ERCC1_MOUSE
ID ERCC1_MOUSE Reviewed; 298 AA.
AC P07903; Q91VP3;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=DNA excision repair protein ERCC-1;
GN Name=Ercc1; Synonyms=Ercc-1;
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 [GENOMIC DNA / MRNA].
RX PubMed=3290851; DOI=10.1093/nar/16.12.5305;
RA van Duin M., van den Tol J., Warmerdam P., Odijk H., Meijer D.,
RA Westerveld A., Hoeijmakers J.H.J.;
RT "Evolution and mutagenesis of the mammalian excision repair gene ERCC-1.";
RL Nucleic Acids Res. 16:5305-5322(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Epididymis, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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: Non-catalytic component of a structure-specific DNA repair
CC endonuclease responsible for the 5'-incision during DNA repair.
CC Responsible, in conjunction with SLX4, for the first step in the repair
CC of interstrand cross-links (ICL). Participates in the processing of
CC anaphase bridge-generating DNA structures, which consist in
CC incompletely processed DNA lesions arising during S or G2 phase, and
CC can result in cytokinesis failure. Also required for homology-directed
CC repair (HDR) of DNA double-strand breaks, in conjunction with SLX4 (By
CC similarity). {ECO:0000250|UniProtKB:P07992}.
CC -!- SUBUNIT: Heterodimer composed of ERCC1 and ERRC4/XPF (By similarity).
CC Interacts with USP4 (By similarity). {ECO:0000250|UniProtKB:P07992}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07992}.
CC -!- PTM: Ubiquitinated with both 'Lys-48' and 'Lys-63' linkages.
CC Deubiquitinated by USP45. {ECO:0000250|UniProtKB:P07992}.
CC -!- SIMILARITY: Belongs to the ERCC1/RAD10/SWI10 family. {ECO:0000305}.
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DR EMBL; X07414; CAA30310.1; -; mRNA.
DR EMBL; X07413; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK088271; BAC40249.1; -; mRNA.
DR EMBL; AK136733; BAE23112.1; -; mRNA.
DR EMBL; AC148988; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466639; EDL23137.1; -; Genomic_DNA.
DR EMBL; BC011224; AAH11224.1; -; mRNA.
DR CCDS; CCDS20898.1; -.
DR PIR; S01202; S01202.
DR RefSeq; NP_001120796.1; NM_001127324.1.
DR RefSeq; NP_031974.2; NM_007948.2.
DR AlphaFoldDB; P07903; -.
DR SMR; P07903; -.
DR BioGRID; 199499; 3.
DR ComplexPortal; CPX-491; Ercc1-Xpf endonuclease complex.
DR STRING; 10090.ENSMUSP00000003645; -.
DR iPTMnet; P07903; -.
DR PhosphoSitePlus; P07903; -.
DR EPD; P07903; -.
DR PaxDb; P07903; -.
DR PeptideAtlas; P07903; -.
DR PRIDE; P07903; -.
DR ProteomicsDB; 275468; -.
DR Antibodypedia; 3826; 1330 antibodies from 44 providers.
DR Ensembl; ENSMUST00000003645; ENSMUSP00000003645; ENSMUSG00000003549.
DR GeneID; 13870; -.
DR KEGG; mmu:13870; -.
DR UCSC; uc009flm.2; mouse.
DR CTD; 2067; -.
DR MGI; MGI:95412; Ercc1.
DR VEuPathDB; HostDB:ENSMUSG00000003549; -.
DR eggNOG; KOG2841; Eukaryota.
DR GeneTree; ENSGT00390000011275; -.
DR HOGENOM; CLU_041616_3_1_1; -.
DR InParanoid; P07903; -.
DR OMA; LNPDYIC; -.
DR OrthoDB; 1336192at2759; -.
DR PhylomeDB; P07903; -.
DR TreeFam; TF101231; -.
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-6782135; Dual incision in TC-NER.
DR Reactome; R-MMU-6783310; Fanconi Anemia Pathway.
DR BioGRID-ORCS; 13870; 7 hits in 111 CRISPR screens.
DR ChiTaRS; Ercc1; mouse.
DR PRO; PR:P07903; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; P07903; protein.
DR Bgee; ENSMUSG00000003549; Expressed in internal carotid artery and 241 other tissues.
DR ExpressionAtlas; P07903; baseline and differential.
DR Genevisible; P07903; MM.
DR GO; GO:0000781; C:chromosome, telomeric region; ISO:MGI.
DR GO; GO:0070522; C:ERCC4-ERCC1 complex; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0000109; C:nucleotide-excision repair complex; ISS:UniProtKB.
DR GO; GO:0000110; C:nucleotide-excision repair factor 1 complex; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IPI:MGI.
DR GO; GO:1990599; F:3' overhang single-stranded DNA endodeoxyribonuclease activity; ISO:MGI.
DR GO; GO:0003684; F:damaged DNA binding; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; ISO:MGI.
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:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0003697; F:single-stranded DNA binding; ISO:MGI.
DR GO; GO:0000014; F:single-stranded DNA endodeoxyribonuclease activity; ISO:MGI.
DR GO; GO:0001094; F:TFIID-class transcription factor complex binding; IDA:MGI.
DR GO; GO:0048468; P:cell development; IMP:MGI.
DR GO; GO:0008283; P:cell population proliferation; IMP:MGI.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:MGI.
DR GO; GO:0051276; P:chromosome organization; IMP:MGI.
DR GO; GO:0006310; P:DNA recombination; IMP:MGI.
DR GO; GO:0006281; P:DNA repair; IMP:MGI.
DR GO; GO:0006302; P:double-strand break repair; IMP:MGI.
DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; ISO:MGI.
DR GO; GO:0048568; P:embryonic organ development; IEA:Ensembl.
DR GO; GO:0007281; P:germ cell development; IMP:MGI.
DR GO; GO:0036297; P:interstrand cross-link repair; IMP:MGI.
DR GO; GO:0045190; P:isotype switching; IMP:MGI.
DR GO; GO:0008584; P:male gonad development; IMP:MGI.
DR GO; GO:0000710; P:meiotic mismatch repair; IBA:GO_Central.
DR GO; GO:0006312; P:mitotic recombination; ISO:MGI.
DR GO; GO:0010259; P:multicellular organism aging; IMP:MGI.
DR GO; GO:0035264; P:multicellular organism growth; IMP:MGI.
DR GO; GO:1905765; P:negative regulation of protection from non-homologous end joining at telomere; ISO:MGI.
DR GO; GO:0032205; P:negative regulation of telomere maintenance; ISO:MGI.
DR GO; GO:0006289; P:nucleotide-excision repair; IMP:MGI.
DR GO; GO:0033683; P:nucleotide-excision repair, DNA incision; ISO:MGI.
DR GO; GO:0006296; P:nucleotide-excision repair, DNA incision, 5'-to lesion; IBA:GO_Central.
DR GO; GO:0048477; P:oogenesis; IMP:MGI.
DR GO; GO:1904431; P:positive regulation of t-circle formation; IMP:BHF-UCL.
DR GO; GO:0060261; P:positive regulation of transcription initiation from RNA polymerase II promoter; IMP:MGI.
DR GO; GO:0035166; P:post-embryonic hemopoiesis; IMP:MGI.
DR GO; GO:0000720; P:pyrimidine dimer repair by nucleotide-excision repair; IMP:MGI.
DR GO; GO:0090399; P:replicative senescence; IMP:MGI.
DR GO; GO:0046686; P:response to cadmium ion; IEA:Ensembl.
DR GO; GO:0035902; P:response to immobilization stress; IEA:Ensembl.
DR GO; GO:0007584; P:response to nutrient; IEA:Ensembl.
DR GO; GO:0006979; P:response to oxidative stress; ISO:MGI.
DR GO; GO:0009744; P:response to sucrose; IEA:Ensembl.
DR GO; GO:0010165; P:response to X-ray; IMP:MGI.
DR GO; GO:0007283; P:spermatogenesis; IMP:MGI.
DR GO; GO:0006949; P:syncytium formation; IMP:MGI.
DR GO; GO:0090656; P:t-circle formation; IMP:BHF-UCL.
DR GO; GO:0061819; P:telomeric DNA-containing double minutes formation; ISO:MGI.
DR GO; GO:0009650; P:UV protection; IMP:MGI.
DR GO; GO:0070914; P:UV-damage excision repair; IBA:GO_Central.
DR InterPro; IPR004579; ERCC1/RAD10/SWI10.
DR InterPro; IPR000445; HhH_motif.
DR InterPro; IPR011335; Restrct_endonuc-II-like.
DR InterPro; IPR010994; RuvA_2-like.
DR PANTHER; PTHR12749; PTHR12749; 1.
DR Pfam; PF00633; HHH; 1.
DR Pfam; PF03834; Rad10; 1.
DR SUPFAM; SSF47781; SSF47781; 1.
DR SUPFAM; SSF52980; SSF52980; 1.
DR TIGRFAMs; TIGR00597; rad10; 1.
PE 2: Evidence at transcript level;
KW Acetylation; DNA damage; DNA repair; DNA-binding; Isopeptide bond; Nucleus;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..298
FT /note="DNA excision repair protein ERCC-1"
FT /id="PRO_0000087007"
FT DNA_BIND 134..156
FT /evidence="ECO:0000255"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 66..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 220..298
FT /note="HhH2, dimerization with ERRC4/XPF"
FT /evidence="ECO:0000250|UniProtKB:P07992"
FT MOTIF 17..23
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 82..99
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P07992"
FT CROSSLNK 21
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P07992"
FT CROSSLNK 37
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P07992"
FT CROSSLNK 243
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P07992"
FT CONFLICT 55
FT /note="V -> M (in Ref. 1; CAA30310)"
FT /evidence="ECO:0000305"
FT CONFLICT 213
FT /note="K -> R (in Ref. 1; CAA30310)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 298 AA; 32910 MW; 264DF6865A3ED847 CRC64;
MDPGKDEESR PQPSGPPTRR KFVIPLEEEE VPCAGVKPLF RSSRNPTIPA TSAHVAPQTY
AEYAITQPPG GAGATVPTGS EPAAGENPSQ TLKTGAKSNS IIVSPRQRGN PVLKFVRNVP
WEFGEVIPDY VLGQSTCALF LSLRYHNLHP DYIHERLQSL GKNFALRVLL VQVDVKDPQQ
ALKELAKMCI LADCTLVLAW SAEEAGRYLE TYKAYEQKPA DLLMEKLEQN FLSRATECLT
TVKSVNKTDS QTLLATFGSL EQLFTASRED LALCPGLGPQ KARRLFEVLH EPFLKVPR
