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P49135 (ERCC3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 127. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 89 kDa subunit
Xeroderma pigmentosum group B-complementing protein
Gene names
Name:Ercc3
Synonyms:Xpb, Xpbc
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length783 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript 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.

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 By similarity. Interacts with ATF7IP By similarity.

Subcellular location

Nucleus.

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 processDNA damage
DNA repair
Transcription
Transcription regulation
   Cellular componentNucleus
   LigandATP-binding
DNA-binding
Nucleotide-binding
   Molecular functionHelicase
Hydrolase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA topological change

Inferred from sequence or structural similarity. Source: UniProtKB

UV protection

Inferred from genetic interaction Ref.1. Source: MGI

apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

hair cell differentiation

Inferred from electronic annotation. Source: Ensembl

nucleotide-excision repair, DNA duplex unwinding

Inferred from electronic annotation. Source: Ensembl

nucleotide-excision repair, DNA incision

Inferred from electronic annotation. Source: Ensembl

positive regulation of apoptotic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

protein localization

Inferred from electronic annotation. Source: Ensembl

regulation of mitotic cell cycle phase transition

Inferred from electronic annotation. Source: Ensembl

response to hypoxia

Inferred from electronic annotation. Source: Ensembl

response to oxidative stress

Inferred from electronic annotation. Source: Ensembl

transcription from RNA polymerase II promoter

Inferred from sequence or structural similarity. Source: UniProtKB

transcription-coupled nucleotide-excision repair

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentholo TFIIH complex

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_function3'-5' DNA helicase activity

Inferred from sequence or structural similarity. Source: UniProtKB

ATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ATP-dependent DNA helicase activity

Inferred from electronic annotation. Source: Ensembl

DNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

GTP binding

Inferred from electronic annotation. Source: Ensembl

RNA polymerase II carboxy-terminal domain kinase activity

Inferred from electronic annotation. Source: Ensembl

dATP binding

Inferred from electronic annotation. Source: Ensembl

peptide binding

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 783783TFIIH basal transcription factor complex helicase XPB subunit
PRO_0000101989

Regions

Domain328 – 489162Helicase ATP-binding
Domain543 – 703161Helicase C-terminal
Nucleotide binding341 – 3488ATP By similarity
Motif6 – 1813Nuclear localization signal Potential
Motif442 – 4454DEVH box
Compositional bias20 – 289Asp/Glu-rich (acidic)
Compositional bias257 – 26610Asp/Glu-rich (acidic)
Compositional bias698 – 7014Asp/Glu-rich (acidic)
Compositional bias722 – 7298Asp/Glu-rich (acidic)

Sequences

Sequence LengthMass (Da)Tools
P49135 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: 6D204EF6A831D8AF

FASTA78389,126
        10         20         30         40         50         60 
MGKRDRVDRD KKKSKKRQYE EEEEDEDDIP GNESQEAVPS AAGKQVDESS TKVDEYGAKD 

        70         80         90        100        110        120 
YRQQMPLKGD HTSRPLWVAP DGHIFLEAFS PVYKYAQDFL VAIAEPVCRP THVHEYKLTA 

       130        140        150        160        170        180 
YSLYAAVSVG LQTSDITEYL RKLSKTGVPD GIIQFIKLCT VSYGKVKLVL KHNRYFVESS 

       190        200        210        220        230        240 
HPDVIQHLLQ DPVIRECRLR NAEGEATELI TETFTSKSAI SKTAAEGSGG PSTSQGVDAQ 

       250        260        270        280        290        300 
ATSDIPKDLF DFYEQMDKDE EEEEETQTVS FEVKQEMIEE LQKRCICLEY PLLAEYDFRN 

       310        320        330        340        350        360 
DTLNPDINID LKPTAVLRPY QEKSLRKMFG NGRARSGVIV LPCGAGKSLV GVTAACTVRK 

       370        380        390        400        410        420 
RCLVLGNSAV SVEQWKAQFK MWSTIDDSQI CRFTSDAKDK PIGCSVAIST YSMLGHTTKR 

       430        440        450        460        470        480 
SWEAERVMEW LKTQEWGLMI LDEVHTIPAR MFRRVLTIVQ AHCKLGLTAT LVREDDKIVD 

       490        500        510        520        530        540 
LNFLIGPKLY EANWMELQNN GYIAKVQCAE VWCPMSPEFY REYVAIKTKK RILLYTMNPN 

       550        560        570        580        590        600 
KFRACQFLIK FHERRNDKII VFADNVFALK EYAIRLNKPY IYGPTSQGER MQILQNFKHN 

       610        620        630        640        650        660 
PKINTIFISK VGDTSFDLPE ANVLIQISSH GGSRRQEAQR LGRVLRAKKG MVAEEYNAFF 

       670        680        690        700        710        720 
YSLVSQDTQE MAYSTKRQRF LVDQGYSFKV ITKLAGMEEE ELAFSTKEEQ QQLLQKVLAA 

       730        740        750        760        770        780 
TDLDAEEEVV AGEFGSRSGQ ASRRCGTMSS LSGADDTVYM EYHSSRSKAS SKHVHPLFKR 


FRK 

« Hide

References

« Hide 'large scale' references
[1]"Characterization of the mouse homolog of the XPBC/ERCC-3 gene implicated in xeroderma pigmentosum and Cockayne's syndrome."
Weeda G., Ma L., van Ham R.C., Bootsma D., der Eb A.J., Hoeijmakers J.H.
Carcinogenesis 12:2361-2368(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"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].
Strain: FVB/N.
Tissue: Mammary gland.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
S71186 mRNA. Translation: AAB20614.1.
BC016595 mRNA. Translation: AAH16595.1.
BC026575 mRNA. Translation: AAH26575.1.
CCDSCCDS29118.1.
PIRA48994.
RefSeqNP_598419.1. NM_133658.1.
UniGeneMm.282335.

3D structure databases

ProteinModelPortalP49135.
SMRP49135. Positions 284-731.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid199501. 6 interactions.
IntActP49135. 1 interaction.
MINTMINT-4094657.

PTM databases

PhosphoSiteP49135.

Proteomic databases

MaxQBP49135.
PaxDbP49135.
PRIDEP49135.

Protocols and materials databases

DNASU13872.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000025241; ENSMUSP00000025241; ENSMUSG00000024382.
GeneID13872.
KEGGmmu:13872.
UCSCuc008eje.1. mouse.

Organism-specific databases

CTD2071.
MGIMGI:95414. Ercc3.

Phylogenomic databases

eggNOGCOG1061.
GeneTreeENSGT00390000002204.
HOGENOMHOG000160172.
HOVERGENHBG051499.
InParanoidP49135.
KOK10843.
OMAAPSKHVH.
OrthoDBEOG7DNNTM.
PhylomeDBP49135.
TreeFamTF101233.

Gene expression databases

BgeeP49135.
GenevestigatorP49135.

Family and domain databases

Gene3D3.40.50.300. 2 hits.
InterProIPR006935. Helicase/UvrB_dom.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR001161. Helicase_Ercc3.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamPF00271. Helicase_C. 1 hit.
PF04851. ResIII. 1 hit.
[Graphical view]
PRINTSPR00851. XRODRMPGMNTB.
SMARTSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 3 hits.
TIGRFAMsTIGR00603. rad25. 1 hit.
PROSITEPS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio284792.
PROP49135.
SOURCESearch...

Entry information

Entry nameERCC3_MOUSE
AccessionPrimary (citable) accession number: P49135
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: July 9, 2014
This is version 127 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot