ERCC3_MOUSE
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 03-AUG-2022, entry version 182.
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; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC 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., Hoeijmakers J.H.;
RT "Characterization of the mouse homolog of the XPBC/ERCC-3 gene implicated
RT 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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: ATP-dependent 3'-5' DNA helicase, component of the general
CC transcription and DNA repair factor IIH (TFIIH) core complex, which is
CC involved in general and transcription-coupled nucleotide excision
CC repair (NER) of damaged DNA and, when complexed to CAK, in RNA
CC transcription by RNA polymerase II. In NER, TFIIH acts by opening DNA
CC around the lesion to allow the excision of the damaged oligonucleotide
CC and its replacement by a new DNA fragment. The ATPase activity of
CC XPB/ERCC3, but not its helicase activity, is required for DNA opening.
CC In transcription, TFIIH has an essential role in transcription
CC initiation. When the pre-initiation complex (PIC) has been established,
CC TFIIH is 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 tail
CC (CTD) of the largest subunit of RNA polymerase II by the kinase module
CC 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, which
CC is active in NER. The core complex associates with the 3-subunit CDK-
CC activating kinase (CAK) module composed of CCNH/cyclin H, CDK7 and
CC MNAT1 to form the 10-subunit holoenzyme (holo-TFIIH) active in
CC transcription. Interacts with PUF60. Interacts with ATF7IP. Interacts
CC with KAT2A; leading to KAT2A recruitment to promoters and acetylation
CC of histones. {ECO:0000250|UniProtKB:P19447}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- SIMILARITY: Belongs to the helicase family. RAD25/XPB subfamily.
CC {ECO:0000305}.
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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 AlphaFoldDB; P49135; -.
DR SMR; P49135; -.
DR BioGRID; 199501; 9.
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 ProteomicsDB; 275532; -.
DR Antibodypedia; 18449; 242 antibodies from 38 providers.
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 VEuPathDB; HostDB:ENSMUSG00000024382; -.
DR eggNOG; KOG1123; Eukaryota.
DR GeneTree; ENSGT00390000002204; -.
DR HOGENOM; CLU_008213_0_0_1; -.
DR InParanoid; P49135; -.
DR OMA; PTHIHEY; -.
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 BioGRID-ORCS; 13872; 19 hits in 111 CRISPR screens.
DR ChiTaRS; Ercc3; mouse.
DR PRO; PR:P49135; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; P49135; protein.
DR Bgee; ENSMUSG00000024382; Expressed in spermatid and 267 other tissues.
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:transcription 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:ATP hydrolysis activity; IMP:MGI.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:1990841; F:promoter-specific chromatin binding; IDA:MGI.
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: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; IBA:GO_Central.
DR GO; GO:0043065; P:positive regulation of apoptotic process; 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; EXP: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 Gene3D; 3.40.50.300; -; 2.
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; DNA damage; DNA repair; DNA-binding; Helicase; Hydrolase;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..783
FT /note="General transcription and DNA repair factor IIH
FT helicase subunit XPB"
FT /id="PRO_0000101989"
FT DOMAIN 328..489
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 543..703
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 6..18
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 442..445
FT /note="DEVH box"
FT COMPBIAS 1..20
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 341..348
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 34
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q4G005"
FT MOD_RES 687
FT /note="Phosphoserine"
FT /evidence="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
