CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-019557
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Serine/threonine-protein phosphatase 1 regulatory subunit 10 
Protein Synonyms/Alias
 MHC class I region proline-rich protein CAT53; PP1-binding protein of 114 kDa; Phosphatase 1 nuclear targeting subunit; Protein FB19; p99 
Gene Name
 PPP1R10 
Gene Synonyms/Alias
 CAT53; FB19; PNUTS 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
13IDPKELLKGLDSFLNubiquitination[1]
33KSVDGISKIFSLMKEubiquitination[1]
207TTAPSHAKFRSTGLEacetylation[2]
239VSDKYNLKPIPLKRQacetylation[2, 3]
239VSDKYNLKPIPLKRQubiquitination[1]
261DATPPAEKKYKPLNTacetylation[4]
274NTTPNATKEIKVKIIacetylation[2, 4]
Reference
 [1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [2] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [3] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [4] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302] 
Functional Description
 Scaffold protein which mediates the formation of the PTW/PP1 phosphatase complex by providing a binding platform to each component of the complex. The PTW/PP1 phosphatase complex plays a role in the control of chromatin structure and cell cycle progression during the transition from mitosis into interphase. Mediates interaction of WDR82 and PPP1CA. Inhibitor of PPP1CA and PPP1CC phosphatase activities. Has inhibitory activity on PPP1CA only when phosphorylated. Binds to mRNA, single-stranded DNA (ssDNA), poly(A) and poly(G) homopolymers (By similarity). 
Sequence Annotation
 DOMAIN 73 147 TFIIS N-terminal.
 ZN_FING 906 934 C3H1-type.
 REGION 1 348 Interaction with TOX4 (By similarity).
 REGION 382 450 Essential for PPP1CA inhibition (By
 REGION 388 417 Necessary for interaction with PPP1CA (By
 REGION 393 408 Necessary for interaction with PPP1CC.
 REGION 418 619 Interaction with WDR82 (By similarity).
 MOTIF 420 423 PP1-binding motif.
 MOD_RES 256 256 Phosphothreonine.
 MOD_RES 313 313 Phosphoserine.
 MOD_RES 398 398 Phosphoserine; by PKA (By similarity).
 MOD_RES 400 400 Phosphothreonine; by PKA (By similarity).
 MOD_RES 591 591 Phosphoserine.  
Keyword
 Complete proteome; Direct protein sequencing; DNA-binding; Metal-binding; Nucleus; Phosphoprotein; Polymorphism; Protein phosphatase inhibitor; Reference proteome; RNA-binding; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 940 AA 
Protein Sequence
MGSGPIDPKE LLKGLDSFLN RDGEVKSVDG ISKIFSLMKE ARKMVSRCTY LNILLQTRSP 60
EILVKFIDVG GYKLLNNWLT YSKTTNNIPL LQQILLTLQH LPLTVDHLKQ NNTAKLVKQL 120
SKSSEDEELR KLASVLVSDW MAVIRSQSST QPAEKDKKKR KDEGKSRTTL PERPLTEVKA 180
ETRAEEAPEK KREKPKSLRT TAPSHAKFRS TGLELETPSL VPVKKNASTV VVSDKYNLKP 240
IPLKRQSNVA APGDATPPAE KKYKPLNTTP NATKEIKVKI IPPQPMEGLG FLDALNSAPV 300
PGIKIKKKKK VLSPTAAKPS PFEGKTSTEP STAKPSSPEP APPSEAMDAD RPGTPVPPVE 360
VPELMDTASL EPGALDAKPV ESPGDPNQLT RKGRKRKSVT WPEEGKLREY FYFELDETER 420
VNVNKIKDFG EAAKREILSD RHAFETARRL SHDNMEEKVP WVCPRPLVLP SPLVTPGSNS 480
QERYIQAERE KGILQELFLN KESPHEPDPE PYEPIPPKLI PLDEECSMDE TPYVETLEPG 540
GSGGSPDGAG GSKLPPVLAN LMGSMGAGKG PQGPGGGGIN VQEILTSIMG SPNSHPSEEL 600
LKQPDYSDKI KQMLVPHGLL GPGPIANGFP PGGPGGPKGM QHFPPGPGGP MPGPHGGPGG 660
PVGPRLLGPP PPPRGGDPFW DGPGDPMRGG PMRGGPGPGP GPYHRGRGGR GGNEPPPPPP 720
PFRGARGGRS GGGPPNGRGG PGGGMVGGGG HRPHEGPGGG MGNSSGHRPH EGPGGGMGSG 780
HRPHEGPGGS MGGGGGHRPH EGPGGGISGG SGHRPHEGPG GGMGAGGGHR PHEGPGGSMG 840
GSGGHRPHEG PGHGGPHGHR PHDVPGHRGH DHRGPPPHEH RGHDGPGHGG GGHRGHDGGH 900
SHGGDMSNRP VCRHFMMKGN CRYENNCAFY HPGVNGPPLP 940 
Gene Ontology
 GO:0000785; C:chromatin; ISS:UniProtKB.
 GO:0005634; C:nucleus; TAS:ProtInc.
 GO:0072357; C:PTW/PP1 phosphatase complex; ISS:UniProtKB.
 GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
 GO:0004864; F:protein phosphatase inhibitor activity; IEA:UniProtKB-KW.
 GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0006606; P:protein import into nucleus; TAS:ProtInc.
 GO:0006351; P:transcription, DNA-dependent; IEA:InterPro. 
Interpro
 IPR003617; TFIIS/CRSP70_N_sub.
 IPR017923; TFIIS_N.
 IPR000571; Znf_CCCH. 
Pfam
 PF08711; Med26
 PF00642; zf-CCCH 
SMART
 SM00509; TFS2N
 SM00356; ZnF_C3H1 
PROSITE
 PS51319; TFIIS_N
 PS50103; ZF_C3H1 
PRINTS