CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-000043
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 E3 SUMO-protein ligase CBX4 
Protein Synonyms/Alias
 Chromobox protein homolog 4; Polycomb 2 homolog; Pc2; hPc2 
Gene Name
 CBX4 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
38KWRGWSPKYNTWEPEubiquitination[1]
114LDLGAQGKGQGHQYEubiquitination[1]
149PPPGKSGKYYYQLNSacetylation[2]
178LQYQGGHKEAPSPTCubiquitination[1]
212KGYLGAVKPLAGAAGubiquitination[1, 3, 4]
249TGNGIGGKMKIVKNKubiquitination[1]
278ENGMQAVKIKSGEVAubiquitination[1]
280GMQAVKIKSGEVAEGubiquitination[1]
365QPLQLTTKPDLLAWDubiquitination[5]
494PPSSLQVKPETPASAsumoylation[6]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [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] 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]
 [6] ZNF198, a zinc finger protein rearranged in myeloproliferative disease, localizes to the PML nuclear bodies and interacts with SUMO-1 and PML.
 Kunapuli P, Kasyapa CS, Chin SF, Caldas C, Cowell JK.
 Exp Cell Res. 2006 Nov 15;312(19):3739-51. [PMID: 17027752] 
Functional Description
 E3 SUMO-protein ligase which facilitates SUMO1 conjugation by UBE2I. Involved in the sumoylation of HNRNPK, a p53/TP53 transcriptional coactivator, hence indirectly regulates p53/TP53 transcriptional activation resulting in p21/CDKN1A expression. Monosumoylates ZNF131. 
Sequence Annotation
 DOMAIN 11 69 Chromo.
 REGION 1 539 Interaction with BMI1.
 REGION 540 560 Interaction with RNF2.
 MOD_RES 149 149 N6-acetyllysine.
 CROSSLNK 494 494 Glycyl lysine isopeptide (Lys-Gly)  
Keyword
 3D-structure; Acetylation; Alternative splicing; Chromatin regulator; Complete proteome; Isopeptide bond; Ligase; Nucleus; Phosphoprotein; Reference proteome; Repressor; Transcription; Transcription regulation; Ubl conjugation; Ubl conjugation pathway. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 560 AA 
Protein Sequence
MELPAVGEHV FAVESIEKKR IRKGRVEYLV KWRGWSPKYN TWEPEENILD PRLLIAFQNR 60
ERQEQLMGYR KRGPKPKPLV VQVPTFARRS NVLTGLQDSS TDNRAKLDLG AQGKGQGHQY 120
ELNSKKHHQY QPHSKERAGK PPPPGKSGKY YYQLNSKKHH PYQPDPKMYD LQYQGGHKEA 180
PSPTCPDLGA KSHPPDKWAQ GAGAKGYLGA VKPLAGAAGA PGKGSEKGPP NGMMPAPKEA 240
VTGNGIGGKM KIVKNKNKNG RIVIVMSKYM ENGMQAVKIK SGEVAEGEAR SPSHKKRAAD 300
ERHPPADRTF KKAAGAEEKK VEAPPKRREE EVSGVSDPQP QDAGSRKLSP TKEAFGEQPL 360
QLTTKPDLLA WDPARNTHPP SHHPHPHPHH HHHHHHHHHH AVGLNLSHVR KRCLSETHGE 420
REPCKKRLTA RSISTPTCLG GSPAAERPAD LPPAAALPQP EVILLDSDLD EPIDLRCVKT 480
RSEAGEPPSS LQVKPETPAS AAVAVAAAAA PTTTAEKPPA EAQDEPAESL SEFKPFFGNI 540
IITDVTANCL TVTFKEYVTV 560 
Gene Ontology
 GO:0005794; C:Golgi apparatus; IDA:HPA.
 GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
 GO:0035102; C:PRC1 complex; IDA:UniProtKB.
 GO:0003682; F:chromatin binding; IEA:Compara.
 GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
 GO:0003727; F:single-stranded RNA binding; IEA:Compara.
 GO:0032183; F:SUMO binding; IDA:MGI.
 GO:0003714; F:transcription corepressor activity; TAS:ProtInc.
 GO:0044212; F:transcription regulatory region DNA binding; IEA:Compara.
 GO:0016568; P:chromatin modification; IEA:UniProtKB-KW.
 GO:0043066; P:negative regulation of apoptotic process; TAS:ProtInc.
 GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IMP:UniProtKB.
 GO:0016925; P:protein sumoylation; IEA:UniProtKB-UniPathway.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
Interpro
 IPR017984; Chromo_dom_subgr.
 IPR023780; Chromo_domain.
 IPR000953; Chromo_domain/shadow.
 IPR016197; Chromodomain-like.
 IPR023779; Chromodomain_CS. 
Pfam
 PF00385; Chromo 
SMART
 SM00298; CHROMO 
PROSITE
 PS00598; CHROMO_1
 PS50013; CHROMO_2 
PRINTS
 PR00504; CHROMODOMAIN.