Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

DNA repair endonuclease XPF

Gene

ERCC4

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic component of a structure-specific DNA repair endonuclease responsible for the 5-prime incision during DNA repair. Involved in homologous recombination that assists in removing interstrand cross-link.1 Publication

Cofactori

GO - Molecular functioni

  • damaged DNA binding Source: UniProtKB
  • endodeoxyribonuclease activity Source: UniProtKB
  • protein C-terminus binding Source: UniProtKB
  • protein N-terminus binding Source: UniProtKB
  • single-stranded DNA binding Source: UniProtKB
  • single-stranded DNA endodeoxyribonuclease activity Source: GO_Central

GO - Biological processi

  • cellular response to UV Source: BHF-UCL
  • DNA repair Source: UniProtKB
  • double-strand break repair via homologous recombination Source: UniProtKB
  • negative regulation of telomere maintenance Source: UniProtKB
  • nucleotide-excision repair Source: UniProtKB
  • nucleotide-excision repair, DNA damage removal Source: Reactome
  • nucleotide-excision repair, DNA incision Source: UniProtKB
  • nucleotide-excision repair, DNA incision, 3'-to lesion Source: UniProtKB
  • nucleotide-excision repair, DNA incision, 5'-to lesion Source: UniProtKB
  • nucleotide-excision repair involved in interstrand cross-link repair Source: GO_Central
  • resolution of meiotic recombination intermediates Source: GO_Central
  • response to UV Source: UniProtKB
  • telomere maintenance Source: BHF-UCL
  • transcription-coupled nucleotide-excision repair Source: Reactome
  • UV protection Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Hydrolase, Nuclease

Keywords - Biological processi

DNA damage, DNA repair

Keywords - Ligandi

DNA-binding, Magnesium

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 repair endonuclease XPF (EC:3.1.-.-)
Alternative name(s):
DNA excision repair protein ERCC-4
DNA repair protein complementing XP-F cells
Xeroderma pigmentosum group F-complementing protein
Gene namesi
Name:ERCC4
Synonyms:ERCC11, XPF
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:3436. ERCC4.

Subcellular locationi

GO - Cellular componenti

  • chromosome, telomeric region Source: BHF-UCL
  • ERCC4-ERCC1 complex Source: BHF-UCL
  • nuclear chromosome, telomeric region Source: UniProtKB
  • nucleoplasm Source: Reactome
  • nucleotide-excision repair complex Source: MGI
  • nucleotide-excision repair factor 1 complex Source: UniProtKB
  • nucleus Source: UniProtKB
  • transcription factor TFIID complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

Xeroderma pigmentosum complementation group F (XP-F)3 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionAn autosomal recessive pigmentary skin disorder characterized by solar hypersensitivity of the skin, high predisposition for developing cancers on areas exposed to sunlight and, in some cases, neurological abnormalities. The skin develops marked freckling and other pigmentation abnormalities. XP-F patients show a mild phenotype.

See also OMIM:278760
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti225 – 2251I → M in XP-F. 1 Publication
VAR_008200
Natural varianti454 – 4541R → W in XP-F. 1 Publication
VAR_008201
Natural varianti490 – 4901R → Q in XP-F. 1 Publication
VAR_008202
Natural varianti502 – 5021E → K in XP-F. 1 Publication
VAR_008203
Natural varianti513 – 5131G → R in XP-F. 1 Publication
VAR_008204
Natural varianti529 – 5291I → T in XP-F. 1 Publication
VAR_008205
Natural varianti567 – 5671T → A in XP-F. 1 Publication
VAR_008206
Natural varianti605 – 6117Missing in XP-F. 1 Publication
VAR_008207
Natural varianti608 – 6081L → P in XP-F. 1 Publication
VAR_013398
Natural varianti799 – 7991R → W in XP-F; mild; significant residual repair activity. 2 Publications
VAR_005850
XFE progeroid syndrome (XFEPS)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA syndrome characterized by aged bird-like facies, lack of subcutaneous fat, dwarfism, cachexia and microcephaly. Additional features include sun-sensitivity from birth, learning disabilities, hearing loss, and visual impairment.

See also OMIM:610965
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti153 – 1531R → P in XFEPS. 1 Publication
VAR_034802
Xeroderma pigmentosum type F/Cockayne syndrome (XPF/CS)

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA variant form of Cockayne syndrome, a disorder characterized by growth retardation, microcephaly, impairment of nervous system development, pigmentary retinopathy, peculiar facies, and progeria together with abnormal skin photosensitivity. Cockayne syndrome dermatological features are milder than those in xeroderma pigmentosum and skin cancers are not found in affected individuals. XPF/CS patients, however, present with severe skin phenotypes, including severe photosensitivity, abnormal skin pigmentation, and skin cancer predisposition.

See also OMIM:278760
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti236 – 2361C → R in XPF/CS. 1 Publication
VAR_070087
Natural varianti589 – 5891R → W in XPF/CS. 1 Publication
VAR_070088
Fanconi anemia complementation group Q (FANCQ)2 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA disorder affecting all bone marrow elements and resulting in anemia, leukopenia and thrombopenia. It is associated with cardiac, renal and limb malformations, dermal pigmentary changes, and a predisposition to the development of malignancies. At the cellular level it is associated with hypersensitivity to DNA-damaging agents, chromosomal instability (increased chromosome breakage) and defective DNA repair.

See also OMIM:615272
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti230 – 2301L → P in FANCQ. 1 Publication
VAR_070086
Natural varianti689 – 6891R → S in FANCQ; disruption of interstrand cross-link repair activity; no effect on protein stability. 2 Publications
VAR_070089
Natural varianti786 – 7861S → F in FANCQ; disruption of interstrand cross-link repair activity; no effect on protein stability. 1 Publication
VAR_072087

Keywords - Diseasei

Cockayne syndrome, Disease mutation, Dwarfism, Fanconi anemia, Xeroderma pigmentosum

Organism-specific databases

MIMi278760. phenotype.
610965. phenotype.
615272. phenotype.
Orphaneti90321. Cockayne syndrome type 1.
84. Fanconi anemia.
276264. Xeroderma pigmentosum complementation group F.
PharmGKBiPA27850.

Polymorphism and mutation databases

BioMutaiERCC4.
DMDMi229463004.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 916916DNA repair endonuclease XPFPRO_0000198853Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei289 – 2891N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ92889.
PaxDbiQ92889.
PRIDEiQ92889.

PTM databases

PhosphoSiteiQ92889.

Expressioni

Gene expression databases

BgeeiQ92889.
CleanExiHS_ERCC4.
ExpressionAtlasiQ92889. baseline and differential.
GenevisibleiQ92889. HS.

Organism-specific databases

HPAiCAB000156.
HPA045828.

Interactioni

Subunit structurei

Heterodimer composed of ERCC1 and XPF/ERCC4. Interacts with SLX4/BTBD12; this interaction is direct and links the ERCC1-XPF/ERCC1 complex to SLX4, which may coordinate the action of the structure-specific endonuclease during DNA repair.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ERCC1P079928EBI-2370770,EBI-750962
SLX4Q8IY9210EBI-2370770,EBI-2370740

Protein-protein interaction databases

BioGridi108384. 23 interactions.
DIPiDIP-42006N.
IntActiQ92889. 10 interactions.
MINTiMINT-192303.
STRINGi9606.ENSP00000310520.

Structurei

Secondary structure

1
916
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni835 – 8373Combined sources
Helixi839 – 8424Combined sources
Helixi850 – 8534Combined sources
Helixi860 – 86910Combined sources
Beta strandi870 – 8723Combined sources
Helixi873 – 8775Combined sources
Helixi881 – 8888Combined sources
Helixi891 – 90212Combined sources
Helixi905 – 9084Combined sources
Beta strandi911 – 9133Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Z00NMR-B834-916[»]
2A1JX-ray2.70A848-909[»]
2AQ0NMR-A/B834-916[»]
2KN7NMR-A/D842-908[»]
ProteinModelPortaliQ92889.
SMRiQ92889. Positions 679-916.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ92889.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini683 – 76381ERCC4Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 457457Helicase-likeAdd
BLAST
Regioni233 – 25422Leucine-zipper 1Add
BLAST
Regioni270 – 29829Leucine-zipper 2Add
BLAST
Regioni658 – 813156NucleaseAdd
BLAST
Regioni837 – 90569HhH2, dimerization with ERCC1Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi486 – 4916Nuclear localization signalSequence Analysis

Sequence similaritiesi

Belongs to the XPF family.Curated
Contains 1 ERCC4 domain.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG1948.
GeneTreeiENSGT00390000004394.
HOGENOMiHOG000202204.
HOVERGENiHBG051500.
InParanoidiQ92889.
KOiK10848.
OMAiQQSIVVD.
OrthoDBiEOG7VTDM8.
PhylomeDBiQ92889.
TreeFamiTF101234.

Family and domain databases

Gene3Di3.40.50.10130. 1 hit.
InterProiIPR020819. DNA_repair_nuc_XPF/helicase.
IPR006166. ERCC4_domain.
IPR006167. Rad1.
IPR011335. Restrct_endonuc-II-like.
IPR010994. RuvA_2-like.
[Graphical view]
PfamiPF02732. ERCC4. 1 hit.
[Graphical view]
SMARTiSM00891. ERCC4. 1 hit.
[Graphical view]
SUPFAMiSSF47781. SSF47781. 1 hit.
SSF52980. SSF52980. 1 hit.
TIGRFAMsiTIGR00596. rad1. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q92889-1) [UniParc]FASTAAdd to basket

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
MESGQPARRI AMAPLLEYER QLVLELLDTD GLVVCARGLG ADRLLYHFLQ
60 70 80 90 100
LHCHPACLVL VLNTQPAEEE YFINQLKIEG VEHLPRRVTN EITSNSRYEV
110 120 130 140 150
YTQGGVIFAT SRILVVDFLT DRIPSDLITG ILVYRAHRII ESCQEAFILR
160 170 180 190 200
LFRQKNKRGF IKAFTDNAVA FDTGFCHVER VMRNLFVRKL YLWPRFHVAV
210 220 230 240 250
NSFLEQHKPE VVEIHVSMTP TMLAIQTAIL DILNACLKEL KCHNPSLEVE
260 270 280 290 300
DLSLENAIGK PFDKTIRHYL DPLWHQLGAK TKSLVQDLKI LRTLLQYLSQ
310 320 330 340 350
YDCVTFLNLL ESLRATEKAF GQNSGWLFLD SSTSMFINAR ARVYHLPDAK
360 370 380 390 400
MSKKEKISEK MEIKEGEETK KELVLESNPK WEALTEVLKE IEAENKESEA
410 420 430 440 450
LGGPGQVLIC ASDDRTCSQL RDYITLGAEA FLLRLYRKTF EKDSKAEEVW
460 470 480 490 500
MKFRKEDSSK RIRKSHKRPK DPQNKERAST KERTLKKKKR KLTLTQMVGK
510 520 530 540 550
PEELEEEGDV EEGYRREISS SPESCPEEIK HEEFDVNLSS DAAFGILKEP
560 570 580 590 600
LTIIHPLLGC SDPYALTRVL HEVEPRYVVL YDAELTFVRQ LEIYRASRPG
610 620 630 640 650
KPLRVYFLIY GGSTEEQRYL TALRKEKEAF EKLIREKASM VVPEEREGRD
660 670 680 690 700
ETNLDLVRGT ASADVSTDTR KAGGQEQNGT QQSIVVDMRE FRSELPSLIH
710 720 730 740 750
RRGIDIEPVT LEVGDYILTP EMCVERKSIS DLIGSLNNGR LYSQCISMSR
760 770 780 790 800
YYKRPVLLIE FDPSKPFSLT SRGALFQEIS SNDISSKLTL LTLHFPRLRI
810 820 830 840 850
LWCPSPHATA ELFEELKQSK PQPDAATALA ITADSETLPE SEKYNPGPQD
860 870 880 890 900
FLLKMPGVNA KNCRSLMHHV KNIAELAALS QDELTSILGN AANAKQLYDF
910
IHTSFAEVVS KGKGKK
Length:916
Mass (Da):104,486
Last modified:May 5, 2009 - v3
Checksum:iC58CDE900378CCA8
GO
Isoform 2 (identifier: Q92889-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     368-372: ETKKE → GILWG
     373-916: Missing.

Note: No experimental confirmation available.
Show »
Length:372
Mass (Da):42,745
Checksum:i98642E13DB2EAF52
GO

Sequence cautioni

The sequence AAB07689.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti33 – 331V → L.
Corresponds to variant rs34205098 [ dbSNP | Ensembl ].
VAR_057477
Natural varianti150 – 1501R → C Rare functional polymorphism; causes mild disruption of interstrand cross-link repair activity; partial loss of protein stability. 1 Publication
VAR_072084
Natural varianti153 – 1531R → P in XFEPS. 1 Publication
VAR_034802
Natural varianti168 – 1681A → V.1 Publication
Corresponds to variant rs2020961 [ dbSNP | Ensembl ].
VAR_014769
Natural varianti225 – 2251I → M in XP-F. 1 Publication
VAR_008200
Natural varianti230 – 2301L → P in FANCQ. 1 Publication
VAR_070086
Natural varianti236 – 2361C → R in XPF/CS. 1 Publication
VAR_070087
Natural varianti267 – 2671R → H.1 Publication
VAR_072085
Natural varianti379 – 3791P → S.2 Publications
Corresponds to variant rs1799802 [ dbSNP | Ensembl ].
VAR_013395
Natural varianti415 – 4151R → Q.3 Publications
Corresponds to variant rs1800067 [ dbSNP | Ensembl ].
VAR_013396
Natural varianti454 – 4541R → W in XP-F. 1 Publication
VAR_008201
Natural varianti490 – 4901R → Q in XP-F. 1 Publication
VAR_008202
Natural varianti502 – 5021E → K in XP-F. 1 Publication
VAR_008203
Natural varianti513 – 5131G → R in XP-F. 1 Publication
VAR_008204
Natural varianti529 – 5291I → T in XP-F. 1 Publication
VAR_008205
Natural varianti567 – 5671T → A in XP-F. 1 Publication
VAR_008206
Natural varianti576 – 5761R → T.1 Publication
Corresponds to variant rs1800068 [ dbSNP | Ensembl ].
VAR_013397
Natural varianti589 – 5891R → W in XPF/CS. 1 Publication
VAR_070088
Natural varianti605 – 6117Missing in XP-F. 1 Publication
VAR_008207
Natural varianti608 – 6081L → P in XP-F. 1 Publication
VAR_013398
Natural varianti621 – 6211T → A.1 Publication
VAR_072086
Natural varianti662 – 6621S → P.1 Publication
Corresponds to variant rs2020955 [ dbSNP | Ensembl ].
VAR_014770
Natural varianti689 – 6891R → S in FANCQ; disruption of interstrand cross-link repair activity; no effect on protein stability. 2 Publications
VAR_070089
Natural varianti703 – 7031G → D.1 Publication
VAR_005849
Natural varianti706 – 7061I → T.1 Publication
Corresponds to variant rs1800069 [ dbSNP | Ensembl ].
VAR_014771
Natural varianti717 – 7171I → T.1 Publication
VAR_013399
Natural varianti768 – 7681S → F.
Corresponds to variant rs12928650 [ dbSNP | Ensembl ].
VAR_057478
Natural varianti786 – 7861S → F in FANCQ; disruption of interstrand cross-link repair activity; no effect on protein stability. 1 Publication
VAR_072087
Natural varianti799 – 7991R → W in XP-F; mild; significant residual repair activity. 2 Publications
VAR_005850
Natural varianti860 – 8601A → D.
Corresponds to variant rs4986933 [ dbSNP | Ensembl ].
VAR_057479
Natural varianti873 – 8731I → V.1 Publication
Corresponds to variant rs2020957 [ dbSNP | Ensembl ].
VAR_019201
Natural varianti875 – 8751E → G.2 Publications
Corresponds to variant rs1800124 [ dbSNP | Ensembl ].
VAR_013408
Natural varianti912 – 9121G → E.
Corresponds to variant rs2020956 [ dbSNP | Ensembl ].
VAR_014772

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei368 – 3725ETKKE → GILWG in isoform 2. 1 PublicationVSP_056341
Alternative sequencei373 – 916544Missing in isoform 2. 1 PublicationVSP_056342Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L77890 Genomic DNA. Translation: AAB50174.1.
AF491814 Genomic DNA. Translation: AAL91593.1.
AK289726 mRNA. Translation: BAF82415.1.
AC010401 Genomic DNA. No translation available.
BC142631 mRNA. Translation: AAI42632.1.
U64315 mRNA. Translation: AAB07689.1. Different initiation.
CCDSiCCDS32390.1. [Q92889-1]
RefSeqiNP_005227.1. NM_005236.2. [Q92889-1]
UniGeneiHs.567265.

Genome annotation databases

EnsembliENST00000311895; ENSP00000310520; ENSG00000175595.
ENST00000575156; ENSP00000459933; ENSG00000175595. [Q92889-2]
GeneIDi2072.
KEGGihsa:2072.
UCSCiuc002dce.2. human. [Q92889-1]
uc010bva.3. human.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Allelic variations of the XP genes
Atlas of Genetics and Cytogenetics in Oncology and Haematology
NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L77890 Genomic DNA. Translation: AAB50174.1.
AF491814 Genomic DNA. Translation: AAL91593.1.
AK289726 mRNA. Translation: BAF82415.1.
AC010401 Genomic DNA. No translation available.
BC142631 mRNA. Translation: AAI42632.1.
U64315 mRNA. Translation: AAB07689.1. Different initiation.
CCDSiCCDS32390.1. [Q92889-1]
RefSeqiNP_005227.1. NM_005236.2. [Q92889-1]
UniGeneiHs.567265.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Z00NMR-B834-916[»]
2A1JX-ray2.70A848-909[»]
2AQ0NMR-A/B834-916[»]
2KN7NMR-A/D842-908[»]
ProteinModelPortaliQ92889.
SMRiQ92889. Positions 679-916.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108384. 23 interactions.
DIPiDIP-42006N.
IntActiQ92889. 10 interactions.
MINTiMINT-192303.
STRINGi9606.ENSP00000310520.

PTM databases

PhosphoSiteiQ92889.

Polymorphism and mutation databases

BioMutaiERCC4.
DMDMi229463004.

Proteomic databases

MaxQBiQ92889.
PaxDbiQ92889.
PRIDEiQ92889.

Protocols and materials databases

DNASUi2072.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000311895; ENSP00000310520; ENSG00000175595.
ENST00000575156; ENSP00000459933; ENSG00000175595. [Q92889-2]
GeneIDi2072.
KEGGihsa:2072.
UCSCiuc002dce.2. human. [Q92889-1]
uc010bva.3. human.

Organism-specific databases

CTDi2072.
GeneCardsiGC16P014014.
GeneReviewsiERCC4.
H-InvDBHIX0038603.
HIX0173284.
HGNCiHGNC:3436. ERCC4.
HPAiCAB000156.
HPA045828.
MIMi133520. gene.
278760. phenotype.
610965. phenotype.
615272. phenotype.
neXtProtiNX_Q92889.
Orphaneti90321. Cockayne syndrome type 1.
84. Fanconi anemia.
276264. Xeroderma pigmentosum complementation group F.
PharmGKBiPA27850.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1948.
GeneTreeiENSGT00390000004394.
HOGENOMiHOG000202204.
HOVERGENiHBG051500.
InParanoidiQ92889.
KOiK10848.
OMAiQQSIVVD.
OrthoDBiEOG7VTDM8.
PhylomeDBiQ92889.
TreeFamiTF101234.

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.

Miscellaneous databases

EvolutionaryTraceiQ92889.
GeneWikiiERCC4.
GenomeRNAii2072.
NextBioi35462247.
PROiQ92889.
SOURCEiSearch...

Gene expression databases

BgeeiQ92889.
CleanExiHS_ERCC4.
ExpressionAtlasiQ92889. baseline and differential.
GenevisibleiQ92889. HS.

Family and domain databases

Gene3Di3.40.50.10130. 1 hit.
InterProiIPR020819. DNA_repair_nuc_XPF/helicase.
IPR006166. ERCC4_domain.
IPR006167. Rad1.
IPR011335. Restrct_endonuc-II-like.
IPR010994. RuvA_2-like.
[Graphical view]
PfamiPF02732. ERCC4. 1 hit.
[Graphical view]
SMARTiSM00891. ERCC4. 1 hit.
[Graphical view]
SUPFAMiSSF47781. SSF47781. 1 hit.
SSF52980. SSF52980. 1 hit.
TIGRFAMsiTIGR00596. rad1. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "ERCC4 (XPF) encodes a human nucleotide excision repair protein with eukaryotic recombination homologs."
    Brookman K.W., Lamerdin J.E., Thelen M.P., Hwang M., Reardon J.T., Sancar A., Zhou Z.-Q., Walter C.A., Parris C.N., Thompson L.H.
    Mol. Cell. Biol. 16:6553-6562(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. NIEHS SNPs program
    Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS VAL-168; SER-379; GLN-415; PRO-662; THR-706; VAL-873 AND GLY-875.
  3. "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] (ISOFORM 1), VARIANT GLN-415.
    Tissue: Brain.
  4. "The sequence and analysis of duplication-rich human chromosome 16."
    Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
    , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
    Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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] (ISOFORM 2).
  6. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 7-916 (ISOFORM 1), VARIANT ASP-703, VARIANT XP-F TRP-799.
    Tissue: Fibroblast.
  7. "A summary of mutations in the UV-sensitive disorders: xeroderma pigmentosum, Cockayne syndrome, and trichothiodystrophy."
    Cleaver J.E., Thompson L.H., Richardson A.S., States J.C.
    Hum. Mutat. 14:9-22(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON VARIANTS XP-F.
  8. "Mammalian BTBD12/SLX4 assembles a Holliday junction resolvase and is required for DNA repair."
    Svendsen J.M., Smogorzewska A., Sowa M.E., O'Connell B.C., Gygi S.P., Elledge S.J., Harper J.W.
    Cell 138:63-77(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SLX4.
  9. "Human SLX4 is a Holliday junction resolvase subunit that binds multiple DNA repair/recombination endonucleases."
    Fekairi S., Scaglione S., Chahwan C., Taylor E.R., Tissier A., Coulon S., Dong M.-Q., Ruse C., Yates J.R. III, Russell P., Fuchs R.P., McGowan C.H., Gaillard P.-H.L.
    Cell 138:78-89(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SLX4.
  10. Cited for: INTERACTION WITH SLX4.
  11. "Drosophila MUS312 and the vertebrate ortholog BTBD12 interact with DNA structure-specific endonucleases in DNA repair and recombination."
    Andersen S.L., Bergstralh D.T., Kohl K.P., LaRocque J.R., Moore C.B., Sekelsky J.
    Mol. Cell 35:128-135(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SLX4.
  12. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-289, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "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 (2.7 ANGSTROMS) OF 848-909 IN COMPLEX WITH ERCC1, DNA-BINDING, DOMAINS, SUBUNIT.
  16. "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 834-916 IN COMPLEX WITH ERCC1, SUBUNIT.
  17. "Nonconservative amino acid substitution variants exist at polymorphic frequency in DNA repair genes in healthy humans."
    Shen M.R., Jones I.M., Mohrenweiser H.
    Cancer Res. 58:604-608(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT SER-379.
  18. "Characterization of molecular defects in Xeroderma pigmentosum group F in relation to its clinically mild symptoms."
    Matsumura Y., Nishigori C., Yagi T., Imamura S., Takebe H.
    Hum. Mol. Genet. 7:969-974(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS XP-F MET-225; TRP-454; GLN-490; LYS-502; ARG-513; THR-529; ALA-567; 605-VAL--GLY-611 DEL AND PRO-608.
  19. "Homozygous R788W point mutation in the XPF gene of a patient with xeroderma pigmentosum and late-onset neurologic disease."
    Sijbers A.M., van Voorst Vader P.C., Snoek J.W., Raams A., Jaspers N.G.J., Kleijer W.J.
    J. Invest. Dermatol. 110:832-836(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT XP-F TRP-799.
  20. "Polymorphisms in the human DNA repair gene XPF."
    Fan F., Liu C., Tavare S., Arnheim N.
    Mutat. Res. 406:115-120(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS GLN-415; THR-576; THR-717 AND GLY-875.
  21. Cited for: VARIANT XFEPS PRO-153.
  22. Cited for: VARIANTS FANCQ PRO-230 AND SER-689.
  23. "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: VARIANTS XPF/CS ARG-236 AND TRP-589.
  24. Cited for: VARIANTS CYS-150; HIS-267 AND ALA-621, VARIANTS FANCQ SER-689 AND PHE-786, CHARACTERIZATION OF VARIANT CYS-150, CHARACTERIZATION OF VARIANTS FANCQ SER-689 AND PHE-786.

Entry informationi

Entry nameiXPF_HUMAN
AccessioniPrimary (citable) accession number: Q92889
Secondary accession number(s): A5PKV6
, A8K111, O00140, Q8TD83
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 5, 2009
Last modified: July 22, 2015
This is version 163 of the entry and version 3 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 16
    Human chromosome 16: 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.