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Protein

TFIIH basal transcription factor complex helicase XPB subunit

Gene

ERCC3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.2 Publications

Catalytic activityi

ATP + H2O = ADP + phosphate.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi340 – 347ATPPROSITE-ProRule annotation8

GO - Molecular functioni

  • 3'-5' DNA helicase activity Source: UniProtKB
  • ATPase activity Source: UniProtKB
  • ATP binding Source: UniProtKB-KW
  • ATP-dependent DNA helicase activity Source: Ensembl
  • damaged DNA binding Source: UniProtKB
  • dATP binding Source: Ensembl
  • DNA binding Source: UniProtKB
  • GTP binding Source: Ensembl
  • helicase activity Source: Reactome
  • peptide binding Source: Ensembl
  • protein C-terminus binding Source: UniProtKB
  • protein N-terminus binding Source: UniProtKB
  • RNA polymerase II carboxy-terminal domain kinase activity Source: Ensembl
  • transcription factor binding Source: MGI

GO - Biological processi

  • 7-methylguanosine mRNA capping Source: Reactome
  • apoptotic process Source: UniProtKB
  • DNA repair Source: UniProtKB
  • DNA topological change Source: UniProtKB
  • embryonic organ development Source: Ensembl
  • global genome nucleotide-excision repair Source: Reactome
  • hair cell differentiation Source: UniProtKB
  • nucleotide-excision repair Source: UniProtKB
  • nucleotide-excision repair, DNA duplex unwinding Source: UniProtKB
  • nucleotide-excision repair, DNA incision Source: UniProtKB
  • nucleotide-excision repair, DNA incision, 3'-to lesion Source: Reactome
  • nucleotide-excision repair, DNA incision, 5'-to lesion Source: Reactome
  • nucleotide-excision repair, preincision complex assembly Source: Reactome
  • nucleotide-excision repair, preincision complex stabilization Source: Reactome
  • positive regulation of apoptotic process Source: UniProtKB
  • positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • protein localization Source: UniProtKB
  • regulation of mitotic cell cycle phase transition Source: UniProtKB
  • response to hypoxia Source: Ensembl
  • response to oxidative stress Source: UniProtKB
  • response to UV Source: UniProtKB
  • termination of RNA polymerase I transcription Source: Reactome
  • transcription-coupled nucleotide-excision repair Source: UniProtKB
  • transcription elongation from RNA polymerase II promoter Source: Reactome
  • transcription elongation from RNA polymerase I promoter Source: Reactome
  • transcription from RNA polymerase II promoter Source: UniProtKB
  • transcription initiation from RNA polymerase II promoter Source: Reactome
  • transcription initiation from RNA polymerase I promoter Source: Reactome
  • UV protection Source: Ensembl
  • viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase

Keywords - Biological processi

DNA damage, DNA repair, Host-virus interaction, Transcription, Transcription regulation

Keywords - Ligandi

ATP-binding, DNA-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000163161-MONOMER.
ReactomeiR-HSA-112382. Formation of RNA Pol II elongation complex.
R-HSA-113418. Formation of the Early Elongation Complex.
R-HSA-167152. Formation of HIV elongation complex in the absence of HIV Tat.
R-HSA-167158. Formation of the HIV-1 Early Elongation Complex.
R-HSA-167160. RNA Pol II CTD phosphorylation and interaction with CE.
R-HSA-167161. HIV Transcription Initiation.
R-HSA-167162. RNA Polymerase II HIV Promoter Escape.
R-HSA-167172. Transcription of the HIV genome.
R-HSA-167200. Formation of HIV-1 elongation complex containing HIV-1 Tat.
R-HSA-167246. Tat-mediated elongation of the HIV-1 transcript.
R-HSA-427413. NoRC negatively regulates rRNA expression.
R-HSA-5696395. Formation of Incision Complex in GG-NER.
R-HSA-5696400. Dual Incision in GG-NER.
R-HSA-674695. RNA Polymerase II Pre-transcription Events.
R-HSA-6781823. Formation of TC-NER Pre-Incision Complex.
R-HSA-6781827. Transcription-Coupled Nucleotide Excision Repair (TC-NER).
R-HSA-6782135. Dual incision in TC-NER.
R-HSA-6782210. Gap-filling DNA repair synthesis and ligation in TC-NER.
R-HSA-6796648. TP53 Regulates Transcription of DNA Repair Genes.
R-HSA-72086. mRNA Capping.
R-HSA-73762. RNA Polymerase I Transcription Initiation.
R-HSA-73772. RNA Polymerase I Promoter Escape.
R-HSA-73776. RNA Polymerase II Promoter Escape.
R-HSA-73777. RNA Polymerase I Chain Elongation.
R-HSA-73779. RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
R-HSA-73863. RNA Polymerase I Transcription Termination.
R-HSA-75953. RNA Polymerase II Transcription Initiation.
R-HSA-75955. RNA Polymerase II Transcription Elongation.
R-HSA-76042. RNA Polymerase II Transcription Initiation And Promoter Clearance.
R-HSA-77075. RNA Pol II CTD phosphorylation and interaction with CE.
SIGNORiP19447.

Names & Taxonomyi

Protein namesi
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 namesi
Name:ERCC3
Synonyms:XPB, XPBC
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:3435. ERCC3.

Subcellular locationi

GO - Cellular componenti

  • core TFIIH complex Source: Ensembl
  • holo TFIIH complex Source: UniProtKB
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
  • transcription factor TFIID complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

Xeroderma pigmentosum complementation group B (XP-B)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn 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.
See also OMIM:610651
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_00363299F → S in XP-B; combined with features of Cockayne syndrome; mild. 2 PublicationsCorresponds to variant rs121913045dbSNPEnsembl.1
Trichothiodystrophy 2, photosensitive (TTD2)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:616390
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_008186119T → P in TTD2; mild. 1 PublicationCorresponds to variant rs121913046dbSNPEnsembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi346K → R: No transcriptional activity of the reconstituted TFIIH complex. 1 Publication1
Mutagenesisi782Missing : Impairs protein folding. 1 Publication1

Keywords - Diseasei

Cockayne syndrome, Deafness, Disease mutation, Dwarfism, Ichthyosis, Xeroderma pigmentosum

Organism-specific databases

DisGeNETi2071.
MalaCardsiERCC3.
MIMi610651. phenotype.
616390. phenotype.
OpenTargetsiENSG00000163161.
Orphaneti33364. Trichothiodystrophy.
276252. Xeroderma pigmentosum complementation group B.
PharmGKBiPA27849.

Polymorphism and mutation databases

BioMutaiERCC3.
DMDMi119541.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001019871 – 782TFIIH basal transcription factor complex helicase XPB subunitAdd BLAST782

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei686PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiP19447.
MaxQBiP19447.
PaxDbiP19447.
PeptideAtlasiP19447.
PRIDEiP19447.

PTM databases

iPTMnetiP19447.
PhosphoSitePlusiP19447.

Expressioni

Gene expression databases

BgeeiENSG00000163161.
CleanExiHS_ERCC3.
ExpressionAtlasiP19447. baseline and differential.
GenevisibleiP19447. HS.

Organism-specific databases

HPAiCAB037153.
HPA046077.
HPA064560.

Interactioni

Subunit structurei

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 EBNA2.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CEP70Q8NHQ13EBI-1183307,EBI-739624
KPNA3O005053EBI-1183307,EBI-358297
PSMC5P621954EBI-1183307,EBI-357745
Psmc5P621966EBI-1183307,EBI-357713From a different organism.
RAD23BP547272EBI-1183307,EBI-954531
XIAPP981703EBI-1183307,EBI-517127
XPCQ018312EBI-1183307,EBI-372610

GO - Molecular functioni

  • protein C-terminus binding Source: UniProtKB
  • protein N-terminus binding Source: UniProtKB
  • transcription factor binding Source: MGI

Protein-protein interaction databases

BioGridi108383. 58 interactors.
DIPiDIP-83N.
IntActiP19447. 32 interactors.
MINTiMINT-3009064.
STRINGi9606.ENSP00000285398.

Structurei

Secondary structure

1782
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi505 – 512Combined sources8
Helixi516 – 524Combined sources9
Helixi528 – 530Combined sources3
Helixi531 – 536Combined sources6
Helixi538 – 552Combined sources15
Turni553 – 555Combined sources3
Beta strandi558 – 561Combined sources4
Helixi565 – 574Combined sources10
Helixi586 – 598Combined sources13
Beta strandi604 – 607Combined sources4
Helixi609 – 611Combined sources3
Turni612 – 614Combined sources3
Beta strandi620 – 626Combined sources7
Helixi633 – 643Combined sources11
Beta strandi651 – 654Combined sources4
Beta strandi656 – 664Combined sources9
Helixi668 – 670Combined sources3
Helixi671 – 682Combined sources12
Beta strandi686 – 692Combined sources7
Helixi696 – 698Combined sources3
Helixi706 – 718Combined sources13
Helixi721 – 724Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4ERNX-ray1.80A494-782[»]
5IVWelectron microscopy10.00V1-782[»]
5IY6electron microscopy7.20V1-782[»]
5IY7electron microscopy8.60V1-782[»]
5IY8electron microscopy7.90V1-782[»]
5IY9electron microscopy6.30V1-782[»]
ProteinModelPortaliP19447.
SMRiP19447.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini327 – 488Helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST162
Domaini542 – 702Helicase C-terminalPROSITE-ProRule annotationAdd BLAST161

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi6 – 18Nuclear localization signalSequence analysisAdd BLAST13
Motifi441 – 444DEVH box4

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi20 – 28Asp/Glu-rich (acidic)9
Compositional biasi256 – 265Asp/Glu-rich (acidic)10
Compositional biasi697 – 700Asp/Glu-rich (acidic)4
Compositional biasi721 – 728Asp/Glu-rich (acidic)8

Sequence similaritiesi

Belongs to the helicase family. RAD25/XPB subfamily.Curated
Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation
Contains 1 helicase C-terminal domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG1123. Eukaryota.
COG1061. LUCA.
GeneTreeiENSGT00390000002204.
HOGENOMiHOG000160172.
HOVERGENiHBG051499.
InParanoidiP19447.
KOiK10843.
OMAiEANWIEL.
OrthoDBiEOG091G0291.
PhylomeDBiP19447.
TreeFamiTF101233.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR032438. ERCC3_RAD25_C.
IPR006935. Helicase/UvrB_N.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR001161. XPB/Ssl2.
IPR032830. XPB/Ssl2_N.
[Graphical view]
PfamiPF16203. ERCC3_RAD25_C. 1 hit.
PF13625. Helicase_C_3. 1 hit.
PF04851. ResIII. 1 hit.
[Graphical view]
SMARTiSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 3 hits.
TIGRFAMsiTIGR00603. rad25. 1 hit.
PROSITEiPS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P19447-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGKRDRADRD KKKSRKRHYE DEEDDEEDAP GNDPQEAVPS AAGKQVDESG
60 70 80 90 100
TKVDEYGAKD YRLQMPLKDD HTSRPLWVAP DGHIFLEAFS PVYKYAQDFL
110 120 130 140 150
VAIAEPVCRP THVHEYKLTA YSLYAAVSVG LQTSDITEYL RKLSKTGVPD
160 170 180 190 200
GIMQFIKLCT VSYGKVKLVL KHNRYFVESC HPDVIQHLLQ DPVIRECRLR
210 220 230 240 250
NSEGEATELI TETFTSKSAI SKTAESSGGP STSRVTDPQG KSDIPMDLFD
260 270 280 290 300
FYEQMDKDEE EEEETQTVSF EVKQEMIEEL QKRCIHLEYP LLAEYDFRND
310 320 330 340 350
SVNPDINIDL KPTAVLRPYQ EKSLRKMFGN GRARSGVIVL PCGAGKSLVG
360 370 380 390 400
VTAACTVRKR CLVLGNSAVS VEQWKAQFKM WSTIDDSQIC RFTSDAKDKP
410 420 430 440 450
IGCSVAISTY SMLGHTTKRS WEAERVMEWL KTQEWGLMIL DEVHTIPAKM
460 470 480 490 500
FRRVLTIVQA HCKLGLTATL VREDDKIVDL NFLIGPKLYE ANWMELQNNG
510 520 530 540 550
YIAKVQCAEV WCPMSPEFYR EYVAIKTKKR ILLYTMNPNK FRACQFLIKF
560 570 580 590 600
HERRNDKIIV FADNVFALKE YAIRLNKPYI YGPTSQGERM QILQNFKHNP
610 620 630 640 650
KINTIFISKV GDTSFDLPEA NVLIQISSHG GSRRQEAQRL GRVLRAKKGM
660 670 680 690 700
VAEEYNAFFY SLVSQDTQEM AYSTKRQRFL VDQGYSFKVI TKLAGMEEED
710 720 730 740 750
LAFSTKEEQQ QLLQKVLAAT DLDAEEEVVA GEFGSRSSQA SRRFGTMSSM
760 770 780
SGADDTVYME YHSSRSKAPS KHVHPLFKRF RK
Length:782
Mass (Da):89,278
Last modified:February 1, 1991 - v1
Checksum:iF5F4D3A89A7DF826
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_00363299F → S in XP-B; combined with features of Cockayne syndrome; mild. 2 PublicationsCorresponds to variant rs121913045dbSNPEnsembl.1
Natural variantiVAR_014766117K → R.1 PublicationCorresponds to variant rs1805161dbSNPEnsembl.1
Natural variantiVAR_008186119T → P in TTD2; mild. 1 PublicationCorresponds to variant rs121913046dbSNPEnsembl.1
Natural variantiVAR_014767402G → C.1 PublicationCorresponds to variant rs1805162dbSNPEnsembl.1
Natural variantiVAR_035942418K → Q in a breast cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_017294704S → L.1 PublicationCorresponds to variant rs4150521dbSNPEnsembl.1
Natural variantiVAR_014344735S → P.1 PublicationCorresponds to variant rs4150522dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS2144.1.
PIRiA35661.
RefSeqiNP_000113.1. NM_000122.1.
UniGeneiHs.469872.

Genome annotation databases

EnsembliENST00000285398; ENSP00000285398; ENSG00000163161.
GeneIDi2071.
KEGGihsa:2071.
UCSCiuc002toh.1. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Allelic variations of the XP genes
Atlas of Genetics and Cytogenetics in Oncology and Haematology
NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS2144.1.
PIRiA35661.
RefSeqiNP_000113.1. NM_000122.1.
UniGeneiHs.469872.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4ERNX-ray1.80A494-782[»]
5IVWelectron microscopy10.00V1-782[»]
5IY6electron microscopy7.20V1-782[»]
5IY7electron microscopy8.60V1-782[»]
5IY8electron microscopy7.90V1-782[»]
5IY9electron microscopy6.30V1-782[»]
ProteinModelPortaliP19447.
SMRiP19447.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108383. 58 interactors.
DIPiDIP-83N.
IntActiP19447. 32 interactors.
MINTiMINT-3009064.
STRINGi9606.ENSP00000285398.

PTM databases

iPTMnetiP19447.
PhosphoSitePlusiP19447.

Polymorphism and mutation databases

BioMutaiERCC3.
DMDMi119541.

Proteomic databases

EPDiP19447.
MaxQBiP19447.
PaxDbiP19447.
PeptideAtlasiP19447.
PRIDEiP19447.

Protocols and materials databases

DNASUi2071.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000285398; ENSP00000285398; ENSG00000163161.
GeneIDi2071.
KEGGihsa:2071.
UCSCiuc002toh.1. human.

Organism-specific databases

CTDi2071.
DisGeNETi2071.
GeneCardsiERCC3.
GeneReviewsiERCC3.
HGNCiHGNC:3435. ERCC3.
HPAiCAB037153.
HPA046077.
HPA064560.
MalaCardsiERCC3.
MIMi133510. gene.
610651. phenotype.
616390. phenotype.
neXtProtiNX_P19447.
OpenTargetsiENSG00000163161.
Orphaneti33364. Trichothiodystrophy.
276252. Xeroderma pigmentosum complementation group B.
PharmGKBiPA27849.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1123. Eukaryota.
COG1061. LUCA.
GeneTreeiENSGT00390000002204.
HOGENOMiHOG000160172.
HOVERGENiHBG051499.
InParanoidiP19447.
KOiK10843.
OMAiEANWIEL.
OrthoDBiEOG091G0291.
PhylomeDBiP19447.
TreeFamiTF101233.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000163161-MONOMER.
ReactomeiR-HSA-112382. Formation of RNA Pol II elongation complex.
R-HSA-113418. Formation of the Early Elongation Complex.
R-HSA-167152. Formation of HIV elongation complex in the absence of HIV Tat.
R-HSA-167158. Formation of the HIV-1 Early Elongation Complex.
R-HSA-167160. RNA Pol II CTD phosphorylation and interaction with CE.
R-HSA-167161. HIV Transcription Initiation.
R-HSA-167162. RNA Polymerase II HIV Promoter Escape.
R-HSA-167172. Transcription of the HIV genome.
R-HSA-167200. Formation of HIV-1 elongation complex containing HIV-1 Tat.
R-HSA-167246. Tat-mediated elongation of the HIV-1 transcript.
R-HSA-427413. NoRC negatively regulates rRNA expression.
R-HSA-5696395. Formation of Incision Complex in GG-NER.
R-HSA-5696400. Dual Incision in GG-NER.
R-HSA-674695. RNA Polymerase II Pre-transcription Events.
R-HSA-6781823. Formation of TC-NER Pre-Incision Complex.
R-HSA-6781827. Transcription-Coupled Nucleotide Excision Repair (TC-NER).
R-HSA-6782135. Dual incision in TC-NER.
R-HSA-6782210. Gap-filling DNA repair synthesis and ligation in TC-NER.
R-HSA-6796648. TP53 Regulates Transcription of DNA Repair Genes.
R-HSA-72086. mRNA Capping.
R-HSA-73762. RNA Polymerase I Transcription Initiation.
R-HSA-73772. RNA Polymerase I Promoter Escape.
R-HSA-73776. RNA Polymerase II Promoter Escape.
R-HSA-73777. RNA Polymerase I Chain Elongation.
R-HSA-73779. RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
R-HSA-73863. RNA Polymerase I Transcription Termination.
R-HSA-75953. RNA Polymerase II Transcription Initiation.
R-HSA-75955. RNA Polymerase II Transcription Elongation.
R-HSA-76042. RNA Polymerase II Transcription Initiation And Promoter Clearance.
R-HSA-77075. RNA Pol II CTD phosphorylation and interaction with CE.
SIGNORiP19447.

Miscellaneous databases

ChiTaRSiERCC3. human.
GeneWikiiXPB.
GenomeRNAii2071.
PROiP19447.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000163161.
CleanExiHS_ERCC3.
ExpressionAtlasiP19447. baseline and differential.
GenevisibleiP19447. HS.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR032438. ERCC3_RAD25_C.
IPR006935. Helicase/UvrB_N.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR001161. XPB/Ssl2.
IPR032830. XPB/Ssl2_N.
[Graphical view]
PfamiPF16203. ERCC3_RAD25_C. 1 hit.
PF13625. Helicase_C_3. 1 hit.
PF04851. ResIII. 1 hit.
[Graphical view]
SMARTiSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 3 hits.
TIGRFAMsiTIGR00603. rad25. 1 hit.
PROSITEiPS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiERCC3_HUMAN
AccessioniPrimary (citable) accession number: P19447
Secondary accession number(s): Q53QM0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: November 30, 2016
This is version 196 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.