ERCC1_HUMAN
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 03-AUG-2022, entry version 207.
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="http://atlasgeneticsoncology.org/Genes/ERCC1ID40481ch19q13.html";
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/ercc1/";
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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 SMR; P07992; -.
DR BioGRID; 108379; 53.
DR ComplexPortal; CPX-478; ERCC1-XPF endonuclease complex. [P07992-1]
DR CORUM; P07992; -.
DR DIP; DIP-24235N; -.
DR IntAct; P07992; 26.
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; P07992; -.
DR PeptideAtlas; P07992; -.
DR PRIDE; P07992; -.
DR ProteomicsDB; 3611; -.
DR ProteomicsDB; 52055; -. [P07992-1]
DR ProteomicsDB; 52056; -. [P07992-2]
DR ProteomicsDB; 52057; -. [P07992-3]
DR Antibodypedia; 3826; 1330 antibodies from 44 providers.
DR DNASU; 2067; -.
DR Ensembl; ENST00000013807.9; ENSP00000013807.4; ENSG00000012061.16. [P07992-3]
DR Ensembl; ENST00000300853.8; ENSP00000300853.3; ENSG00000012061.16. [P07992-1]
DR Ensembl; ENST00000340192.11; ENSP00000345203.6; ENSG00000012061.16. [P07992-2]
DR Ensembl; ENST00000423698.6; ENSP00000394875.2; ENSG00000012061.16. [P07992-4]
DR Ensembl; ENST00000589165.5; ENSP00000468035.1; ENSG00000012061.16. [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 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; LNPDYIC; -.
DR OrthoDB; 1336192at2759; -.
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; 79 hits in 1079 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 199 other tissues.
DR ExpressionAtlas; P07992; baseline and differential.
DR Genevisible; P07992; HS.
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:0008022; F:protein C-terminus binding; IPI:UniProtKB.
DR GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
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:0006310; P:DNA recombination; IGI:MGI.
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: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:0000710; P:meiotic mismatch repair; IBA:GO_Central.
DR GO; GO:0006312; P:mitotic recombination; IMP:UniProtKB.
DR GO; GO:0010259; P:multicellular organism aging; IEA:Ensembl.
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:MGI.
DR GO; GO:0033683; P:nucleotide-excision repair, DNA incision; IDA:ComplexPortal.
DR GO; GO:0006296; P:nucleotide-excision repair, DNA incision, 5'-to lesion; IBA:GO_Central.
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 from RNA polymerase II promoter; 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 IDEAL; IID00364; -.
DR InterPro; IPR004579; ERCC1/RAD10/SWI10.
DR InterPro; IPR011335; Restrct_endonuc-II-like.
DR InterPro; IPR010994; RuvA_2-like.
DR PANTHER; PTHR12749; PTHR12749; 1.
DR Pfam; PF03834; Rad10; 1.
DR SUPFAM; SSF47781; SSF47781; 1.
DR SUPFAM; SSF52980; SSF52980; 1.
DR TIGRFAMs; TIGR00597; rad10; 1.
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
