CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-000336
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Protein phosphatase 1 regulatory subunit 12A 
Protein Synonyms/Alias
 Myosin phosphatase-targeting subunit 1; Myosin phosphatase target subunit 1; Protein phosphatase myosin-binding subunit 
Gene Name
 PPP1R12A 
Gene Synonyms/Alias
 MBS; MYPT1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
286YLEELQKKQNLLHSEubiquitination[1]
442TWRLGLRKTGSYGALmethylation[2]
945QILAENEKLKAQLHDubiquitination[1]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] Demethylation of RB regulator MYPT1 by histone demethylase LSD1 promotes cell cycle progression in cancer cells.
 Cho HS, Suzuki T, Dohmae N, Hayami S, Unoki M, Yoshimatsu M, Toyokawa G, Takawa M, Chen T, Kurash JK, Field HI, Ponder BA, Nakamura Y, Hamamoto R.
 Cancer Res. 2011 Feb 1;71(3):655-60. [PMID: 21115810
Functional Description
 Key regulator of protein phosphatase 1C (PPP1C). Mediates binding to myosin. As part of the PPP1C complex, involved in dephosphorylation of PLK1. Capable of inhibiting HIF1AN- dependent suppression of HIF1A activity. 
Sequence Annotation
 REPEAT 39 68 ANK 1.
 REPEAT 72 101 ANK 2.
 REPEAT 105 134 ANK 3.
 REPEAT 138 164 ANK 4.
 REPEAT 198 227 ANK 5.
 REPEAT 231 260 ANK 6.
 REGION 682 864 Interaction with ROCK2.
 MOTIF 35 38 KVKF motif.
 MOD_RES 67 67 (3S)-3-hydroxyasparagine; by HIF1AN;
 MOD_RES 100 100 (3S)-3-hydroxyasparagine; by HIF1AN;
 MOD_RES 226 226 (3S)-3-hydroxyasparagine; by HIF1AN;
 MOD_RES 299 299 Phosphoserine.
 MOD_RES 422 422 Phosphoserine.
 MOD_RES 432 432 Phosphoserine.
 MOD_RES 443 443 Phosphothreonine (By similarity).
 MOD_RES 445 445 Phosphoserine; by NUAK1.
 MOD_RES 472 472 Phosphoserine; by NUAK1.
 MOD_RES 473 473 Phosphoserine; by CDK1.
 MOD_RES 477 477 Phosphoserine.
 MOD_RES 507 507 Phosphoserine.
 MOD_RES 601 601 Phosphoserine.
 MOD_RES 668 668 Phosphoserine (By similarity).
 MOD_RES 692 692 Phosphoserine; by PKA and PKG; in vitro.
 MOD_RES 695 695 Phosphoserine; by PKA and PKG; in vitro.
 MOD_RES 696 696 Phosphothreonine; by ROCK1; ROCK2;
 MOD_RES 852 852 Phosphoserine; by ROCK2.
 MOD_RES 862 862 Phosphoserine.
 MOD_RES 871 871 Phosphoserine.
 MOD_RES 910 910 Phosphoserine; by NUAK1.
 MOD_RES 995 995 Phosphoserine (By similarity).  
Keyword
 3D-structure; Alternative splicing; ANK repeat; Complete proteome; Cytoplasm; Direct protein sequencing; Hydroxylation; Phosphoprotein; Polymorphism; Reference proteome; Repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1030 AA 
Protein Sequence
MKMADAKQKR NEQLKRWIGS ETDLEPPVVK RQKTKVKFDD GAVFLAACSS GDTDEVLKLL 60
HRGADINYAN VDGLTALHQA CIDDNVDMVK FLVENGANIN QPDNEGWIPL HAAASCGYLD 120
IAEFLIGQGA HVGAVNSEGD TPLDIAEEEA MEELLQNEVN RQGVDIEAAR KEEERIMLRD 180
ARQWLNSGHI NDVRHAKSGG TALHVAAAKG YTEVLKLLIQ AGYDVNIKDY DGWTPLHAAA 240
HWGKEEACRI LVDNLCDMEM VNKVGQTAFD VADEDILGYL EELQKKQNLL HSEKRDKKSP 300
LIESTANMDN NQSQKTFKNK ETLIIEPEKN ASRIESLEQE KVDEEEEGKK DESSCSSEED 360
EEDDSESEAE TDKTKPLASV TNANTSSTQA APVAVTTPTV SSGQATPTSP IKKFPTTATK 420
ISPKEEERKD ESPATWRLGL RKTGSYGALA EITASKEGQK EKDTAGVTRS ASSPRLSSSL 480
DNKEKEKDSK GTRLAYVAPT IPRRLASTSD IEEKENRDSS SLRTSSSYTR RKWEDDLKKN 540
SSVNEGSTYH KSCSFGRRQD DLISSSVPST TSTPTVTSAA GLQKSLLSST STTTKITTGS 600
SSAGTQSSTS NRLWAEDSTE KEKDSVPTAV TIPVAPTVVN AAASTTTLTT TTAGTVSSTT 660
EVRERRRSYL TPVRDEESES QRKARSRQAR QSRRSTQGVT LTDLQEAEKT IGRSRSTRTR 720
EQENEEKEKE EKEKQDKEKQ EEKKESETSR EDEYKQKYSR TYDETYQRYR PVSTSSSTTP 780
SSSLSTMSSS LYASSQLNRP NSLVGITSAY SRGITKENER EGEKREEEKE GEDKSQPKSI 840
RERRRPREKR RSTGVSFWTQ DSDENEQEQQ SDTEEGSNKK ETQTDSISRY ETSSTSAGDR 900
YDSLLGRSGS YSYLEERKPY SSRLEKDDST DFKKLYEQIL AENEKLKAQL HDTNMELTDL 960
KLQLEKATQR QERFADRSLL EMEKRERRAL ERRISEMEEE LKMLPDLKAD NQRLKDENGA 1020
LIRVISKLSK 1030 
Gene Ontology
 GO:0005813; C:centrosome; IDA:UniProtKB.
 GO:0043292; C:contractile fiber; IDA:UniProtKB.
 GO:0000776; C:kinetochore; IDA:UniProtKB.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0072357; C:PTW/PP1 phosphatase complex; IDA:UniProtKB.
 GO:0071889; F:14-3-3 protein binding; IDA:UniProtKB.
 GO:0004857; F:enzyme inhibitor activity; IDA:UniProtKB.
 GO:0019208; F:phosphatase regulator activity; IDA:UniProtKB.
 GO:0004871; F:signal transducer activity; NAS:ProtInc.
 GO:0051297; P:centrosome organization; IMP:UniProtKB.
 GO:0000086; P:G2/M transition of mitotic cell cycle; TAS:Reactome.
 GO:0007067; P:mitosis; IMP:UniProtKB.
 GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
 GO:0006470; P:protein dephosphorylation; IMP:UniProtKB.
 GO:0030155; P:regulation of cell adhesion; IDA:UniProtKB.
 GO:0035507; P:regulation of myosin-light-chain-phosphatase activity; IDA:UniProtKB.
 GO:0046822; P:regulation of nucleocytoplasmic transport; IEA:Compara. 
Interpro
 IPR002110; Ankyrin_rpt.
 IPR020683; Ankyrin_rpt-contain_dom.
 IPR017401; Pase-1_reg_su_12A/B/C_euk. 
Pfam
 PF00023; Ank 
SMART
 SM00248; ANK 
PROSITE
 PS50297; ANK_REP_REGION
 PS50088; ANK_REPEAT 
PRINTS
 PR01415; ANKYRIN.