Q03468 (ERCC6_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
DNA excision repair protein ERCC-6
EC=3.6.4.-

Alternative name(s):
ATP-dependent helicase ERCC6
Cockayne syndrome protein CSB

Gene names

Name:	ERCC6
Synonyms:	CSB

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1493 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.11 Ref.14 Ref.18
Subunit structure	Homodimer. Binds DNA. Interacts with ERCC8. Interacts with a subunit of RNA polymerase II TFIIH. Component of the B-WICH complex, at least composed of SMARCA5/SNF2H, BAZ1B/WSTF, SF3B1, DEK, MYO1C, ERCC6, MYBBP1A and DDX21. Interacts with KIAA1530/UVSSA. Ref.10 Ref.11 Ref.12 Ref.13 Ref.24
Subcellular location	Nucleus Ref.10.
Domain	A C-terminal ubiquitin-binding domain (UBD) is essential for transcription-coupled nucleotide excision repair to proceed. Ref.18
Post-translational modification	Ubiquitinated at the C-terminus. Ubiquitination by the CSA complex leads to ERCC6 proteasomal degradation in a UV-dependent manner. Stabilized following interaction with KIAA1530/UVSSA, which promotes recruitment of deubiquitinating enzyme USP7, leading to deubiquitination of ERCC6 thereby preventing UV-induced degradation of ERCC6 by the proteasome. Ref.12 Ref.18 Ref.22 Ref.23 Ref.24
Involvement in disease	Cockayne syndrome B (CSB) [MIM:133540]: A rare disorder characterized by cutaneous sensitivity to sunlight, abnormal and slow growth, cachectic dwarfism, progeroid appearance, progressive pigmentary retinopathy and sensorineural deafness. There is delayed neural development and severe progressive neurologic degeneration resulting in mental retardation. Two clinical forms are recognized: in the classical form or Cockayne syndrome type 1, the symptoms are progressive and typically become apparent within the first few years or life; the less common Cockayne syndrome type 2 is characterized by more severe symptoms that manifest prenatally. Cockayne syndrome shows some overlap with certain forms of xeroderma pigmentosum. Unlike xeroderma pigmentosum, patients with Cockayne syndrome do not manifest increased freckling and other pigmentation abnormalities in the skin and have no significant increase in skin cancer. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.7 Ref.8 Ref.25 Ref.28 Cerebro-oculo-facio-skeletal syndrome 1 (COFS1) [MIM:214150]: A disorder of prenatal onset characterized by microcephaly, congenital cataracts, facial dysmorphism, neurogenic arthrogryposis, growth failure and severe psychomotor retardation. COFS is considered to be part of the nucleotide-excision repair disorders spectrum that include also xeroderma pigmentosum, trichothiodystrophy and Cockayne syndrome. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.7 Ref.8 Ref.28 De Sanctis-Cacchione syndrome (DSC) [MIM:278800]: An autosomal recessive syndrome consisting of xeroderma pigmentosum associated with severe neurological and developmental involvement. In addition to the clinical signs of xeroderma pigmentosum, patients present with mental retardation, dwarfism, gonadal hypoplasia, microcephaly and various neurologic complications of early onset. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.7 Ref.8 Age-related macular degeneration 5 (ARMD5) [MIM:613761]: A form of age-related macular degeneration, a multifactorial eye disease and the most common cause of irreversible vision loss in the developed world. In most patients, the disease is manifest as ophthalmoscopically visible yellowish accumulations of protein and lipid that lie beneath the retinal pigment epithelium and within an elastin-containing structure known as Bruch membrane. Note: Disease susceptibility is associated with variations affecting the gene represented in this entry. Ref.7 Ref.8 Ref.15 UV-sensitive syndrome 1 (UVSS1) [MIM:600630]: An autosomal recessive disorder characterized by cutaneous photosensitivity and mild freckling in the absence of neurological abnormalities or skin tumors. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.7 Ref.8 Ref.9
Sequence similarities	Belongs to the SNF2/RAD54 helicase family. Contains 1 helicase ATP-binding domain. Contains 1 helicase C-terminal domain.

Ontologies

Keywords
Biological process	DNA damage DNA repair Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Polymorphism
Disease	Age-related macular degeneration Cataract Cockayne syndrome Deafness Disease mutation Dwarfism Mental retardation Xeroderma pigmentosum
Ligand	ATP-binding DNA-binding Nucleotide-binding
Molecular function	Helicase Hydrolase
PTM	Methylation Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	activation of JNKK activity Inferred from electronic annotation. Source: Compara activation of JUN kinase activity Inferred from electronic annotation. Source: Compara base-excision repair Inferred from mutant phenotype PubMed 9973627. Source: UniProtKB intrinsic apoptotic signaling pathway in response to DNA damage Inferred from electronic annotation. Source: Compara photoreceptor cell maintenance Inferred from electronic annotation. Source: Compara positive regulation of DNA-dependent transcription, elongation Inferred from direct assay PubMed 9326587. Source: UniProtKB pyrimidine dimer repair Inferred from electronic annotation. Source: Compara response to UV Inferred from direct assay Ref.14. Source: UniProtKB response to UV-B Inferred from electronic annotation. Source: Compara response to X-ray Inferred from electronic annotation. Source: Compara response to gamma radiation Inferred from electronic annotation. Source: Compara response to oxidative stress Inferred from direct assay PubMed 16107709. Source: UniProtKB response to superoxide Inferred from electronic annotation. Source: Compara response to toxin Inferred from electronic annotation. Source: Compara transcription from RNA polymerase II promoter Non-traceable author statement PubMed 7664335. Source: UniProtKB transcription-coupled nucleotide-excision repair Inferred from mutant phenotype PubMed 10564257Ref.14. Source: UniProtKB
Cellular_component	nucleolus Inferred from direct assay PubMed 16107709. Source: UniProtKB transcription elongation factor complex Inferred from direct assay PubMed 9326587. Source: UniProtKB
Molecular_function	ATP binding Inferred from direct assay PubMed 12560492PubMed 16107709. Source: UniProtKB DNA binding Inferred from direct assay PubMed 12560492PubMed 16107709PubMed 8999876. Source: UniProtKB DNA-dependent ATPase activity Inferred from direct assay PubMed 12560492PubMed 16107709PubMed 8999876. Source: UniProtKB chromatin binding Inferred from direct assay Ref.14. Source: UniProtKB helicase activity Inferred from electronic annotation. Source: UniProtKB-KW protein complex binding Inferred from direct assay Ref.14. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ERCC8	Q13216-1	2	EBI-295284,EBI-596556

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1493	1493	DNA excision repair protein ERCC-6		PRO_0000074314
Regions
	Domain	519 – 695	177	Helicase ATP-binding
	Domain	843 – 1002	160	Helicase C-terminal
	Nucleotide binding	532 – 539	8	ATP Potential
	Region	1400 – 1428	29	Ubiquitin-binding domain (UBD)
	Motif	466 – 481	16	Nuclear localization signal Potential
	Motif	646 – 649	4	DEGH box
	Motif	1038 – 1055	18	Nuclear localization signal Potential
	Compositional bias	356 – 394	39	Asp/Glu-rich (acidic)
	Compositional bias	442 – 446	5	Gly-rich
Amino acid modifications
	Modified residue	170	1	N6-methylated lysine; by EHMT2 Ref.16
	Modified residue	297	1	N6-methylated lysine; by EHMT2 Ref.16
	Modified residue	448	1	N6-methylated lysine; by EHMT2 Ref.16
	Modified residue	486	1	Phosphoserine Ref.21
	Modified residue	489	1	Phosphoserine Ref.21
	Modified residue	1054	1	N6-methylated lysine; by EHMT2 Ref.16
	Modified residue	1142	1	Phosphoserine Ref.17
	Modified residue	1348	1	Phosphoserine Ref.17
Natural variations
	Natural variant	134	1	R → W. Ref.27		VAR_054153
	Natural variant	255	1	K → T. Ref.25		VAR_001216
	Natural variant	399	1	G → D. Ref.3 Ref.25 Corresponds to variant rs2228528 [ dbSNP | Ensembl ].		VAR_001217
	Natural variant	425	1	D → A. Ref.3 Corresponds to variant rs4253046 [ dbSNP | Ensembl ].		VAR_016301
	Natural variant	446	1	G → D. Ref.3 Corresponds to variant rs4253047 [ dbSNP | Ensembl ].		VAR_016302
	Natural variant	591	1	P → A in a colorectal cancer sample; somatic mutation. Ref.26		VAR_036021
	Natural variant	652	1	R → L in a colorectal cancer sample; somatic mutation. Ref.26		VAR_036022
	Natural variant	670	1	R → W in CSB. Ref.25 Ref.28		VAR_001218
	Natural variant	680	1	N → D in CSB. Ref.28		VAR_063511
	Natural variant	686	1	W → C in CSB. Ref.28		VAR_063512
	Natural variant	687	1	S → L in CSB. Ref.28		VAR_063513
	Natural variant	851	1	W → R in CSB. Ref.25 Ref.28		VAR_001219
	Natural variant	871	1	L → P in COFS1. Ref.28		VAR_063514
	Natural variant	942	1	T → M. Ref.3 Corresponds to variant rs2228525 [ dbSNP | Ensembl ].		VAR_016303
	Natural variant	957	1	V → G in CSB. Ref.25 Ref.28		VAR_001220
	Natural variant	987	1	L → P in COFS1. Ref.28		VAR_063515
	Natural variant	1002	1	Y → C. Ref.3 Corresponds to variant rs4253206 [ dbSNP | Ensembl ].		VAR_016304
	Natural variant	1038	1	R → T in a breast cancer sample; somatic mutation. Ref.26		VAR_036023
	Natural variant	1042	1	P → L in CSB. Ref.25 Ref.28		VAR_001221
	Natural variant	1095	1	P → R. Ref.3 Ref.25 Ref.28 Corresponds to variant rs4253208 [ dbSNP | Ensembl ].		VAR_001222
	Natural variant	1097	1	M → V. Ref.3 Ref.25 Corresponds to variant rs2228526 [ dbSNP | Ensembl ].		VAR_001223
	Natural variant	1119	1	E → Q in a breast cancer sample; somatic mutation. Ref.26		VAR_036024
	Natural variant	1119	1	E → V in a breast cancer sample; somatic mutation. Ref.26		VAR_036025
	Natural variant	1213	1	R → G. Ref.3 Ref.25 Ref.28 Corresponds to variant rs2228527 [ dbSNP | Ensembl ].		VAR_001224
	Natural variant	1220	1	T → I. Corresponds to variant rs34704611 [ dbSNP | Ensembl ].		VAR_037436
	Natural variant	1230	1	R → P. Ref.3 Corresponds to variant rs4253211 [ dbSNP | Ensembl ].		VAR_016305
	Natural variant	1308	1	V → L. Ref.3 Corresponds to variant rs2229761 [ dbSNP | Ensembl ].		VAR_016306
	Natural variant	1322	1	G → V. Ref.3 Corresponds to variant rs4253219 [ dbSNP | Ensembl ].		VAR_016307
	Natural variant	1355	1	D → E. Corresponds to variant rs34917815 [ dbSNP | Ensembl ].		VAR_037437
	Natural variant	1372	1	G → R. Ref.3 Corresponds to variant rs4253227 [ dbSNP | Ensembl ].		VAR_016308
	Natural variant	1382	1	G → R. Ref.3 Corresponds to variant rs4253228 [ dbSNP | Ensembl ].		VAR_016309
	Natural variant	1410	1	G → R. Ref.3 Corresponds to variant rs4253229 [ dbSNP | Ensembl ].		VAR_016310
	Natural variant	1413	1	Q → R. Ref.3 Ref.25 Corresponds to variant rs2228529 [ dbSNP | Ensembl ].		VAR_001225
	Natural variant	1441	1	T → I. Ref.3 Corresponds to variant rs4253230 [ dbSNP | Ensembl ].		VAR_016311
Experimental info
	Mutagenesis	1427 – 1428	2	LL → GG: Fails to bind polyubiquitin chains. Ref.18

Sequences

	Sequence		Length	Mass (Da)
	Q03468 [UniParc]. Last modified October 1, 1993. Version 1. Checksum: 285257E2AEC071AC	FASTA	1,493	168,416
	10 20 30 40 50 60 MPNEGIPHSS QTQEQDCLQS QPVSNNEEMA IKQESGGDGE VEEYLSFRSV GDGLSTSAVG 70 80 90 100 110 120 CASAAPRRGP ALLHIDRHQI QAVEPSAQAL ELQGLGVDVY DQDVLEQGVL QQVDNAIHEA 130 140 150 160 170 180 SRASQLVDVE KEYRSVLDDL TSCTTSLRQI NKIIEQLSPQ AATSRDINRK LDSVKRQKYN 190 200 210 220 230 240 KEQQLKKITA KQKHLQAILG GAEVKIELDH ASLEEDAEPG PSSLGSMLMP VQETAWEELI 250 260 270 280 290 300 RTGQMTPFGT QIPQKQEKKP RKIMLNEASG FEKYLADQAK LSFERKKQGC NKRAARKAPA 310 320 330 340 350 360 PVTPPAPVQN KNKPNKKARV LSKKEERLKK HIKKLQKRAL QFQGKVGLPK ARRPWESDMR 370 380 390 400 410 420 PEAEGDSEGE ESEYFPTEEE EEEEDDEVEG AEADLSGDGT DYELKPLPKG GKRQKKVPVQ 430 440 450 460 470 480 EIDDDFFPSS GEEAEAASVG EGGGGGRKVG RYRDDGDEDY YKQRLRRWNK LRLQDKEKRL 490 500 510 520 530 540 KLEDDSEESD AEFDEGFKVP GFLFKKLFKY QQTGVRWLWE LHCQQAGGIL GDEMGLGKTI 550 560 570 580 590 600 QIIAFLAGLS YSKIRTRGSN YRFEGLGPTV IVCPTTVMHQ WVKEFHTWWP PFRVAILHET 610 620 630 640 650 660 GSYTHKKEKL IRDVAHCHGI LITSYSYIRL MQDDISRYDW HYVILDEGHK IRNPNAAVTL 670 680 690 700 710 720 ACKQFRTPHR IILSGSPMQN NLRELWSLFD FIFPGKLGTL PVFMEQFSVP ITMGGYSNAS 730 740 750 760 770 780 PVQVKTAYKC ACVLRDTINP YLLRRMKSDV KMSLSLPDKN EQVLFCRLTD EQHKVYQNFV 790 800 810 820 830 840 DSKEVYRILN GEMQIFSGLI ALRKICNHPD LFSGGPKNLK GLPDDELEED QFGYWKRSGK 850 860 870 880 890 900 MIVVESLLKI WHKQGQRVLL FSQSRQMLDI LEVFLRAQKY TYLKMDGTTT IASRQPLITR 910 920 930 940 950 960 YNEDTSIFVF LLTTRVGGLG VNLTGANRVV IYDPDWNPST DTQARERAWR IGQKKQVTVY 970 980 990 1000 1010 1020 RLLTAGTIEE KIYHRQIFKQ FLTNRVLKDP KQRRFFKSND LYELFTLTSP DASQSTETSA 1030 1040 1050 1060 1070 1080 IFAGTGSDVQ TPKCHLKRRI QPAFGADHDV PKRKKFPASN ISVNDATSSE EKSEAKGAEV 1090 1100 1110 1120 1130 1140 NAVTSNRSDP LKDDPHMSSN VTSNDRLGEE TNAVSGPEEL SVISGNGECS NSSGTGKTSM 1150 1160 1170 1180 1190 1200 PSGDESIDEK LGLSYKRERP SQAQTEAFWE NKQMENNFYK HKSKTKHHSV AEEETLEKHL 1210 1220 1230 1240 1250 1260 RPKQKPKNSK HCRDAKFEGT RIPHLVKKRR YQKQDSENKS EAKEQSNDDY VLEKLFKKSV 1270 1280 1290 1300 1310 1320 GVHSVMKHDA IMDGASPDYV LVEAEANRVA QDALKALRLS RQRCLGAVSG VPTWTGHRGI 1330 1340 1350 1360 1370 1380 SGAPAGKKSR FGKKRNSNFS VQHPSSTSPT EKCQDGIMKK EGKDNVPEHF SGRAEDADSS 1390 1400 1410 1420 1430 1440 SGPLASSSLL AKMRARNHLI LPERLESESG HLQEASALLP TTEHDDLLVE MRNFIAFQAH 1450 1460 1470 1480 1490 TDGQASTREI LQEFESKLSA SQSCVFRELL RNLCTFHRTS GGEGIWKLKP EYC

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"ERCC6, a member of a subfamily of putative helicases, is involved in Cockayne's syndrome and preferential repair of active genes." Troelstra C., van Gool A., de Wit J., Vermeulen W., Bootsma D., Hoeijmakers J.H.J. Cell 71:939-953(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Structure and expression of the excision repair gene ERCC6, involved in the human disorder Cockayne's syndrome group B." Troelstra C., Hesen V., Bootsma D., Hoeijmakers J.H.J. Nucleic Acids Res. 21:419-426(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	NIEHS SNPs program Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ASP-399; ALA-425; ASP-446; MET-942; CYS-1002; ARG-1095; VAL-1097; GLY-1213; PRO-1230; LEU-1308; VAL-1322; ARG-1372; ARG-1382; ARG-1410; ARG-1413 AND ILE-1441.
[4]	"The DNA sequence and comparative analysis of human chromosome 10." Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J. Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"A summary of mutations in the UV-sensitive disorders: xeroderma pigmentosum, Cockayne syndrome, and trichothiodystrophy." Cleaver J.E., Thompson L.H., Richardson A.S., States J.C. Hum. Mutat. 14:9-22(1999) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON VARIANTS CSB.
[7]	"Manitoba aboriginal kindred with original cerebro-oculo-facio-skeletal syndrome has a mutation in the Cockayne syndrome group B (CSB) gene." Meira L.B., Graham J.M. Jr., Greenberg C.R., Busch D.B., Doughty A.T.B., Ziffer D.W., Coleman D.M., Savre-Train I., Friedberg E.C. Am. J. Hum. Genet. 66:1221-1228(2000) [PubMed] [Europe PMC] [Abstract] Cited for: DISEASE.
[8]	"Identical mutations in the CSB gene associated with either Cockayne syndrome or the DeSanctis-Cacchione variant of xeroderma pigmentosum." Colella S., Nardo T., Botta E., Lehmann A.R., Stefanini M. Hum. Mol. Genet. 9:1171-1175(2000) [PubMed] [Europe PMC] [Abstract] Cited for: DISEASE.
[9]	"Complete absence of Cockayne syndrome group B gene product gives rise to UV-sensitive syndrome but not Cockayne syndrome." Horibata K., Iwamoto Y., Kuraoka I., Jaspers N.G.J., Kurimasa A., Oshimura M., Ichihashi M., Tanaka K. Proc. Natl. Acad. Sci. U.S.A. 101:15410-15415(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN UVSS1.
[10]	"The Cockayne syndrome group B protein is a functional dimer." Christiansen M., Thorslund T., Jochimsen B., Bohr V.A., Stevnsner T. FEBS J. 272:4306-4314(2005) [PubMed] [Europe PMC] [Abstract] Cited for: SUBUNIT, SUBCELLULAR LOCATION.
[11]	"The CSB protein actively wraps DNA." Beerens N., Hoeijmakers J.H., Kanaar R., Vermeulen W., Wyman C. J. Biol. Chem. 280:4722-4729(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBUNIT, DNA-BINDING.
[12]	"CSA-dependent degradation of CSB by the ubiquitin-proteasome pathway establishes a link between complementation factors of the Cockayne syndrome." Groisman R., Kuraoka I., Chevallier O., Gaye N., Magnaldo T., Tanaka K., Kisselev A.F., Harel-Bellan A., Nakatani Y. Genes Dev. 20:1429-1434(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ERCC8, UBIQUITINATION BY THE CSA COMPLEX, PROTEASOMAL DEGRADATION.
[13]	"The WSTF-SNF2h chromatin remodeling complex interacts with several nuclear proteins in transcription." Cavellan E., Asp P., Percipalle P., Oestlund Farrants A.-K. J. Biol. Chem. 281:16264-16271(2006) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE B-WICH COMPLEX.
[14]	"Cockayne syndrome A and B proteins differentially regulate recruitment of chromatin remodeling and repair factors to stalled RNA polymerase II in vivo." Fousteri M., Vermeulen W., van Zeeland A.A., Mullenders L.H. Mol. Cell 23:471-482(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[15]	"Synergic effect of polymorphisms in ERCC6 5' flanking region and complement factor H on age-related macular degeneration predisposition." Tuo J., Ning B., Bojanowski C.M., Lin Z.-N., Ross R.J., Reed G.F., Shen D., Jiao X., Zhou M., Chew E.Y., Kadlubar F.F., Chan C.-C. Proc. Natl. Acad. Sci. U.S.A. 103:9256-9261(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN ARMD5.
[16]	"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. 4:344-346(2008) [PubMed] [Europe PMC] [Abstract] Cited for: METHYLATION AT LYS-170; LYS-297; LYS-448 AND LYS-1054.
[17]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1142 AND SER-1348, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[18]	"A ubiquitin-binding domain in cockayne syndrome B required for transcription-coupled nucleotide excision repair." Anindya R., Mari P.O., Kristensen U., Kool H., Giglia-Mari G., Mullenders L.H., Fousteri M., Vermeulen W., Egly J.M., Svejstrup J.Q. Mol. Cell 38:637-648(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, DOMAIN, UBIQUITIN-BINDING, UBIQUITINATION AT THE C-TERMINUS, MUTAGENESIS OF 1427-LEU-LEU-1428.
[19]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[20]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-486 AND SER-489, MASS SPECTROMETRY.
[22]	"Mutations in UVSSA cause UV-sensitive syndrome and impair RNA polymerase IIo processing in transcription-coupled nucleotide-excision repair." Nakazawa Y., Sasaki K., Mitsutake N., Matsuse M., Shimada M., Nardo T., Takahashi Y., Ohyama K., Ito K., Mishima H., Nomura M., Kinoshita A., Ono S., Takenaka K., Masuyama R., Kudo T., Slor H., Utani A. , Tateishi S., Yamashita S., Stefanini M., Lehmann A.R., Yoshiura K.I., Ogi T. Nat. Genet. 44:586-592(2012) [PubMed] [Europe PMC] [Abstract] Cited for: UBIQUITINATION.
[23]	"UV-sensitive syndrome protein UVSSA recruits USP7 to regulate transcription-coupled repair." Schwertman P., Lagarou A., Dekkers D.H., Raams A., van der Hoek A.C., Laffeber C., Hoeijmakers J.H., Demmers J.A., Fousteri M., Vermeulen W., Marteijn J.A. Nat. Genet. 44:598-602(2012) [PubMed] [Europe PMC] [Abstract] Cited for: UBIQUITINATION.
[24]	"Mutations in UVSSA cause UV-sensitive syndrome and destabilize ERCC6 in transcription-coupled DNA repair." Zhang X., Horibata K., Saijo M., Ishigami C., Ukai A., Kanno S.I., Tahara H., Neilan E.G., Honma M., Nohmi T., Yasui A., Tanaka K. Nat. Genet. 44:593-597(2012) [PubMed] [Europe PMC] [Abstract] Cited for: UBIQUITINATION, INTERACTION WITH UVSSA.
[25]	"Molecular analysis of mutations in the CSB (ERCC6) gene in patients with Cockayne syndrome." Mallery D.L., Tanganelli B., Colella S., Steingrimsdottir H., van Gool A.J., Troelstra C., Stefanini M., Lehmann A.R. Am. J. Hum. Genet. 62:77-85(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS CSB TRP-670; ARG-851; GLY-957 AND LEU-1042, VARIANTS THR-255; ASP-399; ARG-1095; VAL-1097; GLY-1213 AND ARG-1413.
[26]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] ALA-591; LEU-652; THR-1038; GLN-1119 AND VAL-1119.
[27]	"DNA sequencing of a cytogenetically normal acute myeloid leukaemia genome." Ley T.J., Mardis E.R., Ding L., Fulton B., McLellan M.D., Chen K., Dooling D., Dunford-Shore B.H., McGrath S., Hickenbotham M., Cook L., Abbott R., Larson D.E., Koboldt D.C., Pohl C., Smith S., Hawkins A., Abbott S. , Locke D., Hillier L.W., Miner T., Fulton L., Magrini V., Wylie T., Glasscock J., Conyers J., Sander N., Shi X., Osborne J.R., Minx P., Gordon D., Chinwalla A., Zhao Y., Ries R.E., Payton J.E., Westervelt P., Tomasson M.H., Watson M., Baty J., Ivanovich J., Heath S., Shannon W.D., Nagarajan R., Walter M.J., Link D.C., Graubert T.A., DiPersio J.F., Wilson R.K. Nature 456:66-72(2008) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] TRP-134.
[28]	"Mutation update for the CSB/ERCC6 and CSA/ERCC8 genes involved in Cockayne syndrome." Laugel V., Dalloz C., Durand M., Sauvanaud F., Kristensen U., Vincent M.C., Pasquier L., Odent S., Cormier-Daire V., Gener B., Tobias E.S., Tolmie J.L., Martin-Coignard D., Drouin-Garraud V., Heron D., Journel H., Raffo E., Vigneron J. , Lyonnet S., Murday V., Gubser-Mercati D., Funalot B., Brueton L., Sanchez Del Pozo J., Munoz E., Gennery A.R., Salih M., Noruzinia M., Prescott K., Ramos L., Stark Z., Fieggen K., Chabrol B., Sarda P., Edery P., Bloch-Zupan A., Fawcett H., Pham D., Egly J.M., Lehmann A.R., Sarasin A., Dollfus H. Hum. Mutat. 31:113-126(2010) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS CSB TRP-670; ASP-680; CYS-686; LEU-687; ARG-851; GLY-957 AND LEU-1042, VARIANTS COFS1 PRO-871 AND PRO-987, VARIANTS ARG-1095 AND GLY-1213.
+	Additional computationally mapped references.

Web resources

Allelic variations of the XP genes

Atlas of Genetics and Cytogenetics in Oncology and Haematology

GeneReviews

NIEHS-SNPs

Cross-references

Sequence databases
EMBL GenBank DDBJ	L04791 mRNA. Translation: AAA52397.1. AY204752 Genomic DNA. Translation: AAO13487.1. AL138760 Genomic DNA. Translation: CAH70291.1. CH471187 Genomic DNA. Translation: EAW93094.1. CH471187 Genomic DNA. Translation: EAW93097.1.
IPI	IPI00414779.
PIR	A44224.
RefSeq	NP_000115.1. NM_000124.3.
UniGene	Hs.654449.
3D structure databases
ProteinModelPortal	Q03468.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-193N.
IntAct	Q03468. 5 interactions.
MINT	MINT-1193928.
STRING	9606.ENSP00000348089.
PTM databases
PhosphoSite	Q03468.
Polymorphism databases
DMDM	416959.
Proteomic databases
PaxDb	Q03468.
PRIDE	Q03468.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000355832; ENSP00000348089; ENSG00000225830.
GeneID	2074.
KEGG	hsa:2074.
UCSC	uc001jhr.4. human.
Organism-specific databases
CTD	2074.
GeneCards	GC10M050663.
HGNC	HGNC:3438. ERCC6.
MIM	133540. phenotype. 214150. phenotype. 278800. phenotype. 600630. phenotype. 609413. gene. 613761. phenotype.
neXtProt	NX_Q03468.
Orphanet	279. Age-related macular degeneration. 90321. Cockayne syndrome type 1. 90322. Cockayne syndrome type 2. 90324. Cockayne syndrome type 3. 1466. COFS syndrome. 1569. De Sanctis-Cacchione syndrome. 178338. UV-sensitive syndrome.
PharmGKB	PA27852.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0553.
HOGENOM	HOG000170952.
HOVERGEN	HBG051502.
InParanoid	Q03468.
KO	K10841.
OMA	NGEMQIF.
OrthoDB	EOG476JZF.
PhylomeDB	Q03468.
Enzyme and pathway databases
Reactome	REACT_216. DNA Repair.
Gene expression databases
ArrayExpress	Q03468.
Bgee	Q03468.
CleanEx	HS_ERCC6.
Genevestigator	Q03468.
GermOnline	ENSG00000032514. Homo sapiens.
Family and domain databases
InterPro	IPR014001. Helicase_ATP-bd. IPR001650. Helicase_C. IPR000330. SNF2_N. [Graphical view]
Pfam	PF00271. Helicase_C. 1 hit. PF00176. SNF2_N. 1 hit. [Graphical view]
SMART	SM00487. DEXDc. 1 hit. SM00490. HELICc. 1 hit. [Graphical view]
PROSITE	PS51192. HELICASE_ATP_BIND_1. 1 hit. PS51194. HELICASE_CTER. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	ERCC6. human.
GenomeRNAi	2074.
NextBio	8437.
SOURCE	Search...

Entry information

Entry name

ERCC6_HUMAN

Accession

Primary (citable) accession number: Q03468
Secondary accession number(s): D3DX94, Q5W0L9

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	October 1, 1993
Last modified:	May 1, 2013
This is version 147 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.