Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q03468

- ERCC6_HUMAN

UniProt

Q03468 - ERCC6_HUMAN

Protein

DNA excision repair protein ERCC-6

Gene

ERCC6

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 162 (01 Oct 2014)
      Sequence version 1 (01 Oct 1993)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    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.3 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi532 – 5398ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB
    2. chromatin binding Source: UniProtKB
    3. DNA binding Source: UniProtKB
    4. DNA-dependent ATPase activity Source: UniProtKB
    5. helicase activity Source: UniProtKB-KW
    6. protein binding Source: UniProtKB
    7. protein complex binding Source: UniProtKB
    8. protein C-terminus binding Source: UniProtKB
    9. protein N-terminus binding Source: UniProtKB

    GO - Biological processi

    1. activation of JNKK activity Source: Ensembl
    2. activation of JUN kinase activity Source: Ensembl
    3. ATP catabolic process Source: GOC
    4. base-excision repair Source: UniProtKB
    5. DNA repair Source: Reactome
    6. intrinsic apoptotic signaling pathway in response to DNA damage Source: Ensembl
    7. multicellular organism growth Source: Ensembl
    8. nucleotide-excision repair Source: Reactome
    9. photoreceptor cell maintenance Source: Ensembl
    10. positive regulation of DNA-templated transcription, elongation Source: UniProtKB
    11. pyrimidine dimer repair Source: Ensembl
    12. regulation of DNA-templated transcription, elongation Source: UniProtKB
    13. response to gamma radiation Source: Ensembl
    14. response to oxidative stress Source: UniProtKB
    15. response to superoxide Source: Ensembl
    16. response to toxic substance Source: Ensembl
    17. response to UV Source: UniProtKB
    18. response to UV-B Source: Ensembl
    19. response to X-ray Source: Ensembl
    20. transcription-coupled nucleotide-excision repair Source: UniProtKB
    21. transcription from RNA polymerase II promoter Source: UniProtKB

    Keywords - Molecular functioni

    Helicase, Hydrolase

    Keywords - Biological processi

    DNA damage, DNA repair, Transcription, Transcription regulation

    Keywords - Ligandi

    ATP-binding, DNA-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_1941. Formation of transcription-coupled NER (TC-NER) repair complex.
    REACT_2222. Dual incision reaction in TC-NER.
    REACT_953. RNA Polymerase I Transcription Initiation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    DNA excision repair protein ERCC-6 (EC:3.6.4.-)
    Alternative name(s):
    ATP-dependent helicase ERCC6
    Cockayne syndrome protein CSB
    Gene namesi
    Name:ERCC6
    Synonyms:CSB
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:3438. ERCC6.

    Subcellular locationi

    Nucleus 1 Publication

    GO - Cellular componenti

    1. nucleolus Source: UniProtKB
    2. nucleoplasm Source: UniProtKB
    3. nucleus Source: UniProtKB
    4. transcription elongation factor complex Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    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.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti670 – 6701R → W in CSB. 2 Publications
    VAR_001218
    Natural varianti680 – 6801N → D in CSB. 1 Publication
    VAR_063511
    Natural varianti686 – 6861W → C in CSB. 1 Publication
    VAR_063512
    Natural varianti687 – 6871S → L in CSB. 1 Publication
    VAR_063513
    Natural varianti851 – 8511W → R in CSB. 2 Publications
    VAR_001219
    Natural varianti957 – 9571V → G in CSB. 2 Publications
    VAR_001220
    Natural varianti1042 – 10421P → L in CSB. 2 Publications
    VAR_001221
    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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti871 – 8711L → P in COFS1. 1 Publication
    VAR_063514
    Natural varianti987 – 9871L → P in COFS1. 1 Publication
    VAR_063515
    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.
    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.1 Publication
    Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.
    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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi1427 – 14282LL → GG: Fails to bind polyubiquitin chains. 1 Publication

    Keywords - Diseasei

    Age-related macular degeneration, Cataract, Cockayne syndrome, Deafness, Disease mutation, Dwarfism, Mental retardation, Xeroderma pigmentosum

    Organism-specific databases

    MIMi133540. phenotype.
    214150. phenotype.
    278800. phenotype.
    600630. phenotype.
    613761. phenotype.
    Orphaneti279. 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.
    PharmGKBiPA27852.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 14931493DNA excision repair protein ERCC-6PRO_0000074314Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei170 – 1701N6-methylated lysine; by EHMT21 Publication
    Modified residuei297 – 2971N6-methylated lysine; by EHMT21 Publication
    Modified residuei448 – 4481N6-methylated lysine; by EHMT21 Publication
    Modified residuei486 – 4861Phosphoserine1 Publication
    Modified residuei489 – 4891Phosphoserine1 Publication
    Modified residuei1054 – 10541N6-methylated lysine; by EHMT21 Publication
    Modified residuei1142 – 11421Phosphoserine1 Publication
    Modified residuei1348 – 13481Phosphoserine1 Publication

    Post-translational modificationi

    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.5 Publications

    Keywords - PTMi

    Methylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ03468.
    PaxDbiQ03468.
    PRIDEiQ03468.

    PTM databases

    PhosphoSiteiQ03468.

    Expressioni

    Gene expression databases

    ArrayExpressiQ03468.
    BgeeiQ03468.
    CleanExiHS_ERCC6.
    GenevestigatoriQ03468.

    Interactioni

    Subunit structurei

    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.5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ERCC8Q13216-12EBI-295284,EBI-596556

    Protein-protein interaction databases

    BioGridi108386. 40 interactions.
    DIPiDIP-193N.
    IntActiQ03468. 6 interactions.
    MINTiMINT-1193928.
    STRINGi9606.ENSP00000348089.

    Structurei

    Secondary structure

    1
    1493
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi93 – 964
    Helixi102 – 1043
    Helixi109 – 15547

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4CVOX-ray1.85A84-160[»]
    ProteinModelPortaliQ03468.
    SMRiQ03468. Positions 503-1015.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini519 – 695177Helicase ATP-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini843 – 1002160Helicase C-terminalPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1400 – 142829Ubiquitin-binding domain (UBD)Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi466 – 48116Nuclear localization signalSequence AnalysisAdd
    BLAST
    Motifi646 – 6494DEGH box
    Motifi1038 – 105518Nuclear localization signalSequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi356 – 39439Asp/Glu-rich (acidic)Add
    BLAST
    Compositional biasi442 – 4465Gly-rich

    Domaini

    A C-terminal ubiquitin-binding domain (UBD) is essential for transcription-coupled nucleotide excision repair to proceed.1 Publication

    Sequence similaritiesi

    Belongs to the SNF2/RAD54 helicase family.Curated
    Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation
    Contains 1 helicase C-terminal domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0553.
    HOGENOMiHOG000170952.
    HOVERGENiHBG051502.
    InParanoidiQ03468.
    KOiK10841.
    OMAiHSVMKHD.
    OrthoDBiEOG7060QC.
    PhylomeDBiQ03468.
    TreeFamiTF101236.

    Family and domain databases

    Gene3Di3.40.50.300. 2 hits.
    InterProiIPR014001. Helicase_ATP-bd.
    IPR001650. Helicase_C.
    IPR027417. P-loop_NTPase.
    IPR000330. SNF2_N.
    [Graphical view]
    PfamiPF00271. Helicase_C. 1 hit.
    PF00176. SNF2_N. 1 hit.
    [Graphical view]
    SMARTiSM00487. DEXDc. 1 hit.
    SM00490. HELICc. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 2 hits.
    PROSITEiPS51192. HELICASE_ATP_BIND_1. 1 hit.
    PS51194. HELICASE_CTER. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q03468-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPNEGIPHSS QTQEQDCLQS QPVSNNEEMA IKQESGGDGE VEEYLSFRSV     50
    GDGLSTSAVG CASAAPRRGP ALLHIDRHQI QAVEPSAQAL ELQGLGVDVY 100
    DQDVLEQGVL QQVDNAIHEA SRASQLVDVE KEYRSVLDDL TSCTTSLRQI 150
    NKIIEQLSPQ AATSRDINRK LDSVKRQKYN KEQQLKKITA KQKHLQAILG 200
    GAEVKIELDH ASLEEDAEPG PSSLGSMLMP VQETAWEELI RTGQMTPFGT 250
    QIPQKQEKKP RKIMLNEASG FEKYLADQAK LSFERKKQGC NKRAARKAPA 300
    PVTPPAPVQN KNKPNKKARV LSKKEERLKK HIKKLQKRAL QFQGKVGLPK 350
    ARRPWESDMR PEAEGDSEGE ESEYFPTEEE EEEEDDEVEG AEADLSGDGT 400
    DYELKPLPKG GKRQKKVPVQ EIDDDFFPSS GEEAEAASVG EGGGGGRKVG 450
    RYRDDGDEDY YKQRLRRWNK LRLQDKEKRL KLEDDSEESD AEFDEGFKVP 500
    GFLFKKLFKY QQTGVRWLWE LHCQQAGGIL GDEMGLGKTI QIIAFLAGLS 550
    YSKIRTRGSN YRFEGLGPTV IVCPTTVMHQ WVKEFHTWWP PFRVAILHET 600
    GSYTHKKEKL IRDVAHCHGI LITSYSYIRL MQDDISRYDW HYVILDEGHK 650
    IRNPNAAVTL ACKQFRTPHR IILSGSPMQN NLRELWSLFD FIFPGKLGTL 700
    PVFMEQFSVP ITMGGYSNAS PVQVKTAYKC ACVLRDTINP YLLRRMKSDV 750
    KMSLSLPDKN EQVLFCRLTD EQHKVYQNFV DSKEVYRILN GEMQIFSGLI 800
    ALRKICNHPD LFSGGPKNLK GLPDDELEED QFGYWKRSGK MIVVESLLKI 850
    WHKQGQRVLL FSQSRQMLDI LEVFLRAQKY TYLKMDGTTT IASRQPLITR 900
    YNEDTSIFVF LLTTRVGGLG VNLTGANRVV IYDPDWNPST DTQARERAWR 950
    IGQKKQVTVY RLLTAGTIEE KIYHRQIFKQ FLTNRVLKDP KQRRFFKSND 1000
    LYELFTLTSP DASQSTETSA IFAGTGSDVQ TPKCHLKRRI QPAFGADHDV 1050
    PKRKKFPASN ISVNDATSSE EKSEAKGAEV NAVTSNRSDP LKDDPHMSSN 1100
    VTSNDRLGEE TNAVSGPEEL SVISGNGECS NSSGTGKTSM PSGDESIDEK 1150
    LGLSYKRERP SQAQTEAFWE NKQMENNFYK HKSKTKHHSV AEEETLEKHL 1200
    RPKQKPKNSK HCRDAKFEGT RIPHLVKKRR YQKQDSENKS EAKEQSNDDY 1250
    VLEKLFKKSV GVHSVMKHDA IMDGASPDYV LVEAEANRVA QDALKALRLS 1300
    RQRCLGAVSG VPTWTGHRGI SGAPAGKKSR FGKKRNSNFS VQHPSSTSPT 1350
    EKCQDGIMKK EGKDNVPEHF SGRAEDADSS SGPLASSSLL AKMRARNHLI 1400
    LPERLESESG HLQEASALLP TTEHDDLLVE MRNFIAFQAH TDGQASTREI 1450
    LQEFESKLSA SQSCVFRELL RNLCTFHRTS GGEGIWKLKP EYC 1493
    Length:1,493
    Mass (Da):168,416
    Last modified:October 1, 1993 - v1
    Checksum:i285257E2AEC071AC
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti134 – 1341R → W.1 Publication
    VAR_054153
    Natural varianti255 – 2551K → T.1 Publication
    VAR_001216
    Natural varianti399 – 3991G → D.2 Publications
    Corresponds to variant rs2228528 [ dbSNP | Ensembl ].
    VAR_001217
    Natural varianti425 – 4251D → A.1 Publication
    Corresponds to variant rs4253046 [ dbSNP | Ensembl ].
    VAR_016301
    Natural varianti446 – 4461G → D.1 Publication
    Corresponds to variant rs4253047 [ dbSNP | Ensembl ].
    VAR_016302
    Natural varianti591 – 5911P → A in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_036021
    Natural varianti652 – 6521R → L in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_036022
    Natural varianti670 – 6701R → W in CSB. 2 Publications
    VAR_001218
    Natural varianti680 – 6801N → D in CSB. 1 Publication
    VAR_063511
    Natural varianti686 – 6861W → C in CSB. 1 Publication
    VAR_063512
    Natural varianti687 – 6871S → L in CSB. 1 Publication
    VAR_063513
    Natural varianti851 – 8511W → R in CSB. 2 Publications
    VAR_001219
    Natural varianti871 – 8711L → P in COFS1. 1 Publication
    VAR_063514
    Natural varianti942 – 9421T → M.1 Publication
    Corresponds to variant rs2228525 [ dbSNP | Ensembl ].
    VAR_016303
    Natural varianti957 – 9571V → G in CSB. 2 Publications
    VAR_001220
    Natural varianti987 – 9871L → P in COFS1. 1 Publication
    VAR_063515
    Natural varianti1002 – 10021Y → C.1 Publication
    Corresponds to variant rs4253206 [ dbSNP | Ensembl ].
    VAR_016304
    Natural varianti1038 – 10381R → T in a breast cancer sample; somatic mutation. 1 Publication
    VAR_036023
    Natural varianti1042 – 10421P → L in CSB. 2 Publications
    VAR_001221
    Natural varianti1095 – 10951P → R.3 Publications
    Corresponds to variant rs4253208 [ dbSNP | Ensembl ].
    VAR_001222
    Natural varianti1097 – 10971M → V.2 Publications
    Corresponds to variant rs2228526 [ dbSNP | Ensembl ].
    VAR_001223
    Natural varianti1119 – 11191E → Q in a breast cancer sample; somatic mutation. 1 Publication
    VAR_036024
    Natural varianti1119 – 11191E → V in a breast cancer sample; somatic mutation. 1 Publication
    VAR_036025
    Natural varianti1213 – 12131R → G.3 Publications
    Corresponds to variant rs2228527 [ dbSNP | Ensembl ].
    VAR_001224
    Natural varianti1220 – 12201T → I.
    Corresponds to variant rs34704611 [ dbSNP | Ensembl ].
    VAR_037436
    Natural varianti1230 – 12301R → P.1 Publication
    Corresponds to variant rs4253211 [ dbSNP | Ensembl ].
    VAR_016305
    Natural varianti1308 – 13081V → L.1 Publication
    Corresponds to variant rs2229761 [ dbSNP | Ensembl ].
    VAR_016306
    Natural varianti1322 – 13221G → V.1 Publication
    Corresponds to variant rs4253219 [ dbSNP | Ensembl ].
    VAR_016307
    Natural varianti1355 – 13551D → E.
    Corresponds to variant rs34917815 [ dbSNP | Ensembl ].
    VAR_037437
    Natural varianti1372 – 13721G → R.1 Publication
    Corresponds to variant rs4253227 [ dbSNP | Ensembl ].
    VAR_016308
    Natural varianti1382 – 13821G → R.1 Publication
    Corresponds to variant rs4253228 [ dbSNP | Ensembl ].
    VAR_016309
    Natural varianti1410 – 14101G → R.1 Publication
    Corresponds to variant rs4253229 [ dbSNP | Ensembl ].
    VAR_016310
    Natural varianti1413 – 14131Q → R.2 Publications
    Corresponds to variant rs2228529 [ dbSNP | Ensembl ].
    VAR_001225
    Natural varianti1441 – 14411T → I.1 Publication
    Corresponds to variant rs4253230 [ dbSNP | Ensembl ].
    VAR_016311

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS7229.1.
    PIRiA44224.
    RefSeqiNP_000115.1. NM_000124.3.
    UniGeneiHs.49063.

    Genome annotation databases

    EnsembliENST00000355832; ENSP00000348089; ENSG00000225830.
    GeneIDi2074.
    KEGGihsa:2074.
    UCSCiuc001jhr.5. human.

    Polymorphism databases

    DMDMi416959.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    Allelic variations of the XP genes
    Atlas of Genetics and Cytogenetics in Oncology and Haematology
    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS7229.1.
    PIRi A44224.
    RefSeqi NP_000115.1. NM_000124.3.
    UniGenei Hs.49063.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4CVO X-ray 1.85 A 84-160 [» ]
    ProteinModelPortali Q03468.
    SMRi Q03468. Positions 503-1015.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108386. 40 interactions.
    DIPi DIP-193N.
    IntActi Q03468. 6 interactions.
    MINTi MINT-1193928.
    STRINGi 9606.ENSP00000348089.

    PTM databases

    PhosphoSitei Q03468.

    Polymorphism databases

    DMDMi 416959.

    Proteomic databases

    MaxQBi Q03468.
    PaxDbi Q03468.
    PRIDEi Q03468.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000355832 ; ENSP00000348089 ; ENSG00000225830 .
    GeneIDi 2074.
    KEGGi hsa:2074.
    UCSCi uc001jhr.5. human.

    Organism-specific databases

    CTDi 2074.
    GeneCardsi GC10M050663.
    GeneReviewsi ERCC6.
    HGNCi HGNC:3438. ERCC6.
    MIMi 133540. phenotype.
    214150. phenotype.
    278800. phenotype.
    600630. phenotype.
    609413. gene.
    613761. phenotype.
    neXtProti NX_Q03468.
    Orphaneti 279. 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.
    PharmGKBi PA27852.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0553.
    HOGENOMi HOG000170952.
    HOVERGENi HBG051502.
    InParanoidi Q03468.
    KOi K10841.
    OMAi HSVMKHD.
    OrthoDBi EOG7060QC.
    PhylomeDBi Q03468.
    TreeFami TF101236.

    Enzyme and pathway databases

    Reactomei REACT_1941. Formation of transcription-coupled NER (TC-NER) repair complex.
    REACT_2222. Dual incision reaction in TC-NER.
    REACT_953. RNA Polymerase I Transcription Initiation.

    Miscellaneous databases

    ChiTaRSi ERCC6. human.
    GeneWikii ERCC6.
    GenomeRNAii 2074.
    NextBioi 8437.
    PROi Q03468.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q03468.
    Bgeei Q03468.
    CleanExi HS_ERCC6.
    Genevestigatori Q03468.

    Family and domain databases

    Gene3Di 3.40.50.300. 2 hits.
    InterProi IPR014001. Helicase_ATP-bd.
    IPR001650. Helicase_C.
    IPR027417. P-loop_NTPase.
    IPR000330. SNF2_N.
    [Graphical view ]
    Pfami PF00271. Helicase_C. 1 hit.
    PF00176. SNF2_N. 1 hit.
    [Graphical view ]
    SMARTi SM00487. DEXDc. 1 hit.
    SM00490. HELICc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 2 hits.
    PROSITEi PS51192. HELICASE_ATP_BIND_1. 1 hit.
    PS51194. HELICASE_CTER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. 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. 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. Cited for: METHYLATION AT LYS-170; LYS-297; LYS-448 AND LYS-1054.
    17. 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. 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.
      , 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. 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. Cited for: VARIANTS [LARGE SCALE ANALYSIS] ALA-591; LEU-652; THR-1038; GLN-1119 AND VAL-1119.
    27. Cited for: VARIANT [LARGE SCALE ANALYSIS] TRP-134.
    28. 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.

    Entry informationi

    Entry nameiERCC6_HUMAN
    AccessioniPrimary (citable) accession number: Q03468
    Secondary accession number(s): D3DX94, Q5W0L9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1993
    Last sequence update: October 1, 1993
    Last modified: October 1, 2014
    This is version 162 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 10
      Human chromosome 10: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3