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ERCC3_RAT
ID   ERCC3_RAT               Reviewed;         782 AA.
AC   Q4G005;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2005, sequence version 1.
DT   03-AUG-2022, entry version 132.
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=DNA excision repair protein ERCC-3;
GN   Name=Ercc3;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Thymus;
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).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
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 {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the helicase family. RAD25/XPB subfamily.
CC       {ECO:0000305}.
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DR   EMBL; BC098856; AAH98856.1; -; mRNA.
DR   RefSeq; NP_001026814.1; NM_001031644.1.
DR   AlphaFoldDB; Q4G005; -.
DR   SMR; Q4G005; -.
DR   STRING; 10116.ENSRNOP00000018422; -.
DR   iPTMnet; Q4G005; -.
DR   PhosphoSitePlus; Q4G005; -.
DR   PaxDb; Q4G005; -.
DR   PRIDE; Q4G005; -.
DR   Ensembl; ENSRNOT00000018422; ENSRNOP00000018422; ENSRNOG00000013180.
DR   GeneID; 291703; -.
DR   KEGG; rno:291703; -.
DR   UCSC; RGD:1307139; rat.
DR   CTD; 2071; -.
DR   RGD; 1307139; Ercc3.
DR   eggNOG; KOG1123; Eukaryota.
DR   GeneTree; ENSGT00390000002204; -.
DR   HOGENOM; CLU_008213_0_0_1; -.
DR   InParanoid; Q4G005; -.
DR   OMA; PTHIHEY; -.
DR   OrthoDB; 100698at2759; -.
DR   PhylomeDB; Q4G005; -.
DR   TreeFam; TF101233; -.
DR   Reactome; R-RNO-112382; Formation of RNA Pol II elongation complex.
DR   Reactome; R-RNO-113418; Formation of the Early Elongation Complex.
DR   Reactome; R-RNO-5696395; Formation of Incision Complex in GG-NER.
DR   Reactome; R-RNO-5696400; Dual Incision in GG-NER.
DR   Reactome; R-RNO-674695; RNA Polymerase II Pre-transcription Events.
DR   Reactome; R-RNO-6781823; Formation of TC-NER Pre-Incision Complex.
DR   Reactome; R-RNO-6782135; Dual incision in TC-NER.
DR   Reactome; R-RNO-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR   Reactome; R-RNO-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR   Reactome; R-RNO-72086; mRNA Capping.
DR   Reactome; R-RNO-73762; RNA Polymerase I Transcription Initiation.
DR   Reactome; R-RNO-73772; RNA Polymerase I Promoter Escape.
DR   Reactome; R-RNO-73776; RNA Polymerase II Promoter Escape.
DR   Reactome; R-RNO-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
DR   Reactome; R-RNO-73863; RNA Polymerase I Transcription Termination.
DR   Reactome; R-RNO-75953; RNA Polymerase II Transcription Initiation.
DR   Reactome; R-RNO-75955; RNA Polymerase II Transcription Elongation.
DR   Reactome; R-RNO-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance.
DR   Reactome; R-RNO-77075; RNA Pol II CTD phosphorylation and interaction with CE.
DR   PRO; PR:Q4G005; -.
DR   Proteomes; UP000002494; Chromosome 18.
DR   Bgee; ENSRNOG00000013180; Expressed in spleen and 19 other tissues.
DR   Genevisible; Q4G005; RN.
DR   GO; GO:0000112; C:nucleotide-excision repair factor 3 complex; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IDA:RGD.
DR   GO; GO:0005669; C:transcription factor TFIID complex; ISO:RGD.
DR   GO; GO:0000439; C:transcription factor TFIIH core complex; IDA:RGD.
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; ISO:RGD.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; ISO:RGD.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:1990841; F:promoter-specific chromatin binding; ISO:RGD.
DR   GO; GO:0008022; F:protein C-terminus binding; ISO:RGD.
DR   GO; GO:0047485; F:protein N-terminus binding; ISO:RGD.
DR   GO; GO:0006915; P:apoptotic process; ISO:RGD.
DR   GO; GO:0006281; P:DNA repair; ISO:RGD.
DR   GO; GO:0006265; P:DNA topological change; ISO:RGD.
DR   GO; GO:0048568; P:embryonic organ development; IEP:RGD.
DR   GO; GO:0035315; P:hair cell differentiation; ISO:RGD.
DR   GO; GO:0006289; P:nucleotide-excision repair; ISO:RGD.
DR   GO; GO:0000717; P:nucleotide-excision repair, DNA duplex unwinding; ISO:RGD.
DR   GO; GO:0033683; P:nucleotide-excision repair, DNA incision; ISO:RGD.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; ISO:RGD.
DR   GO; GO:0008104; P:protein localization; ISO:RGD.
DR   GO; GO:1901990; P:regulation of mitotic cell cycle phase transition; ISO:RGD.
DR   GO; GO:0001666; P:response to hypoxia; IEP:RGD.
DR   GO; GO:0006979; P:response to oxidative stress; ISO:RGD.
DR   GO; GO:0009411; P:response to UV; ISO:RGD.
DR   GO; GO:0006366; P:transcription by RNA polymerase II; ISS:UniProtKB.
DR   GO; GO:0006362; P:transcription elongation from RNA polymerase I promoter; ISO:RGD.
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; ISO:RGD.
DR   GO; GO:0009650; P:UV protection; ISO:RGD.
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   1: Evidence at protein 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..782
FT                   /note="General transcription and DNA repair factor IIH
FT                   helicase subunit XPB"
FT                   /id="PRO_0000323742"
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:0007744|PubMed:22673903"
FT   MOD_RES         686
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P19447"
SQ   SEQUENCE   782 AA;  89099 MW;  7548181D98079B31 CRC64;
     MGKRDRVDRD KKKSKKRQYE EEEEDEDDAP GNESQEAVPS AAGKQVDESS TKVDEYGAKD
     YRQQMPLKGD HTSRPLWVAP DGHIFLEAFS PVYKYAQDFL VAIAEPVCRP THVHEYKLTA
     YSLYAAVSVG LQTSDITEYL RKLSKTGVPD GIIQFIKLCT VSYGKVKLVL KHNRYFVESS
     HPDVIQHLLQ DPVIRECRLR NAEGEATELI TETFTSKSAI SKTVEGSGGA STSQGVDAQA
     KSDIPKDLFD FYEQMDKDEE EEEETQTVSF EVKQEMIEEL QKRCICLEYP LLAEYDFRND
     SLNPDINIDL KPTAVLRPYQ EKSLRKMFGN GRARSGVIVL PCGAGKSLVG VTAACTVRKR
     CLVLGNSAVS VEQWKAQFKM WSTIDDSQIC RFTSDAKDKP IGCSIAISTY SMLGHTTKRS
     WEAERVMEWL KTQEWGLMIL DEVHTIPAKM FRRVLTIVQA HCKLGLTATL VREDDKIVDL
     NFLIGPKLYE ANWMELQNNG YIAKVQCAEV WCPMSPEFYR EYVAIKTKKR ILLYTMNPNK
     FRACQFLIKF HERRNDKIIV FADNVFALKE YAIRLNKPYI YGPTSQGERM QILQNFKHNP
     KINTIFISKV GDTSFDLPEA NVLIQISSHG GSRRQEAQRL GRVLRAKKGM VAEEYNAFFY
     SLVSQDTQEM AYSTKRQRFL VDQGYSFKVI TKLAGMEEEE LAFSTKEEQQ QLLQKVLAAT
     DLDAEEEVVA GEFGSRSGQA SRRFGTMSSL SGADDTVYME YHSSRNKAST KHVHPLFKRF
     RK
 
 
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