CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-011082
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 DNA excision repair protein ERCC-6 
Protein Synonyms/Alias
 ATP-dependent helicase ERCC6; Cockayne syndrome protein CSB 
Gene Name
 ERCC6 
Gene Synonyms/Alias
 CSB 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
170TSRDINRKLDSVKRQmethylation[1, 2]
297CNKRAARKAPAPVTPmethylation[1, 2]
448EGGGGGRKVGRYRDDmethylation[1, 2]
783YQNFVDSKEVYRILNubiquitination[3]
1054DHDVPKRKKFPASNImethylation[1, 2]
1457ILQEFESKLSASQSCubiquitination[4, 5, 6, 7]
Reference
 [1] Protein lysine methyltransferase G9a acts on non-histone targets.
 Rathert P, Dhayalan A, Murakami M, Zhang X, Tamas R, Jurkowska R, Komatsu Y, Shinkai Y, Cheng X, Jeltsch A.
 Nat Chem Biol. 2008 Jun;4(6):344-6. [PMID: 18438403]
 [2] Update on activities at the Universal Protein Resource (UniProt) in 2013.
 e="String">UniProt Consortium.
 Nucleic Acids Res. 2013 Jan;41(Database issue):D43-7. [PMID: 23161681]
 [3] 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]
 [4] 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]
 [5] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [6] 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]
 [7] 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
 Essential factor involved in transcription-coupled nucleotide excision repair which allows RNA polymerase II-blocking lesions to be rapidly removed from the transcribed strand of active genes. Upon DNA-binding, it locally modifies DNA conformation by wrapping the DNA around itself, thereby modifying the interface between stalled RNA polymerase II and DNA. It is required for transcription-coupled repair complex formation. It recruits the CSA complex (DCX(ERCC8) complex), nucleotide excision repair proteins and EP300 to the at sites of RNA polymerase II- blocking lesions. 
Sequence Annotation
 DOMAIN 519 695 Helicase ATP-binding.
 DOMAIN 843 1002 Helicase C-terminal.
 NP_BIND 532 539 ATP (Potential).
 REGION 1400 1428 Ubiquitin-binding domain (UBD).
 MOTIF 466 481 Nuclear localization signal (Potential).
 MOTIF 646 649 DEGH box.
 MOTIF 1038 1055 Nuclear localization signal (Potential).
 MOD_RES 170 170 N6-methylated lysine; by EHMT2.
 MOD_RES 297 297 N6-methylated lysine; by EHMT2.
 MOD_RES 448 448 N6-methylated lysine; by EHMT2.
 MOD_RES 486 486 Phosphoserine.
 MOD_RES 489 489 Phosphoserine.
 MOD_RES 1054 1054 N6-methylated lysine; by EHMT2.
 MOD_RES 1142 1142 Phosphoserine.
 MOD_RES 1348 1348 Phosphoserine.  
Keyword
 Age-related macular degeneration; ATP-binding; Cataract; Cockayne syndrome; Complete proteome; Deafness; Disease mutation; DNA damage; DNA repair; DNA-binding; Dwarfism; Helicase; Hydrolase; Mental retardation; Methylation; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Transcription; Transcription regulation; Ubl conjugation; Xeroderma pigmentosum. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1493 AA 
Protein Sequence
MPNEGIPHSS QTQEQDCLQS QPVSNNEEMA IKQESGGDGE VEEYLSFRSV GDGLSTSAVG 60
CASAAPRRGP ALLHIDRHQI QAVEPSAQAL ELQGLGVDVY DQDVLEQGVL QQVDNAIHEA 120
SRASQLVDVE KEYRSVLDDL TSCTTSLRQI NKIIEQLSPQ AATSRDINRK LDSVKRQKYN 180
KEQQLKKITA KQKHLQAILG GAEVKIELDH ASLEEDAEPG PSSLGSMLMP VQETAWEELI 240
RTGQMTPFGT QIPQKQEKKP RKIMLNEASG FEKYLADQAK LSFERKKQGC NKRAARKAPA 300
PVTPPAPVQN KNKPNKKARV LSKKEERLKK HIKKLQKRAL QFQGKVGLPK ARRPWESDMR 360
PEAEGDSEGE ESEYFPTEEE EEEEDDEVEG AEADLSGDGT DYELKPLPKG GKRQKKVPVQ 420
EIDDDFFPSS GEEAEAASVG EGGGGGRKVG RYRDDGDEDY YKQRLRRWNK LRLQDKEKRL 480
KLEDDSEESD AEFDEGFKVP GFLFKKLFKY QQTGVRWLWE LHCQQAGGIL GDEMGLGKTI 540
QIIAFLAGLS YSKIRTRGSN YRFEGLGPTV IVCPTTVMHQ WVKEFHTWWP PFRVAILHET 600
GSYTHKKEKL IRDVAHCHGI LITSYSYIRL MQDDISRYDW HYVILDEGHK IRNPNAAVTL 660
ACKQFRTPHR IILSGSPMQN NLRELWSLFD FIFPGKLGTL PVFMEQFSVP ITMGGYSNAS 720
PVQVKTAYKC ACVLRDTINP YLLRRMKSDV KMSLSLPDKN EQVLFCRLTD EQHKVYQNFV 780
DSKEVYRILN GEMQIFSGLI ALRKICNHPD LFSGGPKNLK GLPDDELEED QFGYWKRSGK 840
MIVVESLLKI WHKQGQRVLL FSQSRQMLDI LEVFLRAQKY TYLKMDGTTT IASRQPLITR 900
YNEDTSIFVF LLTTRVGGLG VNLTGANRVV IYDPDWNPST DTQARERAWR IGQKKQVTVY 960
RLLTAGTIEE KIYHRQIFKQ FLTNRVLKDP KQRRFFKSND LYELFTLTSP DASQSTETSA 1020
IFAGTGSDVQ TPKCHLKRRI QPAFGADHDV PKRKKFPASN ISVNDATSSE EKSEAKGAEV 1080
NAVTSNRSDP LKDDPHMSSN VTSNDRLGEE TNAVSGPEEL SVISGNGECS NSSGTGKTSM 1140
PSGDESIDEK LGLSYKRERP SQAQTEAFWE NKQMENNFYK HKSKTKHHSV AEEETLEKHL 1200
RPKQKPKNSK HCRDAKFEGT RIPHLVKKRR YQKQDSENKS EAKEQSNDDY VLEKLFKKSV 1260
GVHSVMKHDA IMDGASPDYV LVEAEANRVA QDALKALRLS RQRCLGAVSG VPTWTGHRGI 1320
SGAPAGKKSR FGKKRNSNFS VQHPSSTSPT EKCQDGIMKK EGKDNVPEHF SGRAEDADSS 1380
SGPLASSSLL AKMRARNHLI LPERLESESG HLQEASALLP TTEHDDLLVE MRNFIAFQAH 1440
TDGQASTREI LQEFESKLSA SQSCVFRELL RNLCTFHRTS GGEGIWKLKP EYC 1493 
Gene Ontology
 GO:0005730; C:nucleolus; IDA:UniProtKB.
 GO:0008023; C:transcription elongation factor complex; IDA:UniProtKB.
 GO:0005524; F:ATP binding; IDA:UniProtKB.
 GO:0003682; F:chromatin binding; IDA:UniProtKB.
 GO:0003677; F:DNA binding; IDA:UniProtKB.
 GO:0008094; F:DNA-dependent ATPase activity; IDA:UniProtKB.
 GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
 GO:0032403; F:protein complex binding; IDA:UniProtKB.
 GO:0007256; P:activation of JNKK activity; IEA:Compara.
 GO:0007257; P:activation of JUN kinase activity; IEA:Compara.
 GO:0006284; P:base-excision repair; IMP:UniProtKB.
 GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IEA:Compara.
 GO:0045494; P:photoreceptor cell maintenance; IEA:Compara.
 GO:0032786; P:positive regulation of DNA-dependent transcription, elongation; IDA:UniProtKB.
 GO:0006290; P:pyrimidine dimer repair; IEA:Compara.
 GO:0010332; P:response to gamma radiation; IEA:Compara.
 GO:0006979; P:response to oxidative stress; IDA:UniProtKB.
 GO:0000303; P:response to superoxide; IEA:Compara.
 GO:0009636; P:response to toxic substance; IEA:Compara.
 GO:0009411; P:response to UV; IDA:UniProtKB.
 GO:0010224; P:response to UV-B; IEA:Compara.
 GO:0010165; P:response to X-ray; IEA:Compara.
 GO:0006366; P:transcription from RNA polymerase II promoter; NAS:UniProtKB.
 GO:0006283; P:transcription-coupled nucleotide-excision repair; IMP:UniProtKB. 
Interpro
 IPR014001; Helicase_ATP-bd.
 IPR001650; Helicase_C.
 IPR027417; P-loop_NTPase.
 IPR000330; SNF2_N. 
Pfam
 PF00271; Helicase_C
 PF00176; SNF2_N 
SMART
 SM00487; DEXDc
 SM00490; HELICc 
PROSITE
 PS51192; HELICASE_ATP_BIND_1
 PS51194; HELICASE_CTER 
PRINTS