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P18074 (ERCC2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 177. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
TFIIH basal transcription factor complex helicase XPD subunit

EC=3.6.4.12
Alternative name(s):
Basic transcription factor 2 80 kDa subunit
Short name=BTF2 p80
CXPD
DNA excision repair protein ERCC-2
DNA repair protein complementing XP-D cells
TFIIH basal transcription factor complex 80 kDa subunit
Short name=TFIIH 80 kDa subunit
Short name=TFIIH p80
Xeroderma pigmentosum group D-complementing protein
Gene names
Name:ERCC2
Synonyms:XPD, XPDC
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length760 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

ATP-dependent 5'-3' DNA helicase, component of the core-TFIIH basal transcription factor. Involved in nucleotide excision repair (NER) of DNA by opening DNA around the damage, and in RNA transcription by RNA polymerase II by anchoring the CDK-activating kinase (CAK) complex, composed of CDK7, cyclin H and MAT1, to the core-TFIIH complex. Involved in the regulation of vitamin-D receptor activity. As part of the mitotic spindle-associated MMXD complex it plays a role in chromosome segregation. Might have a role in aging process and could play a causative role in the generation of skin cancers. Ref.8 Ref.12 Ref.13 Ref.16

Catalytic activity

ATP + H2O = ADP + phosphate.

Cofactor

Magnesium. Ref.18

Binds 1 4Fe-4S cluster. Ref.18

Subunit structure

One of the six subunits forming the core-TFIIH basal transcription factor which associates with the CAK complex composed of CDK7, CCNH/cyclin H and MNAT1 to form the TFIIH basal transcription factor. The interaction with GTF2H2 results in the stimulation of the 5'-->3' helicase activity. Component of the MMXD complex, which includes CIAO1, ERCC2, FAM96B, MMS19 and SLC25A5. Interacts with FAM196B; the interaction is direct. Interacts with ATF7IP. Interacts with Epstein-Barr virus EBNA2. Ref.9 Ref.10 Ref.11 Ref.15 Ref.16

Subcellular location

Nucleus. Cytoplasmcytoskeletonspindle Ref.16.

Post-translational modification

ISGylated Probable. Ref.14

Involvement in disease

Xeroderma pigmentosum complementation group D (XP-D) [MIM:278730]: An autosomal recessive pigmentary skin disorder characterized by solar hypersensitivity of the skin, high predisposition for developing cancers on areas exposed to sunlight and, in some cases, neurological abnormalities. The skin develops marked freckling and other pigmentation abnormalities. Some XP-D patients present features of Cockayne syndrome, including cachectic dwarfism, pigmentary retinopathy, ataxia, decreased nerve conduction velocities. The phenotype combining xeroderma pigmentosum and Cockayne syndrome traits is referred to as XP-CS complex.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.13 Ref.19 Ref.21 Ref.22 Ref.24 Ref.34

Trichothiodystrophy photosensitive (TTDP) [MIM:601675]: TTDP is an autosomal recessive disease characterized by sulfur-deficient brittle hair and nails, ichthyosis, mental retardation, impaired sexual development, abnormal facies and cutaneous photosensitivity correlated with a nucleotide excision repair (NER) defect. Neonates with trichothiodystrophy and ichthyosis are usually born with a collodion membrane. The severity of the ichthyosis after the membrane is shed is variable, ranging from a mild to severe lamellar ichthyotic phenotype. There are no reports of skin cancer associated with TTDP.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.20 Ref.23 Ref.25 Ref.26 Ref.27 Ref.35

Cerebro-oculo-facio-skeletal syndrome 2 (COFS2) [MIM:610756]: 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.29

Sequence similarities

Belongs to the helicase family. RAD3/XPD subfamily.

Contains 1 helicase ATP-binding domain.

Sequence caution

The sequence AAM45142.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Biological processChromosome partition
DNA damage
DNA repair
Host-virus interaction
Transcription
Transcription regulation
   Cellular componentCytoplasm
Cytoskeleton
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseCataract
Cockayne syndrome
Deafness
Disease mutation
Dwarfism
Ichthyosis
Xeroderma pigmentosum
   Ligand4Fe-4S
ATP-binding
DNA-binding
Iron
Iron-sulfur
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionHelicase
Hydrolase
   PTMUbl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_process7-methylguanosine mRNA capping

Traceable author statement. Source: Reactome

ATP catabolic process

Inferred from direct assay Ref.10. Source: GOC

DNA duplex unwinding

Inferred from direct assay PubMed 11445587PubMed 8663148. Source: GOC

DNA repair

Traceable author statement. Source: Reactome

UV protection

Inferred from genetic interaction PubMed 2835663. Source: MGI

aging

Inferred from electronic annotation. Source: Ensembl

apoptotic process

Inferred from mutant phenotype PubMed 8675009. Source: UniProtKB

bone mineralization

Inferred from electronic annotation. Source: Ensembl

cell proliferation

Inferred from electronic annotation. Source: Ensembl

central nervous system myelin formation

Inferred from electronic annotation. Source: Ensembl

chromosome segregation

Inferred from mutant phenotype Ref.16. Source: UniProtKB

embryonic cleavage

Inferred from electronic annotation. Source: Ensembl

erythrocyte maturation

Inferred from electronic annotation. Source: Ensembl

extracellular matrix organization

Inferred from electronic annotation. Source: Ensembl

gene expression

Traceable author statement. Source: Reactome

hair cell differentiation

Inferred from mutant phenotype PubMed 11335038. Source: UniProtKB

hair follicle maturation

Inferred from electronic annotation. Source: Ensembl

hematopoietic stem cell differentiation

Inferred from electronic annotation. Source: Ensembl

in utero embryonic development

Inferred from electronic annotation. Source: Ensembl

multicellular organism growth

Inferred from electronic annotation. Source: Ensembl

nucleotide-excision repair

Non-traceable author statement Ref.1. Source: UniProtKB

nucleotide-excision repair, DNA damage removal

Traceable author statement. Source: Reactome

nucleotide-excision repair, DNA incision

Inferred from mutant phenotype PubMed 8692841. Source: UniProtKB

positive regulation of DNA binding

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 8692841. Source: UniProtKB

positive regulation of transcription, DNA-templated

Inferred from direct assay PubMed 8692842. Source: UniProtKB

positive regulation of viral transcription

Traceable author statement. Source: Reactome

post-embryonic development

Inferred from electronic annotation. Source: Ensembl

protein phosphorylation

Inferred from direct assay Ref.10. Source: GOC

regulation of mitotic cell cycle phase transition

Inferred from mutant phenotype PubMed 17088560. Source: UniProtKB

response to hypoxia

Inferred from electronic annotation. Source: Ensembl

response to oxidative stress

Inferred from mutant phenotype PubMed 17614221. Source: UniProtKB

small molecule metabolic process

Traceable author statement. Source: Reactome

spinal cord development

Inferred from electronic annotation. Source: Ensembl

termination of RNA polymerase I transcription

Traceable author statement. Source: Reactome

transcription elongation from RNA polymerase I promoter

Traceable author statement. Source: Reactome

transcription elongation from RNA polymerase II promoter

Traceable author statement. Source: Reactome

transcription from RNA polymerase I promoter

Traceable author statement. Source: Reactome

transcription from RNA polymerase II promoter

Inferred from direct assay Ref.10. Source: UniProtKB

transcription initiation from RNA polymerase I promoter

Traceable author statement. Source: Reactome

transcription initiation from RNA polymerase II promoter

Traceable author statement. Source: Reactome

transcription-coupled nucleotide-excision repair

Inferred from direct assay PubMed 8663148. Source: UniProtKB

viral process

Traceable author statement. Source: Reactome

   Cellular_componentMMXD complex

Inferred from direct assay Ref.16. Source: UniProtKB

cytoplasm

Inferred from direct assay Ref.16. Source: UniProtKB

holo TFIIH complex

Inferred from direct assay Ref.10. Source: UniProtKB

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay Ref.16. Source: UniProtKB

spindle

Inferred from direct assay Ref.16. Source: UniProtKB

   Molecular_function4 iron, 4 sulfur cluster binding

Inferred from electronic annotation. Source: UniProtKB-KW

5'-3' DNA helicase activity

Inferred from direct assay PubMed 11445587PubMed 8663148. Source: UniProtKB

ATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ATP-dependent DNA helicase activity

Inferred from electronic annotation. Source: InterPro

DNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

DNA-dependent ATPase activity

Traceable author statement PubMed 8663148. Source: UniProtKB

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein C-terminus binding

Inferred from physical interaction PubMed 10801852. Source: UniProtKB

protein N-terminus binding

Inferred from physical interaction PubMed 8652557. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 11445587Ref.16PubMed 7663514PubMed 8652557. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P18074-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P18074-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-24: Missing.
     414-429: FTIIIEPFDDRTPTIA → QAQHCGSSRNQKRSHP
     430-760: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 760760TFIIH basal transcription factor complex helicase XPD subunit
PRO_0000101980

Regions

Domain7 – 283277Helicase ATP-binding
Nucleotide binding42 – 498ATP By similarity
Region438 – 637200Mediates interaction with MMS19
Motif234 – 2374DEAH box
Motif682 – 69514Nuclear localization signal Potential

Sites

Metal binding1161Iron-sulfur (4Fe-4S) By similarity
Metal binding1341Iron-sulfur (4Fe-4S) By similarity
Metal binding1551Iron-sulfur (4Fe-4S) By similarity
Metal binding1901Iron-sulfur (4Fe-4S) Probable

Natural variations

Alternative sequence1 – 2424Missing in isoform 2.
VSP_043132
Alternative sequence414 – 42916FTIII…TPTIA → QAQHCGSSRNQKRSHP in isoform 2.
VSP_043133
Alternative sequence430 – 760331Missing in isoform 2.
VSP_043134
Natural variant471G → R in XP-D.
VAR_008187
Natural variant761T → A in XP-D.
VAR_017282
Natural variant1121R → H in TTDP and XP-D. Ref.20 Ref.27 Ref.34
VAR_003622
Natural variant1991I → M.
Corresponds to variant rs1799791 [ dbSNP | Ensembl ].
VAR_011412
Natural variant2011H → Y.
Corresponds to variant rs1799792 [ dbSNP | Ensembl ].
VAR_011413
Natural variant2341D → N in XP-D.
VAR_008188
Natural variant2591C → Y in TTDP. Ref.27
VAR_008189
Natural variant3121D → N. Ref.3 Ref.31 Ref.32 Ref.34
Corresponds to variant rs1799793 [ dbSNP | Ensembl ].
VAR_011414
Natural variant4611L → V in XP-D and TTDP. Ref.19 Ref.25 Ref.27
VAR_003623
Natural variant4821Missing in TTDP. Ref.27
VAR_008190
Natural variant4851L → P in XP-D; the corresponding mutation in fission yeast causes complete loss of activity. Ref.34
VAR_017283
Natural variant4871R → G in TTDP.
VAR_017284
Natural variant488 – 4936Missing in TTDP; mild.
VAR_003624
Natural variant5111R → Q in XP-D.
VAR_017285
Natural variant5411S → R in XP-D; mild. Ref.24
Corresponds to variant rs121913019 [ dbSNP | Ensembl ].
VAR_003625
Natural variant5421Y → C in XP-D.
VAR_008191
Natural variant582 – 5832EK → VSE in XP-D.
VAR_017286
Natural variant5921R → P in TTDP.
VAR_017287
Natural variant5941A → P in TTDP.
VAR_017288
Natural variant6011R → L in XP-D.
VAR_008192
Natural variant6011R → W in XP-D.
VAR_017289
Natural variant6021G → D in XP-D; combined with features of Cockayne syndrome.
VAR_003627
Natural variant6161R → C. Ref.30
VAR_011415
Natural variant6161R → P in XP-D and TTDP. Ref.20
VAR_003626
Natural variant6161R → W in XP-D and COFS2. Ref.29
VAR_008193
Natural variant6581R → C in TTDP. Ref.23 Ref.35
VAR_008194
Natural variant6581R → G in TTDP.
VAR_017290
Natural variant6581R → H in TTDP.
VAR_008195
Natural variant6631C → R in TTDP.
VAR_017291
Natural variant6661R → W in XP-D.
VAR_017292
Natural variant6731D → G in TTDP. Ref.27
VAR_008196
Natural variant6751G → R in XP-D/CS; severe form. Ref.21
VAR_003628
Natural variant6811D → N in XP-D and COFS2. Ref.29
VAR_017293
Natural variant6831R → Q in XP-D; CNS.
VAR_008197
Natural variant6831R → W in XP-D; CNS; vitamin D-mediated activation of CYP24A1 is impaired in patient fibroblasts due to altered TFIIH-dependent phosphorylation of ETS1, subsequent impaired cooperation of ETS1 with VDR and altered VDR recruitment to CYP24A1 promoter. Ref.13
Corresponds to variant rs41556519 [ dbSNP | Ensembl ].
VAR_008198
Natural variant7131G → R in TTDP. Ref.23 Ref.35
VAR_008199
Natural variant716 – 73015Missing in XP-D and TTDP.
VAR_003629
Natural variant7221R → W in TTDP. Ref.20 Ref.27
VAR_003630
Natural variant7251A → P in TTDP. Ref.25
VAR_003631
Natural variant7511K → Q May be linked to a reduced activity. Ref.3 Ref.5 Ref.6 Ref.31 Ref.32 Ref.34
Corresponds to variant rs13181 [ dbSNP | Ensembl ].
VAR_011416

Experimental info

Mutagenesis481K → R: Decreased transcriptional activity of the reconstituted TFIIH complex. Ref.12
Mutagenesis1901C → S: Reduced iron-sulfur-binding. Iron-sulfur-binding is further decreased in absence of MMS19. Ref.18

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 1, 1990. Version 1.
Checksum: 746C0888CDF2E331

FASTA76086,909
        10         20         30         40         50         60 
MKLNVDGLLV YFPYDYIYPE QFSYMRELKR TLDAKGHGVL EMPSGTGKTV SLLALIMAYQ 

        70         80         90        100        110        120 
RAYPLEVTKL IYCSRTVPEI EKVIEELRKL LNFYEKQEGE KLPFLGLALS SRKNLCIHPE 

       130        140        150        160        170        180 
VTPLRFGKDV DGKCHSLTAS YVRAQYQHDT SLPHCRFYEE FDAHGREVPL PAGIYNLDDL 

       190        200        210        220        230        240 
KALGRRQGWC PYFLARYSIL HANVVVYSYH YLLDPKIADL VSKELARKAV VVFDEAHNID 

       250        260        270        280        290        300 
NVCIDSMSVN LTRRTLDRCQ GNLETLQKTV LRIKETDEQR LRDEYRRLVE GLREASAARE 

       310        320        330        340        350        360 
TDAHLANPVL PDEVLQEAVP GSIRTAEHFL GFLRRLLEYV KWRLRVQHVV QESPPAFLSG 

       370        380        390        400        410        420 
LAQRVCIQRK PLRFCAERLR SLLHTLEITD LADFSPLTLL ANFATLVSTY AKGFTIIIEP 

       430        440        450        460        470        480 
FDDRTPTIAN PILHFSCMDA SLAIKPVFER FQSVIITSGT LSPLDIYPKI LDFHPVTMAT 

       490        500        510        520        530        540 
FTMTLARVCL CPMIIGRGND QVAISSKFET REDIAVIRNY GNLLLEMSAV VPDGIVAFFT 

       550        560        570        580        590        600 
SYQYMESTVA SWYEQGILEN IQRNKLLFIE TQDGAETSVA LEKYQEACEN GRGAILLSVA 

       610        620        630        640        650        660 
RGKVSEGIDF VHHYGRAVIM FGVPYVYTQS RILKARLEYL RDQFQIREND FLTFDAMRHA 

       670        680        690        700        710        720 
AQCVGRAIRG KTDYGLMVFA DKRFARGDKR GKLPRWIQEH LTDANLNLTV DEGVQVAKYF 

       730        740        750        760 
LRQMAQPFHR EDQLGLSLLS LEQLESEETL KRIEQIAQQL 

« Hide

Isoform 2 [UniParc].

Checksum: D56A486AC3C9D222
Show »

FASTA40546,274

References

« Hide 'large scale' references
[1]"ERCC2: cDNA cloning and molecular characterization of a human nucleotide excision repair gene with high homology to yeast RAD3."
Weber C.A., Salazar E.P., Stewart S.A., Thompson L.H.
EMBO J. 9:1437-1447(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Fibroblast.
[2]"Sequence analysis of the ERCC2 gene regions in human, mouse, and hamster reveals three linked genes."
Lamerdin J.E., Stilwagen S.A., Ramirez M.H., Stubbs L., Carrano A.V.
Genomics 34:399-409(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Fibroblast.
[3]NIEHS SNPs program
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ASN-312 AND GLN-751.
[4]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[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 (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT GLN-751.
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT GLN-751.
Tissue: Testis.
[7]"Correction of Xeroderma pigmentosum complementation group D mutant cell phenotypes by chromosome and gene transfer: involvement of the human ERCC2 DNA repair gene."
Fletjer W.L., McDaniel L.D., Johns D., Friedberg E.C., Schultz R.A.
Proc. Natl. Acad. Sci. U.S.A. 89:261-265(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[8]"Human Xeroderma pigmentosum group D gene encodes a DNA helicase."
Sung P., Bailly V., Weber C.A., Thompson L.H., Prakash L., Prakash S.
Nature 365:852-855(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[9]"The 62- and 80-kDa subunits of transcription factor IIH mediate the interaction with Epstein-Barr virus nuclear protein 2."
Tong X., Drapkin R., Reinberg D., Kieff E.
Proc. Natl. Acad. Sci. U.S.A. 92:3259-3263(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH EBV EBNA2.
[10]"Immunoaffinity purification and functional characterization of human transcription factor IIH and RNA polymerase II from clonal cell lines that conditionally express epitope-tagged subunits of the multiprotein complexes."
Kershnar E., Wu S.-Y., Chiang C.-M.
J. Biol. Chem. 273:34444-34453(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE TFIIH BASAL TRANSCRIPTION FACTOR.
[11]"Mutations in the XPD helicase gene result in XP and TTD phenotypes, preventing interaction between XPD and the p44 subunit of TFIIH."
Coin F., Marinoni J.-C., Rodolfo C., Fribourg S., Pedrini A.M., Egly J.-M.
Nat. Genet. 20:184-188(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GTF2H2.
[12]"Reconstitution of the transcription factor TFIIH: assignment of functions for the three enzymatic subunits, XPB, XPD, and cdk7."
Tirode F., Busso D., Coin F., Egly J.-M.
Mol. Cell 3:87-95(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF LYS-48, FUNCTION.
[13]"Selective regulation of vitamin D receptor-responsive genes by TFIIH."
Drane P., Compe E., Catez P., Chymkowitch P., Egly J.-M.
Mol. Cell 16:187-197(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, POSSIBLE PATHOLOGICAL MECHANISM OF VARIANT XP-D TRP-683.
[14]"Identification and Herc5-mediated ISGylation of novel target proteins."
Takeuchi T., Inoue S., Yokosawa H.
Biochem. Biophys. Res. Commun. 348:473-477(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: ISGYLATION.
[15]"MCAF1/AM is involved in Sp1-mediated maintenance of cancer-associated telomerase activity."
Liu L., Ishihara K., Ichimura T., Fujita N., Hino S., Tomita S., Watanabe S., Saitoh N., Ito T., Nakao M.
J. Biol. Chem. 284:5165-5174(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ATF7IP.
[16]"MMXD, a TFIIH-independent XPD-MMS19 protein complex involved in chromosome segregation."
Ito S., Tan L.J., Andoh D., Narita T., Seki M., Hirano Y., Narita K., Kuraoka I., Hiraoka Y., Tanaka K.
Mol. Cell 39:632-640(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN MMXD COMPLEX, INTERACTION WITH FAM196B, SUBCELLULAR LOCATION.
[17]"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].
[18]"MMS19 links cytoplasmic iron-sulfur cluster assembly to DNA metabolism."
Gari K., Leon Ortiz A.M., Borel V., Flynn H., Skehel J.M., Boulton S.J.
Science 337:243-245(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IRON-SULFUR-BINDING, COFACTOR, MUTAGENESIS OF CYS-190.
[19]"Structural and mutational analysis of the xeroderma pigmentosum group D (XPD) gene."
Frederick G.D., Amirkhan R.H., Schultz R.A., Friedberg E.C.
Hum. Mol. Genet. 3:1783-1788(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT XP-D VAL-461.
[20]"Mutations in the xeroderma pigmentosum group D DNA repair/transcription gene in patients with trichothiodystrophy."
Broughton B.C., Steingrimsdottir H., Weber C.A., Lehmann A.R.
Nat. Genet. 7:189-194(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS TTDP HIS-112; PRO-616; TRP-722 AND 488-VAL--MET-493 DEL.
[21]"Molecular and cellular analysis of the DNA repair defect in a patient in xeroderma pigmentosum complementation group D who has the clinical features of xeroderma pigmentosum and Cockayne syndrome."
Broughton B.C., Thompson A.F., Harcourt S.A., Vermeulen W., Hoeijmakers J.H.J., Botta E., Stefanini M., King M.D., Weber C.A., Cole J., Arlett C.F., Lehmann A.R.
Am. J. Hum. Genet. 56:167-174(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT XP-D ARG-675.
[22]"Defects in the DNA repair and transcription gene ERCC2 in the cancer-prone disorder xeroderma pigmentosum group D."
Takayama K., Salazar E.P., Lehmann A.R., Stefanini M., Thompson L.H., Weber C.A.
Cancer Res. 55:5656-5663(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS XP-D.
[23]"Defects in the DNA repair and transcription gene ERCC2(XPD) in trichothiodystrophy."
Takayama K., Salazar E.P., Broughton B.C., Lehmann A.R., Sarasin A., Thompson L.H., Weber C.A.
Am. J. Hum. Genet. 58:263-270(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS TTDP CYS-658 AND ARG-713.
[24]"Mutations in the XPD gene leading to Xeroderma pigmentosum symptoms."
Kobayashi T., Kuraoka I., Saijo M., Nakatsu Y., Tanaka A., Someda Y., Fukuro S., Tanaka K.
Hum. Mutat. 9:322-331(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT XP-D ARG-541.
[25]"DNA repair characteristics and mutations in the ERCC2 DNA repair and transcription gene in a trichothiodystrophy patient."
Takayama K., Danks D.M., Salazar E.P., Cleaver J.E., Weber C.A.
Hum. Mutat. 9:519-525(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS TTDP VAL-461; 716-VAL--ARG-730 DEL AND PRO-725.
[26]"Xeroderma pigmentosum and trichothiodystrophy are associated with different mutations in the XPD (ERCC2) repair/transcription gene."
Taylor E.M., Broughton B.C., Botta E., Stefanini M., Sarasin A., Jaspers N.G.J., Fawcett H., Harcourt S.A., Arlett C.F., Lehmann A.R.
Proc. Natl. Acad. Sci. U.S.A. 94:8658-8663(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS TTDP/XP.
[27]"Analysis of mutations in the XPD gene in Italian patients with trichothiodystrophy: site of mutation correlates with repair deficiency, but gene dosage appears to determine clinical severity."
Botta E., Nardo T., Broughton B.C., Marinoni S., Lehmann A.R., Stefanini M.
Am. J. Hum. Genet. 63:1036-1048(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS TTDP HIS-112; TYR-259; VAL-461; THR-482 DEL; GLY-673 AND TRP-722.
[28]"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 XP-D.
[29]"Cerebro-oculo-facio-skeletal syndrome with a nucleotide excision-repair defect and a mutated XPD gene, with prenatal diagnosis in a triplet pregnancy."
Graham J.M. Jr., Anyane-Yeboa K., Raams A., Appeldoorn E., Kleijer W.J., Garritsen V.H., Busch D., Edersheim T.G., Jaspers N.G.J.
Am. J. Hum. Genet. 69:291-300(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS COFS2 TRP-616 AND ASN-681.
[30]"Associations between ercc2 polymorphisms and gliomas."
Caggana M., Kilgallen J., Conroy J.M., Wiencke J.K., Kelsey K.T., Miike R., Chen P., Wrensch M.R.
Cancer Epidemiol. Biomarkers Prev. 10:355-360(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CYS-616.
[31]"Modulation of nucleotide excision repair capacity by XPD polymorphisms in lung cancer patients."
Spitz M.R., Wu X., Wang Y., Wang L.E., Shete S., Amos C.I., Guo Z., Lei L., Mohrenweiser H., Wei Q.
Cancer Res. 61:1354-1357(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ASN-312 AND GLN-751.
[32]"XPD exon 10 and 23 polymorphisms and DNA repair in human skin in situ."
Hemminki K., Xu G., Angelini S., Snellman E., Jansen C.T., Lambert B., Hou S.M.
Carcinogenesis 22:1185-1188(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ASN-312 AND GLN-751.
[33]"The xeroderma pigmentosum group D (XPD) gene: one gene, two functions, three diseases."
Lehmann A.R.
Genes Dev. 15:15-23(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON VARIANTS.
[34]"Two individuals with features of both xeroderma pigmentosum and trichothiodystrophy highlight the complexity of the clinical outcomes of mutations in the XPD gene."
Broughton B.C., Berneburg M., Fawcett H., Taylor E.M., Arlett C.F., Nardo T., Stefanini M., Menefee E., Price V.H., Queille S., Sarasin A., Bohnert E., Krutmann J., Davidson R., Kraemer K.H., Lehmann A.R.
Hum. Mol. Genet. 10:2539-2547(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS XP-D HIS-112; PRO-485 AND 582-GLU-LYS-583 DELINS VAL-SER-GLU, VARIANTS ASN-312 AND GLN-751.
[35]"A temperature-sensitive disorder in basal transcription and DNA repair in humans."
Vermeulen W., Rademakers S., Jaspers N.G.J., Appeldoorn E., Raams A., Klein B., Kleijer W.J., Hansen L.K., Hoeijmakers J.H.J.
Nat. Genet. 27:299-303(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS TTDP CYS-658 AND ARG-713.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X52221 mRNA. Translation: CAA36463.1.
X52222 mRNA. Translation: CAA36464.1.
L47234 Genomic DNA. Translation: AAL48323.1.
AY092780 Genomic DNA. Translation: AAM45142.1. Sequence problems.
BT006883 mRNA. Translation: AAP35529.1.
CH471126 Genomic DNA. Translation: EAW57341.1.
BC108255 mRNA. Translation: AAI08256.1.
BC110523 mRNA. Translation: AAI10524.1.
CCDSCCDS33049.1. [P18074-1]
CCDS46112.1. [P18074-2]
PIRS10888.
RefSeqNP_000391.1. NM_000400.3. [P18074-1]
NP_001124339.1. NM_001130867.1. [P18074-2]
XP_005258696.1. XM_005258639.1.
UniGeneHs.487294.

3D structure databases

ProteinModelPortalP18074.
SMRP18074. Positions 35-258.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108380. 25 interactions.
DIPDIP-644N.
IntActP18074. 1 interaction.
MINTMINT-3008891.
STRING9606.ENSP00000375809.

PTM databases

PhosphoSiteP18074.

Polymorphism databases

DMDM119540.

Proteomic databases

MaxQBP18074.
PaxDbP18074.
PRIDEP18074.

Protocols and materials databases

DNASU2068.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000391940; ENSP00000375804; ENSG00000104884. [P18074-2]
ENST00000391945; ENSP00000375809; ENSG00000104884. [P18074-1]
ENST00000485403; ENSP00000431229; ENSG00000104884. [P18074-2]
GeneID2068.
KEGGhsa:2068.
UCSCuc002pbj.2. human. [P18074-1]
uc002pbl.4. human. [P18074-2]

Organism-specific databases

CTD2068.
GeneCardsGC19M045854.
GeneReviewsERCC2.
HGNCHGNC:3434. ERCC2.
HPACAB005375.
HPA038057.
MIM126340. gene.
278730. phenotype.
601675. phenotype.
610756. phenotype.
neXtProtNX_P18074.
Orphanet1466. COFS syndrome.
33364. Trichothiodystrophy.
276258. Xeroderma pigmentosum complementation group D.
PharmGKBPA27848.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1199.
HOGENOMHOG000205390.
HOVERGENHBG051498.
InParanoidP18074.
KOK10844.
OMADEVWKYK.
OrthoDBEOG70W3CM.
PhylomeDBP18074.
TreeFamTF101232.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
REACT_116125. Disease.
REACT_1788. Transcription.
REACT_216. DNA Repair.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressP18074.
BgeeP18074.
CleanExHS_ERCC2.
GenevestigatorP18074.

Family and domain databases

Gene3D3.40.50.300. 2 hits.
InterProIPR006555. ATP-dep_Helicase_C.
IPR010614. DEAD_2.
IPR002464. DNA/RNA_helicase_DEAH_CS.
IPR013020. DNA_helicase_DNA-repair_Rad3.
IPR010643. DUF1227.
IPR014013. Helic_SF1/SF2_ATP-bd_DinG/Rad3.
IPR006554. Helicase-like_DEXD_c2.
IPR027417. P-loop_NTPase.
IPR001945. XPGD_DNA_repair.
[Graphical view]
PfamPF06733. DEAD_2. 1 hit.
PF06777. DUF1227. 1 hit.
PF13307. Helicase_C_2. 1 hit.
[Graphical view]
PRINTSPR00852. XRODRMPGMNTD.
SMARTSM00488. DEXDc2. 1 hit.
SM00491. HELICc2. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 4 hits.
TIGRFAMsTIGR00604. rad3. 1 hit.
PROSITEPS00690. DEAH_ATP_HELICASE. 1 hit.
PS51193. HELICASE_ATP_BIND_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSERCC2. human.
GeneWikiERCC2.
GenomeRNAi2068.
NextBio8409.
PROP18074.
SOURCESearch...

Entry information

Entry nameERCC2_HUMAN
AccessionPrimary (citable) accession number: P18074
Secondary accession number(s): Q2TB78 expand/collapse secondary AC list , Q2YDY2, Q7KZU6, Q8N721
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: July 9, 2014
This is version 177 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

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 19

Human chromosome 19: entries, gene names and cross-references to MIM