Overview
| Uniprot ID | Q767K9 |
| Protein Name | Serine/threonine-protein phosphatase 1 regulatory subunit 10 |
| Gene Name | PPP1R10 |
| Organism | Sus scrofa |
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 190 |
RAEEAPEKKREKPKS |
| 225 |
PSLVPVKKNASAVVV |
| 262 |
AAPPAEKKYKPLNTT |
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. 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. 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. 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. 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 (By similarity). 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. In addition to acts as a substrate-recognition component, PPP1R10/PNUTS also acts as a nuclear targeting subunit for the PNUTS-PP1 complex. In some context, PPP1R10/PNUTS also acts as an inhibitor of protein phosphatase 1 (PP1) activity by preventing access to substrates, such as RB (By similarity)
Protein Sequence
10
MGSGPIDPKE
20
LLKGLDSFLN
30
RDGEVKSVDG
40
ISKIFSLMKE
50
ARKMVSRCTY
60
LNILLQTRSP
70
EILVKFIDVG
80
GYKLLNNWLT
90
YSKTTNNIPL
100
LQQILLTLQH
110
LPLTVDHLKQ
120
NNTAKLVKQL
130
SKSSEDEELR
140
KLASVLVSDW
150
MAVIRSQSST
160
QPAEKDKKKR
170
KEEGKSRTTP
180
PERPLTEVKA
190
ETRAEEAPEK
200
KREKPKSLRT
210
TAPSHAKFRS
220
TGLELETPSL
230
VPVKKNASAV
240
VVSDKYNLKP
250
IPLKRQSSIA
260
ALGDAAPPAE
270
KKYKPLNTTP
280
NATKEIKVKI
290
IPPQPMEGLG
300
FLDALNSAPV
310
PGIKIKKKKK
320
VLSPTAAKPS
330
PFEGKTSTEP
340
STAKPSSPEP
350
APPSEAMDTD
360
RPGTPVPPVE
370
VPELMDTASL
380
EPGALDAKPV
390
ESPGDPSQLT
400
RKGRKRKTVT
410
WPEEGKLREY
420
FYFELDETER
430
VNVNKIKDFG
440
EAAKREILSD
450
RHAFETARRL
460
SHDNMEEKVP
470
WVCPRPLVLP
480
SPLVTPGSNS
490
QERYIQAERE
500
KGILQELFLN
510
KESPHEPDPE
520
PYEPVPPKLI
530
PLDEECSMDE
540
TPYVETLEPG
550
GAGGSPDGAG
560
GSKLPPVLAN
570
LMGSMGAGKS
580
PQGPGGGGIN
590
VQEILTSIMG
600
SPNSHPSEEL
610
LKQPDYSDKI
620
KQMLVPHGLL
630
GPGPIANGFP
640
PGGPGGPKGM
650
QHFPPGPGGP
660
MPGPHGGPGG
670
PGGPVGPRLL
680
GPPPPPRGGD
690
PFWDGPGDPM
700
RGGPMRGGPG
710
PGPGPYHRGR
720
GGRGGNEPPP
730
PPPPFRGARG
740
GRSGGGPPNG
750
RGGPGGGMVG
760
GGGHRPHEGP
770
GGGMSSGSGH
780
RPHEGPGGGM
790
GGGHRPHEGP
800
GGGMGGGHRP
810
HEGPGGGMGG
820
GSGHRPHEGP
830
GGGMGAGGGH
840
RPHEGPGHGG
850
PHGHRPHDVP
860
GHRGHDHRGP
870
PPHEHRGHDG
880
PGHGGGGHRG
890
HDGGHNHGGD
900
MSKRPVCRHF
910
MMKGNCRYEN
920
NCAFYHPGVN
GPPLP
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:0000785 |
chromatin |
| Cellular Component |
GO:0005634 |
nucleus |
| Cellular Component |
GO:0072357 |
PTW/PP1 phosphatase complex |
| Molecular Function |
GO:0003677 |
DNA binding |
| Molecular Function |
GO:0140767 |
enzyme-substrate adaptor activity |
| Molecular Function |
GO:0008157 |
protein phosphatase 1 binding |
| Molecular Function |
GO:0019888 |
protein phosphatase regulator activity |
| Molecular Function |
GO:0003723 |
RNA binding |
| Molecular Function |
GO:0008270 |
zinc ion binding |
| Biological Process |
GO:0034244 |
negative regulation of transcription elongation by RNA polymerase II |
| Biological Process |
GO:2000806 |
positive regulation of termination of RNA polymerase II transcription, poly(A)-coupled |
| Biological Process |
GO:0032968 |
positive regulation of transcription elongation by RNA polymerase II |
| Biological Process |
GO:0001111 |
RNA polymerase II promoter clearance |
Reference
[1] Fan S, Zhou R, Wen H, Ye H, Ma S et al.. Global profiling of protein lactylome in porcine granulosa cells.. J Ovarian Res 18(1):177. 2025 Aug 8. PMID: 40781717.