Reviewed, UniProtKB/Swiss-Prot P18074 (ERCC2_HUMAN)

Names and origin

Protein names

Recommended name:
    TFIIH basal transcription factor complex helicase subunit
    EC=3.6.1.-
Alternative name(s):
    DNA repair protein complementing XP-D cells
    Xeroderma pigmentosum group D-complementing protein
    CXPD
    DNA excision repair protein ERCC-2

Gene names

Name:	ERCC2
Synonyms:	XPD, XPDC

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	760 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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. Might also have a role in aging process and could play a causative role in the generation of skin cancers. Ref.6 Ref.9 Ref.10
Cofactor	Magnesium.
Subunit structure	One of the six subunits forming the core-TFIIH basal transcription factor. The interaction with p44 results in the stimulation of the 5'-->3' helicase activity. Interacts with Epstein-Barr virus EBNA2.
Subcellular location	Nucleus.
Involvement in disease	Defects in ERCC2 are the cause of xeroderma pigmentosum complementation group D (XP-D) [MIM:278730]; also known as XP group D (XPD). Xeroderma pigmentosum is 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. Some XP-D patients present features of Cockayne syndrome, including dwarfism, sensorineural deafness, microcephaly, mental retardation, pigmentary retinopathy, ataxia, decreased nerve conduction velocities. Ref.10 Ref.12 Ref.14 Ref.15 Ref.17 Ref.27 Defects in ERCC2 are a cause of 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. Ref.13 Ref.16 Ref.18 Ref.19 Ref.20 Ref.28 Defects in ERCC2 are the cause of cerebro-oculo-facio-skeletal syndrome type 2 (COFS2) [MIM:610756]. COFS is a degenerative autosomal recessive disorder of prenatal onset affecting the brain, eye and spinal cord. After birth, it leads to brain atrophy, hypoplasia of the corpus callosum, hypotonia, cataracts, microcornea, optic atrophy, progressive joint contractures and growth failure. Facial dysmorphism is a constant feature. Abnormalities of the skull, eyes, limbs, heart and kidney also occur. Ref.22
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 process	DNA damage DNA repair Host-virus interaction Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Polymorphism
Disease	Cataract Cockayne syndrome Deafness Disease mutation Dwarfism Ichthyosis Xeroderma pigmentosum
Ligand	ATP-binding DNA-binding Iron Iron-sulfur Magnesium Metal-binding Nucleotide-binding
Molecular function	Helicase Hydrolase
Gene Ontology (GO)
Biological process	RNA elongation from RNA polymerase II promoter Inferred from Experiment. Source: Reactome UV protection Inferred from genetic interaction. Source: MGI cell cycle checkpoint Inferred from mutant phenotype. Source: UniProtKB hair cell differentiation Inferred from mutant phenotype. Source: UniProtKB induction of apoptosis Inferred from mutant phenotype. Source: UniProtKB nucleotide-excision repair, DNA damage removal Inferred from Experiment. Source: Reactome nucleotide-excision repair, DNA incision Inferred from mutant phenotype. Source: UniProtKB positive regulation of transcription from RNA polymerase II promoter Inferred from direct assay. Source: UniProtKB response to oxidative stress Inferred from mutant phenotype. Source: UniProtKB sensory perception of sound Inferred from electronic annotation. Source: UniProtKB-KW transcription initiation from RNA polymerase II promoter Inferred from Experiment. Source: Reactome transcription-coupled nucleotide-excision repair Inferred from direct assay. Source: UniProtKB
Cellular component	holo TFIIH complex Traceable author statement. Source: UniProtKB
Molecular function	5'-3' DNA helicase activity Inferred from direct assay. 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 iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW iron-sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein C-terminus binding Inferred from physical interaction. Source: UniProtKB protein N-terminus binding Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 760	760	TFIIH basal transcription factor complex helicase subunit		PRO_0000101980
Regions
	Domain	7 – 283	277	Helicase ATP-binding
	Nucleotide binding	42 – 49	8	ATP By similarity
	Motif	234 – 237	4	DEAH box
	Motif	682 – 695	14	Nuclear localization signal Potential
Sites
	Metal binding	116	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	134	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	155	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	190	1	Iron-sulfur (4Fe-4S) By similarity
Natural variations
	Natural variant	47	1	G → R in XP-D.		VAR_008187
	Natural variant	76	1	T → A in XP-D.		VAR_017282
	Natural variant	112	1	R → H in TTDP and XP-D.		VAR_003622
	Natural variant	199	1	I → M: dbSNP rs1799791.		VAR_011412
	Natural variant	201	1	H → Y: dbSNP rs1799792.		VAR_011413
	Natural variant	234	1	D → N in XP-D.		VAR_008188
	Natural variant	259	1	C → Y in TTDP. Ref.20		VAR_008189
	Natural variant	312	1	D → N: dbSNP rs1799793. Ref.27 Ref.24 Ref.25		VAR_011414
	Natural variant	461	1	L → V in XP-D and TTDP.		VAR_003623
	Natural variant	482	1	Missing in TTDP. Ref.20		VAR_008190
	Natural variant	485	1	L → P in XP-D; the corresponding mutation in fission yeast causes complete loss of activity. Ref.27		VAR_017283
	Natural variant	487	1	R → G in TTDP.		VAR_017284
	Natural variant	488 – 493	6	Missing in TTDP; mild. Ref.13		VAR_003624
	Natural variant	511	1	R → Q in XP-D.		VAR_017285
	Natural variant	541	1	S → R in XP-D; mild. Ref.17		VAR_003625
	Natural variant	542	1	Y → C in XP-D.		VAR_008191
	Natural variant	582 – 583	2	EK → VSE in XP-D.		VAR_017286
	Natural variant	592	1	R → P in TTDP.		VAR_017287
	Natural variant	594	1	A → P in TTDP.		VAR_017288
	Natural variant	601	1	R → L in XP-D.		VAR_008192
	Natural variant	601	1	R → W in XP-D.		VAR_017289
	Natural variant	602	1	G → D in XP-D; combined with features of Cockayne syndrome.		VAR_003627
	Natural variant	616	1	R → C Ref.13 Ref.22 Ref.23		VAR_011415
	Natural variant	616	1	R → P in XP-D and TTDP.		VAR_003626
	Natural variant	616	1	R → W in XP-D and COFS2.		VAR_008193
	Natural variant	658	1	R → C in TTDP. Ref.16 Ref.28		VAR_008194
	Natural variant	658	1	R → G in TTDP. Ref.16 Ref.28		VAR_017290
	Natural variant	658	1	R → H in TTDP. Ref.16 Ref.28		VAR_008195
	Natural variant	663	1	C → R in TTDP.		VAR_017291
	Natural variant	666	1	R → W in XP-D.		VAR_017292
	Natural variant	673	1	D → G in TTDP. Ref.20		VAR_008196
	Natural variant	675	1	G → R in XP-D/CS; severe form.		VAR_003628
	Natural variant	681	1	D → N in XP-D and COFS2.		VAR_017293
	Natural variant	683	1	R → Q in XP-D; CNS. Ref.10		VAR_008197
	Natural variant	683	1	R → 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 recruitement to CYP24A1 promoter. Ref.10		VAR_008198
	Natural variant	713	1	G → R in TTDP. Ref.16 Ref.28		VAR_008199
	Natural variant	716 – 730	15	Missing in XP-D and TTDP.		VAR_003629
	Natural variant	722	1	R → W in TTDP. Ref.13 Ref.20		VAR_003630
	Natural variant	725	1	A → P in TTDP. Ref.18		VAR_003631
	Natural variant	751	1	K → Q May be linked to a reduced activity. dbSNP rs13181. Ref.27 Ref.24 Ref.25		VAR_011416
Experimental info
	Mutagenesis	48	1	K → R: Decreased transcriptional activity of the reconstituted TFIIH complex. Ref.9

Sequences

	Sequence		Length	Mass (Da)
	P18074-1 [UniParc]. Last modified November 1, 1990. Version 1. Checksum: 746C0888CDF2E331	FASTA	760	86,909
	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

References

	« Hide 'large scale' referencesShow '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: 2184031] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. 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: 8786141] [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]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Testis.
[5]	"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: 1729695] [Abstract] Cited for: CHARACTERIZATION.
[6]	"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: 8413672] [Abstract] Cited for: FUNCTION.
[7]	"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: 7724549] [Abstract] Cited for: INTERACTION WITH EBV EBNA2.
[8]	"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: 9771713] [Abstract] Cited for: INTERACTION WITH P44.
[9]	"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: 10024882] [Abstract] Cited for: MUTAGENESIS OF LYS-48, FUNCTION.
[10]	"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: 15494306] [Abstract] Cited for: FUNCTION, POSSIBLE PATHOLOGICAL MECHANISM OF VARIANT XP-D TRP-683.
[11]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[12]	"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: 7849702] [Abstract] Cited for: VARIANT XP-D VAL-461.
[13]	"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: 7920640] [Abstract] Cited for: VARIANTS TTDP HIS-112; PRO-616; TRP-722 AND 488-VAL--MET-493 DEL.
[14]	"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: 7825573] [Abstract] Cited for: VARIANT XP-D ARG-675.
[15]	"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: 7585650] [Abstract] Cited for: VARIANTS XP-D.
[16]	"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: 8571952] [Abstract] Cited for: VARIANTS TTDP CYS-658 AND ARG-713.
[17]	"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: 9101292] [Abstract] Cited for: VARIANT XP-D ARG-541.
[18]	"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: 9195225] [Abstract] Cited for: VARIANTS TTDP VAL-461; 716-VAL--ARG-730 DEL AND PRO-725.
[19]	"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: 9238033] [Abstract] Cited for: VARIANTS TTDP/XP.
[20]	"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: 9758621] [Abstract] Cited for: VARIANTS TTDP HIS-112; TYR-259; VAL-461; THR-482 DEL; GLY-673 AND TRP-722.
[21]	"A summary of mutations in the UV-sensitive disorders: xeroderma pigmentosum, Cockayne syndrome, and trichothiodystrophy." Cleaver J.E., Thompson L.H., Richardson A.S., States J.C. Hum. Mutat. 14:9-22(1999) [PubMed: 10447254] [Abstract] Cited for: REVIEW ON VARIANTS XP-D.
[22]	"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: 11443545] [Abstract] Cited for: VARIANTS COFS2 TRP-616 AND ASN-681.
[23]	"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: 11319176] [Abstract] Cited for: VARIANT CYS-616.
[24]	"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: 11245433] [Abstract] Cited for: VARIANTS ASN-312 AND GLN-751.
[25]	"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: 11470747] [Abstract] Cited for: VARIANTS ASN-312 AND GLN-751.
[26]	"The xeroderma pigmentosum group D (XPD) gene: one gene, two functions, three diseases." Lehmann A.R. Genes Dev. 15:15-23(2001) [PubMed: 11156600] [Abstract] Cited for: REVIEW ON VARIANTS.
[27]	"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: 11709541] [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.
[28]	"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: 11242112] [Abstract] Cited for: VARIANTS TTDP CYS-658 AND ARG-713.
+	Additional computationally mapped references.

Web resources

Allelic variations of the XP genes

Atlas of Genetics and Cytogenetics in Oncology and Haematology

GeneReviews

NIEHS-SNPs

Cross-references

Sequence databases
EMBLGenBankDDBJ	X52221 mRNA. Translation: CAA36463.1. X52222 mRNA. Translation: CAA36464.1. L47234 Genomic DNA. Translation: AAL48323.1. AY092780 Genomic DNA. Translation: AAM45142.1. Sequence problems. BC108255 mRNA. Translation: AAI08256.1.
IPI	IPI00029728.
PIR	S10888.
RefSeq	NP_000391.1.
UniGene	Hs.487294
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:644N.
Proteomic databases
PRIDE	P18074.
Genome annotation databases
Ensembl	ENSG00000104884. Homo sapiens. [Contig view]
GeneID	2068.
KEGG	hsa:2068.
NMPDR	fig|9606.3.peg.16687.
Organism-specific databases
GeneCards	GC19M050546.
H-InvDB	HIX0015230.
HGNC	HGNC:3434. ERCC2.
MIM	126340. gene. 278730. phenotype. 601675. phenotype. 610756. phenotype.
Orphanet	1466. COFS syndrome. 453. IBIDS syndrome. 670. PIBIDS syndrome. 910. Xeroderma pigmentosum.
PharmGKB	PA27848.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	P18074.
HOVERGEN	P18074.
Enzyme and pathway databases
Reactome	REACT_1675. mRNA Processing. REACT_1788. Transcription. REACT_216. DNA Repair. REACT_6185. HIV Infection. REACT_71. Gene Expression.
Gene expression databases
ArrayExpress	P18074.
Bgee	P18074.
CleanEx	HS_ERCC2.
GermOnline	ENSG00000104884. Homo sapiens.
Family and domain databases
InterPro	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. IPR006555. Helicase_ATP-dep_c2. IPR001945. XPGD_DNA_repair. [Graphical view]
Pfam	PF06733. DEAD_2. 1 hit. PF06777. DUF1227. 1 hit. [Graphical view]
PRINTS	PR00852. XRODRMPGMNTD.
SMART	SM00488. DEXDc2. 1 hit. SM00491. HELICc2. 1 hit. [Graphical view]
TIGRFAMs	TIGR00604. rad3. 1 hit.
PROSITE	PS00690. DEAH_ATP_HELICASE. 1 hit. PS51193. HELICASE_ATP_BIND_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	8409.
SOURCE	Search...

Entry information

Entry name

ERCC2_HUMAN

Accession

Primary (citable) accession number: P18074
Secondary accession number(s): Q2YDY2, Q8N721

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1990
Last sequence update:	November 1, 1990
Last modified:	June 16, 2009
This is version 122 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)