CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-015863
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 RNA polymerase II subunit A C-terminal domain phosphatase 
Protein Synonyms/Alias
 TFIIF-associating CTD phosphatase 
Gene Name
 Ctdp1 
Gene Synonyms/Alias
 Fcp1 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
770IYDSNTGKLIRMGPQacetylation[1, 2, 3]
770IYDSNTGKLIRMGPQubiquitination[4]
Reference
 [1] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [2] 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]
 [3] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
 [4] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023] 
Functional Description
 Processively dephosphorylates 'Ser-2' and 'Ser-5' of the heptad repeats YSPTSPS in the C-terminal domain of the largest RNA polymerase II subunit. This promotes the activity of RNA polymerase II. Plays a role in the exit from mitosis by dephosphorylating crucial mitotic substrates (USP44, CDC20 and WEE1) that are required for M-phase-promoting factor (MPF)/CDK1 inactivation (By similarity). 
Sequence Annotation
 DOMAIN 178 341 FCP1 homology.
 DOMAIN 619 718 BRCT.
 MOD_RES 502 502 Phosphoserine.
 MOD_RES 664 664 Phosphoserine (By similarity).
 MOD_RES 770 770 N6-acetyllysine (By similarity).
 MOD_RES 860 860 Phosphoserine.
 MOD_RES 863 863 Phosphoserine.  
Keyword
 Acetylation; Alternative splicing; Cell cycle; Cell division; Complete proteome; Cytoplasm; Cytoskeleton; Hydrolase; Mitosis; Nucleus; Phosphoprotein; Protein phosphatase; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 960 AA 
Protein Sequence
MEAPPAAGVP TECTPAVAGA EVRCPGPTPL RLLEWKVAAG ATVRIGSVLA VCETAASAQP 60
AGPAPARAAS GGCVRAARTE RRLRSERAGV VRELCAQPGQ VVAPGALLVR LEGCSHPVVM 120
KGLCAECGQD LTQLQSKNGR QQVPLSTATV SMVHSVPELM VSSEQAEKLG REDQQRLHRN 180
RKLVLMVDLD QTLIHTTEQH CPQMSNKGIF HFQLGRGEPM LHTRLRPHCK DFLEKIAKLY 240
ELHVFTFGSR LYAHTIAGFL DPEKKLFSHR ILSRDECIDP FSKTGNLRNL FPCGDSMVCI 300
IDDREDVWKF APNLITVKKY VYFPGTGDVN APPAARETQA RRKVNHSSKG GDALEQALSV 360
RDPEDGRPAP GVEHSNGLGK ASRELNGGEA VPGVFPSKAD EKEAWPLTRA SPASSSSGHE 420
PTEAPELPVS CEWDGRTTPG VQPTQGDAAT QDLDFDLSSD SESSESSSRS EGQRAPAPQE 480
RTKAAPEHSG PQDTSGGRAA ASPLGESGPS IHPHDKGSDL DTQEEGERDS LCGLGNGSVD 540
RKEAETESQN SEQSGVTAGE SLDQSVGEEE EEDTDDDDHL IHLEEILVRV HTDYYTKYDR 600
YLNKELEEAP DIRKIVPELK SKVLADVAVI FSGLHPTNFP VEKTREHYHA TALGAKVLTQ 660
LVLSPDAPDR ATHLIAARAG TEKVRQAQEC KHLHVVSPDW LWSCLERWDK VEEQLFPLID 720
DDTRTHRDNS PAVFPDRHSV LPTALFHPTP IHSKAHPGPE VRIYDSNTGK LIRMGPQGSA 780
PAPSSAPLNH GEPSSFRAVQ PHQQQMFGEE LPESQDGEQP GPARRKRQPS MSEAMPLYTL 840
CKEDLESMDK EVDDILGEGS DDSDIEKKKP EDQDNEQERA PKPRKPRAPG IRREQPVGLP 900
SSGERSTPGM RGPRGHKRKL NEEDAASESS GESSNDDEEG SSSEADEMAA ALEAELNDLM 960 
Gene Ontology
 GO:0015629; C:actin cytoskeleton; IEA:Compara.
 GO:0005813; C:centrosome; ISS:UniProtKB.
 GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
 GO:0030496; C:midbody; ISS:UniProtKB.
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 GO:0051233; C:spindle midzone; ISS:UniProtKB.
 GO:0000922; C:spindle pole; ISS:UniProtKB.
 GO:0008420; F:CTD phosphatase activity; IEA:Compara.
 GO:0051301; P:cell division; IEA:UniProtKB-KW.
 GO:0010458; P:exit from mitosis; ISS:UniProtKB.
 GO:0006470; P:protein dephosphorylation; ISS:UniProtKB. 
Interpro
 IPR001357; BRCT_dom.
 IPR015388; FCP1_C.
 IPR011947; FCP1_euk.
 IPR023214; HAD-like_dom.
 IPR004274; NIF. 
Pfam
 PF09309; FCP1_C
 PF03031; NIF
 PF12738; PTCB-BRCT 
SMART
 SM00292; BRCT
 SM00577; CPDc 
PROSITE
 PS50172; BRCT
 PS50969; FCP1 
PRINTS