DNA excision repair protein ERCC-1

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functionⁱ

Regions

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functionⁱ

• damaged DNA binding Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ
  • "Analysis of the XPA and ssDNA-binding surfaces on the central domain of human ERCC1 reveals evidence for subfunctionalization."
    Tripsianes K., Folkers G.E., Zheng C., Das D., Grinstead J.S., Kaptein R., Boelens R.
    Nucleic Acids Res 35:5789-5798(2007) [PubMed] [Europe PMC] [Abstract]
• endonuclease activity Source: UniProtKB-KW
• promoter-specific chromatin binding Source: Ensembl
• protein C-terminus binding Source: UniProtKB <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#ipi">GO evidence code guide</a></p> Inferred from physical interactionⁱ
  • "Mapping of interaction domains between human repair proteins ERCC1 and XPF."
    de Laat W.L., Sijbers A.M., Odijk H., Jaspers N.G., Hoeijmakers J.H.
    Nucleic Acids Res 26:4146-4152(1998) [PubMed] [Europe PMC] [Abstract]
• protein domain specific binding Source: UniProtKBInferred from physical interactionⁱ
  • "Analysis of the XPA and ssDNA-binding surfaces on the central domain of human ERCC1 reveals evidence for subfunctionalization."
    Tripsianes K., Folkers G.E., Zheng C., Das D., Grinstead J.S., Kaptein R., Boelens R.
    Nucleic Acids Res 35:5789-5798(2007) [PubMed] [Europe PMC] [Abstract]
• single-stranded DNA binding Source: UniProtKBInferred from direct assayⁱ
  • Ref.16

    "Crystal structure and DNA binding functions of ERCC1, a subunit of the DNA structure-specific endonuclease XPF-ERCC1."
    Tsodikov O.V., Enzlin J.H., Scharer O.D., Ellenberger T.
    Proc. Natl. Acad. Sci. U.S.A. 102:11236-11241(2005) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 96-227, X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 96-220-296 IN COMPLEX WIRH ERCC4, SUBUNIT.
  • "Analysis of the XPA and ssDNA-binding surfaces on the central domain of human ERCC1 reveals evidence for subfunctionalization."
    Tripsianes K., Folkers G.E., Zheng C., Das D., Grinstead J.S., Kaptein R., Boelens R.
    Nucleic Acids Res 35:5789-5798(2007) [PubMed] [Europe PMC] [Abstract]
• TFIID-class transcription factor complex binding Source: Ensembl

GO - Biological processⁱ

• cell population proliferation Source: Ensembl
• DNA recombination Source: MGI <p>Inferred from Genetic Interaction</p> <p>Used to describe "traditional" genetic interactions such as suppressors and synthetic lethals as well as other techniques such as functional complementation, rescue experiments, or inferences about a gene drawn from the phenotype of a mutation in a different gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#igi">GO evidence code guide</a></p> Inferred from genetic interactionⁱ
  • "The structure-specific endonuclease Ercc1-Xpf is required for targeted gene replacement in embryonic stem cells."
    Niedernhofer L.J., Essers J., Weeda G., Beverloo B., de Wit J., Muijtjens M., Odijk H., Hoeijmakers J.H., Kanaar R.
    EMBO J 20:6540-6549(2001) [PubMed] [Europe PMC] [Abstract]
• DNA repair Source: MGI <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypeⁱ
  • Ref.14

    "USP45 deubiquitylase controls ERCC1-XPF endonuclease-mediated DNA damage responses."
    Perez-Oliva A.B., Lachaud C., Szyniarowski P., Munoz I., Macartney T., Hickson I., Rouse J., Alessi D.R.
    EMBO J. 34:326-343(2015) [PubMed] [Europe PMC] [Abstract]

    Cited for: INTERACTION WITH USP45 AND ERCC4, UBIQUITINATION, DEUBIQUITINATION BY USP45.
• double-strand break repair via nonhomologous end joining Source: BHF-UCLInferred from mutant phenotypeⁱ
  • "ERCC1/XPF removes the 3' overhang from uncapped telomeres and represses formation of telomeric DNA-containing double minute chromosomes."
    Zhu X.D., Niedernhofer L., Kuster B., Mann M., Hoeijmakers J.H., de Lange T.
    Mol Cell 12:1489-1498(2003) [PubMed] [Europe PMC] [Abstract]
• embryonic organ development Source: Ensembl
• global genome nucleotide-excision repair Source: Reactome
• interstrand cross-link repair Source: Reactome
• isotype switching Source: Ensembl
• male gonad development Source: Ensembl
• meiotic mismatch repair Source: GO_Central <p>Inferred from Biological aspect of Ancestor</p> <p>A type of phylogenetic evidence whereby an aspect of a descendent is inferred through the characterization of an aspect of a ancestral gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#iba">GO evidence code guide</a></p> Inferred from biological aspect of ancestorⁱ
  • "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
    Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
    Brief Bioinform 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
• mitotic recombination Source: UniProtKBInferred from mutant phenotypeⁱ
  • "Mutational analysis of the human nucleotide excision repair gene ERCC1."
    Sijbers A.M., van der Spek P.J., Odijk H., van den Berg J., van Duin M., Westerveld A., Jaspers N.G., Bootsma D., Hoeijmakers J.H.
    Nucleic Acids Res 24:3370-3380(1996) [PubMed] [Europe PMC] [Abstract]
• multicellular organism aging Source: Ensembl
• multicellular organism growth Source: Ensembl
• negative regulation of protection from non-homologous end joining at telomere Source: BHF-UCLInferred from mutant phenotypeⁱ
  • "ERCC1/XPF removes the 3' overhang from uncapped telomeres and represses formation of telomeric DNA-containing double minute chromosomes."
    Zhu X.D., Niedernhofer L., Kuster B., Mann M., Hoeijmakers J.H., de Lange T.
    Mol Cell 12:1489-1498(2003) [PubMed] [Europe PMC] [Abstract]
• negative regulation of telomere maintenance Source: UniProtKBInferred from mutant phenotypeⁱ
  • "XPF with mutations in its conserved nuclease domain is defective in DNA repair but functions in TRF2-mediated telomere shortening."
    Wu Y., Zacal N.J., Rainbow A.J., Zhu X.D.
    DNA Repair (Amst) 6:157-166(2007) [PubMed] [Europe PMC] [Abstract]
• nucleotide-excision repair Source: MGIInferred from direct assayⁱ
  • "Evolution and mutagenesis of the mammalian excision repair gene ERCC-1."
    van Duin M., van den Tol J., Warmerdam P., Odijk H., Meijer D., Westerveld A., Hoeijmakers J.H.J.
    Nucleic Acids Res. 16:5305-5322(1988) [PubMed] [Europe PMC] [Abstract]
• nucleotide-excision repair, DNA incision Source: Reactome
• nucleotide-excision repair, DNA incision, 3'-to lesion Source: UniProtKBInferred from mutant phenotypeⁱ
  • "Human DNA repair excision nuclease. Analysis of the roles of the subunits involved in dual incisions by using anti-XPG and anti-ERCC1 antibodies."
    Matsunaga T., Mu D., Park C.H., Reardon J.T., Sancar A.
    J Biol Chem 270:20862-20869(1995) [PubMed] [Europe PMC] [Abstract]
• nucleotide-excision repair, DNA incision, 5'-to lesion Source: UniProtKBInferred from mutant phenotypeⁱ
  • "Human DNA repair excision nuclease. Analysis of the roles of the subunits involved in dual incisions by using anti-XPG and anti-ERCC1 antibodies."
    Matsunaga T., Mu D., Park C.H., Reardon J.T., Sancar A.
    J Biol Chem 270:20862-20869(1995) [PubMed] [Europe PMC] [Abstract]
• nucleotide-excision repair, preincision complex stabilization Source: Reactome
• oogenesis Source: Ensembl
• positive regulation of t-circle formation Source: BHF-UCL
• positive regulation of transcription initiation from RNA polymerase II promoter Source: Ensembl
• post-embryonic hemopoiesis Source: Ensembl
• pyrimidine dimer repair by nucleotide-excision repair Source: Ensembl
• replicative senescence Source: Ensembl
• response to cadmium ion Source: Ensembl
• response to immobilization stress Source: Ensembl
• response to nutrient Source: Ensembl
• response to oxidative stress Source: UniProtKBInferred from mutant phenotypeⁱ
  • "Genetic susceptibility of newborn daughters to oxidative stress."
    Decordier I., De Bont K., De Bock K., Mateuca R., Roelants M., Ciardelli R., Haumont D., Knudsen L.E., Kirsch-Volders M.
    Toxicol Lett 172:68-84(2007) [PubMed] [Europe PMC] [Abstract]
  • "In vitro repair of oxidative DNA damage by human nucleotide excision repair system: possible explanation for neurodegeneration in xeroderma pigmentosum patients."
    Reardon J.T., Bessho T., Kung H.C., Bolton P.H., Sancar A.
    Proc Natl Acad Sci U S A 94:9463-9468(1997) [PubMed] [Europe PMC] [Abstract]
• response to sucrose Source: Ensembl
• response to X-ray Source: Ensembl
• spermatogenesis Source: Ensembl
• syncytium formation Source: Ensembl
• t-circle formation Source: BHF-UCL
• telomeric DNA-containing double minutes formation Source: BHF-UCLInferred from mutant phenotypeⁱ
  • "ERCC1/XPF removes the 3' overhang from uncapped telomeres and represses formation of telomeric DNA-containing double minute chromosomes."
    Zhu X.D., Niedernhofer L., Kuster B., Mann M., Hoeijmakers J.H., de Lange T.
    Mol Cell 12:1489-1498(2003) [PubMed] [Europe PMC] [Abstract]
• transcription-coupled nucleotide-excision repair Source: Reactome
• UV-damage excision repair Source: GO_CentralInferred from biological aspect of ancestorⁱ
  • "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
    Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
    Brief Bioinform 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
• UV protection Source: Ensembl

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsⁱ

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyⁱ

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationⁱ

Keywords - Cellular componentⁱ

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechⁱ

<p>This subsection of the 'Pathology and Biotech' section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseaseⁱ

Keywords - Diseaseⁱ

Organism-specific databases

Miscellaneous databases

Chemistry databases

Genetic variation databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingⁱ

Molecule processing

Amino acid modifications

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationⁱ

Keywords - PTMⁱ

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressionⁱ

Gene expression databases

Organism-specific databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactionⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structureⁱ

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsⁱ

GO - Molecular functionⁱ

• protein C-terminus binding Source: UniProtKBInferred from physical interactionⁱ
  • "Mapping of interaction domains between human repair proteins ERCC1 and XPF."
    de Laat W.L., Sijbers A.M., Odijk H., Jaspers N.G., Hoeijmakers J.H.
    Nucleic Acids Res 26:4146-4152(1998) [PubMed] [Europe PMC] [Abstract]
• protein domain specific binding Source: UniProtKBInferred from physical interactionⁱ
  • "Analysis of the XPA and ssDNA-binding surfaces on the central domain of human ERCC1 reveals evidence for subfunctionalization."
    Tripsianes K., Folkers G.E., Zheng C., Das D., Grinstead J.S., Kaptein R., Boelens R.
    Nucleic Acids Res 35:5789-5798(2007) [PubMed] [Europe PMC] [Abstract]
• TFIID-class transcription factor complex binding Source: Ensembl

Protein-protein interaction databases

Miscellaneous databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structureⁱ

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsⁱ

Region

Motif

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesⁱ

Phylogenomic databases

Family and domain databases

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (4+)ⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusⁱ: Complete.

This entry has 4 described isoforms and 8 potential isoforms that are computationally mapped.Show allAlign All

        10         20         30         40         50
MDPGKDKEGV PQPSGPPARK KFVIPLDEDE VPPGVAKPLF RSTQSLPTVD 
        60         70         80         90        100
TSAQAAPQTY AEYAISQPLE GAGATCPTGS EPLAGETPNQ ALKPGAKSNS 
       110        120        130        140        150
IIVSPRQRGN PVLKFVRNVP WEFGDVIPDY VLGQSTCALF LSLRYHNLHP 
       160        170        180        190        200
DYIHGRLQSL GKNFALRVLL VQVDVKDPQQ ALKELAKMCI LADCTLILAW 
       210        220        230        240        250
SPEEAGRYLE TYKAYEQKPA DLLMEKLEQD FVSRVTECLT TVKSVNKTDS 
       260        270        280        290 
QTLLTTFGSL EQLIAASRED LALCPGLGPQ KARRLFDVLH EPFLKVP    

        10         20         30         40         50
MDPGKDKEGV PQPSGPPARK KFVIPLDEDE VPPGVAKPLF RSTQSLPTVD 
        60         70         80         90        100
TSAQAAPQTY AEYAISQPLE GAGATCPTGS EPLAGETPNQ ALKPGAKSNS 
       110        120        130        140        150
IIVSPRQRGN PVLKFVRNVP WEFGDVIPDY VLGQSTCALF LSLRYHNLHP 
       160        170        180        190        200
DYIHGRLQSL GKNFALRVLL VQVDVKDPQQ ALKELAKMCI LADCTLILAW 
       210        220        230        240        250
SPEEAGRYLE TYKAYEQKPA DLLMEKLEQD FVSRSLEQLI AASREDLALC 
       260        270 
PGLGPQKARR LFDVLHEPFL KVP                              

        10         20         30         40         50
MDPGKDKEGV PQPSGPPARK KFVIPLDEDE VPPGVAKPLF RSTQSLPTVD 
        60         70         80         90        100
TSAQAAPQTY AEYAISQPLE GAGATCPTGS EPLAGETPNQ ALKPGAKSNS 
       110        120        130        140        150
IIVSPRQRGN PVLKFVRNVP WEFGDVIPDY VLGQSTCALF LSLRYHNLHP 
       160        170        180        190        200
DYIHGRLQSL GKNFALRVLL VQVDVKDPQQ ALKELAKMCI LADCTLILAW 
       210        220        230        240        250
SPEEAGRYLE TYKAYEQKPA DLLMEKLEQD FVSRVTECLT TVKSVNKTDS 
       260        270        280        290        300
QTLLTTFGSL EQLIAASRED LALCPGLGPQ KVRALGKNPR SWGKERAPNK 
       310        320 
HNLRPQSFKV KKEPKTRHSG FRL                              

        10         20         30         40         50
MDPGKDKEGV PQPSGPPARK KFVIPLDEDE VPPGVRGNPV LKFVRNVPWE 
        60         70         80         90        100
FGDVIPDYVL GQSTCALFLS LRYHNLHPDY IHGRLQSLGK NFALRVLLVQ 
       110        120        130        140        150
VDVKDPQQAL KELAKMCILA DCTLILAWSP EEAGRYLETY KAYEQKPADL 
       160        170        180        190        200
LMEKLEQDFV SRVTECLTTV KSVNKTDSQT LLTTFGSLEQ LIAASREDLA 
       210        220 
LCPGLGPQKA RRLFDVLHEP FLKVP                            

Experimental Info

Natural variant

Alternative sequence

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityⁱ

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsⁱ

• 100% Identity
• 90% Identity
• 50% Identity

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesⁱ

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross%5Freferences%5Fsection">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesⁱ

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

PTM databases

Genetic variation databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationⁱ

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousⁱ

Keywords - Technical termⁱ

Documents

1. Human variants curated from literature reports
   Index of human variants curated from literature reports
2. MIM cross-references
   Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
3. PDB cross-references
   Index of Protein Data Bank (PDB) cross-references
4. SIMILARITY comments
   Index of protein domains and families
5. Human chromosome 19
   Human chromosome 19: entries, gene names and cross-references to MIM
6. Human entries with genetic variants
   List of human entries with genetic variants