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P07992

- ERCC1_HUMAN

UniProt

P07992 - ERCC1_HUMAN

Protein

DNA excision repair protein ERCC-1

Gene

ERCC1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 151 (01 Oct 2014)
      Sequence version 1 (01 Aug 1988)
      Previous versions | rss
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    Functioni

    Isoform 1: Non-catalytic component of a structure-specific DNA repair endonuclease responsible for the 5'-incision during DNA repair. Responsible, in conjunction with SLX4, for the first step in the repair of interstrand cross-links (ICL). Participates in the processing of anaphase bridge-generating DNA structures, which consist in incompletely processed DNA lesions arising during S or G2 phase, and can result in cytokinesis failure. Also required for homology-directed repair (HDR) of DNA double-strand breaks, in conjunction with SLX4.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    DNA bindingi134 – 15623Sequence AnalysisAdd
    BLAST

    GO - Molecular functioni

    1. damaged DNA binding Source: UniProtKB
    2. endonuclease activity Source: UniProtKB-KW
    3. protein binding Source: UniProtKB
    4. protein C-terminus binding Source: UniProtKB
    5. protein domain specific binding Source: UniProtKB
    6. single-stranded DNA binding Source: UniProtKB

    GO - Biological processi

    1. cell proliferation Source: Ensembl
    2. chromosome organization Source: Ensembl
    3. DNA catabolic process, endonucleolytic Source: GOC
    4. DNA recombination Source: MGI
    5. DNA repair Source: Reactome
    6. double-strand break repair Source: Ensembl
    7. embryonic organ development Source: Ensembl
    8. isotype switching Source: Ensembl
    9. male gonad development Source: Ensembl
    10. mitotic recombination Source: UniProtKB
    11. multicellular organismal aging Source: Ensembl
    12. multicellular organism growth Source: Ensembl
    13. negative regulation of telomere maintenance Source: UniProtKB
    14. nucleotide-excision repair Source: MGI
    15. nucleotide-excision repair, DNA damage removal Source: Reactome
    16. nucleotide-excision repair, DNA incision, 3'-to lesion Source: UniProtKB
    17. nucleotide-excision repair, DNA incision, 5'-to lesion Source: UniProtKB
    18. oogenesis Source: Ensembl
    19. post-embryonic hemopoiesis Source: Ensembl
    20. pyrimidine dimer repair by nucleotide-excision repair Source: Ensembl
    21. replicative cell aging Source: Ensembl
    22. response to nutrient Source: Ensembl
    23. response to oxidative stress Source: UniProtKB
    24. response to sucrose Source: Ensembl
    25. response to X-ray Source: Ensembl
    26. spermatogenesis Source: Ensembl
    27. syncytium formation Source: Ensembl
    28. transcription-coupled nucleotide-excision repair Source: Reactome
    29. UV protection Source: Ensembl

    Keywords - Molecular functioni

    Endonuclease, Hydrolase, Nuclease

    Keywords - Biological processi

    DNA damage, DNA repair

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_1941. Formation of transcription-coupled NER (TC-NER) repair complex.
    REACT_2222. Dual incision reaction in TC-NER.
    REACT_257. Formation of incision complex in GG-NER.
    REACT_311. Dual incision reaction in GG-NER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    DNA excision repair protein ERCC-1
    Gene namesi
    Name:ERCC1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:3433. ERCC1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. nuclear chromosome, telomeric region Source: UniProtKB
    3. nucleoplasm Source: Reactome
    4. nucleotide-excision repair complex Source: UniProtKB
    5. nucleus Source: HPA
    6. transcription factor TFIID complex Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Cerebro-oculo-facio-skeletal syndrome 4 (COFS4) [MIM:610758]: A disorder of prenatal onset characterized by microcephaly, congenital cataracts, facial dysmorphism, neurogenic arthrogryposis, growth failure and severe psychomotor retardation. COFS is considered to be part of the nucleotide-excision repair disorders spectrum that include also xeroderma pigmentosum, trichothiodystrophy and Cockayne syndrome.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti231 – 2311F → L in COFS4; does not alter interaction with XPF/ERCC4 or GTF2H1. 2 Publications
    VAR_032776

    Keywords - Diseasei

    Cataract

    Organism-specific databases

    MIMi610758. phenotype.
    Orphaneti90322. Cockayne syndrome type 2.
    1466. COFS syndrome.
    PharmGKBiPA155.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 297297DNA excision repair protein ERCC-1PRO_0000087006Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP07992.
    PaxDbiP07992.
    PRIDEiP07992.

    PTM databases

    PhosphoSiteiP07992.

    Expressioni

    Gene expression databases

    ArrayExpressiP07992.
    BgeeiP07992.
    CleanExiHS_ERCC1.
    GenevestigatoriP07992.

    Organism-specific databases

    HPAiCAB004390.
    HPA029773.
    HPA050182.

    Interactioni

    Subunit structurei

    Heterodimer composed of ERCC1 isoform 1 and XPF/ERRC4.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    SLX4Q8IY926EBI-750962,EBI-2370740

    Protein-protein interaction databases

    BioGridi108379. 16 interactions.
    DIPiDIP-24235N.
    IntActiP07992. 7 interactions.
    MINTiMINT-1457664.
    STRINGi9606.ENSP00000013807.

    Structurei

    Secondary structure

    1
    297
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi101 – 1033
    Helixi105 – 1073
    Helixi111 – 1155
    Beta strandi121 – 1233
    Beta strandi127 – 1337
    Beta strandi136 – 1427
    Helixi143 – 1486
    Helixi152 – 1609
    Beta strandi163 – 17210
    Beta strandi175 – 1773
    Helixi179 – 19214
    Beta strandi195 – 2017
    Helixi202 – 21312
    Helixi222 – 2265
    Beta strandi242 – 2443
    Helixi247 – 25711
    Helixi260 – 2645
    Helixi268 – 2725
    Beta strandi274 – 2763
    Helixi280 – 29011
    Beta strandi293 – 2953

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1Z00NMR-A220-297[»]
    2A1IX-ray1.90A96-227[»]
    2A1JX-ray2.70B220-296[»]
    2JNWNMR-A96-214[»]
    2JPDNMR-A96-219[»]
    ProteinModelPortaliP07992.
    SMRiP07992. Positions 99-297.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP07992.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni220 – 29778HhH2, dimerization with ERCC4Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi17 – 237Nuclear localization signalSequence Analysis

    Sequence similaritiesi

    Belongs to the ERCC1/RAD10/SWI10 family.Curated

    Phylogenomic databases

    eggNOGiCOG5241.
    HOGENOMiHOG000037440.
    HOVERGENiHBG051497.
    KOiK10849.
    OMAiHPDYIHQ.
    OrthoDBiEOG7XH6Q8.
    PhylomeDBiP07992.
    TreeFamiTF101231.

    Family and domain databases

    InterProiIPR004579. DNA_repair_Rad10.
    IPR000445. HhH_motif.
    IPR003583. Hlx-hairpin-Hlx_DNA-bd_motif.
    IPR011335. Restrct_endonuc-II-like.
    IPR010994. RuvA_2-like.
    [Graphical view]
    PfamiPF00633. HHH. 1 hit.
    PF03834. Rad10. 1 hit.
    [Graphical view]
    ProDomiPD013585. DNA_repair_Rad10. 1 hit.
    [Graphical view] [Entries sharing at least one domain]
    SMARTiSM00278. HhH1. 1 hit.
    [Graphical view]
    SUPFAMiSSF47781. SSF47781. 1 hit.
    SSF52980. SSF52980. 1 hit.
    TIGRFAMsiTIGR00597. rad10. 1 hit.

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P07992-1) [UniParc]FASTAAdd to Basket

    Also known as: 202

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MDPGKDKEGV PQPSGPPARK KFVIPLDEDE VPPGVAKPLF RSTQSLPTVD    50
    TSAQAAPQTY AEYAISQPLE GAGATCPTGS EPLAGETPNQ ALKPGAKSNS 100
    IIVSPRQRGN PVLKFVRNVP WEFGDVIPDY VLGQSTCALF LSLRYHNLHP 150
    DYIHGRLQSL GKNFALRVLL VQVDVKDPQQ ALKELAKMCI LADCTLILAW 200
    SPEEAGRYLE TYKAYEQKPA DLLMEKLEQD FVSRVTECLT TVKSVNKTDS 250
    QTLLTTFGSL EQLIAASRED LALCPGLGPQ KARRLFDVLH EPFLKVP 297
    Length:297
    Mass (Da):32,562
    Last modified:August 1, 1988 - v1
    Checksum:i6FCE3615732349E5
    GO
    Isoform 2 (identifier: P07992-2) [UniParc]FASTAAdd to Basket

    Also known as: 203

    The sequence of this isoform differs from the canonical sequence as follows:
         235-258: Missing.

    Note: Not functional in the nucleotide excision repair pathway. Does not interact with XPF/ERCC4.

    Show »
    Length:273
    Mass (Da):29,993
    Checksum:i04DA21E774A33524
    GO
    Isoform 3 (identifier: P07992-3) [UniParc]FASTAAdd to Basket

    Also known as: 201

    The sequence of this isoform differs from the canonical sequence as follows:
         282-297: ARRLFDVLHEPFLKVP → VRALGKNPRSWGKERAPNKHNLRPQSFKVKKEPKTRHSGFRL

    Note: Not functional in the nucleotide excision repair pathway. Does not interact with XPF/ERCC4.

    Show »
    Length:323
    Mass (Da):35,563
    Checksum:iD99BFAC9CE8E912E
    GO
    Isoform 4 (identifier: P07992-4) [UniParc]FASTAAdd to Basket

    Also known as: 204

    The sequence of this isoform differs from the canonical sequence as follows:
         36-107: Missing.

    Note: Not functional in the nucleotide excision repair pathway. Does not interact with XPF/ERCC4.

    Show »
    Length:225
    Mass (Da):25,211
    Checksum:iAF78F4C26AC7DA7E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti53 – 531A → P in BAG37398. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti231 – 2311F → L in COFS4; does not alter interaction with XPF/ERCC4 or GTF2H1. 2 Publications
    VAR_032776
    Natural varianti266 – 2661A → T.1 Publication
    Corresponds to variant rs3212977 [ dbSNP | Ensembl ].
    VAR_019167

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei36 – 10772Missing in isoform 4. 1 PublicationVSP_053474Add
    BLAST
    Alternative sequencei235 – 25824Missing in isoform 2. 1 PublicationVSP_042727Add
    BLAST
    Alternative sequencei282 – 29716ARRLF…FLKVP → VRALGKNPRSWGKERAPNKH NLRPQSFKVKKEPKTRHSGF RL in isoform 3. 1 PublicationVSP_043455Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M13194 mRNA. Translation: AAA52394.1.
    M26163 Genomic DNA. Translation: AAA52395.1.
    M28650 mRNA. Translation: AAA35810.1.
    AF001925 mRNA. Translation: AAC16253.1.
    AB069681 mRNA. Translation: BAB62810.1.
    BT019806 mRNA. Translation: AAV38609.1.
    AF512555 Genomic DNA. Translation: AAM34796.1.
    AK092039 mRNA. Translation: BAG52472.1.
    AK314884 mRNA. Translation: BAG37398.1.
    AC092309 Genomic DNA. No translation available.
    AC138128 Genomic DNA. No translation available.
    AC138534 Genomic DNA. No translation available.
    AC139353 Genomic DNA. No translation available.
    CH471126 Genomic DNA. Translation: EAW57349.1.
    BC008930 mRNA. Translation: AAH08930.1.
    BC052813 mRNA. Translation: AAH52813.1.
    CCDSiCCDS12662.1. [P07992-1]
    CCDS12663.1. [P07992-3]
    CCDS54279.1. [P07992-2]
    PIRiA32875. A24781.
    RefSeqiNP_001159521.1. NM_001166049.1. [P07992-2]
    NP_001974.1. NM_001983.3. [P07992-1]
    NP_973730.1. NM_202001.2. [P07992-3]
    XP_005258691.1. XM_005258634.1. [P07992-3]
    XP_005258692.1. XM_005258635.1. [P07992-3]
    XP_005258693.1. XM_005258636.2. [P07992-3]
    UniGeneiHs.435981.

    Genome annotation databases

    EnsembliENST00000013807; ENSP00000013807; ENSG00000012061. [P07992-3]
    ENST00000300853; ENSP00000300853; ENSG00000012061. [P07992-1]
    ENST00000340192; ENSP00000345203; ENSG00000012061. [P07992-2]
    ENST00000423698; ENSP00000394875; ENSG00000012061. [P07992-4]
    ENST00000589165; ENSP00000468035; ENSG00000012061. [P07992-1]
    GeneIDi2067.
    KEGGihsa:2067.
    UCSCiuc002pbs.2. human. [P07992-1]
    uc002pbt.2. human. [P07992-2]
    uc002pbu.2. human.
    uc002pbv.3. human. [P07992-3]

    Polymorphism databases

    DMDMi119538.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology
    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M13194 mRNA. Translation: AAA52394.1 .
    M26163 Genomic DNA. Translation: AAA52395.1 .
    M28650 mRNA. Translation: AAA35810.1 .
    AF001925 mRNA. Translation: AAC16253.1 .
    AB069681 mRNA. Translation: BAB62810.1 .
    BT019806 mRNA. Translation: AAV38609.1 .
    AF512555 Genomic DNA. Translation: AAM34796.1 .
    AK092039 mRNA. Translation: BAG52472.1 .
    AK314884 mRNA. Translation: BAG37398.1 .
    AC092309 Genomic DNA. No translation available.
    AC138128 Genomic DNA. No translation available.
    AC138534 Genomic DNA. No translation available.
    AC139353 Genomic DNA. No translation available.
    CH471126 Genomic DNA. Translation: EAW57349.1 .
    BC008930 mRNA. Translation: AAH08930.1 .
    BC052813 mRNA. Translation: AAH52813.1 .
    CCDSi CCDS12662.1. [P07992-1 ]
    CCDS12663.1. [P07992-3 ]
    CCDS54279.1. [P07992-2 ]
    PIRi A32875. A24781.
    RefSeqi NP_001159521.1. NM_001166049.1. [P07992-2 ]
    NP_001974.1. NM_001983.3. [P07992-1 ]
    NP_973730.1. NM_202001.2. [P07992-3 ]
    XP_005258691.1. XM_005258634.1. [P07992-3 ]
    XP_005258692.1. XM_005258635.1. [P07992-3 ]
    XP_005258693.1. XM_005258636.2. [P07992-3 ]
    UniGenei Hs.435981.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1Z00 NMR - A 220-297 [» ]
    2A1I X-ray 1.90 A 96-227 [» ]
    2A1J X-ray 2.70 B 220-296 [» ]
    2JNW NMR - A 96-214 [» ]
    2JPD NMR - A 96-219 [» ]
    ProteinModelPortali P07992.
    SMRi P07992. Positions 99-297.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108379. 16 interactions.
    DIPi DIP-24235N.
    IntActi P07992. 7 interactions.
    MINTi MINT-1457664.
    STRINGi 9606.ENSP00000013807.

    PTM databases

    PhosphoSitei P07992.

    Polymorphism databases

    DMDMi 119538.

    Proteomic databases

    MaxQBi P07992.
    PaxDbi P07992.
    PRIDEi P07992.

    Protocols and materials databases

    DNASUi 2067.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000013807 ; ENSP00000013807 ; ENSG00000012061 . [P07992-3 ]
    ENST00000300853 ; ENSP00000300853 ; ENSG00000012061 . [P07992-1 ]
    ENST00000340192 ; ENSP00000345203 ; ENSG00000012061 . [P07992-2 ]
    ENST00000423698 ; ENSP00000394875 ; ENSG00000012061 . [P07992-4 ]
    ENST00000589165 ; ENSP00000468035 ; ENSG00000012061 . [P07992-1 ]
    GeneIDi 2067.
    KEGGi hsa:2067.
    UCSCi uc002pbs.2. human. [P07992-1 ]
    uc002pbt.2. human. [P07992-2 ]
    uc002pbu.2. human.
    uc002pbv.3. human. [P07992-3 ]

    Organism-specific databases

    CTDi 2067.
    GeneCardsi GC19M045912.
    GeneReviewsi ERCC1.
    HGNCi HGNC:3433. ERCC1.
    HPAi CAB004390.
    HPA029773.
    HPA050182.
    MIMi 126380. gene.
    610758. phenotype.
    neXtProti NX_P07992.
    Orphaneti 90322. Cockayne syndrome type 2.
    1466. COFS syndrome.
    PharmGKBi PA155.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5241.
    HOGENOMi HOG000037440.
    HOVERGENi HBG051497.
    KOi K10849.
    OMAi HPDYIHQ.
    OrthoDBi EOG7XH6Q8.
    PhylomeDBi P07992.
    TreeFami TF101231.

    Enzyme and pathway databases

    Reactomei REACT_1941. Formation of transcription-coupled NER (TC-NER) repair complex.
    REACT_2222. Dual incision reaction in TC-NER.
    REACT_257. Formation of incision complex in GG-NER.
    REACT_311. Dual incision reaction in GG-NER.

    Miscellaneous databases

    ChiTaRSi ERCC1. human.
    EvolutionaryTracei P07992.
    GeneWikii ERCC1.
    GenomeRNAii 2067.
    NextBioi 35469580.
    PROi P07992.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P07992.
    Bgeei P07992.
    CleanExi HS_ERCC1.
    Genevestigatori P07992.

    Family and domain databases

    InterProi IPR004579. DNA_repair_Rad10.
    IPR000445. HhH_motif.
    IPR003583. Hlx-hairpin-Hlx_DNA-bd_motif.
    IPR011335. Restrct_endonuc-II-like.
    IPR010994. RuvA_2-like.
    [Graphical view ]
    Pfami PF00633. HHH. 1 hit.
    PF03834. Rad10. 1 hit.
    [Graphical view ]
    ProDomi PD013585. DNA_repair_Rad10. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    SMARTi SM00278. HhH1. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47781. SSF47781. 1 hit.
    SSF52980. SSF52980. 1 hit.
    TIGRFAMsi TIGR00597. rad10. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Molecular characterization of the human excision repair gene ERCC-1: cDNA cloning and amino acid homology with the yeast DNA repair gene RAD10."
      van Duin M., de Wit J., Odijk H., Westerveld A., Yasui A., Koken M.H.M., Hoeijmakers J.H.J., Bootsma D.
      Cell 44:913-923(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Identification of DNA repair genes in the human genome."
      Hoeijmakers J.H.J., van Duin M., Westerveld A., Yasui A., Bootsma D.
      Cold Spring Harb. Symp. Quant. Biol. 51:91-101(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "A nucleotide polymorphism in ERCC1 in human ovarian cancer cell lines and tumor tissues."
      Yu J.J., Mu C.J., Lee K.B., Okamoto A., Reed E.L., Bostick-Bruton F., Mitchell K.C., Reed E.
      Mutat. Res. 382:13-20(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    4. "Human excision repair protein 1, transcript variant, mRNA."
      Hisatomi H., Nagao K., Ishikawa H., Yokoyama Y., Ishihara Y., Hikiji K., Iizuka T.
      Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    5. NIEHS SNPs program
      Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT THR-266.
    6. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
      Tissue: Cerebellum.
    7. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    8. "The DNA sequence and biology of human chromosome 19."
      Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
      , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
      Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    10. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
      Tissue: Lung and Uterus.
    11. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "ERCC1 function in nuclear excision and interstrand crosslink repair pathways is mediated exclusively by the ERCC1-202 isoform."
      Friboulet L., Postel-Vinay S., Sourisseau T., Adam J., Stoclin A., Ponsonnailles F., Dorvault N., Commo F., Saulnier P., Salome-Desmoulez S., Pottier G., Andre F., Kroemer G., Soria J.C., Olaussen K.A.
      Cell Cycle 12:3298-3306(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION (ISOFORM 1), SUBCELLULAR LOCATION, SUBUNIT.
    13. Cited for: ALTERNATIVE SPLICING.
    14. "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.
    15. "The structure of the human ERCC1/XPF interaction domains reveals a complementary role for the two proteins in nucleotide excision repair."
      Tripsianes K., Folkers G., Ab E., Das D., Odijk H., Jaspers N.G., Hoeijmakers J.H., Kaptein R., Boelens R.
      Structure 13:1849-1858(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 220-297 IN COMPLEX WIRH ERCC4, SUBUNIT.
    16. "First reported patient with human ERCC1 deficiency has cerebro-oculo-facio-skeletal syndrome with a mild defect in nucleotide excision repair and severe developmental failure."
      Jaspers N.G.J., Raams A., Silengo M.C., Wijgers N., Niedernhofer L.J., Robinson A.R., Giglia-Mari G., Hoogstraten D., Kleijer W.J., Hoeijmakers J.H.J., Vermeulen W.
      Am. J. Hum. Genet. 80:457-466(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT COFS4 LEU-231.
    17. "Malfunction of nuclease ERCC1-XPF results in diverse clinical manifestations and causes Cockayne syndrome, xeroderma pigmentosum, and Fanconi anemia."
      Kashiyama K., Nakazawa Y., Pilz D.T., Guo C., Shimada M., Sasaki K., Fawcett H., Wing J.F., Lewin S.O., Carr L., Li T.S., Yoshiura K., Utani A., Hirano A., Yamashita S., Greenblatt D., Nardo T., Stefanini M.
      , McGibbon D., Sarkany R., Fassihi H., Takahashi Y., Nagayama Y., Mitsutake N., Lehmann A.R., Ogi T.
      Am. J. Hum. Genet. 92:807-819(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT COFS4 LEU-231, CHARACTERIZATION OF VARIANT COFS4 LEU-231.

    Entry informationi

    Entry nameiERCC1_HUMAN
    AccessioniPrimary (citable) accession number: P07992
    Secondary accession number(s): B2RC01
    , B3KRR0, Q7Z7F5, Q96S40
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: August 1, 1988
    Last modified: October 1, 2014
    This is version 151 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3