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TFIIH basal transcription factor complex helicase XPD subunit (EC 3.6.4.12) (Basic transcription factor 2 80 kDa subunit) (BTF2 p80) (CXPD) (DNA excision repair protein ERCC-2) (DNA repair protein complementing XP-D cells) (TFIIH basal transcription factor complex 80 kDa subunit) (TFIIH 80 kDa subunit) (TFIIH p80) (Xeroderma pigmentosum group D-complementing protein)

 ERCC2_HUMAN             Reviewed;         760 AA.
P18074; Q2TB78; Q2YDY2; Q7KZU6; Q8N721;
01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
01-NOV-1990, sequence version 1.
25-OCT-2017, entry version 210.
RecName: Full=TFIIH basal transcription factor complex helicase XPD subunit;
EC=3.6.4.12;
AltName: Full=Basic transcription factor 2 80 kDa subunit;
Short=BTF2 p80;
AltName: Full=CXPD;
AltName: Full=DNA excision repair protein ERCC-2;
AltName: Full=DNA repair protein complementing XP-D cells;
AltName: Full=TFIIH basal transcription factor complex 80 kDa subunit;
Short=TFIIH 80 kDa subunit;
Short=TFIIH p80;
AltName: Full=Xeroderma pigmentosum group D-complementing protein;
Name=ERCC2; Synonyms=XPD, XPDC;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Fibroblast;
PubMed=2184031;
Weber C.A., Salazar E.P., Stewart S.A., Thompson L.H.;
"ERCC2: cDNA cloning and molecular characterization of a human
nucleotide excision repair gene with high homology to yeast RAD3.";
EMBO J. 9:1437-1447(1990).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Fibroblast;
PubMed=8786141; DOI=10.1006/geno.1996.0303;
Lamerdin J.E., Stilwagen S.A., Ramirez M.H., Stubbs L., Carrano A.V.;
"Sequence analysis of the ERCC2 gene regions in human, mouse, and
hamster reveals three linked genes.";
Genomics 34:399-409(1996).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ASN-312 AND GLN-751.
NIEHS SNPs program;
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT GLN-751.
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., 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.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
GLN-751.
TISSUE=Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
CHARACTERIZATION.
PubMed=1729695; DOI=10.1073/pnas.89.1.261;
Fletjer W.L., McDaniel L.D., Johns D., Friedberg E.C., Schultz R.A.;
"Correction of Xeroderma pigmentosum complementation group D mutant
cell phenotypes by chromosome and gene transfer: involvement of the
human ERCC2 DNA repair gene.";
Proc. Natl. Acad. Sci. U.S.A. 89:261-265(1992).
[8]
FUNCTION.
PubMed=8413672; DOI=10.1038/365852a0;
Sung P., Bailly V., Weber C.A., Thompson L.H., Prakash L., Prakash S.;
"Human Xeroderma pigmentosum group D gene encodes a DNA helicase.";
Nature 365:852-855(1993).
[9]
INTERACTION WITH EBV EBNA2.
PubMed=7724549; DOI=10.1073/pnas.92.8.3259;
Tong X., Drapkin R., Reinberg D., Kieff E.;
"The 62- and 80-kDa subunits of transcription factor IIH mediate the
interaction with Epstein-Barr virus nuclear protein 2.";
Proc. Natl. Acad. Sci. U.S.A. 92:3259-3263(1995).
[10]
IDENTIFICATION IN THE TFIIH BASAL TRANSCRIPTION FACTOR.
PubMed=9852112; DOI=10.1074/jbc.273.51.34444;
Kershnar E., Wu S.-Y., Chiang C.-M.;
"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.";
J. Biol. Chem. 273:34444-34453(1998).
[11]
INTERACTION WITH GTF2H2.
PubMed=9771713; DOI=10.1038/2491;
Coin F., Marinoni J.-C., Rodolfo C., Fribourg S., Pedrini A.M.,
Egly J.-M.;
"Mutations in the XPD helicase gene result in XP and TTD phenotypes,
preventing interaction between XPD and the p44 subunit of TFIIH.";
Nat. Genet. 20:184-188(1998).
[12]
MUTAGENESIS OF LYS-48, AND FUNCTION.
PubMed=10024882; DOI=10.1016/S1097-2765(00)80177-X;
Tirode F., Busso D., Coin F., Egly J.-M.;
"Reconstitution of the transcription factor TFIIH: assignment of
functions for the three enzymatic subunits, XPB, XPD, and cdk7.";
Mol. Cell 3:87-95(1999).
[13]
FUNCTION, AND POSSIBLE PATHOLOGICAL MECHANISM OF VARIANT XP-D TRP-683.
PubMed=15494306; DOI=10.1016/j.molcel.2004.10.007;
Drane P., Compe E., Catez P., Chymkowitch P., Egly J.-M.;
"Selective regulation of vitamin D receptor-responsive genes by
TFIIH.";
Mol. Cell 16:187-197(2004).
[14]
ISGYLATION.
PubMed=16884686; DOI=10.1016/j.bbrc.2006.07.076;
Takeuchi T., Inoue S., Yokosawa H.;
"Identification and Herc5-mediated ISGylation of novel target
proteins.";
Biochem. Biophys. Res. Commun. 348:473-477(2006).
[15]
INTERACTION WITH ATF7IP.
PubMed=19106100; DOI=10.1074/jbc.M807098200;
Liu L., Ishihara K., Ichimura T., Fujita N., Hino S., Tomita S.,
Watanabe S., Saitoh N., Ito T., Nakao M.;
"MCAF1/AM is involved in Sp1-mediated maintenance of cancer-associated
telomerase activity.";
J. Biol. Chem. 284:5165-5174(2009).
[16]
FUNCTION, IDENTIFICATION IN MMXD COMPLEX, INTERACTION WITH FAM196B,
AND SUBCELLULAR LOCATION.
PubMed=20797633; DOI=10.1016/j.molcel.2010.07.029;
Ito S., Tan L.J., Andoh D., Narita T., Seki M., Hirano Y., Narita K.,
Kuraoka I., Hiraoka Y., Tanaka K.;
"MMXD, a TFIIH-independent XPD-MMS19 protein complex involved in
chromosome segregation.";
Mol. Cell 39:632-640(2010).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[18]
IRON-SULFUR-BINDING, COFACTOR, AND MUTAGENESIS OF CYS-190.
PubMed=22678361; DOI=10.1126/science.1219664;
Gari K., Leon Ortiz A.M., Borel V., Flynn H., Skehel J.M.,
Boulton S.J.;
"MMS19 links cytoplasmic iron-sulfur cluster assembly to DNA
metabolism.";
Science 337:243-245(2012).
[19]
VARIANT XP-D VAL-461.
PubMed=7849702; DOI=10.1093/hmg/3.10.1783;
Frederick G.D., Amirkhan R.H., Schultz R.A., Friedberg E.C.;
"Structural and mutational analysis of the xeroderma pigmentosum group
D (XPD) gene.";
Hum. Mol. Genet. 3:1783-1788(1994).
[20]
VARIANTS TTD1 HIS-112; PRO-616; TRP-722 AND 488-VAL--MET-493 DEL.
PubMed=7920640; DOI=10.1038/ng0694-189;
Broughton B.C., Steingrimsdottir H., Weber C.A., Lehmann A.R.;
"Mutations in the xeroderma pigmentosum group D DNA
repair/transcription gene in patients with trichothiodystrophy.";
Nat. Genet. 7:189-194(1994).
[21]
VARIANT XP-D ARG-675.
PubMed=7825573;
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.;
"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.";
Am. J. Hum. Genet. 56:167-174(1995).
[22]
VARIANTS XP-D.
PubMed=7585650;
Takayama K., Salazar E.P., Lehmann A.R., Stefanini M., Thompson L.H.,
Weber C.A.;
"Defects in the DNA repair and transcription gene ERCC2 in the cancer-
prone disorder xeroderma pigmentosum group D.";
Cancer Res. 55:5656-5663(1995).
[23]
VARIANTS TTD1 CYS-658 AND ARG-713.
PubMed=8571952;
Takayama K., Salazar E.P., Broughton B.C., Lehmann A.R., Sarasin A.,
Thompson L.H., Weber C.A.;
"Defects in the DNA repair and transcription gene ERCC2(XPD) in
trichothiodystrophy.";
Am. J. Hum. Genet. 58:263-270(1996).
[24]
VARIANT XP-D ARG-541.
PubMed=9101292;
DOI=10.1002/(SICI)1098-1004(1997)9:4<322::AID-HUMU4>3.0.CO;2-7;
Kobayashi T., Kuraoka I., Saijo M., Nakatsu Y., Tanaka A., Someda Y.,
Fukuro S., Tanaka K.;
"Mutations in the XPD gene leading to Xeroderma pigmentosum
symptoms.";
Hum. Mutat. 9:322-331(1997).
[25]
VARIANTS TTD1 VAL-461; 716-VAL--ARG-730 DEL AND PRO-725.
PubMed=9195225;
DOI=10.1002/(SICI)1098-1004(1997)9:6<519::AID-HUMU4>3.3.CO;2-N;
Takayama K., Danks D.M., Salazar E.P., Cleaver J.E., Weber C.A.;
"DNA repair characteristics and mutations in the ERCC2 DNA repair and
transcription gene in a trichothiodystrophy patient.";
Hum. Mutat. 9:519-525(1997).
[26]
VARIANTS TTD1/XP.
PubMed=9238033; DOI=10.1073/pnas.94.16.8658;
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.;
"Xeroderma pigmentosum and trichothiodystrophy are associated with
different mutations in the XPD (ERCC2) repair/transcription gene.";
Proc. Natl. Acad. Sci. U.S.A. 94:8658-8663(1997).
[27]
VARIANTS TTD1 HIS-112; TYR-259; VAL-461; THR-482 DEL; GLY-673 AND
TRP-722.
PubMed=9758621; DOI=10.1086/302063;
Botta E., Nardo T., Broughton B.C., Marinoni S., Lehmann A.R.,
Stefanini M.;
"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.";
Am. J. Hum. Genet. 63:1036-1048(1998).
[28]
REVIEW ON VARIANTS XP-D.
PubMed=10447254;
DOI=10.1002/(SICI)1098-1004(1999)14:1<9::AID-HUMU2>3.0.CO;2-6;
Cleaver J.E., Thompson L.H., Richardson A.S., States J.C.;
"A summary of mutations in the UV-sensitive disorders: xeroderma
pigmentosum, Cockayne syndrome, and trichothiodystrophy.";
Hum. Mutat. 14:9-22(1999).
[29]
VARIANTS COFS2 TRP-616 AND ASN-681.
PubMed=11443545; DOI=10.1086/321295;
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.;
"Cerebro-oculo-facio-skeletal syndrome with a nucleotide excision-
repair defect and a mutated XPD gene, with prenatal diagnosis in a
triplet pregnancy.";
Am. J. Hum. Genet. 69:291-300(2001).
[30]
VARIANT CYS-616.
PubMed=11319176;
Caggana M., Kilgallen J., Conroy J.M., Wiencke J.K., Kelsey K.T.,
Miike R., Chen P., Wrensch M.R.;
"Associations between ercc2 polymorphisms and gliomas.";
Cancer Epidemiol. Biomarkers Prev. 10:355-360(2001).
[31]
VARIANTS ASN-312 AND GLN-751.
PubMed=11245433;
Spitz M.R., Wu X., Wang Y., Wang L.E., Shete S., Amos C.I., Guo Z.,
Lei L., Mohrenweiser H., Wei Q.;
"Modulation of nucleotide excision repair capacity by XPD
polymorphisms in lung cancer patients.";
Cancer Res. 61:1354-1357(2001).
[32]
VARIANTS ASN-312 AND GLN-751.
PubMed=11470747; DOI=10.1093/carcin/22.8.1185;
Hemminki K., Xu G., Angelini S., Snellman E., Jansen C.T., Lambert B.,
Hou S.M.;
"XPD exon 10 and 23 polymorphisms and DNA repair in human skin in
situ.";
Carcinogenesis 22:1185-1188(2001).
[33]
REVIEW ON VARIANTS.
PubMed=11156600; DOI=10.1101/gad.859501;
Lehmann A.R.;
"The xeroderma pigmentosum group D (XPD) gene: one gene, two
functions, three diseases.";
Genes Dev. 15:15-23(2001).
[34]
VARIANTS XP-D HIS-112; PRO-485 AND 582-GLU-LYS-583 DELINS VAL-SER-GLU,
AND VARIANTS ASN-312 AND GLN-751.
PubMed=11709541; DOI=10.1093/hmg/10.22.2539;
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.;
"Two individuals with features of both xeroderma pigmentosum and
trichothiodystrophy highlight the complexity of the clinical outcomes
of mutations in the XPD gene.";
Hum. Mol. Genet. 10:2539-2547(2001).
[35]
VARIANTS TTD1 CYS-658 AND ARG-713.
PubMed=11242112; DOI=10.1038/85864;
Vermeulen W., Rademakers S., Jaspers N.G.J., Appeldoorn E., Raams A.,
Klein B., Kleijer W.J., Hansen L.K., Hoeijmakers J.H.J.;
"A temperature-sensitive disorder in basal transcription and DNA
repair in humans.";
Nat. Genet. 27:299-303(2001).
-!- 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. {ECO:0000269|PubMed:10024882,
ECO:0000269|PubMed:15494306, ECO:0000269|PubMed:20797633,
ECO:0000269|PubMed:8413672}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:22678361};
-!- COFACTOR:
Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
Evidence={ECO:0000269|PubMed:22678361};
Note=Binds 1 [4Fe-4S] cluster. {ECO:0000269|PubMed:22678361};
-!- SUBUNIT: 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.
{ECO:0000269|PubMed:19106100, ECO:0000269|PubMed:20797633,
ECO:0000269|PubMed:7724549, ECO:0000269|PubMed:9771713,
ECO:0000269|PubMed:9852112}.
-!- INTERACTION:
P19447:ERCC3; NbExp=4; IntAct=EBI-6380590, EBI-1183307;
Q6P1K8:GTF2H2C_2; NbExp=3; IntAct=EBI-6380590, EBI-8469755;
Q96T76:MMS19; NbExp=7; IntAct=EBI-6380590, EBI-1044169;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20797633}.
Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:20797633}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P18074-1; Sequence=Displayed;
Name=2;
IsoId=P18074-2; Sequence=VSP_043132, VSP_043133, VSP_043134;
Note=No experimental confirmation available.;
-!- PTM: ISGylated. {ECO:0000305|PubMed:16884686}.
-!- 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. {ECO:0000269|PubMed:10447254,
ECO:0000269|PubMed:11709541, ECO:0000269|PubMed:15494306,
ECO:0000269|PubMed:7585650, ECO:0000269|PubMed:7825573,
ECO:0000269|PubMed:7849702, ECO:0000269|PubMed:9101292}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Trichothiodystrophy 1, photosensitive (TTD1)
[MIM:601675]: A form of trichothiodystrophy, an autosomal
recessive disease characterized by sulfur-deficient brittle hair
and multisystem variable abnormalities. The spectrum of clinical
features varies from mild disease with only hair involvement to
severe disease with cutaneous, neurologic and profound
developmental defects. Ichthyosis, intellectual and developmental
disabilities, decreased fertility, abnormal characteristics at
birth, ocular abnormalities, short stature, and infections are
common manifestations. There are both photosensitive and non-
photosensitive forms of the disorder. TTD1 patients manifest
cutaneous photosensitivity. {ECO:0000269|PubMed:11242112,
ECO:0000269|PubMed:7920640, ECO:0000269|PubMed:8571952,
ECO:0000269|PubMed:9195225, ECO:0000269|PubMed:9238033,
ECO:0000269|PubMed:9758621}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: 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.
{ECO:0000269|PubMed:11443545}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the helicase family. RAD3/XPD subfamily.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAM45142.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/XPDID297.html";
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/ercc2/";
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EMBL; X52221; CAA36463.1; -; mRNA.
EMBL; X52222; CAA36464.1; -; mRNA.
EMBL; L47234; AAL48323.1; -; Genomic_DNA.
EMBL; AY092780; AAM45142.1; ALT_SEQ; Genomic_DNA.
EMBL; BT006883; AAP35529.1; -; mRNA.
EMBL; CH471126; EAW57341.1; -; Genomic_DNA.
EMBL; BC108255; AAI08256.1; -; mRNA.
EMBL; BC110523; AAI10524.1; -; mRNA.
CCDS; CCDS33049.1; -. [P18074-1]
CCDS; CCDS46112.1; -. [P18074-2]
PIR; S10888; S10888.
RefSeq; NP_000391.1; NM_000400.3. [P18074-1]
RefSeq; NP_001124339.1; NM_001130867.1. [P18074-2]
UniGene; Hs.487294; -.
PDB; 5IVW; EM; 10.00 A; W=1-760.
PDB; 5IY6; EM; 7.20 A; W=1-760.
PDB; 5IY7; EM; 8.60 A; W=1-760.
PDB; 5IY8; EM; 7.90 A; W=1-760.
PDB; 5IY9; EM; 6.30 A; W=1-760.
PDB; 5OF4; EM; 4.40 A; B=1-760.
PDBsum; 5IVW; -.
PDBsum; 5IY6; -.
PDBsum; 5IY7; -.
PDBsum; 5IY8; -.
PDBsum; 5IY9; -.
PDBsum; 5OF4; -.
ProteinModelPortal; P18074; -.
SMR; P18074; -.
BioGrid; 108380; 35.
CORUM; P18074; -.
DIP; DIP-644N; -.
IntAct; P18074; 45.
MINT; MINT-3008891; -.
STRING; 9606.ENSP00000375809; -.
iPTMnet; P18074; -.
PhosphoSitePlus; P18074; -.
BioMuta; ERCC2; -.
DMDM; 119540; -.
EPD; P18074; -.
MaxQB; P18074; -.
PaxDb; P18074; -.
PeptideAtlas; P18074; -.
PRIDE; P18074; -.
DNASU; 2068; -.
Ensembl; ENST00000391945; ENSP00000375809; ENSG00000104884. [P18074-1]
Ensembl; ENST00000485403; ENSP00000431229; ENSG00000104884. [P18074-2]
GeneID; 2068; -.
KEGG; hsa:2068; -.
UCSC; uc002pbj.3; human. [P18074-1]
CTD; 2068; -.
DisGeNET; 2068; -.
EuPathDB; HostDB:ENSG00000104884.14; -.
GeneCards; ERCC2; -.
GeneReviews; ERCC2; -.
HGNC; HGNC:3434; ERCC2.
HPA; CAB005375; -.
HPA; HPA038057; -.
HPA; HPA069266; -.
MalaCards; ERCC2; -.
MIM; 126340; gene.
MIM; 278730; phenotype.
MIM; 601675; phenotype.
MIM; 610756; phenotype.
neXtProt; NX_P18074; -.
OpenTargets; ENSG00000104884; -.
Orphanet; 1466; COFS syndrome.
Orphanet; 33364; Trichothiodystrophy.
Orphanet; 276258; Xeroderma pigmentosum complementation group D.
PharmGKB; PA27848; -.
eggNOG; KOG1131; Eukaryota.
eggNOG; COG1199; LUCA.
GeneTree; ENSGT00550000075092; -.
HOGENOM; HOG000205390; -.
HOVERGEN; HBG051498; -.
InParanoid; P18074; -.
KO; K10844; -.
OMA; PSVVRNY; -.
OrthoDB; EOG091G0262; -.
PhylomeDB; P18074; -.
TreeFam; TF101232; -.
Reactome; R-HSA-112382; Formation of RNA Pol II elongation complex.
Reactome; R-HSA-113418; Formation of the Early Elongation Complex.
Reactome; R-HSA-167152; Formation of HIV elongation complex in the absence of HIV Tat.
Reactome; R-HSA-167158; Formation of the HIV-1 Early Elongation Complex.
Reactome; R-HSA-167160; RNA Pol II CTD phosphorylation and interaction with CE during HIV infection.
Reactome; R-HSA-167161; HIV Transcription Initiation.
Reactome; R-HSA-167162; RNA Polymerase II HIV Promoter Escape.
Reactome; R-HSA-167172; Transcription of the HIV genome.
Reactome; R-HSA-167200; Formation of HIV-1 elongation complex containing HIV-1 Tat.
Reactome; R-HSA-167246; Tat-mediated elongation of the HIV-1 transcript.
Reactome; R-HSA-2564830; Cytosolic iron-sulfur cluster assembly.
Reactome; R-HSA-427413; NoRC negatively regulates rRNA expression.
Reactome; R-HSA-5696395; Formation of Incision Complex in GG-NER.
Reactome; R-HSA-5696400; Dual Incision in GG-NER.
Reactome; R-HSA-674695; RNA Polymerase II Pre-transcription Events.
Reactome; R-HSA-6781823; Formation of TC-NER Pre-Incision Complex.
Reactome; R-HSA-6781827; Transcription-Coupled Nucleotide Excision Repair (TC-NER).
Reactome; R-HSA-6782135; Dual incision in TC-NER.
Reactome; R-HSA-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
Reactome; R-HSA-6796648; TP53 Regulates Transcription of DNA Repair Genes.
Reactome; R-HSA-72086; mRNA Capping.
Reactome; R-HSA-73762; RNA Polymerase I Transcription Initiation.
Reactome; R-HSA-73772; RNA Polymerase I Promoter Escape.
Reactome; R-HSA-73776; RNA Polymerase II Promoter Escape.
Reactome; R-HSA-73777; RNA Polymerase I Chain Elongation.
Reactome; R-HSA-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
Reactome; R-HSA-73863; RNA Polymerase I Transcription Termination.
Reactome; R-HSA-75953; RNA Polymerase II Transcription Initiation.
Reactome; R-HSA-75955; RNA Polymerase II Transcription Elongation.
Reactome; R-HSA-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance.
Reactome; R-HSA-77075; RNA Pol II CTD phosphorylation and interaction with CE.
SIGNOR; P18074; -.
ChiTaRS; ERCC2; human.
GeneWiki; ERCC2; -.
GenomeRNAi; 2068; -.
PRO; PR:P18074; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000104884; -.
CleanEx; HS_ERCC2; -.
ExpressionAtlas; P18074; baseline and differential.
Genevisible; P18074; HS.
GO; GO:0000439; C:core TFIIH complex; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005675; C:holo TFIIH complex; IDA:UniProtKB.
GO; GO:0071817; C:MMXD complex; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005819; C:spindle; IDA:UniProtKB.
GO; GO:0005669; C:transcription factor TFIID complex; IDA:UniProtKB.
GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
GO; GO:0043139; F:5'-3' DNA helicase activity; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004003; F:ATP-dependent DNA helicase activity; IEA:InterPro.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0008094; F:DNA-dependent ATPase activity; TAS:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
GO; GO:0047485; F:protein N-terminus binding; IPI:UniProtKB.
GO; GO:0006370; P:7-methylguanosine mRNA capping; TAS:Reactome.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0006915; P:apoptotic process; IMP:UniProtKB.
GO; GO:0030282; P:bone mineralization; IEA:Ensembl.
GO; GO:0008283; P:cell proliferation; IEA:Ensembl.
GO; GO:0032289; P:central nervous system myelin formation; IEA:Ensembl.
GO; GO:0007059; P:chromosome segregation; IMP:UniProtKB.
GO; GO:0040016; P:embryonic cleavage; IEA:Ensembl.
GO; GO:0048568; P:embryonic organ development; IEA:Ensembl.
GO; GO:0043249; P:erythrocyte maturation; IEA:Ensembl.
GO; GO:0030198; P:extracellular matrix organization; IEA:Ensembl.
GO; GO:0070911; P:global genome nucleotide-excision repair; TAS:Reactome.
GO; GO:0035315; P:hair cell differentiation; IMP:UniProtKB.
GO; GO:0048820; P:hair follicle maturation; IEA:Ensembl.
GO; GO:0060218; P:hematopoietic stem cell differentiation; IEA:Ensembl.
GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
GO; GO:0035264; P:multicellular organism growth; IEA:Ensembl.
GO; GO:0006289; P:nucleotide-excision repair; IGI:MGI.
GO; GO:0000717; P:nucleotide-excision repair, DNA duplex unwinding; TAS:Reactome.
GO; GO:0033683; P:nucleotide-excision repair, DNA incision; IMP:UniProtKB.
GO; GO:0006295; P:nucleotide-excision repair, DNA incision, 3'-to lesion; TAS:Reactome.
GO; GO:0006296; P:nucleotide-excision repair, DNA incision, 5'-to lesion; TAS:Reactome.
GO; GO:0006294; P:nucleotide-excision repair, preincision complex assembly; TAS:Reactome.
GO; GO:0006293; P:nucleotide-excision repair, preincision complex stabilization; TAS:Reactome.
GO; GO:0043388; P:positive regulation of DNA binding; IEA:Ensembl.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0009791; P:post-embryonic development; IEA:Ensembl.
GO; GO:0006468; P:protein phosphorylation; IEA:GOC.
GO; GO:1901990; P:regulation of mitotic cell cycle phase transition; IMP:UniProtKB.
GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
GO; GO:0006979; P:response to oxidative stress; IMP:UniProtKB.
GO; GO:0021510; P:spinal cord development; IEA:Ensembl.
GO; GO:0006363; P:termination of RNA polymerase I transcription; TAS:Reactome.
GO; GO:0006362; P:transcription elongation from RNA polymerase I promoter; TAS:Reactome.
GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; TAS:Reactome.
GO; GO:0006366; P:transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:0006361; P:transcription initiation from RNA polymerase I promoter; TAS:Reactome.
GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:Reactome.
GO; GO:0006283; P:transcription-coupled nucleotide-excision repair; IDA:UniProtKB.
GO; GO:0009650; P:UV protection; IGI:MGI.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
InterPro; IPR006555; ATP-dep_Helicase_C.
InterPro; IPR010614; DEAD_2.
InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
InterPro; IPR013020; DNA_helicase_DNA-repair_Rad3.
InterPro; IPR010643; HBB.
InterPro; IPR014013; Helic_SF1/SF2_ATP-bd_DinG/Rad3.
InterPro; IPR006554; Helicase-like_DEXD_c2.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR001945; RAD3/XPD.
Pfam; PF06733; DEAD_2; 1.
Pfam; PF06777; HBB; 1.
Pfam; PF13307; Helicase_C_2; 1.
PRINTS; PR00852; XRODRMPGMNTD.
SMART; SM00488; DEXDc2; 1.
SMART; SM00491; HELICc2; 1.
SUPFAM; SSF52540; SSF52540; 4.
TIGRFAMs; TIGR00604; rad3; 1.
PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
PROSITE; PS51193; HELICASE_ATP_BIND_2; 1.
1: Evidence at protein level;
3D-structure; 4Fe-4S; Alternative splicing; ATP-binding; Cataract;
Chromosome partition; Cockayne syndrome; Complete proteome; Cytoplasm;
Cytoskeleton; Deafness; Disease mutation; DNA damage; DNA repair;
DNA-binding; Dwarfism; Helicase; Host-virus interaction; Hydrolase;
Ichthyosis; Iron; Iron-sulfur; Magnesium; Metal-binding;
Nucleotide-binding; Nucleus; Polymorphism; Reference proteome;
Transcription; Transcription regulation; Ubl conjugation;
Xeroderma pigmentosum.
CHAIN 1 760 TFIIH basal transcription factor complex
helicase XPD subunit.
/FTId=PRO_0000101980.
DOMAIN 7 283 Helicase ATP-binding.
{ECO:0000255|PROSITE-ProRule:PRU00541}.
NP_BIND 42 49 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00541}.
REGION 438 637 Mediates interaction with MMS19.
MOTIF 234 237 DEAH box.
MOTIF 682 695 Nuclear localization signal.
{ECO:0000255}.
METAL 116 116 Iron-sulfur (4Fe-4S). {ECO:0000250}.
METAL 134 134 Iron-sulfur (4Fe-4S). {ECO:0000250}.
METAL 155 155 Iron-sulfur (4Fe-4S). {ECO:0000250}.
METAL 190 190 Iron-sulfur (4Fe-4S). {ECO:0000305}.
VAR_SEQ 1 24 Missing (in isoform 2).
{ECO:0000303|Ref.4}.
/FTId=VSP_043132.
VAR_SEQ 414 429 FTIIIEPFDDRTPTIA -> QAQHCGSSRNQKRSHP (in
isoform 2). {ECO:0000303|Ref.4}.
/FTId=VSP_043133.
VAR_SEQ 430 760 Missing (in isoform 2).
{ECO:0000303|Ref.4}.
/FTId=VSP_043134.
VARIANT 47 47 G -> R (in XP-D).
/FTId=VAR_008187.
VARIANT 76 76 T -> A (in XP-D).
/FTId=VAR_017282.
VARIANT 112 112 R -> H (in TTD1 and XP-D;
dbSNP:rs121913020).
{ECO:0000269|PubMed:11709541,
ECO:0000269|PubMed:7920640,
ECO:0000269|PubMed:9758621}.
/FTId=VAR_003622.
VARIANT 199 199 I -> M (in dbSNP:rs1799791).
/FTId=VAR_011412.
VARIANT 201 201 H -> Y (in dbSNP:rs1799792).
/FTId=VAR_011413.
VARIANT 234 234 D -> N (in XP-D).
/FTId=VAR_008188.
VARIANT 259 259 C -> Y (in TTD1; dbSNP:rs370454709).
{ECO:0000269|PubMed:9758621}.
/FTId=VAR_008189.
VARIANT 312 312 D -> N (in dbSNP:rs1799793).
{ECO:0000269|PubMed:11245433,
ECO:0000269|PubMed:11470747,
ECO:0000269|PubMed:11709541,
ECO:0000269|Ref.3}.
/FTId=VAR_011414.
VARIANT 461 461 L -> V (in XP-D and TTD1;
dbSNP:rs121913016).
{ECO:0000269|PubMed:7849702,
ECO:0000269|PubMed:9195225,
ECO:0000269|PubMed:9758621}.
/FTId=VAR_003623.
VARIANT 482 482 Missing (in TTD1).
{ECO:0000269|PubMed:9758621}.
/FTId=VAR_008190.
VARIANT 485 485 L -> P (in XP-D; the corresponding
mutation in fission yeast causes complete
loss of activity; dbSNP:rs121913025).
{ECO:0000269|PubMed:11709541}.
/FTId=VAR_017283.
VARIANT 487 487 R -> G (in TTD1).
/FTId=VAR_017284.
VARIANT 488 493 Missing (in TTD1; mild).
{ECO:0000269|PubMed:7920640}.
/FTId=VAR_003624.
VARIANT 511 511 R -> Q (in XP-D; dbSNP:rs772572683).
/FTId=VAR_017285.
VARIANT 541 541 S -> R (in XP-D; mild;
dbSNP:rs121913019).
{ECO:0000269|PubMed:9101292}.
/FTId=VAR_003625.
VARIANT 542 542 Y -> C (in XP-D).
/FTId=VAR_008191.
VARIANT 582 583 EK -> VSE (in XP-D).
{ECO:0000269|PubMed:11709541}.
/FTId=VAR_017286.
VARIANT 592 592 R -> P (in TTD1).
/FTId=VAR_017287.
VARIANT 594 594 A -> P (in TTD1).
/FTId=VAR_017288.
VARIANT 601 601 R -> L (in XP-D; dbSNP:rs140522180).
/FTId=VAR_008192.
VARIANT 601 601 R -> W (in XP-D; dbSNP:rs753641926).
/FTId=VAR_017289.
VARIANT 602 602 G -> D (in XP-D; combined with features
of Cockayne syndrome; dbSNP:rs771824813).
/FTId=VAR_003627.
VARIANT 616 616 R -> C. {ECO:0000269|PubMed:11319176}.
/FTId=VAR_011415.
VARIANT 616 616 R -> P (in XP-D and TTD1;
dbSNP:rs376556895).
{ECO:0000269|PubMed:7920640}.
/FTId=VAR_003626.
VARIANT 616 616 R -> W (in XP-D and COFS2;
dbSNP:rs121913024).
{ECO:0000269|PubMed:11443545}.
/FTId=VAR_008193.
VARIANT 658 658 R -> C (in TTD1; dbSNP:rs121913021).
{ECO:0000269|PubMed:11242112,
ECO:0000269|PubMed:8571952}.
/FTId=VAR_008194.
VARIANT 658 658 R -> G (in TTD1).
/FTId=VAR_017290.
VARIANT 658 658 R -> H (in TTD1; dbSNP:rs762141272).
/FTId=VAR_008195.
VARIANT 663 663 C -> R (in TTD1; dbSNP:rs770367713).
/FTId=VAR_017291.
VARIANT 666 666 R -> W (in XP-D; dbSNP:rs752510317).
/FTId=VAR_017292.
VARIANT 673 673 D -> G (in TTD1).
{ECO:0000269|PubMed:9758621}.
/FTId=VAR_008196.
VARIANT 675 675 G -> R (in XP-D/CS; severe form).
{ECO:0000269|PubMed:7825573}.
/FTId=VAR_003628.
VARIANT 681 681 D -> N (in XP-D and COFS2;
dbSNP:rs121913023).
{ECO:0000269|PubMed:11443545}.
/FTId=VAR_017293.
VARIANT 683 683 R -> Q (in XP-D).
/FTId=VAR_008197.
VARIANT 683 683 R -> W (in XP-D; 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; dbSNP:rs41556519).
{ECO:0000269|PubMed:15494306}.
/FTId=VAR_008198.
VARIANT 713 713 G -> R (in TTD1; dbSNP:rs121913022).
{ECO:0000269|PubMed:11242112,
ECO:0000269|PubMed:8571952}.
/FTId=VAR_008199.
VARIANT 716 730 Missing (in XP-D and TTD1).
{ECO:0000269|PubMed:9195225}.
/FTId=VAR_003629.
VARIANT 722 722 R -> W (in TTD1; dbSNP:rs121913026).
{ECO:0000269|PubMed:7920640,
ECO:0000269|PubMed:9758621}.
/FTId=VAR_003630.
VARIANT 725 725 A -> P (in TTD1; dbSNP:rs121913018).
{ECO:0000269|PubMed:9195225}.
/FTId=VAR_003631.
VARIANT 751 751 K -> Q (polymorphism; may be associated
with increased susceptibility to DNA
damage; dbSNP:rs13181).
{ECO:0000269|PubMed:11245433,
ECO:0000269|PubMed:11470747,
ECO:0000269|PubMed:11709541,
ECO:0000269|PubMed:15489334,
ECO:0000269|Ref.3, ECO:0000269|Ref.5}.
/FTId=VAR_011416.
MUTAGEN 48 48 K->R: Decreased transcriptional activity
of the reconstituted TFIIH complex.
{ECO:0000269|PubMed:10024882}.
MUTAGEN 190 190 C->S: Reduced iron-sulfur-binding. Iron-
sulfur-binding is further decreased in
absence of MMS19.
{ECO:0000269|PubMed:22678361}.
SEQUENCE 760 AA; 86909 MW; 746C0888CDF2E331 CRC64;
MKLNVDGLLV YFPYDYIYPE QFSYMRELKR TLDAKGHGVL EMPSGTGKTV SLLALIMAYQ
RAYPLEVTKL IYCSRTVPEI EKVIEELRKL LNFYEKQEGE KLPFLGLALS SRKNLCIHPE
VTPLRFGKDV DGKCHSLTAS YVRAQYQHDT SLPHCRFYEE FDAHGREVPL PAGIYNLDDL
KALGRRQGWC PYFLARYSIL HANVVVYSYH YLLDPKIADL VSKELARKAV VVFDEAHNID
NVCIDSMSVN LTRRTLDRCQ GNLETLQKTV LRIKETDEQR LRDEYRRLVE GLREASAARE
TDAHLANPVL PDEVLQEAVP GSIRTAEHFL GFLRRLLEYV KWRLRVQHVV QESPPAFLSG
LAQRVCIQRK PLRFCAERLR SLLHTLEITD LADFSPLTLL ANFATLVSTY AKGFTIIIEP
FDDRTPTIAN PILHFSCMDA SLAIKPVFER FQSVIITSGT LSPLDIYPKI LDFHPVTMAT
FTMTLARVCL CPMIIGRGND QVAISSKFET REDIAVIRNY GNLLLEMSAV VPDGIVAFFT
SYQYMESTVA SWYEQGILEN IQRNKLLFIE TQDGAETSVA LEKYQEACEN GRGAILLSVA
RGKVSEGIDF VHHYGRAVIM FGVPYVYTQS RILKARLEYL RDQFQIREND FLTFDAMRHA
AQCVGRAIRG KTDYGLMVFA DKRFARGDKR GKLPRWIQEH LTDANLNLTV DEGVQVAKYF
LRQMAQPFHR EDQLGLSLLS LEQLESEETL KRIEQIAQQL


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