Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q03468

- ERCC6_HUMAN

UniProt

Q03468 - ERCC6_HUMAN

(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)

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

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 complex binding Source: UniProtKB
  7. protein C-terminus binding Source: UniProtKB
  8. protein N-terminus binding Source: UniProtKB
  9. protein tyrosine kinase activator activity Source: MGI

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. positive regulation of protein tyrosine kinase activity Source: GOC
  12. pyrimidine dimer repair Source: Ensembl
  13. regulation of DNA-templated transcription, elongation Source: UniProtKB
  14. response to gamma radiation Source: Ensembl
  15. response to oxidative stress Source: UniProtKB
  16. response to superoxide Source: Ensembl
  17. response to toxic substance Source: Ensembl
  18. response to UV Source: UniProtKB
  19. response to UV-B Source: Ensembl
  20. response to X-ray Source: Ensembl
  21. transcription-coupled nucleotide-excision repair Source: UniProtKB
  22. transcription elongation from RNA polymerase I promoter Source: Ensembl
  23. transcription from RNA polymerase II promoter Source: UniProtKB
Complete GO annotation...

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
Complete GO annotation...

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

BgeeiQ03468.
CleanExiHS_ERCC6.
ExpressionAtlasiQ03468. baseline and differential.
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 – 964Combined sources
Helixi102 – 1043Combined sources
Helixi109 – 15547Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4CVOX-ray1.85A84-160[»]
ProteinModelPortaliQ03468.
SMRiQ03468. Positions 90-158, 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.
GeneTreeiENSGT00590000083118.
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

        10         20         30         40         50
MPNEGIPHSS QTQEQDCLQS QPVSNNEEMA IKQESGGDGE VEEYLSFRSV
60 70 80 90 100
GDGLSTSAVG CASAAPRRGP ALLHIDRHQI QAVEPSAQAL ELQGLGVDVY
110 120 130 140 150
DQDVLEQGVL QQVDNAIHEA SRASQLVDVE KEYRSVLDDL TSCTTSLRQI
160 170 180 190 200
NKIIEQLSPQ AATSRDINRK LDSVKRQKYN KEQQLKKITA KQKHLQAILG
210 220 230 240 250
GAEVKIELDH ASLEEDAEPG PSSLGSMLMP VQETAWEELI RTGQMTPFGT
260 270 280 290 300
QIPQKQEKKP RKIMLNEASG FEKYLADQAK LSFERKKQGC NKRAARKAPA
310 320 330 340 350
PVTPPAPVQN KNKPNKKARV LSKKEERLKK HIKKLQKRAL QFQGKVGLPK
360 370 380 390 400
ARRPWESDMR PEAEGDSEGE ESEYFPTEEE EEEEDDEVEG AEADLSGDGT
410 420 430 440 450
DYELKPLPKG GKRQKKVPVQ EIDDDFFPSS GEEAEAASVG EGGGGGRKVG
460 470 480 490 500
RYRDDGDEDY YKQRLRRWNK LRLQDKEKRL KLEDDSEESD AEFDEGFKVP
510 520 530 540 550
GFLFKKLFKY QQTGVRWLWE LHCQQAGGIL GDEMGLGKTI QIIAFLAGLS
560 570 580 590 600
YSKIRTRGSN YRFEGLGPTV IVCPTTVMHQ WVKEFHTWWP PFRVAILHET
610 620 630 640 650
GSYTHKKEKL IRDVAHCHGI LITSYSYIRL MQDDISRYDW HYVILDEGHK
660 670 680 690 700
IRNPNAAVTL ACKQFRTPHR IILSGSPMQN NLRELWSLFD FIFPGKLGTL
710 720 730 740 750
PVFMEQFSVP ITMGGYSNAS PVQVKTAYKC ACVLRDTINP YLLRRMKSDV
760 770 780 790 800
KMSLSLPDKN EQVLFCRLTD EQHKVYQNFV DSKEVYRILN GEMQIFSGLI
810 820 830 840 850
ALRKICNHPD LFSGGPKNLK GLPDDELEED QFGYWKRSGK MIVVESLLKI
860 870 880 890 900
WHKQGQRVLL FSQSRQMLDI LEVFLRAQKY TYLKMDGTTT IASRQPLITR
910 920 930 940 950
YNEDTSIFVF LLTTRVGGLG VNLTGANRVV IYDPDWNPST DTQARERAWR
960 970 980 990 1000
IGQKKQVTVY RLLTAGTIEE KIYHRQIFKQ FLTNRVLKDP KQRRFFKSND
1010 1020 1030 1040 1050
LYELFTLTSP DASQSTETSA IFAGTGSDVQ TPKCHLKRRI QPAFGADHDV
1060 1070 1080 1090 1100
PKRKKFPASN ISVNDATSSE EKSEAKGAEV NAVTSNRSDP LKDDPHMSSN
1110 1120 1130 1140 1150
VTSNDRLGEE TNAVSGPEEL SVISGNGECS NSSGTGKTSM PSGDESIDEK
1160 1170 1180 1190 1200
LGLSYKRERP SQAQTEAFWE NKQMENNFYK HKSKTKHHSV AEEETLEKHL
1210 1220 1230 1240 1250
RPKQKPKNSK HCRDAKFEGT RIPHLVKKRR YQKQDSENKS EAKEQSNDDY
1260 1270 1280 1290 1300
VLEKLFKKSV GVHSVMKHDA IMDGASPDYV LVEAEANRVA QDALKALRLS
1310 1320 1330 1340 1350
RQRCLGAVSG VPTWTGHRGI SGAPAGKKSR FGKKRNSNFS VQHPSSTSPT
1360 1370 1380 1390 1400
EKCQDGIMKK EGKDNVPEHF SGRAEDADSS SGPLASSSLL AKMRARNHLI
1410 1420 1430 1440 1450
LPERLESESG HLQEASALLP TTEHDDLLVE MRNFIAFQAH TDGQASTREI
1460 1470 1480 1490
LQEFESKLSA SQSCVFRELL RNLCTFHRTS GGEGIWKLKP EYC
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4CVO X-ray 1.85 A 84-160 [» ]
ProteinModelPortali Q03468.
SMRi Q03468. Positions 90-158, 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.
GeneTreei ENSGT00590000083118.
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

Bgeei Q03468.
CleanExi HS_ERCC6.
ExpressionAtlasi Q03468. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 164 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