CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-000250
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Carboxy-terminal domain RNA polymerase II polypeptide A small phosphatase 2 
Protein Synonyms/Alias
 Nuclear LIM interactor-interacting factor 2; NLI-interacting factor 2; Protein OS-4; Small C-terminal domain phosphatase 2; Small CTD phosphatase 2; SCP2 
Gene Name
 CTDSP2 
Gene Synonyms/Alias
 NIF2; OS4; SCP2 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
20EDALVLTKQGLVSKSubiquitination[1, 2]
Reference
 [1] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [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
 Preferentially catalyzes the dephosphorylation of 'Ser- 5' within the tandem 7 residues repeats in the C-terminal domain (CTD) of the largest RNA polymerase II subunit POLR2A. Negatively regulates RNA polymerase II transcription, possibly by controlling the transition from initiation/capping to processive transcript elongation. Recruited by REST to neuronal genes that contain RE-1 elements, leading to neuronal gene silencing in non-neuronal cells. May contribute to the development of sarcomas. 
Sequence Annotation
 DOMAIN 97 255 FCP1 homology.
 ACT_SITE 107 107 4-aspartylphosphate intermediate (By
 ACT_SITE 109 109 Proton donor (By similarity).
 METAL 107 107 Magnesium.
 METAL 109 109 Magnesium; via carbonyl oxygen.
 METAL 218 218 Magnesium.  
Keyword
 3D-structure; Complete proteome; Hydrolase; Metal-binding; Nucleus; Protein phosphatase; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 271 AA 
Protein Sequence
MEHGSIITQA RREDALVLTK QGLVSKSSPK KPRGRNIFKA LFCCFRAQHV GQSSSSTELA 60
AYKEEANTIA KSDLLQCLQY QFYQIPGTCL LPEVTEEDQG RICVVIDLDE TLVHSSFKPI 120
NNADFIVPIE IEGTTHQVYV LKRPYVDEFL RRMGELFECV LFTASLAKYA DPVTDLLDRC 180
GVFRARLFRE SCVFHQGCYV KDLSRLGRDL RKTLILDNSP ASYIFHPENA VPVQSWFDDM 240
ADTELLNLIP IFEELSGAED VYTSLGQLRA P 271 
Gene Ontology
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0008420; F:CTD phosphatase activity; IDA:UniProtKB.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0006987; P:activation of signaling protein activity involved in unfolded protein response; TAS:Reactome.
 GO:0006470; P:protein dephosphorylation; IDA:UniProtKB. 
Interpro
 IPR011948; Dullard_phosphatase.
 IPR023214; HAD-like_dom.
 IPR004274; NIF. 
Pfam
 PF03031; NIF 
SMART
 SM00577; CPDc 
PROSITE
 PS50969; FCP1 
PRINTS