Search Results

Overview

Uniprot IDQ96QC0
Protein NameSerine/threonine-protein phosphatase 1 regulatory subunit 10
Gene NamePPP1R10
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
207 TTAPSHAKFRSTGLE
224 TPSLVPVKKNASTVV
225 PSLVPVKKNASTVVV
235 STVVVSDKYNLKPIP
239 VSDKYNLKPIPLKRQ
262 ATPPAEKKYKPLNTT
425 TERVNVNKIKDFGEA

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)

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 KDEGKSRTTL 180 PERPLTEVKA 190 ETRAEEAPEK 200 KREKPKSLRT 210 TAPSHAKFRS 220 TGLELETPSL 230 VPVKKNASTV 240 VVSDKYNLKP 250 IPLKRQSNVA 260 APGDATPPAE 270 KKYKPLNTTP 280 NATKEIKVKI 290 IPPQPMEGLG 300 FLDALNSAPV 310 PGIKIKKKKK 320 VLSPTAAKPS 330 PFEGKTSTEP 340 STAKPSSPEP 350 APPSEAMDAD 360 RPGTPVPPVE 370 VPELMDTASL 380 EPGALDAKPV 390 ESPGDPNQLT 400 RKGRKRKSVT 410 WPEEGKLREY 420 FYFELDETER 430 VNVNKIKDFG 440 EAAKREILSD 450 RHAFETARRL 460 SHDNMEEKVP 470 WVCPRPLVLP 480 SPLVTPGSNS 490 QERYIQAERE 500 KGILQELFLN 510 KESPHEPDPE 520 PYEPIPPKLI 530 PLDEECSMDE 540 TPYVETLEPG 550 GSGGSPDGAG 560 GSKLPPVLAN 570 LMGSMGAGKG 580 PQGPGGGGIN 590 VQEILTSIMG 600 SPNSHPSEEL 610 LKQPDYSDKI 620 KQMLVPHGLL 630 GPGPIANGFP 640 PGGPGGPKGM 650 QHFPPGPGGP 660 MPGPHGGPGG 670 PVGPRLLGPP 680 PPPRGGDPFW 690 DGPGDPMRGG 700 PMRGGPGPGP 710 GPYHRGRGGR 720 GGNEPPPPPP 730 PFRGARGGRS 740 GGGPPNGRGG 750 PGGGMVGGGG 760 HRPHEGPGGG 770 MGNSSGHRPH 780 EGPGGGMGSG 790 HRPHEGPGGS 800 MGGGGGHRPH 810 EGPGGGISGG 820 SGHRPHEGPG 830 GGMGAGGGHR 840 PHEGPGGSMG 850 GSGGHRPHEG 860 PGHGGPHGHR 870 PHDVPGHRGH 880 DHRGPPPHEH 890 RGHDGPGHGG 900 GGHRGHDGGH 910 SHGGDMSNRP 920 VCRHFMMKGN 930 CRYENNCAFY 940 HPGVNGPPLP

Gene Ontology

Classification GO ID Description
Cellular Component GO:0000785 chromatin
Cellular Component GO:0016604 nuclear body
Cellular Component GO:0005654 nucleoplasm
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:0004864 protein phosphatase inhibitor activity
Molecular Function GO:0019888 protein phosphatase regulator activity
Molecular Function GO:0003723 RNA binding
Molecular Function GO:0008270 zinc ion binding
Biological Process GO:0010667 negative regulation of cardiac muscle cell apoptotic process
Biological Process GO:1904290 negative regulation of mitotic DNA damage checkpoint
Biological Process GO:0034244 negative regulation of transcription elongation by RNA polymerase II
Biological Process GO:0032206 positive regulation of telomere maintenance
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:0006606 protein import into nucleus
Biological Process GO:0050821 protein stabilization
Biological Process GO:0001111 RNA polymerase II promoter clearance

Reference

[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.

[2] He C, Zhang J, Bai X, Lu C, Zhang K. Lysine lactylation-based insight to understanding the characterization of cervical cancer.. Biochim Biophys Acta Mol Basis Dis 1870(7):167356. 2024 Oct. PMID: 39025375.

[3] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.