Reviewed, UniProtKB/Swiss-Prot Q03468 (ERCC6_HUMAN)

Names and origin

Protein names

Recommended name:
    DNA excision repair protein ERCC-6
    EC=3.6.1.-
Alternative name(s):
    ATP-dependent helicase ERCC6
    Cockayne syndrome protein CSB

Gene names

Name:	ERCC6
Synonyms:	CSB

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	1493 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Is involved in the preferential repair of active genes. Presumed DNA or RNA unwinding function. Corrects the UV survival and RNA synthesis after UV exposure of Cockayne syndrome complementation group B.
Subunit structure	Interacts with the CSA protein and 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.
Subcellular location	Nucleus Probable.
Post-translational modification	Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12
Involvement in disease	Defects in ERCC6 are the cause of Cockayne syndrome type B (CSB) [MIM:133540]. Cockayne syndrome is 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. Ref.14 Ref.15 Ref.16 Defects in ERCC6 are the cause of cerebro-oculo-facio-skeletal syndrome type 1 (COFS1) [MIM:214150]; also known as COFS syndrome or Pena-Shokeir syndrome type 2. COFS is a degenerative autosomal recessive disorder of prenatal onset affecting the brain, eye and spinal cord. After birth, it leads to brain atrophy, hypoplasia of the corpus callosum, hypotonia, cataracts, microcornea, optic atrophy, progressive joint contractures and growth failure. Facial dysmorphism is a constant feature. Abnormalities of the skull, eyes, limbs, heart and kidney also occur. Ref.15 Ref.16 Defects in ERCC6 are a cause of De Sanctis-Cacchione syndrome (DSC) [MIM:278800]; also known as xerodermic idiocy. DSC is an autosomal recessive syndrome consisting of xeroderma pigmentosum associated with mental retardation, retarded growth, gonadal hypoplasia and sometimes neurologic complications. Ref.15 Ref.16 Genetic variation in ERCC6 is associated with susceptibility to age-related macular degeneration type 5 (ARMD5) [MIM:609413]. ARMD is 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 (known as drusen) that lie beneath the retinal pigment epithelium and within an elastin-containing structure known as Bruch membrane. Ref.15 Ref.16 Defects in ERCC6 are a cause of UV-sensitive syndrome (UVS) [MIM:600630]. UVS is a rare autosomal recessive disorder characterized by photosensitivity and mild freckling but without neurological abnormalities or skin tumors. Ref.15 Ref.16 Ref.17
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	Cataract Cockayne syndrome Deafness Disease mutation Dwarfism
Ligand	ATP-binding DNA-binding Nucleotide-binding
Molecular function	Helicase Hydrolase
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	base-excision repair Inferred from mutant phenotype. Source: UniProtKB positive regulation of RNA elongation Inferred from direct assay. Source: UniProtKB sensory perception of sound Inferred from electronic annotation. Source: UniProtKB-KW transcription from RNA polymerase II promoter Non-traceable author statement. Source: UniProtKB transcription-coupled nucleotide-excision repair Inferred from mutant phenotype. Source: UniProtKB
Cellular component	nucleolus Inferred from direct assay. Source: UniProtKB soluble fraction Inferred from direct assay. Source: UniProtKB transcription elongation factor complex Inferred from direct assay. Source: UniProtKB
Molecular function	ATP binding Inferred from direct assay. Source: UniProtKB DNA binding Inferred from direct assay. Source: UniProtKB DNA-dependent ATPase activity Inferred from direct assay. Source: UniProtKB chromatin binding Inferred from direct assay. Source: UniProtKB helicase activity Inferred from electronic annotation. Source: UniProtKB-KW protein C-terminus binding Inferred from physical interaction. Source: UniProtKB protein N-terminus binding Inferred from physical interaction. Source: UniProtKB protein complex binding Inferred from direct assay. Source: UniProtKB transcription elongation regulator activity Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ERCC8	Q13216-1	1	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
	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	158	1	Phosphoserine Ref.7 Ref.9 Ref.11 Ref.12
	Modified residue	429	1	Phosphoserine Ref.12
	Modified residue	430	1	Phosphoserine Ref.12
	Modified residue	486	1	Phosphoserine Ref.8 Ref.12
	Modified residue	489	1	Phosphoserine Ref.12
	Modified residue	1142	1	Phosphoserine Ref.12
	Modified residue	1348	1	Phosphoserine Ref.12
	Modified residue	1461	1	Phosphoserine Ref.10
Natural variations
	Natural variant	134	1	R → W Ref.20		VAR_054153
	Natural variant	255	1	K → T Ref.14		VAR_001216
	Natural variant	399	1	G → D: dbSNP rs2228528. Ref.14 Ref.3		VAR_001217
	Natural variant	425	1	D → A: dbSNP rs4253046. Ref.3		VAR_016301
	Natural variant	446	1	G → D: dbSNP rs4253047. Ref.3		VAR_016302
	Natural variant	591	1	P → A in a colorectal cancer sample; somatic mutation. Ref.19		VAR_036021
	Natural variant	652	1	R → L in a colorectal cancer sample; somatic mutation. Ref.19		VAR_036022
	Natural variant	670	1	R → W in CSB. Ref.14		VAR_001218
	Natural variant	851	1	W → R in CSB. Ref.14		VAR_001219
	Natural variant	942	1	T → M: dbSNP rs2228525. Ref.3		VAR_016303
	Natural variant	957	1	V → G in CSB. Ref.14		VAR_001220
	Natural variant	1002	1	Y → C: dbSNP rs4253206. Ref.3		VAR_016304
	Natural variant	1038	1	R → T in a breast cancer sample; somatic mutation. Ref.19		VAR_036023
	Natural variant	1042	1	P → L in CSB. Ref.14		VAR_001221
	Natural variant	1095	1	P → R: dbSNP rs4253208. Ref.14 Ref.3		VAR_001222
	Natural variant	1097	1	M → V: dbSNP rs2228526. Ref.14 Ref.3		VAR_001223
	Natural variant	1119	1	E → Q in a breast cancer sample; somatic mutation. Ref.19		VAR_036024
	Natural variant	1119	1	E → V in a breast cancer sample; somatic mutation. Ref.19		VAR_036025
	Natural variant	1213	1	R → G: dbSNP rs2228527. Ref.14 Ref.3		VAR_001224
	Natural variant	1220	1	T → I: dbSNP rs34704611.		VAR_037436
	Natural variant	1230	1	R → P: dbSNP rs4253211. Ref.3		VAR_016305
	Natural variant	1308	1	V → L: dbSNP rs2229761. Ref.3		VAR_016306
	Natural variant	1322	1	G → V: dbSNP rs4253219. Ref.3		VAR_016307
	Natural variant	1355	1	D → E: dbSNP rs34917815.		VAR_037437
	Natural variant	1372	1	G → R: dbSNP rs4253227. Ref.3		VAR_016308
	Natural variant	1382	1	G → R: dbSNP rs4253228. Ref.3		VAR_016309
	Natural variant	1410	1	G → R: dbSNP rs4253229. Ref.3		VAR_016310
	Natural variant	1413	1	Q → R: dbSNP rs2228529. Ref.14 Ref.3		VAR_001225
	Natural variant	1441	1	T → I: dbSNP rs4253230. Ref.3		VAR_016311

Sequences

	Sequence		Length	Mass (Da)
	Q03468-1 [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: 1339317] [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: 8382798] [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: 15164054] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"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: 10447254] [Abstract] Cited for: REVIEW ON VARIANTS CSB.
[6]	"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: 16603771] [Abstract] Cited for: IDENTIFICATION IN THE B-WICH COMPLEX.
[7]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-158, MASS SPECTROMETRY. Tissue: Epithelium.
[8]	"Phosphoproteome analysis of the human mitotic spindle." Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R. Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006) [PubMed: 16565220] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-486, MASS SPECTROMETRY. Tissue: Epithelium.
[9]	"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra." Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D. J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-158, MASS SPECTROMETRY. Tissue: Epithelium.
[10]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1461, MASS SPECTROMETRY.
[11]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-158, MASS SPECTROMETRY.
[12]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-158; SER-429; SER-430; SER-486; SER-489; SER-1142 AND SER-1348, MASS SPECTROMETRY.
[13]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[14]	"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: 9443879] [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.
[15]	"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: 10739753] [Abstract] Cited for: DISEASE.
[16]	"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: 10767341] [Abstract] Cited for: DISEASE.
[17]	"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: 15486090] [Abstract] Cited for: INVOLVEMENT IN UVS.
[18]	"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: 16754848] [Abstract] Cited for: ASSOCIATION WITH ARMD.
[19]	"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: 16959974] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] ALA-591; LEU-652; THR-1038; GLN-1119 AND VAL-1119.
[20]	"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: 18987736] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] TRP-134.
+	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
EMBLGenBankDDBJ	L04791 mRNA. Translation: AAA52397.1. AY204752 Genomic DNA. Translation: AAO13487.1. AL138760 Genomic DNA. Translation: CAH70291.1.
IPI	IPI00414779.
PIR	A44224.
RefSeq	NP_000115.1.
UniGene	Hs.654449
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:193N.
IntAct	Q03468. 3 interactions.
PTM databases
PhosphoSite	Q03468.
Proteomic databases
PRIDE	Q03468.
Genome annotation databases
Ensembl	ENSG00000032514. Homo sapiens. [Contig view]
GeneID	2074.
KEGG	hsa:2074.
Organism-specific databases
GeneCards	GC10M050336.
H-InvDB	HIX0008816.
HGNC	HGNC:3438. ERCC6.
MIM	133540. phenotype. 214150. phenotype. 278800. phenotype. 600630. phenotype. 609413. gene+phenotype.
Orphanet	191. Cockayne syndrome. 1466. COFS syndrome. 1569. De Sanctis-Cacchione syndrome. 910. Xeroderma pigmentosum.
PharmGKB	PA27852.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	Q03468.
HOVERGEN	Q03468.
OMA	Q03468. HDAIMDG.
Enzyme and pathway databases
Reactome	REACT_216. DNA Repair.
Gene expression databases
ArrayExpress	Q03468.
Bgee	Q03468.
CleanEx	HS_ERCC6.
GermOnline	ENSG00000032514. Homo sapiens.
Family and domain databases
InterPro	IPR014001. DEAD-like_N. IPR001650. DNA/RNA_helicase_C. IPR014021. Helicase_SF1/SF2_ATP-bd. 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 Resources
NextBio	8437.
SOURCE	Search...

Entry information

Entry name

ERCC6_HUMAN

Accession

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

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	October 1, 1993
Last modified:	June 16, 2009
This is version 103 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)