CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-007688
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Enhancer of polycomb-like protein 1 
Protein Synonyms/Alias
  
Gene Name
 EPL1 
Gene Synonyms/Alias
 YFL024C 
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
16EINDGSHKSGRSTRRacetylation[1]
39DGLDSFSKGDSGAGAacetylation[1, 2]
96EIETGVEKNEEKEVHacetylation[1]
100GVEKNEEKEVHLHRIacetylation[1]
116QMGSGHTKHKDYIPTacetylation[1]
118GSGHTKHKDYIPTPDacetylation[1]
345HQELKNAKDLALLVAacetylation[1, 2]
353DLALLVAKRENVSLNacetylation[1, 2]
376FDQRVKIKNLKRSLNacetylation[1]
379RVKIKNLKRSLNISGacetylation[1]
395DDDLINHKRKRPTIVacetylation[1]
427AAAAAAAKAKNNKRNacetylation[1, 2]
429AAAAAKAKNNKRNNQacetylation[1]
446DKSSRLTKQQQQQLLacetylation[1]
470ALKTENGKQLANASSacetylation[1]
496YVKLPSSKIPDIVLEacetylation[1]
512VDALLNSKEKNARKFacetylation[1]
569FASIASSKFQIDRSFacetylation[1, 2]
648RVGRSNIKYVDRMPNubiquitination[3]
721PQNEYGIKFSDEPARacetylation[1]
821SLINSEAKQNSSITQacetylation[1]
Reference
 [1] mChIP-KAT-MS, a method to map protein interactions and acetylation sites for lysine acetyltransferases.
 Mitchell L, Huard S, Cotrut M, Pourhanifeh-Lemeri R, Steunou AL, Hamza A, Lambert JP, Zhou H, Ning Z, Basu A, Côté J, Figeys DA, Baetz K.
 Proc Natl Acad Sci U S A. 2013 Apr 23;110(17):E1641-50. [PMID: 23572591]
 [2] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae.
 Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C.
 Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [PMID: 22865919]
 [3] 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
 Component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of selected genes principally by acetylation of nucleosomal histone H4 and H2A. The NuA4 complex is also involved in DNA repair. Involved in gene silencing by neighboring heterochromatin, blockage of the silencing spreading along the chromosome, and required for cell cycle progression through G2/M. 
Sequence Annotation
  
Keyword
 Cell cycle; Complete proteome; Direct protein sequencing; DNA damage; DNA repair; Nucleus; Reference proteome; Transcription; Transcription regulation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 832 AA 
Protein Sequence
MPTPSNAIEI NDGSHKSGRS TRRSGSRSAH DDGLDSFSKG DSGAGASAGS SNSRFRHRKI 60
SVKQHLKIYL PNDLKHLDKD ELQQREVVEI ETGVEKNEEK EVHLHRILQM GSGHTKHKDY 120
IPTPDASMTW NEYDKFYTGS FQETTSYIKF SATVEDCCGT NYNMDERDET FLNEQVNKGS 180
SDILTEDEFE ILCSSFEHAI HERQPFLSMD PESILSFEEL KPTLIKSDMA DFNLRNQLNH 240
EINSHKTHFI TQFDPVSQMN TRPLIQLIEK FGSKIYDYWR ERKIEVNGYE IFPQLKFERP 300
GEKEEIDPYV CFRRREVRHP RKTRRIDILN SQRLRALHQE LKNAKDLALL VAKRENVSLN 360
WINDELKIFD QRVKIKNLKR SLNISGEDDD LINHKRKRPT IVTVEQREAE LRKAELKRAA 420
AAAAAAKAKN NKRNNQLEDK SSRLTKQQQQ QLLQQQQQQQ QNALKTENGK QLANASSSST 480
SQPITSHVYV KLPSSKIPDI VLEDVDALLN SKEKNARKFV QEKMEKRKIE DADVFFNLTD 540
DPFNPVFDMS LPKNFSTSNV PFASIASSKF QIDRSFYSSH LPEYLKGISD DIRIYDSNGR 600
SRNKDNYNLD TKRIKKTELY DPFQENLEIH SREYPIKFRK RVGRSNIKYV DRMPNFTTSS 660
TKSACSLMDF VDFDSIEKEQ YSREGSNDTD SINVYDSKYD EFVRLYDKWK YDSPQNEYGI 720
KFSDEPARLN QISNDTQVIR FGTMLGTKSY EQLREATIKY RRDYITRLKQ KHIQHLQQQQ 780
QQQQQQQQQA QQQKQKSQNN NSNSSNSLKK LNDSLINSEA KQNSSITQKN SS 832 
Gene Ontology
 GO:0032777; C:Piccolo NuA4 histone acetyltransferase complex; IDA:SGD.
 GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
 GO:0006281; P:DNA repair; IDA:SGD.
 GO:0016573; P:histone acetylation; IDA:SGD.
 GO:0016239; P:positive regulation of macroautophagy; IMP:SGD.
 GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IDA:SGD.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
Interpro
 IPR024943; Enhancer_polycomb.
 IPR019542; Enhancer_polycomb-like_N. 
Pfam
 PF10513; EPL1 
SMART
  
PROSITE
  
PRINTS