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Database: UniProt
Entry: P49135
LinkDB: P49135
Original site: P49135 
ID   ERCC3_MOUSE             Reviewed;         783 AA.
AC   P49135;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   16-OCT-2019, entry version 168.
DE   RecName: Full=General transcription and DNA repair factor IIH helicase subunit XPB;
DE            Short=TFIIH subunit XPB;
DE            EC=3.6.4.12;
DE   AltName: Full=Basic transcription factor 2 89 kDa subunit;
DE            Short=BTF2 p89;
DE   AltName: Full=DNA excision repair protein ERCC-3;
DE   AltName: Full=DNA repair protein complementing XP-B cells;
DE   AltName: Full=TFIIH 89 kDa subunit;
DE   AltName: Full=Xeroderma pigmentosum group B-complementing protein;
GN   Name=Ercc3; Synonyms=Xpb, Xpbc;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1747940; DOI=10.1093/carcin/12.12.2361;
RA   Weeda G., Ma L., van Ham R.C., Bootsma D., der Eb A.J.,
RA   Hoeijmakers J.H.;
RT   "Characterization of the mouse homolog of the XPBC/ERCC-3 gene
RT   implicated in xeroderma pigmentosum and Cockayne's syndrome.";
RL   Carcinogenesis 12:2361-2368(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: ATP-dependent 3'-5' DNA helicase, component of the
CC       general transcription and DNA repair factor IIH (TFIIH) core
CC       complex, which is involved in general and transcription-coupled
CC       nucleotide excision repair (NER) of damaged DNA and, when
CC       complexed to CAK, in RNA transcription by RNA polymerase II. In
CC       NER, TFIIH acts by opening DNA around the lesion to allow the
CC       excision of the damaged oligonucleotide and its replacement by a
CC       new DNA fragment. The ATPase activity of XPB/ERCC3, but not its
CC       helicase activity, is required for DNA opening. In transcription,
CC       TFIIH has an essential role in transcription initiation. When the
CC       pre-initiation complex (PIC) has been established, TFIIH is
CC       required for promoter opening and promoter escape. The ATP-
CC       dependent helicase activity of XPB/ERCC3 is required for promoter
CC       opening and promoter escape. Phosphorylation of the C-terminal
CC       tail (CTD) of the largest subunit of RNA polymerase II by the
CC       kinase module CAK controls the initiation of transcription.
CC       {ECO:0000250|UniProtKB:P19447}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC   -!- SUBUNIT: Component of the 7-subunit TFIIH core complex composed of
CC       XPB/ERCC3, XPD/ERCC2, GTF2H1, GTF2H2, GTF2H3, GTF2H4 and GTF2H5,
CC       which is active in NER. The core complex associates with the 3-
CC       subunit CDK-activating kinase (CAK) module composed of CCNH/cyclin
CC       H, CDK7 and MNAT1 to form the 10-subunit holoenzyme (holo-TFIIH)
CC       active in transcription. Interacts with PUF60. Interacts with
CC       ATF7IP. {ECO:0000250|UniProtKB:P19447}.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- SIMILARITY: Belongs to the helicase family. RAD25/XPB subfamily.
CC       {ECO:0000305}.
DR   EMBL; S71186; AAB20614.1; -; mRNA.
DR   EMBL; BC016595; AAH16595.1; -; mRNA.
DR   EMBL; BC026575; AAH26575.1; -; mRNA.
DR   CCDS; CCDS29118.1; -.
DR   PIR; A48994; A48994.
DR   RefSeq; NP_598419.1; NM_133658.1.
DR   SMR; P49135; -.
DR   BioGrid; 199501; 6.
DR   IntAct; P49135; 1.
DR   MINT; P49135; -.
DR   STRING; 10090.ENSMUSP00000025241; -.
DR   iPTMnet; P49135; -.
DR   PhosphoSitePlus; P49135; -.
DR   EPD; P49135; -.
DR   jPOST; P49135; -.
DR   MaxQB; P49135; -.
DR   PaxDb; P49135; -.
DR   PeptideAtlas; P49135; -.
DR   PRIDE; P49135; -.
DR   DNASU; 13872; -.
DR   Ensembl; ENSMUST00000025241; ENSMUSP00000025241; ENSMUSG00000024382.
DR   GeneID; 13872; -.
DR   KEGG; mmu:13872; -.
DR   UCSC; uc008eje.1; mouse.
DR   CTD; 2071; -.
DR   MGI; MGI:95414; Ercc3.
DR   eggNOG; KOG1123; Eukaryota.
DR   eggNOG; COG1061; LUCA.
DR   GeneTree; ENSGT00390000002204; -.
DR   HOGENOM; HOG000160172; -.
DR   InParanoid; P49135; -.
DR   KO; K10843; -.
DR   OMA; PKKFQAC; -.
DR   OrthoDB; 100698at2759; -.
DR   PhylomeDB; P49135; -.
DR   TreeFam; TF101233; -.
DR   Reactome; R-MMU-112382; Formation of RNA Pol II elongation complex.
DR   Reactome; R-MMU-113418; Formation of the Early Elongation Complex.
DR   Reactome; R-MMU-5696395; Formation of Incision Complex in GG-NER.
DR   Reactome; R-MMU-5696400; Dual Incision in GG-NER.
DR   Reactome; R-MMU-674695; RNA Polymerase II Pre-transcription Events.
DR   Reactome; R-MMU-6781823; Formation of TC-NER Pre-Incision Complex.
DR   Reactome; R-MMU-6782135; Dual incision in TC-NER.
DR   Reactome; R-MMU-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR   Reactome; R-MMU-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR   Reactome; R-MMU-72086; mRNA Capping.
DR   Reactome; R-MMU-73762; RNA Polymerase I Transcription Initiation.
DR   Reactome; R-MMU-73772; RNA Polymerase I Promoter Escape.
DR   Reactome; R-MMU-73776; RNA Polymerase II Promoter Escape.
DR   Reactome; R-MMU-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
DR   Reactome; R-MMU-73863; RNA Polymerase I Transcription Termination.
DR   Reactome; R-MMU-75953; RNA Polymerase II Transcription Initiation.
DR   Reactome; R-MMU-75955; RNA Polymerase II Transcription Elongation.
DR   Reactome; R-MMU-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance.
DR   Reactome; R-MMU-77075; RNA Pol II CTD phosphorylation and interaction with CE.
DR   ChiTaRS; Ercc3; mouse.
DR   PRO; PR:P49135; -.
DR   Proteomes; UP000000589; Chromosome 18.
DR   Bgee; ENSMUSG00000024382; Expressed in 283 organ(s), highest expression level in morula.
DR   Genevisible; P49135; MM.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0000112; C:nucleotide-excision repair factor 3 complex; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
DR   GO; GO:0005669; C:transcription factor TFIID complex; ISO:MGI.
DR   GO; GO:0000439; C:transcription factor TFIIH core complex; ISO:MGI.
DR   GO; GO:0005675; C:transcription factor TFIIH holo complex; ISS:UniProtKB.
DR   GO; GO:0097550; C:transcriptional preinitiation complex; IBA:GO_Central.
DR   GO; GO:0043138; F:3'-5' DNA helicase activity; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATPase activity; IMP:MGI.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
DR   GO; GO:0047485; F:protein N-terminus binding; ISO:MGI.
DR   GO; GO:0008353; F:RNA polymerase II CTD heptapeptide repeat kinase activity; IEA:Ensembl.
DR   GO; GO:0008134; F:transcription factor binding; IBA:GO_Central.
DR   GO; GO:0006915; P:apoptotic process; ISS:UniProtKB.
DR   GO; GO:0006281; P:DNA repair; ISO:MGI.
DR   GO; GO:0006265; P:DNA topological change; ISS:UniProtKB.
DR   GO; GO:0048568; P:embryonic organ development; IBA:GO_Central.
DR   GO; GO:0035315; P:hair cell differentiation; ISO:MGI.
DR   GO; GO:0006289; P:nucleotide-excision repair; ISO:MGI.
DR   GO; GO:0000717; P:nucleotide-excision repair, DNA duplex unwinding; ISO:MGI.
DR   GO; GO:0033683; P:nucleotide-excision repair, DNA incision; ISO:MGI.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR   GO; GO:0008104; P:protein localization; ISO:MGI.
DR   GO; GO:1901990; P:regulation of mitotic cell cycle phase transition; ISO:MGI.
DR   GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
DR   GO; GO:0006979; P:response to oxidative stress; ISO:MGI.
DR   GO; GO:0009411; P:response to UV; ISO:MGI.
DR   GO; GO:0006366; P:transcription by RNA polymerase II; ISS:UniProtKB.
DR   GO; GO:0006362; P:transcription elongation from RNA polymerase I promoter; IMP:MGI.
DR   GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; IBA:GO_Central.
DR   GO; GO:0006283; P:transcription-coupled nucleotide-excision repair; ISS:UniProtKB.
DR   GO; GO:0009650; P:UV protection; IGI:MGI.
DR   InterPro; IPR032438; ERCC3_RAD25_C.
DR   InterPro; IPR006935; Helicase/UvrB_N.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR001161; XPB/Ssl2.
DR   InterPro; IPR032830; XPB/Ssl2_N.
DR   Pfam; PF16203; ERCC3_RAD25_C; 1.
DR   Pfam; PF13625; Helicase_C_3; 1.
DR   Pfam; PF04851; ResIII; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   TIGRFAMs; TIGR00603; rad25; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Complete proteome; DNA damage; DNA repair; DNA-binding;
KW   Helicase; Hydrolase; Nucleotide-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Transcription; Transcription regulation.
FT   CHAIN         1    783       General transcription and DNA repair
FT                                factor IIH helicase subunit XPB.
FT                                /FTId=PRO_0000101989.
FT   DOMAIN      328    489       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      543    703       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND     341    348       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF         6     18       Nuclear localization signal.
FT                                {ECO:0000255}.
FT   MOTIF       442    445       DEVH box.
FT   COMPBIAS     20     28       Asp/Glu-rich (acidic).
FT   COMPBIAS    257    266       Asp/Glu-rich (acidic).
FT   COMPBIAS    698    701       Asp/Glu-rich (acidic).
FT   COMPBIAS    722    729       Asp/Glu-rich (acidic).
FT   MOD_RES      34     34       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q4G005}.
FT   MOD_RES     687    687       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P19447}.
SQ   SEQUENCE   783 AA;  89126 MW;  6D204EF6A831D8AF CRC64;
     MGKRDRVDRD KKKSKKRQYE EEEEDEDDIP GNESQEAVPS AAGKQVDESS TKVDEYGAKD
     YRQQMPLKGD HTSRPLWVAP DGHIFLEAFS PVYKYAQDFL VAIAEPVCRP THVHEYKLTA
     YSLYAAVSVG LQTSDITEYL RKLSKTGVPD GIIQFIKLCT VSYGKVKLVL KHNRYFVESS
     HPDVIQHLLQ DPVIRECRLR NAEGEATELI TETFTSKSAI SKTAAEGSGG PSTSQGVDAQ
     ATSDIPKDLF DFYEQMDKDE EEEEETQTVS FEVKQEMIEE LQKRCICLEY PLLAEYDFRN
     DTLNPDINID LKPTAVLRPY QEKSLRKMFG NGRARSGVIV LPCGAGKSLV GVTAACTVRK
     RCLVLGNSAV SVEQWKAQFK MWSTIDDSQI CRFTSDAKDK PIGCSVAIST YSMLGHTTKR
     SWEAERVMEW LKTQEWGLMI LDEVHTIPAR MFRRVLTIVQ AHCKLGLTAT LVREDDKIVD
     LNFLIGPKLY EANWMELQNN GYIAKVQCAE VWCPMSPEFY REYVAIKTKK RILLYTMNPN
     KFRACQFLIK FHERRNDKII VFADNVFALK EYAIRLNKPY IYGPTSQGER MQILQNFKHN
     PKINTIFISK VGDTSFDLPE ANVLIQISSH GGSRRQEAQR LGRVLRAKKG MVAEEYNAFF
     YSLVSQDTQE MAYSTKRQRF LVDQGYSFKV ITKLAGMEEE ELAFSTKEEQ QQLLQKVLAA
     TDLDAEEEVV AGEFGSRSGQ ASRRCGTMSS LSGADDTVYM EYHSSRSKAS SKHVHPLFKR
     FRK
//
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