:39603239, PubMed:39603240). The PNUTS-PP1 complex mediates the release of RNA polymerase II from promoter-proximal region of genes by catalyzing dephosphorylation of proteins involved in transcription, such as AFF4, CDK9, MEPCE, INTS12, NCBP1, POLR2M/GDOWN1 and SUPT6H (PubMed:39603239, PubMed:39603240). The PNUTS-PP1 complex also regulates RNA polymerase II transcription termination by mediating dephosphorylation of SUPT5H in termination zones downstream of poly(A) sites, thereby promoting deceleration of RNA polymerase II transcription (PubMed:31677974). PNUTS-PP1 complex is also involved in the response to replication stress by mediating dephosphorylation of POLR2A at 'Ser-5' of the CTD, promoting RNA polymerase II degradation (PubMed:33264625). The PNUTS-PP1 complex also plays a role in the control of chromatin structure and cell cycle progression during the transition from mitosis into interphase (By similarity). PNUTS-PP1 complex mediates dephosphorylation of MYC, promoting MYC stability by preventing MYC ubiquitination by the SCF(FBXW7) complex (PubMed:30158517). In addition to acts as a substrate-recognition component, PPP1R10/PNUTS also acts as a nuclear targeting subunit for the PNUTS-PP1 complex (PubMed:9450550). In some context, PPP1R10/PNUTS also acts as an inhibitor of protein phosphatase 1 (PP1) activity by preventing access to substrates, such as RB (PubMed:18360108). {ECO:0000250|UniProtKB:Q80W00, ECO:0000269|PubMed:18360108, ECO:0000269|PubMed:30158517, ECO:0000269|PubMed:31677974, ECO:0000269|PubMed:33264625, ECO:0000269|PubMed:39603239, ECO:0000269|PubMed:39603240, ECO:0000269|PubMed:9450550}.
uniprot
proteins
mass_dalton
99058
uniprot
proteins
mutagenesis
MUTAGEN 140; /note="W->A: Abolished interaction with PPP1CA, preventing ability to regulate transcription-pause release and transcription termination."; /evidence="ECO:0000269|PubMed:31677974, ECO:0000269|PubMed:39603239, ECO:0000269|PubMed:39603240
uniprot
proteins
post_translational_modification
PTM: Phosphorylated on Ser-398 by PKA within the region necessary for interaction with PPP1CA. {ECO:0000250|UniProtKB:O55000}.
uniprot
proteins
pubmed
14574404
uniprot
proteins
pubmed
16964243
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
18360108
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24129315
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
28112733
uniprot
proteins
pubmed
30158517
uniprot
proteins
pubmed
31677974
uniprot
proteins
pubmed
33264625
uniprot
proteins
pubmed
39446389
uniprot
proteins
pubmed
39603239
uniprot
proteins
pubmed
39603240
uniprot
proteins
pubmed
40473212
uniprot
proteins
pubmed
9450550
uniprot
proteins
pubmed
9784381
uniprot
proteins
sequence_length
940
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00649, ECO:0000269|PubMed:9450550}. Chromosome {ECO:0000269|PubMed:39603239, ECO:0000269|PubMed:39603240}. Note=Found in discrete nucleoplasmic bodies and within nucleoli (PubMed:9450550). Associates with RNA polymerase II (Pol II) on chromatin during pause-release checkpoint (PubMed:39603239, PubMed:39603240). Associates with chromatin during interphase, excluded from condensed chromosomes during early mitosis and is reloaded onto chromosomes at the late telophase (By similarity). {ECO:0000250|UniProtKB:Q80W00, ECO:0000269|PubMed:39603239, ECO:0000269|PubMed:39603240, ECO:0000269|PubMed:9450550}.
uniprot
proteins