CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-017075
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Putative RNA polymerase II subunit B1 CTD phosphatase RPAP2 
Protein Synonyms/Alias
 RNA polymerase II-associated protein 2 
Gene Name
 RPAP2 
Gene Synonyms/Alias
 C1orf82 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
107CGYPLCQKKLGIVPKubiquitination[1]
363QVCPEVGKRNLLKVLubiquitination[2]
453LPSYENLKKETEKLNubiquitination[1]
479VLGEETTKSQDSEEHubiquitination[1]
Reference
 [1] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [2] 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] 
Functional Description
 Protein phosphatase that displays CTD phosphatase activity and regulates transcription of snRNA genes. Recognizes and binds phosphorylated 'Ser-7' of the C-terminal heptapeptide repeat domain (CTD) of the largest RNA polymerase II subunit POLR2A, and mediates dephosphorylation of 'Ser-5' of the CTD, thereby promoting transcription of snRNA genes. 
Sequence Annotation
 ZN_FING 77 160 RTR1-type.
 MOD_RES 433 433 Phosphoserine.
 MOD_RES 480 480 Phosphoserine.  
Keyword
 Alternative splicing; Coiled coil; Complete proteome; Cytoplasm; Hydrolase; Metal-binding; Nucleus; Phosphoprotein; Protein phosphatase; Reference proteome; Transcription; Transcription regulation; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 612 AA 
Protein Sequence
MADFAGPSSA GRKAGAPRCS RKAAGTKQTS TLKQEDASKR KAELEAAVRK KIEFERKALH 60
IVEQLLEENI TEEFLMECGR FITPAHYSDV VDERSIVKLC GYPLCQKKLG IVPKQKYKIS 120
TKTNKVYDIT ERKSFCSNFC YQASKFFEAQ IPKTPVWVRE EERHPDFQLL KEEQSGHSGE 180
EVQLCSKAIK TSDIDNPSHF EKQYESSSSS THSDSSSDNE QDFVSSILPG NRPNSTNIRP 240
QLHQKSIMKK KAGHKANSKH KDKEQTVVDV TEQLGDCKLD SQEKDATCEL PLQKVNTQSS 300
SNSTLPERLK ASENSESEYS RSEITLVGIS KKSAEHFKRK FAKSNQVSRS VSSSVQVCPE 360
VGKRNLLKVL KETLIEWKTE ETLRFLYGQN YASVCLKPEA SLVKEELDED DIISDPDSHF 420
PAWRESQNSL DESLPFRGSG TAIKPLPSYE NLKKETEKLN LRIREFYRGR YVLGEETTKS 480
QDSEEHDSTF PLIDSSSQNQ IRKRIVLEKL SKVLPGLLVP LQITLGDIYT QLKNLVRTFR 540
LTNRNIIHKP AEWTLIAMVL LSLLTPILGI QKHSQEGMVF TRFLDTLLEE LHLKNEDLES 600
LTIIFRTSCL PE 612 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:UniProtKB.
 GO:0016591; C:DNA-directed RNA polymerase II, holoenzyme; IDA:UniProtKB.
 GO:0008420; F:CTD phosphatase activity; IMP:UniProtKB.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0070940; P:dephosphorylation of RNA polymerase II C-terminal domain; IMP:UniProtKB.
 GO:0009301; P:snRNA transcription; IMP:UniProtKB. 
Interpro
 IPR007308; DUF408. 
Pfam
 PF04181; RPAP2_Rtr1 
SMART
  
PROSITE
 PS51479; ZF_RTR1 
PRINTS