CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-011056
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 RNA polymerase II subunit A C-terminal domain phosphatase 
Protein Synonyms/Alias
 CTD phosphatase FCP1 
Gene Name
 FCP1 
Gene Synonyms/Alias
 YMR277W; YM8021.03 
Created Date
 July 27, 2013 
Organism
 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 
NCBI Taxa ID
 559292 
Lysine Modification
Position
Peptide
Type
References
74NGVSPPTKQLRESIEubiquitination[1, 2]
Reference
 [1] Sites of ubiquitin attachment in Saccharomyces cerevisiae.
 Starita LM, Lo RS, Eng JK, von Haller PD, Fields S.
 Proteomics. 2012 Jan;12(2):236-40. [PMID: 22106047]
 [2] Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation.
 Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, Villén J.
 Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301] 
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 (RPB1). This promotes the activity of RNA polymerase II. 
Sequence Annotation
 DOMAIN 170 363 FCP1 homology.
 DOMAIN 499 593 BRCT.
 MOD_RES 701 701 Phosphoserine.
 MOD_RES 718 718 Phosphoserine.
 MOD_RES 720 720 Phosphoserine.  
Keyword
 Complete proteome; Hydrolase; Nucleus; Phosphoprotein; Protein phosphatase; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 732 AA 
Protein Sequence
MTTQIRSPQG LPYPIQIDKL IPSVGSYLHE GDRLLVYKFW YLVERASDTG DDDNEHDVSP 60
GGSAGSNGVS PPTKQLRESI EFFESPYEGD LISWNVDVGD EVATANQVIC EIKRPCNHDI 120
VYGGLCTQCG KEVSADAFDG VPLDVVGDVD LQISETEAIR TGKALKEHLR RDKKLILVVD 180
LDQTIIHCGV DPTIAEWKND PNNPNFETLR DVKSFTLDEE LVLPLMYMND DGSMLRPPPV 240
RKCWYYVKVR PGLKEFFAKV APLFEMHIYT MATRAYALQI AKIVDPTGEL FGDRILSRDE 300
NGSLTTKSLA KLFPTDQSMV VVIDDRGDVW NWCPNLIKVV PYNFFVGVGD INSNFLPKQS 360
TGMLQLGRKT RQKSQESQEL LTDIMDNEKK LQEKIDKEVK RQEEKLNHQL ATAEEPPANE 420
SKEELTKKLE YSASLEVQQQ NRPLAKLQKH LHDQKLLVDD DDELYYLMGT LSNIHKTYYD 480
MLSQQNEPEP NLMEIIPSLK QKVFQNCYFV FSGLIPLGTD IQRSDIVIWT STFGATSTPD 540
IDYLTTHLIT KNPSTYKARL AKKFNPQIKI VHPDWIFECL VNWKKVDEKP YTLIVDSPIS 600
DEELQNFQTQ LQKRQEYLEE TQEQQHMLTS QENLNLFAAG TSWLNNDDDE DIPDTASDDD 660
EDDDHDDESD DENNSEGIDR KRSIEDNHDD TSQKKTKAEP SQDGPVQHKG EGDDNEDSDS 720
QLEEELMDML DD 732 
Gene Ontology
 GO:0005829; C:cytosol; IDA:SGD.
 GO:0005634; C:nucleus; IDA:SGD.
 GO:0004722; F:protein serine/threonine phosphatase activity; IDA:SGD.
 GO:0070940; P:dephosphorylation of RNA polymerase II C-terminal domain; IDA:SGD. 
Interpro
 IPR001357; BRCT_dom.
 IPR011947; FCP1_euk.
 IPR023214; HAD-like_dom.
 IPR004274; NIF. 
Pfam
 PF00533; BRCT
 PF03031; NIF 
SMART
 SM00292; BRCT
 SM00577; CPDc 
PROSITE
 PS50172; BRCT
 PS50969; FCP1 
PRINTS