CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-018322
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Ubiquitin-like domain-containing CTD phosphatase 1 
Protein Synonyms/Alias
 Nuclear proteasome inhibitor UBLCP1 
Gene Name
 UBLCP1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
117NREENLLKISRRVKEacetylation[1, 2, 3, 4]
193NMKWIEAKMKELGVSubiquitination[5]
195KWIEAKMKELGVSTNubiquitination[6, 7]
230RRGLIDVKPLGVIWGubiquitination[6]
245KFSEFYSKKNTIMFDacetylation[1, 4]
245KFSEFYSKKNTIMFDubiquitination[6]
267MNPQNGLKIRPFMKAubiquitination[4, 5, 7, 8, 9]
280KAHLNRDKDKELLKLacetylation[4]
286DKDKELLKLTQYLKEubiquitination[7, 8, 9]
292LKLTQYLKEIAKLDDubiquitination[5, 6, 8, 9]
296QYLKEIAKLDDFLDLubiquitination[8, 9]
306DFLDLNHKYWERYLSacetylation[1, 3]
Reference
 [1] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [2] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
 [3] 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]
 [4] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [5] 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]
 [6] 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]
 [7] 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]
 [8] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [9] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789
Functional Description
 Dephosphorylates 26S nuclear proteasomes, thereby decreasing their proteolytic activity. The dephosphorylation may prevent assembly of the core and regulatory particles (CP and RP) into mature 26S proteasome. 
Sequence Annotation
 DOMAIN 3 81 Ubiquitin-like.
 DOMAIN 133 294 FCP1 homology.
 REGION 133 294 Phosphatase.
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 117 117 N6-acetyllysine.  
Keyword
 3D-structure; Acetylation; Complete proteome; Hydrolase; Nucleus; Protein phosphatase; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 318 AA 
Protein Sequence
MALPIIVKWG GQEYSVTTLS EDDTVLDLKQ FLKTLTGVLP ERQKLLGLKV KGKPAENDVK 60
LGALKLKPNT KIMMMGTREE SLEDVLGPPP DNDDVVNDFD IEDEVVEVEN REENLLKISR 120
RVKEYKVEIL NPPREGKKLL VLDVDYTLFD HRSCAETGVE LMRPYLHEFL TSAYEDYDIV 180
IWSATNMKWI EAKMKELGVS TNANYKITFM LDSAAMITVH TPRRGLIDVK PLGVIWGKFS 240
EFYSKKNTIM FDDIGRNFLM NPQNGLKIRP FMKAHLNRDK DKELLKLTQY LKEIAKLDDF 300
LDLNHKYWER YLSKKQGQ 318 
Gene Ontology
 GO:0005730; C:nucleolus; IDA:HPA.
 GO:0004721; F:phosphoprotein phosphatase activity; IEA:UniProtKB-KW. 
Interpro
 IPR023214; HAD-like_dom.
 IPR011943; HAD-SF_hydro_IIID.
 IPR004274; NIF.
 IPR000626; Ubiquitin.
 IPR019955; Ubiquitin_supergroup. 
Pfam
 PF03031; NIF
 PF00240; ubiquitin 
SMART
 SM00577; CPDc
 SM00213; UBQ 
PROSITE
 PS50969; FCP1
 PS00299; UBIQUITIN_1
 PS50053; UBIQUITIN_2 
PRINTS