P19447 (ERCC3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
TFIIH basal transcription factor complex helicase XPB subunit
EC=3.6.4.12

Alternative name(s):
Basic transcription factor 2 89 kDa subunit
Short name=BTF2 p89
DNA excision repair protein ERCC-3
DNA repair protein complementing XP-B cells
TFIIH basal transcription factor complex 89 kDa subunit
Short name=TFIIH 89 kDa subunit
Short name=TFIIH p89
Xeroderma pigmentosum group B-complementing protein

Gene names

Name:	ERCC3
Synonyms:	XPB, XPBC

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	782 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	ATP-dependent 3'-5' DNA helicase, component of the core-TFIIH basal transcription factor, involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. Acts by opening DNA either around the RNA transcription start site or the DNA damage. Ref.11
Catalytic activity	ATP + H2O = ADP + phosphate.
Subunit structure	One of the 6 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. Interacts with PUF60. Interacts with ATF7IP. Interacts with Epstein-Barr virus EBNA2. Ref.9 Ref.10 Ref.12 Ref.13 Ref.15
Subcellular location	Nucleus.
Involvement in disease	Xeroderma pigmentosum complementation group B (XP-B) [MIM:610651]: 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-B 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.17 Ref.20 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.18
Sequence similarities	Belongs to the helicase family. RAD25/XPB subfamily. Contains 1 helicase ATP-binding domain. Contains 1 helicase C-terminal domain.

Ontologies

Keywords
Biological process	DNA damage DNA repair Host-virus interaction Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Polymorphism
Disease	Cockayne syndrome Deafness Disease mutation Dwarfism Ichthyosis Xeroderma pigmentosum
Ligand	ATP-binding DNA-binding Nucleotide-binding
Molecular function	Helicase Hydrolase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	7-methylguanosine mRNA capping Traceable author statement. Source: Reactome DNA topological change Inferred from mutant phenotype PubMed 8663148. Source: UniProtKB UV protection Inferred from electronic annotation. Source: Compara cell cycle checkpoint Inferred from mutant phenotype PubMed 17088560. Source: UniProtKB hair cell differentiation Inferred from mutant phenotype PubMed 11335038. Source: UniProtKB induction of apoptosis Inferred from direct assay PubMed 16914395. Source: UniProtKB nucleotide-excision repair, DNA damage removal Traceable author statement. Source: Reactome nucleotide-excision repair, DNA duplex unwinding Inferred from mutant phenotype PubMed 17466626. Source: UniProtKB nucleotide-excision repair, DNA incision Inferred from mutant phenotype PubMed 17466626PubMed 8692841. Source: UniProtKB positive regulation of transcription from RNA polymerase II promoter Inferred from direct assay PubMed 8692841. Source: UniProtKB positive regulation of viral transcription Traceable author statement. Source: Reactome protein localization Inferred from mutant phenotype PubMed 17509950. Source: UniProtKB protein phosphorylation Inferred from electronic annotation. Source: Compara response to UV Inferred from mutant phenotype PubMed 17509950. Source: UniProtKB response to hypoxia Inferred from electronic annotation. Source: Compara response to oxidative stress Inferred from mutant phenotype PubMed 17614221. Source: UniProtKB 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 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 reproduction Traceable author statement. Source: Reactome virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	core TFIIH complex Inferred from electronic annotation. Source: InterPro holo TFIIH complex Inferred from direct assay PubMed 8692842Ref.10. Source: UniProtKB
Molecular_function	3'-5' DNA helicase activity Inferred from direct assay PubMed 17466626. Source: UniProtKB ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATP-dependent DNA helicase activity Inferred from electronic annotation. Source: Compara ATPase activity Inferred from direct assay PubMed 17466626. Source: UniProtKB GTP binding Inferred from electronic annotation. Source: Compara dATP binding Inferred from electronic annotation. Source: Compara damaged DNA binding Non-traceable author statement Ref.2. Source: UniProtKB peptide binding Inferred from electronic annotation. Source: Compara transcription factor binding Inferred from direct assay PubMed 9173976. Source: MGI
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PSMC5	P62195	4	EBI-1183307,EBI-357745
Psmc5	P62196	6	EBI-1183307,EBI-357713	From a different organism.
RAD23B	P54727	2	EBI-1183307,EBI-954531
XPC	Q01831	2	EBI-1183307,EBI-372610

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 782

782

TFIIH basal transcription factor complex helicase XPB subunit

PRO_0000101987

Regions

Domain

327 – 488

162

Helicase ATP-binding

Domain

542 – 702

161

Helicase C-terminal

Nucleotide binding

340 – 347

8

ATP By similarity

Motif

6 – 18

13

Nuclear localization signal Potential

Motif

441 – 444

4

DEVH box

Compositional bias

20 – 28

9

Asp/Glu-rich (acidic)

Compositional bias

256 – 265

10

Asp/Glu-rich (acidic)

Compositional bias

697 – 700

4

Asp/Glu-rich (acidic)

Compositional bias

721 – 728

8

Asp/Glu-rich (acidic)

Natural variations

Natural variant

99

1

F → S in XP-B; combined with features of Cockayne syndrome; mild. Ref.17 Ref.20

VAR_003632

Natural variant

117

1

K → R. Ref.19
Corresponds to variant rs1805161 [ dbSNP | Ensembl ].

VAR_014766

Natural variant

119

1

T → P in TTDP; mild. Ref.18

VAR_008186

Natural variant

402

1

G → C. Ref.19
Corresponds to variant rs1805162 [ dbSNP | Ensembl ].

VAR_014767

Natural variant

418

1

K → Q in a breast cancer sample; somatic mutation. Ref.21

VAR_035942

Natural variant

704

1

S → L. Ref.4
Corresponds to variant rs4150521 [ dbSNP | Ensembl ].

VAR_017294

Natural variant

735

1

S → P. Ref.4
Corresponds to variant rs4150522 [ dbSNP | Ensembl ].

VAR_014344

Experimental info

Mutagenesis

346

1

K → R: No transcriptional activity of the reconstituted TFIIH complex. Ref.11

Mutagenesis

782

1

Missing: Impairs protein folding. Ref.16

Secondary structure

1

.

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782

Helix Strand Turn

Details...

Beta strand

505 – 512

8

Helix

516 – 524

9

Helix

528 – 530

3

Helix

531 – 536

6

Helix

538 – 552

15

Turn

553 – 555

3

Beta strand

558 – 561

4

Helix

565 – 574

10

Helix

586 – 598

13

Beta strand

604 – 607

4

Helix

609 – 611

3

Turn

612 – 614

3

Beta strand

620 – 626

7

Helix

633 – 643

11

Beta strand

651 – 654

4

Beta strand

656 – 664

9

Helix

668 – 670

3

Helix

671 – 682

12

Beta strand

686 – 692

7

Helix

696 – 698

3

Helix

706 – 718

13

Helix

721 – 724

4

Sequences

	Sequence		Length	Mass (Da)
	P19447 [UniParc]. Last modified February 1, 1991. Version 1. Checksum: F5F4D3A89A7DF826	FASTA	782	89,278
	10 20 30 40 50 60 MGKRDRADRD KKKSRKRHYE DEEDDEEDAP GNDPQEAVPS AAGKQVDESG TKVDEYGAKD 70 80 90 100 110 120 YRLQMPLKDD HTSRPLWVAP DGHIFLEAFS PVYKYAQDFL VAIAEPVCRP THVHEYKLTA 130 140 150 160 170 180 YSLYAAVSVG LQTSDITEYL RKLSKTGVPD GIMQFIKLCT VSYGKVKLVL KHNRYFVESC 190 200 210 220 230 240 HPDVIQHLLQ DPVIRECRLR NSEGEATELI TETFTSKSAI SKTAESSGGP STSRVTDPQG 250 260 270 280 290 300 KSDIPMDLFD FYEQMDKDEE EEEETQTVSF EVKQEMIEEL QKRCIHLEYP LLAEYDFRND 310 320 330 340 350 360 SVNPDINIDL KPTAVLRPYQ EKSLRKMFGN GRARSGVIVL PCGAGKSLVG VTAACTVRKR 370 380 390 400 410 420 CLVLGNSAVS VEQWKAQFKM WSTIDDSQIC RFTSDAKDKP IGCSVAISTY SMLGHTTKRS 430 440 450 460 470 480 WEAERVMEWL KTQEWGLMIL DEVHTIPAKM FRRVLTIVQA HCKLGLTATL VREDDKIVDL 490 500 510 520 530 540 NFLIGPKLYE ANWMELQNNG YIAKVQCAEV WCPMSPEFYR EYVAIKTKKR ILLYTMNPNK 550 560 570 580 590 600 FRACQFLIKF HERRNDKIIV FADNVFALKE YAIRLNKPYI YGPTSQGERM QILQNFKHNP 610 620 630 640 650 660 KINTIFISKV GDTSFDLPEA NVLIQISSHG GSRRQEAQRL GRVLRAKKGM VAEEYNAFFY 670 680 690 700 710 720 SLVSQDTQEM AYSTKRQRFL VDQGYSFKVI TKLAGMEEED LAFSTKEEQQ QLLQKVLAAT 730 740 750 760 770 780 DLDAEEEVVA GEFGSRSSQA SRRFGTMSSM SGADDTVYME YHSSRSKAPS KHVHPLFKRF RK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and biological characterization of the human excision repair gene ERCC-3." Weeda G., van Ham R.C.A., Masurel R., Westerveld A., Odijk H., de Wit J., Bootsma D., van der Eb A.J., Hoeijmakers J.H.J. Mol. Cell. Biol. 10:2570-2581(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"A presumed DNA helicase encoded by ERCC-3 is involved in the human repair disorders Xeroderma pigmentosum and Cockayne's syndrome." Weeda G., van Ham R.C.A., Vermeulen W., Bootsma D., van der Eb A.J., Hoeijmakers J.H.J. Cell 62:777-791(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Structure and expression of the human XPBC/ERCC-3 gene involved in DNA repair disorders xeroderma pigmentosum and Cockayne's syndrome." Weeda G., Ma L., van Ham R.C.A., van der Eb A.J., Hoeijmakers J.H.J. Nucleic Acids Res. 19:6301-6308(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	NIEHS SNPs program Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS LEU-704 AND PRO-735.
[5]	"Generation and annotation of the DNA sequences of human chromosomes 2 and 4." Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K. Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	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 Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"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]. Tissue: Placenta.
[8]	"Correction of xeroderma pigmentosum repair defect by basal transcription factor BTF2 (TFIIH)." van Vuuren A.J., Vermeulen W., Ma L., Weeda G., Appeldoorn E., Jaspers N.G.J., van der Eb A.J., Bootsma D., Hoeijmakers J.H.J., Humbert S., Schaeffer L., Egly J.-M. EMBO J. 13:1645-1653(1994) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN TRANSCRIPTION.
[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]	"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-346, FUNCTION.
[12]	"The FBP interacting repressor targets TFIIH to inhibit activated transcription." Liu J., He L., Collins I., Ge H., Libutti D., Li J., Egly J.-M., Levens D. Mol. Cell 5:331-341(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PUF60.
[13]	"Defective interplay of activators and repressors with TFIH in xeroderma pigmentosum." Liu J., Akoulitchev S., Weber A., Ge H., Chuikov S., Libutti D., Wang X.W., Conaway J.W., Harris C.C., Conaway R.C., Reinberg D., Levens D. Cell 104:353-363(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PUF60.
[14]	"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-B.
[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]	"Structure of the C-terminal half of human XPB helicase and the impact of the disease-causing mutation XP11BE." Hilario E., Li Y., Nobumori Y., Liu X., Fan L. Acta Crystallogr. D 69:237-246(2013) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 494-782, MUTAGENESIS OF LYS-782.
[17]	"Clinical heterogeneity within xeroderma pigmentosum associated with mutations in the DNA repair and transcription gene ERCC3." Vermeulen W., Scott R.J., Rodgers S., Mueller H.J., Cole J., Arlett C.F., Kleijer W.J., Bootsma D., Hoeijmakers J.H.J., Weeda G. Am. J. Hum. Genet. 54:191-200(1994) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT XP-B SER-99.
[18]	"A mutation in the XPB/ERCC3 DNA repair transcription gene, associated with trichothiodystrophy." Weeda G., Eveno E., Donker I., Vermeulen W., Chevallier-Lagente O., Taieb A., Stary A., Hoeijmakers J.H.J., Mezzina M., Sarasin A. Am. J. Hum. Genet. 60:320-329(1997) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT TTDP PRO-119.
[19]	"Identification of four single nucleotide polymorphisms in DNA repair genes: XPA and XPB (ERCC3) in Polish population." Butkiewicz D., Rusin M., Harris C.C., Chorazy M. Hum. Mutat. 15:577-578(2000) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS ARG-117 AND CYS-402.
[20]	"Phenotypic heterogeneity in the XPB DNA helicase gene (ERCC3): xeroderma pigmentosum without and with Cockayne syndrome." Oh K.-S., Khan S.G., Jaspers N.G.J., Raams A., Ueda T., Lehmann A., Friedmann P.S., Emmert S., Gratchev A., Lachlan K., Lucassan A., Baker C.C., Kraemer K.H. Hum. Mutat. 27:1092-1103(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT XP-B SER-99.
[21]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] GLN-418.
+	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

EMBL
GenBank
DDBJ

M31899 mRNA. Translation: AAA52396.1.
AY163769 Genomic DNA. Translation: AAN46739.1.
AC110926 Genomic DNA. Translation: AAY15069.1.
CH471103 Genomic DNA. Translation: EAW95313.1.
BC008820 mRNA. Translation: AAH08820.1.

IPI

IPI00747053.

PIR

A35661.

RefSeq

NP_000113.1. NM_000122.1.

UniGene

Hs.469872.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
4ERN	X-ray	1.80	A	494-782	[»]

ProteinModelPortal

P19447.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-83N.

IntAct

P19447. 11 interactions.

STRING

9606.ENSP00000285398.

PTM databases

PhosphoSite

P19447.

Polymorphism databases

DMDM

119541.

Proteomic databases

PaxDb

P19447.

PRIDE

P19447.

Protocols and materials databases

DNASU

2071.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000285398; ENSP00000285398; ENSG00000163161.

GeneID

2071.

KEGG

hsa:2071.

UCSC

uc002toe.1. human.

Organism-specific databases

CTD

2071.

GeneCards

GC02M128014.

HGNC

HGNC:3435. ERCC3.

HPA

CAB037153.

MIM

133510. gene.
601675. phenotype.
610651. phenotype.

neXtProt

NX_P19447.

Orphanet

453. IBIDS syndrome.
670. PIBIDS syndrome.
276252. Xeroderma pigmentosum complementation group B.
220295. Xeroderma pigmentosum/Cockayne syndrome complex.

PharmGKB

PA27849.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG1061.

HOGENOM

HOG000160172.

HOVERGEN

HBG051499.

InParanoid

P19447.

KO

K10843.

OMA

SRVTDPQ.

OrthoDB

EOG4KD6KG.

PhylomeDB

P19447.

Enzyme and pathway databases

Reactome

REACT_116125. Disease.
REACT_1675. mRNA Processing.
REACT_1788. Transcription.
REACT_216. DNA Repair.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpress

P19447.

Bgee

P19447.

CleanEx

HS_ERCC3.

Genevestigator

P19447.

GermOnline

ENSG00000163161. Homo sapiens.

Family and domain databases

InterPro

IPR006935. Helicase/UvrB_dom.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR001161. Helicase_Ercc3.
[Graphical view]

Pfam

PF00271. Helicase_C. 1 hit.
PF04851. ResIII. 1 hit.
[Graphical view]

PRINTS

PR00851. XRODRMPGMNTB.

SMART

SM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00603. rad25. 1 hit.

PROSITE

PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

ERCC3. human.

GenomeRNAi

2071.

NextBio

8425.

SOURCE

Search...

Entry information

Entry name

ERCC3_HUMAN

Accession

Primary (citable) accession number: P19447
Secondary accession number(s): Q53QM0

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	February 1, 1991
Last modified:	May 1, 2013
This is version 157 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.