ID ERCC1_HUMAN Reviewed; 297 AA. AC P07992; B2RC01; B3KRR0; Q7Z7F5; Q96S40; DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1988, sequence version 1. DT 27-MAR-2024, entry version 216. DE RecName: Full=DNA excision repair protein ERCC-1; GN Name=ERCC1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=2420469; DOI=10.1016/0092-8674(86)90014-0; RA van Duin M., de Wit J., Odijk H., Westerveld A., Yasui A., Koken M.H.M., RA Hoeijmakers J.H.J., Bootsma D.; RT "Molecular characterization of the human excision repair gene ERCC-1: cDNA RT cloning and amino acid homology with the yeast DNA repair gene RAD10."; RL Cell 44:913-923(1986). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=3034490; DOI=10.1101/sqb.1986.051.01.012; RA Hoeijmakers J.H.J., van Duin M., Westerveld A., Yasui A., Bootsma D.; RT "Identification of DNA repair genes in the human genome."; RL Cold Spring Harb. Symp. Quant. Biol. 51:91-101(1986). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=9360634; DOI=10.1016/s1383-5726(97)00004-6; RA Yu J.J., Mu C.J., Lee K.B., Okamoto A., Reed E.L., Bostick-Bruton F., RA Mitchell K.C., Reed E.; RT "A nucleotide polymorphism in ERCC1 in human ovarian cancer cell lines and RT tumor tissues."; RL Mutat. Res. 382:13-20(1997). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RA Hisatomi H., Nagao K., Ishikawa H., Yokoyama Y., Ishihara Y., Hikiji K., RA Iizuka T.; RT "Human excision repair protein 1, transcript variant, mRNA."; RL Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT THR-266. RG NIEHS SNPs program; RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4). RC TISSUE=Cerebellum; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15057824; DOI=10.1038/nature02399; RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A., RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., RA Rubin E.M., Lucas S.M.; RT "The DNA sequence and biology of human chromosome 19."; RL Nature 428:529-535(2004). RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [10] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3). RC TISSUE=Lung, and Uterus; 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 [11] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [12] RP FUNCTION (ISOFORMS 1; 2; 3 AND 4), SUBCELLULAR LOCATION (ISOFORMS 1; 2; 3 RP AND 4), AND SUBUNIT (ISOFORMS 1; 2; 3 AND 4). RX PubMed=24036546; DOI=10.4161/cc.26309; RA Friboulet L., Postel-Vinay S., Sourisseau T., Adam J., Stoclin A., RA Ponsonnailles F., Dorvault N., Commo F., Saulnier P., Salome-Desmoulez S., RA Pottier G., Andre F., Kroemer G., Soria J.C., Olaussen K.A.; RT "ERCC1 function in nuclear excision and interstrand crosslink repair RT pathways is mediated exclusively by the ERCC1-202 isoform."; RL Cell Cycle 12:3298-3306(2013). RN [13] RP ALTERNATIVE SPLICING. RX PubMed=23514287; DOI=10.1056/nejmoa1214271; RA Friboulet L., Olaussen K.A., Pignon J.P., Shepherd F.A., Tsao M.S., RA Graziano S., Kratzke R., Douillard J.Y., Seymour L., Pirker R., RA Filipits M., Andre F., Solary E., Ponsonnailles F., Robin A., Stoclin A., RA Dorvault N., Commo F., Adam J., Vanhecke E., Saulnier P., Thomale J., RA Le Chevalier T., Dunant A., Rousseau V., Le Teuff G., Brambilla E., RA Soria J.C.; RT "ERCC1 isoform expression and DNA repair in non-small-cell lung cancer."; RL N. Engl. J. Med. 368:1101-1110(2013). RN [14] RP INTERACTION WITH USP45 AND ERCC4, UBIQUITINATION, AND DEUBIQUITINATION BY RP USP45. RX PubMed=25538220; DOI=10.15252/embj.201489184; RA Perez-Oliva A.B., Lachaud C., Szyniarowski P., Munoz I., Macartney T., RA Hickson I., Rouse J., Alessi D.R.; RT "USP45 deubiquitylase controls ERCC1-XPF endonuclease-mediated DNA damage RT responses."; RL EMBO J. 34:326-343(2015). RN [15] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-21; LYS-37 AND LYS-243, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=28112733; DOI=10.1038/nsmb.3366; RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C., RA Nielsen M.L.; RT "Site-specific mapping of the human SUMO proteome reveals co-modification RT with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(2017). RN [16] RP INTERACTION WITH ERCC4, AND MUTAGENESIS OF ASP-221; LEU-223; MET-224; RP GLU-225; LEU-227 AND GLU-228. RX PubMed=32034146; DOI=10.1038/s41467-020-14564-x; RA Wang J., He H., Chen B., Jiang G., Cao L., Jiang H., Zhang G., Chen J., RA Huang J., Yang B., Zhou C., Liu T.; RT "Acetylation of XPF by TIP60 facilitates XPF-ERCC1 complex assembly and RT activation."; RL Nat. Commun. 11:786-786(2020). RN [17] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 96-227, X-RAY CRYSTALLOGRAPHY (2.7 RP ANGSTROMS) OF 96-220-296 IN COMPLEX WIRH ERCC4, AND SUBUNIT. RX PubMed=16076955; DOI=10.1073/pnas.0504341102; RA Tsodikov O.V., Enzlin J.H., Scharer O.D., Ellenberger T.; RT "Crystal structure and DNA binding functions of ERCC1, a subunit of the DNA RT structure-specific endonuclease XPF-ERCC1."; RL Proc. Natl. Acad. Sci. U.S.A. 102:11236-11241(2005). RN [18] RP STRUCTURE BY NMR OF 220-297 IN COMPLEX WIRH ERCC4, AND SUBUNIT. RX PubMed=16338413; DOI=10.1016/j.str.2005.08.014; RA Tripsianes K., Folkers G., Ab E., Das D., Odijk H., Jaspers N.G., RA Hoeijmakers J.H., Kaptein R., Boelens R.; RT "The structure of the human ERCC1/XPF interaction domains reveals a RT complementary role for the two proteins in nucleotide excision repair."; RL Structure 13:1849-1858(2005). RN [19] RP VARIANT COFS4 LEU-231, CHARACTERIZATION OF VARIANT COFS4 LEU-231, FUNCTION, RP AND SUBUNIT. RX PubMed=17273966; DOI=10.1086/512486; RA Jaspers N.G.J., Raams A., Silengo M.C., Wijgers N., Niedernhofer L.J., RA Robinson A.R., Giglia-Mari G., Hoogstraten D., Kleijer W.J., RA Hoeijmakers J.H.J., Vermeulen W.; RT "First reported patient with human ERCC1 deficiency has cerebro-oculo- RT facio-skeletal syndrome with a mild defect in nucleotide excision repair RT and severe developmental failure."; RL Am. J. Hum. Genet. 80:457-466(2007). RN [20] RP VARIANT COFS4 LEU-231, CHARACTERIZATION OF VARIANT COFS4 LEU-231, FUNCTION, RP AND INTERACTION WITH ERCC4. RX PubMed=23623389; DOI=10.1016/j.ajhg.2013.04.007; RA Kashiyama K., Nakazawa Y., Pilz D.T., Guo C., Shimada M., Sasaki K., RA Fawcett H., Wing J.F., Lewin S.O., Carr L., Li T.S., Yoshiura K., Utani A., RA Hirano A., Yamashita S., Greenblatt D., Nardo T., Stefanini M., RA McGibbon D., Sarkany R., Fassihi H., Takahashi Y., Nagayama Y., RA Mitsutake N., Lehmann A.R., Ogi T.; RT "Malfunction of nuclease ERCC1-XPF results in diverse clinical RT manifestations and causes Cockayne syndrome, xeroderma pigmentosum, and RT Fanconi anemia."; RL Am. J. Hum. Genet. 92:807-819(2013). CC -!- FUNCTION: [Isoform 1]: Non-catalytic component of a structure-specific CC DNA repair endonuclease responsible for the 5'-incision during DNA CC repair. Responsible, in conjunction with SLX4, for the first step in CC the repair of interstrand cross-links (ICL). Participates in the CC processing of anaphase bridge-generating DNA structures, which consist CC in 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. CC {ECO:0000269|PubMed:17273966, ECO:0000269|PubMed:23623389, CC ECO:0000269|PubMed:24036546}. CC -!- FUNCTION: [Isoform 2]: Not functional in the nucleotide excision repair CC pathway. {ECO:0000305|PubMed:24036546}. CC -!- FUNCTION: [Isoform 3]: Not functional in the nucleotide excision repair CC pathway. {ECO:0000305|PubMed:24036546}. CC -!- FUNCTION: [Isoform 4]: Not functional in the nucleotide excision repair CC pathway. {ECO:0000305|PubMed:24036546}. CC -!- SUBUNIT: Heterodimer composed of ERCC1 isoform 1 and ERCC4/XPF CC (PubMed:16076955, PubMed:16338413, PubMed:24036546, PubMed:25538220, CC PubMed:32034146). Interacts with USP45 (PubMed:25538220). CC {ECO:0000269|PubMed:16076955, ECO:0000269|PubMed:16338413, CC ECO:0000269|PubMed:24036546, ECO:0000269|PubMed:25538220, CC ECO:0000269|PubMed:32034146}. CC -!- SUBUNIT: [Isoform 2]: Does not interact with ERCC4/XPF. CC {ECO:0000269|PubMed:24036546}. CC -!- SUBUNIT: [Isoform 3]: Does not interact with ERCC4/XPF. CC {ECO:0000269|PubMed:24036546}. CC -!- SUBUNIT: [Isoform 4]: Does not interact with ERCC4/XPF. CC {ECO:0000269|PubMed:24036546}. CC -!- INTERACTION: CC P07992; P00533: EGFR; NbExp=21; IntAct=EBI-750962, EBI-297353; CC P07992; Q92889: ERCC4; NbExp=13; IntAct=EBI-750962, EBI-2370770; CC P07992; Q13064: MKRN3; NbExp=3; IntAct=EBI-750962, EBI-2340269; CC P07992; Q6NSB6: MKRN3; NbExp=3; IntAct=EBI-750962, EBI-10195599; CC P07992; Q8IY92: SLX4; NbExp=6; IntAct=EBI-750962, EBI-2370740; CC P07992; Q96GJ1: TRMT2B; NbExp=3; IntAct=EBI-750962, EBI-10195625; CC P07992; Q96S82: UBL7; NbExp=4; IntAct=EBI-750962, EBI-348604; CC P07992; Q8N6Y0: USHBP1; NbExp=3; IntAct=EBI-750962, EBI-739895; CC P07992; Q9H9H4: VPS37B; NbExp=4; IntAct=EBI-750962, EBI-4400866; CC P07992; P23025: XPA; NbExp=7; IntAct=EBI-750962, EBI-295222; CC P07992-3; O95995: GAS8; NbExp=3; IntAct=EBI-12699417, EBI-1052570; CC P07992-3; Q96S82: UBL7; NbExp=3; IntAct=EBI-12699417, EBI-348604; CC P07992-3; P23025: XPA; NbExp=3; IntAct=EBI-12699417, EBI-295222; CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Nucleus CC {ECO:0000269|PubMed:24036546}. CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm CC {ECO:0000269|PubMed:24036546}. Nucleus {ECO:0000269|PubMed:24036546}. CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Nucleus CC {ECO:0000269|PubMed:24036546}. CC -!- SUBCELLULAR LOCATION: [Isoform 4]: Nucleus CC {ECO:0000269|PubMed:24036546}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; Synonyms=202; CC IsoId=P07992-1; Sequence=Displayed; CC Name=2; Synonyms=203; CC IsoId=P07992-2; Sequence=VSP_042727; CC Name=3; Synonyms=201; CC IsoId=P07992-3; Sequence=VSP_043455; CC Name=4; Synonyms=204; CC IsoId=P07992-4; Sequence=VSP_053474; CC -!- PTM: Ubiquitinated with both 'Lys-48' and 'Lys-63' linkages CC (PubMed:25538220). Deubiquitinated by USP45 (PubMed:25538220). CC {ECO:0000269|PubMed:25538220}. CC -!- DISEASE: Cerebro-oculo-facio-skeletal syndrome 4 (COFS4) [MIM:610758]: CC A disorder of prenatal onset characterized by microcephaly, congenital CC cataracts, facial dysmorphism, neurogenic arthrogryposis, growth CC failure and severe psychomotor retardation. COFS is considered to be CC part of the nucleotide-excision repair disorders spectrum that include CC also xeroderma pigmentosum, trichothiodystrophy and Cockayne syndrome. CC {ECO:0000269|PubMed:17273966, ECO:0000269|PubMed:23623389}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- SIMILARITY: Belongs to the ERCC1/RAD10/SWI10 family. {ECO:0000305}. CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/40481/ERCC1"; CC -!- WEB RESOURCE: Name=NIEHS-SNPs; CC URL="http://egp.gs.washington.edu/data/ercc1/"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M13194; AAA52394.1; -; mRNA. DR EMBL; M26163; AAA52395.1; -; Genomic_DNA. DR EMBL; M28650; AAA35810.1; -; mRNA. DR EMBL; AF001925; AAC16253.1; -; mRNA. DR EMBL; AB069681; BAB62810.1; -; mRNA. DR EMBL; BT019806; AAV38609.1; -; mRNA. DR EMBL; AF512555; AAM34796.1; -; Genomic_DNA. DR EMBL; AK092039; BAG52472.1; -; mRNA. DR EMBL; AK314884; BAG37398.1; -; mRNA. DR EMBL; AC092309; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC138128; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC138534; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC139353; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471126; EAW57349.1; -; Genomic_DNA. DR EMBL; BC008930; AAH08930.1; -; mRNA. DR EMBL; BC052813; AAH52813.1; -; mRNA. DR CCDS; CCDS12662.1; -. [P07992-1] DR CCDS; CCDS12663.1; -. [P07992-3] DR CCDS; CCDS54279.1; -. [P07992-2] DR PIR; A32875; A24781. DR RefSeq; NP_001159521.1; NM_001166049.1. [P07992-2] DR RefSeq; NP_001974.1; NM_001983.3. [P07992-1] DR RefSeq; NP_973730.1; NM_202001.2. [P07992-3] DR RefSeq; XP_005258691.1; XM_005258634.1. DR RefSeq; XP_005258692.1; XM_005258635.2. DR RefSeq; XP_005258693.1; XM_005258636.4. DR RefSeq; XP_011524912.1; XM_011526610.2. DR RefSeq; XP_016881948.1; XM_017026459.1. DR RefSeq; XP_016881949.1; XM_017026460.1. DR RefSeq; XP_016881950.1; XM_017026461.1. DR RefSeq; XP_016881951.1; XM_017026462.1. DR RefSeq; XP_016881952.1; XM_017026463.1. DR RefSeq; XP_016881953.1; XM_017026464.1. DR RefSeq; XP_016881954.1; XM_017026465.1. DR RefSeq; XP_016881955.1; XM_017026466.1. DR PDB; 1Z00; NMR; -; A=220-297. DR PDB; 2A1I; X-ray; 1.90 A; A=96-227. DR PDB; 2A1J; X-ray; 2.70 A; B=220-296. DR PDB; 2JNW; NMR; -; A=96-214. DR PDB; 2JPD; NMR; -; A=96-219. DR PDB; 2MUT; NMR; -; A=220-297. DR PDB; 6SXA; EM; 3.60 A; G=1-297. DR PDB; 6SXB; EM; 7.90 A; G=1-297. DR PDBsum; 1Z00; -. DR PDBsum; 2A1I; -. DR PDBsum; 2A1J; -. DR PDBsum; 2JNW; -. DR PDBsum; 2JPD; -. DR PDBsum; 2MUT; -. DR PDBsum; 6SXA; -. DR PDBsum; 6SXB; -. DR AlphaFoldDB; P07992; -. DR BMRB; P07992; -. DR EMDB; EMD-10337; -. DR EMDB; EMD-10338; -. DR SMR; P07992; -. DR BioGRID; 108379; 57. DR ComplexPortal; CPX-478; ERCC1-XPF endonuclease complex. [P07992-1] DR CORUM; P07992; -. DR DIP; DIP-24235N; -. DR IntAct; P07992; 27. DR MINT; P07992; -. DR STRING; 9606.ENSP00000013807; -. DR BindingDB; P07992; -. DR ChEMBL; CHEMBL3883316; -. DR iPTMnet; P07992; -. DR PhosphoSitePlus; P07992; -. DR BioMuta; ERCC1; -. DR DMDM; 119538; -. DR EPD; P07992; -. DR jPOST; P07992; -. DR MassIVE; P07992; -. DR MaxQB; P07992; -. DR PaxDb; 9606-ENSP00000013807; -. DR PeptideAtlas; P07992; -. DR ProteomicsDB; 3611; -. DR ProteomicsDB; 52055; -. [P07992-1] DR ProteomicsDB; 52056; -. [P07992-2] DR ProteomicsDB; 52057; -. [P07992-3] DR Pumba; P07992; -. DR Antibodypedia; 3826; 1522 antibodies from 44 providers. DR DNASU; 2067; -. DR Ensembl; ENST00000013807.9; ENSP00000013807.4; ENSG00000012061.17. [P07992-3] DR Ensembl; ENST00000300853.8; ENSP00000300853.3; ENSG00000012061.17. [P07992-1] DR Ensembl; ENST00000340192.11; ENSP00000345203.6; ENSG00000012061.17. [P07992-2] DR Ensembl; ENST00000423698.6; ENSP00000394875.2; ENSG00000012061.17. [P07992-4] DR Ensembl; ENST00000589165.5; ENSP00000468035.1; ENSG00000012061.17. [P07992-1] DR GeneID; 2067; -. DR KEGG; hsa:2067; -. DR MANE-Select; ENST00000300853.8; ENSP00000300853.3; NM_001983.4; NP_001974.1. DR UCSC; uc002pbs.3; human. [P07992-1] DR AGR; HGNC:3433; -. DR CTD; 2067; -. DR DisGeNET; 2067; -. DR GeneCards; ERCC1; -. DR GeneReviews; ERCC1; -. DR HGNC; HGNC:3433; ERCC1. DR HPA; ENSG00000012061; Low tissue specificity. DR MalaCards; ERCC1; -. DR MIM; 126380; gene. DR MIM; 610758; phenotype. DR neXtProt; NX_P07992; -. DR OpenTargets; ENSG00000012061; -. DR Orphanet; 90322; Cockayne syndrome type 2. DR Orphanet; 1466; COFS syndrome. DR PharmGKB; PA155; -. DR VEuPathDB; HostDB:ENSG00000012061; -. DR eggNOG; KOG2841; Eukaryota. DR GeneTree; ENSGT00390000011275; -. DR InParanoid; P07992; -. DR OMA; RPPDLIM; -. DR OrthoDB; 12065at2759; -. DR PhylomeDB; P07992; -. DR TreeFam; TF101231; -. DR PathwayCommons; P07992; -. DR Reactome; R-HSA-5685938; HDR through Single Strand Annealing (SSA). DR Reactome; R-HSA-5696395; Formation of Incision Complex in GG-NER. DR Reactome; R-HSA-5696400; Dual Incision in GG-NER. DR Reactome; R-HSA-6782135; Dual incision in TC-NER. DR Reactome; R-HSA-6783310; Fanconi Anemia Pathway. DR SignaLink; P07992; -. DR SIGNOR; P07992; -. DR BioGRID-ORCS; 2067; 103 hits in 1167 CRISPR screens. DR ChiTaRS; ERCC1; human. DR EvolutionaryTrace; P07992; -. DR GeneWiki; ERCC1; -. DR GenomeRNAi; 2067; -. DR Pharos; P07992; Tbio. DR PRO; PR:P07992; -. DR Proteomes; UP000005640; Chromosome 19. DR RNAct; P07992; Protein. DR Bgee; ENSG00000012061; Expressed in apex of heart and 201 other cell types or tissues. DR ExpressionAtlas; P07992; baseline and differential. DR GO; GO:0000781; C:chromosome, telomeric region; IDA:UniProtKB. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0070522; C:ERCC4-ERCC1 complex; IDA:BHF-UCL. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0000109; C:nucleotide-excision repair complex; IDA:UniProtKB. DR GO; GO:0000110; C:nucleotide-excision repair factor 1 complex; IDA:UniProtKB. DR GO; GO:0003684; F:damaged DNA binding; IDA:UniProtKB. DR GO; GO:1990841; F:promoter-specific chromatin binding; IEA:Ensembl. DR GO; GO:0003697; F:single-stranded DNA binding; IDA:UniProtKB. DR GO; GO:0001094; F:TFIID-class transcription factor complex binding; IEA:Ensembl. DR GO; GO:0008283; P:cell population proliferation; IEA:Ensembl. DR GO; GO:0008340; P:determination of adult lifespan; IEA:Ensembl. DR GO; GO:0006281; P:DNA repair; IMP:MGI. DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IMP:BHF-UCL. DR GO; GO:0048568; P:embryonic organ development; IEA:Ensembl. DR GO; GO:0048009; P:insulin-like growth factor receptor signaling pathway; IEA:Ensembl. DR GO; GO:0036297; P:interstrand cross-link repair; IEA:Ensembl. DR GO; GO:0045190; P:isotype switching; IEA:Ensembl. DR GO; GO:0008584; P:male gonad development; IEA:Ensembl. DR GO; GO:0006312; P:mitotic recombination; IMP:UniProtKB. DR GO; GO:0035264; P:multicellular organism growth; IEA:Ensembl. DR GO; GO:1905765; P:negative regulation of protection from non-homologous end joining at telomere; IMP:BHF-UCL. DR GO; GO:0032205; P:negative regulation of telomere maintenance; IMP:UniProtKB. DR GO; GO:0006289; P:nucleotide-excision repair; IDA:ComplexPortal. DR GO; GO:0048477; P:oogenesis; IEA:Ensembl. DR GO; GO:1904431; P:positive regulation of t-circle formation; ISS:BHF-UCL. DR GO; GO:0060261; P:positive regulation of transcription initiation by RNA polymerase II; IEA:Ensembl. DR GO; GO:0035166; P:post-embryonic hemopoiesis; IEA:Ensembl. DR GO; GO:0000720; P:pyrimidine dimer repair by nucleotide-excision repair; IEA:Ensembl. DR GO; GO:0090399; P:replicative senescence; IEA:Ensembl. 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; IMP:UniProtKB. DR GO; GO:0009744; P:response to sucrose; IEA:Ensembl. DR GO; GO:0010165; P:response to X-ray; IEA:Ensembl. DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl. DR GO; GO:0006949; P:syncytium formation; IEA:Ensembl. DR GO; GO:0090656; P:t-circle formation; ISS:BHF-UCL. DR GO; GO:0061819; P:telomeric DNA-containing double minutes formation; IMP:BHF-UCL. DR GO; GO:0009650; P:UV protection; IEA:Ensembl. DR GO; GO:0070914; P:UV-damage excision repair; IBA:GO_Central. DR CDD; cd22325; ERCC1_C-like; 1. DR Gene3D; 3.40.50.10130; -; 1. DR Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1. DR IDEAL; IID00364; -. DR InterPro; IPR047260; ERCC1-like_central_dom. DR InterPro; IPR004579; ERCC1/RAD10/SWI10. DR InterPro; IPR011335; Restrct_endonuc-II-like. DR InterPro; IPR010994; RuvA_2-like. DR NCBIfam; TIGR00597; rad10; 1. DR PANTHER; PTHR12749:SF0; DNA EXCISION REPAIR PROTEIN ERCC-1; 1. DR PANTHER; PTHR12749; EXCISION REPAIR CROSS-COMPLEMENTING 1 ERCC1; 1. DR Pfam; PF14520; HHH_5; 1. DR Pfam; PF03834; Rad10; 1. DR SUPFAM; SSF52980; Restriction endonuclease-like; 1. DR SUPFAM; SSF47781; RuvA domain 2-like; 1. DR Genevisible; P07992; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Cataract; Cytoplasm; KW DNA damage; DNA repair; DNA-binding; Isopeptide bond; Nucleus; KW Reference proteome; Ubl conjugation. FT CHAIN 1..297 FT /note="DNA excision repair protein ERCC-1" FT /id="PRO_0000087006" FT DNA_BIND 134..156 FT /evidence="ECO:0000255" FT REGION 1..39 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 220..297 FT /note="HhH2, dimerization with ERCC4/XPF" FT /evidence="ECO:0000269|PubMed:16338413" FT MOTIF 17..23 FT /note="Nuclear localization signal" FT /evidence="ECO:0000255" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0007744|PubMed:22814378" FT CROSSLNK 21 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 37 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 243 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VAR_SEQ 36..107 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_053474" FT VAR_SEQ 235..258 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|Ref.4" FT /id="VSP_042727" FT VAR_SEQ 282..297 FT /note="ARRLFDVLHEPFLKVP -> VRALGKNPRSWGKERAPNKHNLRPQSFKVKKE FT PKTRHSGFRL (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_043455" FT VARIANT 231 FT /note="F -> L (in COFS4; does not alter interaction with FT ERCC4/XPF; dbSNP:rs121913028)" FT /evidence="ECO:0000269|PubMed:17273966, FT ECO:0000269|PubMed:23623389" FT /id="VAR_032776" FT VARIANT 266 FT /note="A -> T (in dbSNP:rs3212977)" FT /evidence="ECO:0000269|Ref.5" FT /id="VAR_019167" FT MUTAGEN 221 FT /note="D->A: Impaired interaction with ERCC4." FT /evidence="ECO:0000269|PubMed:32034146" FT MUTAGEN 223 FT /note="L->A: Impaired interaction with ERCC4." FT /evidence="ECO:0000269|PubMed:32034146" FT MUTAGEN 224 FT /note="M->A: Impaired interaction with ERCC4." FT /evidence="ECO:0000269|PubMed:32034146" FT MUTAGEN 225 FT /note="E->A: Impaired interaction with ERCC4." FT /evidence="ECO:0000269|PubMed:32034146" FT MUTAGEN 227 FT /note="L->A: Impaired interaction with ERCC4." FT /evidence="ECO:0000269|PubMed:32034146" FT MUTAGEN 228 FT /note="E->A: Impaired interaction with ERCC4." FT /evidence="ECO:0000269|PubMed:32034146" FT CONFLICT 53 FT /note="A -> P (in Ref. 6; BAG37398)" FT /evidence="ECO:0000305" FT STRAND 101..103 FT /evidence="ECO:0007829|PDB:2A1I" FT HELIX 105..107 FT /evidence="ECO:0007829|PDB:2A1I" FT HELIX 111..115 FT /evidence="ECO:0007829|PDB:2A1I" FT STRAND 121..123 FT /evidence="ECO:0007829|PDB:2A1I" FT STRAND 127..133 FT /evidence="ECO:0007829|PDB:2A1I" FT STRAND 136..142 FT /evidence="ECO:0007829|PDB:2A1I" FT HELIX 143..148 FT /evidence="ECO:0007829|PDB:2A1I" FT HELIX 152..160 FT /evidence="ECO:0007829|PDB:2A1I" FT STRAND 163..172 FT /evidence="ECO:0007829|PDB:2A1I" FT STRAND 175..177 FT /evidence="ECO:0007829|PDB:2A1I" FT HELIX 179..192 FT /evidence="ECO:0007829|PDB:2A1I" FT STRAND 195..201 FT /evidence="ECO:0007829|PDB:2A1I" FT HELIX 202..213 FT /evidence="ECO:0007829|PDB:2A1I" FT HELIX 222..226 FT /evidence="ECO:0007829|PDB:2A1I" FT STRAND 242..244 FT /evidence="ECO:0007829|PDB:1Z00" FT HELIX 247..257 FT /evidence="ECO:0007829|PDB:2A1J" FT HELIX 260..264 FT /evidence="ECO:0007829|PDB:2A1J" FT HELIX 268..272 FT /evidence="ECO:0007829|PDB:2A1J" FT STRAND 274..276 FT /evidence="ECO:0007829|PDB:2A1J" FT HELIX 280..290 FT /evidence="ECO:0007829|PDB:2A1J" FT STRAND 293..295 FT /evidence="ECO:0007829|PDB:1Z00" SQ SEQUENCE 297 AA; 32562 MW; 6FCE3615732349E5 CRC64; MDPGKDKEGV PQPSGPPARK KFVIPLDEDE VPPGVAKPLF RSTQSLPTVD TSAQAAPQTY AEYAISQPLE GAGATCPTGS EPLAGETPNQ ALKPGAKSNS IIVSPRQRGN PVLKFVRNVP WEFGDVIPDY VLGQSTCALF LSLRYHNLHP DYIHGRLQSL GKNFALRVLL VQVDVKDPQQ ALKELAKMCI LADCTLILAW SPEEAGRYLE TYKAYEQKPA DLLMEKLEQD FVSRVTECLT TVKSVNKTDS QTLLTTFGSL EQLIAASRED LALCPGLGPQ KARRLFDVLH EPFLKVP //