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P07992

- ERCC1_HUMAN

UniProt

P07992 - ERCC1_HUMAN

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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

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 C-terminus binding Source: UniProtKB
  4. protein domain specific binding Source: UniProtKB
  5. 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. interstrand cross-link repair Source: Ensembl
  9. isotype switching Source: Ensembl
  10. male gonad development Source: Ensembl
  11. mitotic recombination Source: UniProtKB
  12. multicellular organismal aging Source: Ensembl
  13. multicellular organism growth Source: Ensembl
  14. negative regulation of telomere maintenance Source: UniProtKB
  15. nucleotide-excision repair Source: MGI
  16. nucleotide-excision repair, DNA damage removal Source: Reactome
  17. nucleotide-excision repair, DNA incision, 3'-to lesion Source: UniProtKB
  18. nucleotide-excision repair, DNA incision, 5'-to lesion Source: UniProtKB
  19. oogenesis Source: Ensembl
  20. post-embryonic hemopoiesis Source: Ensembl
  21. pyrimidine dimer repair by nucleotide-excision repair Source: Ensembl
  22. replicative cell aging Source: Ensembl
  23. response to nutrient Source: Ensembl
  24. response to oxidative stress Source: UniProtKB
  25. response to sucrose Source: Ensembl
  26. response to X-ray Source: Ensembl
  27. spermatogenesis Source: Ensembl
  28. syncytium formation Source: Ensembl
  29. transcription-coupled nucleotide-excision repair Source: Reactome
  30. UV protection Source: Ensembl
Complete GO annotation...

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
Complete GO annotation...

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

BgeeiP07992.
CleanExiHS_ERCC1.
ExpressionAtlasiP07992. baseline and differential.
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. 19 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 – 1033Combined sources
Helixi105 – 1073Combined sources
Helixi111 – 1155Combined sources
Beta strandi121 – 1233Combined sources
Beta strandi127 – 1337Combined sources
Beta strandi136 – 1427Combined sources
Helixi143 – 1486Combined sources
Helixi152 – 1609Combined sources
Beta strandi163 – 17210Combined sources
Beta strandi175 – 1773Combined sources
Helixi179 – 19214Combined sources
Beta strandi195 – 2017Combined sources
Helixi202 – 21312Combined sources
Helixi222 – 2265Combined sources
Beta strandi242 – 2443Combined sources
Helixi247 – 25711Combined sources
Helixi260 – 2645Combined sources
Helixi268 – 2725Combined sources
Beta strandi274 – 2763Combined sources
Helixi280 – 29011Combined sources
Beta strandi293 – 2953Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00390000011275.
HOGENOMiHOG000037440.
HOVERGENiHBG051497.
InParanoidiP07992.
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

        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
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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. 19 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.
GeneTreei ENSGT00390000011275.
HOGENOMi HOG000037440.
HOVERGENi HBG051497.
InParanoidi P07992.
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

Bgeei P07992.
CleanExi HS_ERCC1.
ExpressionAtlasi P07992. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 153 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