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Q03468 (ERCC6_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 160. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1493 AA.
Sequence statusComplete.
Protein existenceEvidence 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

Macular degeneration, age-related, 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 processDNA damage
DNA repair
Transcription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityPolymorphism
   DiseaseAge-related macular degeneration
Cataract
Cockayne syndrome
Deafness
Disease mutation
Dwarfism
Mental retardation
Xeroderma pigmentosum
   LigandATP-binding
DNA-binding
Nucleotide-binding
   Molecular functionHelicase
Hydrolase
   PTMMethylation
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processATP catabolic process

Inferred from direct assay PubMed 12560492PubMed 16107709PubMed 8999876. Source: GOC

DNA repair

Traceable author statement. Source: Reactome

activation of JNKK activity

Inferred from electronic annotation. Source: Ensembl

activation of JUN kinase activity

Inferred from electronic annotation. Source: Ensembl

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: Ensembl

multicellular organism growth

Inferred from electronic annotation. Source: Ensembl

nucleotide-excision repair

Traceable author statement. Source: Reactome

photoreceptor cell maintenance

Inferred from electronic annotation. Source: Ensembl

positive regulation of DNA-templated transcription, elongation

Inferred from direct assay PubMed 9326587. Source: UniProtKB

pyrimidine dimer repair

Inferred from electronic annotation. Source: Ensembl

regulation of DNA-templated transcription, elongation

Inferred from direct assay PubMed 9326587. Source: UniProtKB

response to UV

Inferred from direct assay Ref.14. Source: UniProtKB

response to UV-B

Inferred from electronic annotation. Source: Ensembl

response to X-ray

Inferred from electronic annotation. Source: Ensembl

response to gamma radiation

Inferred from electronic annotation. Source: Ensembl

response to oxidative stress

Inferred from direct assay PubMed 16107709. Source: UniProtKB

response to superoxide

Inferred from electronic annotation. Source: Ensembl

response to toxic substance

Inferred from electronic annotation. Source: Ensembl

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_componentnucleolus

Inferred from direct assay PubMed 16107709. Source: UniProtKB

nucleoplasm

Inferred from direct assay PubMed 16107709. Source: UniProtKB

nucleus

Inferred from direct assay PubMed 12560492. Source: UniProtKB

transcription elongation factor complex

Inferred from direct assay PubMed 9326587. Source: UniProtKB

   Molecular_functionATP 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 C-terminus binding

Inferred from physical interaction PubMed 16246722. Source: UniProtKB

protein N-terminus binding

Inferred from physical interaction PubMed 7664335. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 10944529PubMed 16107709Ref.24PubMed 7663514PubMed 8999876. Source: UniProtKB

protein complex binding

Inferred from direct assay Ref.14. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ERCC8Q13216-12EBI-295284,EBI-596556

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 14931493DNA excision repair protein ERCC-6
PRO_0000074314

Regions

Domain519 – 695177Helicase ATP-binding
Domain843 – 1002160Helicase C-terminal
Nucleotide binding532 – 5398ATP Potential
Region1400 – 142829Ubiquitin-binding domain (UBD)
Motif466 – 48116Nuclear localization signal Potential
Motif646 – 6494DEGH box
Motif1038 – 105518Nuclear localization signal Potential
Compositional bias356 – 39439Asp/Glu-rich (acidic)
Compositional bias442 – 4465Gly-rich

Amino acid modifications

Modified residue1701N6-methylated lysine; by EHMT2 Ref.16
Modified residue2971N6-methylated lysine; by EHMT2 Ref.16
Modified residue4481N6-methylated lysine; by EHMT2 Ref.16
Modified residue4861Phosphoserine Ref.21
Modified residue4891Phosphoserine Ref.21
Modified residue10541N6-methylated lysine; by EHMT2 Ref.16
Modified residue11421Phosphoserine Ref.17
Modified residue13481Phosphoserine Ref.17

Natural variations

Natural variant1341R → W. Ref.27
VAR_054153
Natural variant2551K → T. Ref.25
VAR_001216
Natural variant3991G → D. Ref.3 Ref.25
Corresponds to variant rs2228528 [ dbSNP | Ensembl ].
VAR_001217
Natural variant4251D → A. Ref.3
Corresponds to variant rs4253046 [ dbSNP | Ensembl ].
VAR_016301
Natural variant4461G → D. Ref.3
Corresponds to variant rs4253047 [ dbSNP | Ensembl ].
VAR_016302
Natural variant5911P → A in a colorectal cancer sample; somatic mutation. Ref.26
VAR_036021
Natural variant6521R → L in a colorectal cancer sample; somatic mutation. Ref.26
VAR_036022
Natural variant6701R → W in CSB. Ref.25 Ref.28
VAR_001218
Natural variant6801N → D in CSB. Ref.28
VAR_063511
Natural variant6861W → C in CSB. Ref.28
VAR_063512
Natural variant6871S → L in CSB. Ref.28
VAR_063513
Natural variant8511W → R in CSB. Ref.25 Ref.28
VAR_001219
Natural variant8711L → P in COFS1. Ref.28
VAR_063514
Natural variant9421T → M. Ref.3
Corresponds to variant rs2228525 [ dbSNP | Ensembl ].
VAR_016303
Natural variant9571V → G in CSB. Ref.25 Ref.28
VAR_001220
Natural variant9871L → P in COFS1. Ref.28
VAR_063515
Natural variant10021Y → C. Ref.3
Corresponds to variant rs4253206 [ dbSNP | Ensembl ].
VAR_016304
Natural variant10381R → T in a breast cancer sample; somatic mutation. Ref.26
VAR_036023
Natural variant10421P → L in CSB. Ref.25 Ref.28
VAR_001221
Natural variant10951P → R. Ref.3 Ref.25 Ref.28
Corresponds to variant rs4253208 [ dbSNP | Ensembl ].
VAR_001222
Natural variant10971M → V. Ref.3 Ref.25
Corresponds to variant rs2228526 [ dbSNP | Ensembl ].
VAR_001223
Natural variant11191E → Q in a breast cancer sample; somatic mutation. Ref.26
VAR_036024
Natural variant11191E → V in a breast cancer sample; somatic mutation. Ref.26
VAR_036025
Natural variant12131R → G. Ref.3 Ref.25 Ref.28
Corresponds to variant rs2228527 [ dbSNP | Ensembl ].
VAR_001224
Natural variant12201T → I.
Corresponds to variant rs34704611 [ dbSNP | Ensembl ].
VAR_037436
Natural variant12301R → P. Ref.3
Corresponds to variant rs4253211 [ dbSNP | Ensembl ].
VAR_016305
Natural variant13081V → L. Ref.3
Corresponds to variant rs2229761 [ dbSNP | Ensembl ].
VAR_016306
Natural variant13221G → V. Ref.3
Corresponds to variant rs4253219 [ dbSNP | Ensembl ].
VAR_016307
Natural variant13551D → E.
Corresponds to variant rs34917815 [ dbSNP | Ensembl ].
VAR_037437
Natural variant13721G → R. Ref.3
Corresponds to variant rs4253227 [ dbSNP | Ensembl ].
VAR_016308
Natural variant13821G → R. Ref.3
Corresponds to variant rs4253228 [ dbSNP | Ensembl ].
VAR_016309
Natural variant14101G → R. Ref.3
Corresponds to variant rs4253229 [ dbSNP | Ensembl ].
VAR_016310
Natural variant14131Q → R. Ref.3 Ref.25
Corresponds to variant rs2228529 [ dbSNP | Ensembl ].
VAR_001225
Natural variant14411T → I. Ref.3
Corresponds to variant rs4253230 [ dbSNP | Ensembl ].
VAR_016311

Experimental info

Mutagenesis1427 – 14282LL → GG: Fails to bind polyubiquitin chains. Ref.18

Secondary structure

....... 1493
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q03468 [UniParc].

Last modified October 1, 1993. Version 1.
Checksum: 285257E2AEC071AC

FASTA1,493168,416
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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.

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.
CCDSCCDS7229.1.
PIRA44224.
RefSeqNP_000115.1. NM_000124.3.
UniGeneHs.49063.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4CVOX-ray1.85A84-160[»]
ProteinModelPortalQ03468.
SMRQ03468. Positions 503-1015.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108386. 40 interactions.
DIPDIP-193N.
IntActQ03468. 6 interactions.
MINTMINT-1193928.
STRING9606.ENSP00000348089.

PTM databases

PhosphoSiteQ03468.

Polymorphism databases

DMDM416959.

Proteomic databases

MaxQBQ03468.
PaxDbQ03468.
PRIDEQ03468.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000355832; ENSP00000348089; ENSG00000225830.
GeneID2074.
KEGGhsa:2074.
UCSCuc001jhr.5. human.

Organism-specific databases

CTD2074.
GeneCardsGC10M050663.
GeneReviewsERCC6.
HGNCHGNC:3438. ERCC6.
MIM133540. phenotype.
214150. phenotype.
278800. phenotype.
600630. phenotype.
609413. gene.
613761. phenotype.
neXtProtNX_Q03468.
Orphanet279. Age-related macular degeneration.
90321. Cockayne syndrome type 1.
90322. Cockayne syndrome type 2.
90324. Cockayne syndrome type 3.
1466. COFS syndrome.
178338. UV-sensitive syndrome.
PharmGKBPA27852.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0553.
HOGENOMHOG000170952.
HOVERGENHBG051502.
InParanoidQ03468.
KOK10841.
OMAHSVMKHD.
OrthoDBEOG7060QC.
PhylomeDBQ03468.
TreeFamTF101236.

Enzyme and pathway databases

ReactomeREACT_216. DNA Repair.

Gene expression databases

ArrayExpressQ03468.
BgeeQ03468.
CleanExHS_ERCC6.
GenevestigatorQ03468.

Family and domain databases

Gene3D3.40.50.300. 2 hits.
InterProIPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR000330. SNF2_N.
[Graphical view]
PfamPF00271. Helicase_C. 1 hit.
PF00176. SNF2_N. 1 hit.
[Graphical view]
SMARTSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 2 hits.
PROSITEPS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSERCC6. human.
GeneWikiERCC6.
GenomeRNAi2074.
NextBio8437.
PROQ03468.
SOURCESearch...

Entry information

Entry nameERCC6_HUMAN
AccessionPrimary (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: July 9, 2014
This is version 160 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM