CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-021391
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 ESF1 homolog 
Protein Synonyms/Alias
 ABT1-associated protein 
Gene Name
 ESF1 
Gene Synonyms/Alias
 ABTAP; C20orf6; HDCMC28P 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
4****MSSKQEIMSDQacetylation[1]
4****MSSKQEIMSDQubiquitination[2, 3, 4]
28RFWEMPEKDRKVKIDubiquitination[3]
55KLNYAVDKRGRPISHubiquitination[5]
69HSTTEDLKRFYDLSDubiquitination[3, 5]
108TKKEIDSKNLVEKKKubiquitination[3]
128NHKGSENKTDLDNSIacetylation[6]
128NHKGSENKTDLDNSIubiquitination[3, 5]
138LDNSIGIKKMKTSCKubiquitination[3]
170QKNKKEKKNIVQHTTubiquitination[5]
184TDSSLEEKQRTLDSGacetylation[7]
184TDSSLEEKQRTLDSGubiquitination[3, 4, 5, 8]
197SGTSEIVKSPRIECSubiquitination[4, 5]
395EFGKERMKEEQVQGPubiquitination[3, 5]
415IPEDAPEKDWTSREKubiquitination[5]
573GKTKKSQKDDEEQIAubiquitination[5]
581DDEEQIAKYRQLLQVubiquitination[3, 5]
597QEKEKKGKENDMEMEubiquitination[3, 4]
612IKWVPGLKESAEEMVubiquitination[3]
628NKLEGKDKLTPWEQFubiquitination[3, 4, 5]
690KKSVKSAKDGTSPEEubiquitination[3, 4, 5]
793MEKILEEKARQRERKubiquitination[3, 4]
800KARQRERKEQELTQAubiquitination[3]
809QELTQAIKKKESEIEubiquitination[5]
810ELTQAIKKKESEIEKubiquitination[5]
817KKESEIEKESQRKSIubiquitination[4]
822IEKESQRKSIDPALSubiquitination[3, 4]
838LIKSIKTKTEQFQARubiquitination[3, 4]
Reference
 [1] 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]
 [2] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [3] 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]
 [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] Spermidine and resveratrol induce autophagy by distinct pathways converging on the acetylproteome.
 Morselli E, Mariño G, Bennetzen MV, Eisenberg T, Megalou E, Schroeder S, Cabrera S, Bénit P, Rustin P, Criollo A, Kepp O, Galluzzi L, Shen S, Malik SA, Maiuri MC, Horio Y, López-Otín C, Andersen JS, Tavernarakis N, Madeo F, Kroemer G.
 J Cell Biol. 2011 Feb 21;192(4):615-29. [PMID: 21339330]
 [7] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]
 [8] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094
Functional Description
 May constitute a novel regulatory system for basal transcription. Negatively regulates ABT1 (By similarity). 
Sequence Annotation
 MOD_RES 75 75 Phosphoserine.
 MOD_RES 77 77 Phosphoserine.
 MOD_RES 79 79 Phosphoserine.
 MOD_RES 82 82 Phosphoserine.
 MOD_RES 153 153 Phosphoserine.
 MOD_RES 179 179 Phosphoserine.
 MOD_RES 180 180 Phosphoserine.
 MOD_RES 198 198 Phosphoserine.
 MOD_RES 296 296 Phosphoserine.
 MOD_RES 298 298 Phosphoserine.
 MOD_RES 311 311 Phosphothreonine.
 MOD_RES 312 312 Phosphoserine.
 MOD_RES 313 313 Phosphoserine.
 MOD_RES 657 657 Phosphoserine.
 MOD_RES 663 663 Phosphoserine.
 MOD_RES 693 693 Phosphothreonine.
 MOD_RES 694 694 Phosphoserine.
 MOD_RES 735 735 Phosphoserine.
 MOD_RES 823 823 Phosphoserine.  
Keyword
 Coiled coil; Complete proteome; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Transcription; Transcription regulation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 851 AA 
Protein Sequence
MSSKQEIMSD QRFRRVAKDP RFWEMPEKDR KVKIDKRFRA MFHDKKFKLN YAVDKRGRPI 60
SHSTTEDLKR FYDLSDSDSN LSGEDSKALS QKKIKKKKTQ TKKEIDSKNL VEKKKETKKA 120
NHKGSENKTD LDNSIGIKKM KTSCKFKIDS NISPKKDSKE FTQKNKKEKK NIVQHTTDSS 180
LEEKQRTLDS GTSEIVKSPR IECSKTRREM QSVVQLIMTR DSDGYENSTD GEMCDKDALE 240
EDSESVSEIG SDEESENEIT SVGRASGDDD GSEDDEEEDE DEEEDEDEDS EDDDKSDSGP 300
DLARGKGNIE TSSEDEDDTA DLFPEESGFE HAWRELDKDA PRADEITRRL AVCNMDWDRL 360
KAKDLLALFN SFKPKGGVIF SVKIYPSEFG KERMKEEQVQ GPVELLSIPE DAPEKDWTSR 420
EKLRDYQFKR LKYYYAVVDC DSPETASKIY EDCDGLEFES SCSFIDLRFI PDDITFDDEP 480
KDVASEVNLT AYKPKYFTSA AMGTSTVEIT WDETDHERIT MLNRKFKKEE LLDMDFQAYL 540
ASSSEDEEEI EEELQGDDGV NVEEDGKTKK SQKDDEEQIA KYRQLLQVIQ EKEKKGKEND 600
MEMEIKWVPG LKESAEEMVK NKLEGKDKLT PWEQFLEKKK EKKRLKRKQK ALAEEASEEE 660
LPSDVDLNDP YFAEEVKQIG INKKSVKSAK DGTSPEEEIE IERQKAEMAL LMMDEDEDSK 720
KHFNYNKIVE HQNLSKKKKK QLMKKKELIE DDFEVNVNDA RFQAMYTSHL FNLDPSDPNF 780
KKTKAMEKIL EEKARQRERK EQELTQAIKK KESEIEKESQ RKSIDPALSM LIKSIKTKTE 840
QFQARKKQKV K 851 
Gene Ontology
 GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
 GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
 GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
Interpro
 IPR012580; NUC153. 
Pfam
 PF08159; NUC153 
SMART
  
PROSITE
  
PRINTS