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Q92889 (XPF_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 152. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:ERCC4
Synonyms:ERCC11, XPF
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length916 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.6

Cofactor

Magnesium.

Subunit structure

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. Ref.6 Ref.7 Ref.8 Ref.9 Ref.13 Ref.14

Subcellular location

Nucleus Probable.

Involvement in disease

Xeroderma pigmentosum complementation group F (XP-F) [MIM:278760]: An 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.4 Ref.16 Ref.17

XFE progeroid syndrome (XFEPS) [MIM:610965]: A 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.19

Xeroderma pigmentosum type F/Cockayne syndrome (XPF/CS) [MIM:278760]: A 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.21

Fanconi anemia complementation group Q (FANCQ) [MIM:615272]: A 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.20

Sequence similarities

Belongs to the XPF family.

Contains 1 ERCC4 domain.

Sequence caution

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

Ontologies

Keywords
   Biological processDNA damage
DNA repair
   Cellular componentNucleus
   Coding sequence diversityPolymorphism
   DiseaseCockayne syndrome
Disease mutation
Dwarfism
Fanconi anemia
Xeroderma pigmentosum
   DomainRepeat
   LigandDNA-binding
Magnesium
   Molecular functionEndonuclease
Hydrolase
Nuclease
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA catabolic process, endonucleolytic

Inferred from direct assay PubMed 10413517PubMed 14734547Ref.4. Source: GOC

DNA repair

Inferred from mutant phenotype Ref.6. Source: UniProtKB

UV protection

Inferred from electronic annotation. Source: Ensembl

double-strand break repair via homologous recombination

Inferred from mutant phenotype PubMed 14728600. Source: UniProtKB

negative regulation of telomere maintenance

Inferred from mutant phenotype PubMed 17055345. Source: UniProtKB

nucleotide-excision repair

Inferred from mutant phenotype Ref.4. Source: UniProtKB

nucleotide-excision repair involved in interstrand cross-link repair

Inferred from Biological aspect of Ancestor. Source: RefGenome

nucleotide-excision repair, DNA damage removal

Traceable author statement. Source: Reactome

nucleotide-excision repair, DNA incision

Inferred from direct assay PubMed 10413517. Source: UniProtKB

nucleotide-excision repair, DNA incision, 3'-to lesion

Inferred from mutant phenotype PubMed 11790111. Source: UniProtKB

nucleotide-excision repair, DNA incision, 5'-to lesion

Inferred from mutant phenotype PubMed 11790111PubMed 14728600. Source: UniProtKB

resolution of meiotic recombination intermediates

Inferred from Biological aspect of Ancestor. Source: RefGenome

response to UV

Inferred from mutant phenotype PubMed 16678501. Source: UniProtKB

telomere maintenance

Inferred from mutant phenotype PubMed 14690602. Source: BHF-UCL

telomere maintenance via telomere shortening

Inferred from mutant phenotype PubMed 17055345. Source: BHF-UCL

transcription-coupled nucleotide-excision repair

Traceable author statement. Source: Reactome

   Cellular_componentchromosome, telomeric region

Inferred from direct assay PubMed 14690602. Source: BHF-UCL

nuclear chromosome, telomeric region

Inferred from direct assay PubMed 14690602. Source: UniProtKB

nucleoplasm

Traceable author statement. Source: Reactome

nucleotide-excision repair complex

Inferred from direct assay PubMed 10644440. Source: MGI

nucleotide-excision repair factor 1 complex

Inferred from direct assay PubMed 10413517. Source: UniProtKB

nucleus

Inferred from direct assay PubMed 12571280. Source: UniProtKB

transcription factor TFIID complex

Inferred from electronic annotation. Source: Ensembl

   Molecular_functiondamaged DNA binding

Inferred from mutant phenotype PubMed 11790111. Source: UniProtKB

endodeoxyribonuclease activity

Inferred from direct assay PubMed 10413517PubMed 14734547. Source: UniProtKB

protein C-terminus binding

Inferred from physical interaction PubMed 9722633. Source: UniProtKB

protein N-terminus binding

Inferred from physical interaction PubMed 14734547. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 12571280PubMed 14690602Ref.8Ref.9Ref.6Ref.7PubMed 7559382. Source: UniProtKB

single-stranded DNA binding

Inferred from direct assay PubMed 10413517. Source: UniProtKB

single-stranded DNA endodeoxyribonuclease activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

SLX4Q8IY9210EBI-2370770,EBI-2370740

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 916916DNA repair endonuclease XPF
PRO_0000198853

Regions

Domain683 – 76381ERCC4
Region1 – 457457Helicase-like
Region233 – 25422Leucine-zipper 1
Region270 – 29829Leucine-zipper 2
Region658 – 813156Nuclease
Region837 – 90569HhH2, dimerization with ERCC1
Motif486 – 4916Nuclear localization signal Potential

Amino acid modifications

Modified residue2891N6-acetyllysine Ref.10

Natural variations

Natural variant331V → L.
Corresponds to variant rs34205098 [ dbSNP | Ensembl ].
VAR_057477
Natural variant1531R → P in XFEPS. Ref.19
VAR_034802
Natural variant1681A → V. Ref.3
Corresponds to variant rs2020961 [ dbSNP | Ensembl ].
VAR_014769
Natural variant2251I → M in XP-F. Ref.16
VAR_008200
Natural variant2301L → P in FANCQ. Ref.20
VAR_070086
Natural variant2361C → R in XPF/CS. Ref.21
VAR_070087
Natural variant3791P → S. Ref.3 Ref.15
Corresponds to variant rs1799802 [ dbSNP | Ensembl ].
VAR_013395
Natural variant4151R → Q. Ref.2 Ref.3 Ref.18
Corresponds to variant rs1800067 [ dbSNP | Ensembl ].
VAR_013396
Natural variant4541R → W in XP-F. Ref.16
VAR_008201
Natural variant4901R → Q in XP-F. Ref.16
VAR_008202
Natural variant5021E → K in XP-F. Ref.16
VAR_008203
Natural variant5131G → R in XP-F. Ref.16
VAR_008204
Natural variant5291I → T in XP-F. Ref.16
VAR_008205
Natural variant5671T → A in XP-F. Ref.16
VAR_008206
Natural variant5761R → T. Ref.18
Corresponds to variant rs1800068 [ dbSNP | Ensembl ].
VAR_013397
Natural variant5891R → W in XPF/CS. Ref.21
VAR_070088
Natural variant605 – 6117Missing in XP-F.
VAR_008207
Natural variant6081L → P in XP-F. Ref.16
VAR_013398
Natural variant6621S → P. Ref.3
Corresponds to variant rs2020955 [ dbSNP | Ensembl ].
VAR_014770
Natural variant6891R → S in FANCQ. Ref.20
VAR_070089
Natural variant7031G → D. Ref.4
VAR_005849
Natural variant7061I → T. Ref.3
Corresponds to variant rs1800069 [ dbSNP | Ensembl ].
VAR_014771
Natural variant7171I → T. Ref.18
VAR_013399
Natural variant7681S → F.
Corresponds to variant rs12928650 [ dbSNP | Ensembl ].
VAR_057478
Natural variant7991R → W in XP-F; mild; significant residual repair activity. Ref.4 Ref.17
VAR_005850
Natural variant8601A → D.
Corresponds to variant rs4986933 [ dbSNP | Ensembl ].
VAR_057479
Natural variant8731I → V. Ref.3
Corresponds to variant rs2020957 [ dbSNP | Ensembl ].
VAR_019201
Natural variant8751E → G. Ref.3 Ref.18
Corresponds to variant rs1800124 [ dbSNP | Ensembl ].
VAR_013408
Natural variant9121G → E.
Corresponds to variant rs2020956 [ dbSNP | Ensembl ].
VAR_014772

Secondary structure

................... 916
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q92889 [UniParc].

Last modified May 5, 2009. Version 3.
Checksum: C58CDE900378CCA8

FASTA916104,486
        10         20         30         40         50         60 
MESGQPARRI AMAPLLEYER QLVLELLDTD GLVVCARGLG ADRLLYHFLQ LHCHPACLVL 

        70         80         90        100        110        120 
VLNTQPAEEE YFINQLKIEG VEHLPRRVTN EITSNSRYEV YTQGGVIFAT SRILVVDFLT 

       130        140        150        160        170        180 
DRIPSDLITG ILVYRAHRII ESCQEAFILR LFRQKNKRGF IKAFTDNAVA FDTGFCHVER 

       190        200        210        220        230        240 
VMRNLFVRKL YLWPRFHVAV NSFLEQHKPE VVEIHVSMTP TMLAIQTAIL DILNACLKEL 

       250        260        270        280        290        300 
KCHNPSLEVE DLSLENAIGK PFDKTIRHYL DPLWHQLGAK TKSLVQDLKI LRTLLQYLSQ 

       310        320        330        340        350        360 
YDCVTFLNLL ESLRATEKAF GQNSGWLFLD SSTSMFINAR ARVYHLPDAK MSKKEKISEK 

       370        380        390        400        410        420 
MEIKEGEETK KELVLESNPK WEALTEVLKE IEAENKESEA LGGPGQVLIC ASDDRTCSQL 

       430        440        450        460        470        480 
RDYITLGAEA FLLRLYRKTF EKDSKAEEVW MKFRKEDSSK RIRKSHKRPK DPQNKERAST 

       490        500        510        520        530        540 
KERTLKKKKR KLTLTQMVGK PEELEEEGDV EEGYRREISS SPESCPEEIK HEEFDVNLSS 

       550        560        570        580        590        600 
DAAFGILKEP LTIIHPLLGC SDPYALTRVL HEVEPRYVVL YDAELTFVRQ LEIYRASRPG 

       610        620        630        640        650        660 
KPLRVYFLIY GGSTEEQRYL TALRKEKEAF EKLIREKASM VVPEEREGRD ETNLDLVRGT 

       670        680        690        700        710        720 
ASADVSTDTR KAGGQEQNGT QQSIVVDMRE FRSELPSLIH RRGIDIEPVT LEVGDYILTP 

       730        740        750        760        770        780 
EMCVERKSIS DLIGSLNNGR LYSQCISMSR YYKRPVLLIE FDPSKPFSLT SRGALFQEIS 

       790        800        810        820        830        840 
SNDISSKLTL LTLHFPRLRI LWCPSPHATA ELFEELKQSK PQPDAATALA ITADSETLPE 

       850        860        870        880        890        900 
SEKYNPGPQD FLLKMPGVNA KNCRSLMHHV KNIAELAALS QDELTSILGN AANAKQLYDF 

       910 
IHTSFAEVVS KGKGKK 

« Hide

References

« Hide 'large scale' references
[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]"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. expand/collapse author list , 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], VARIANT GLN-415.
Tissue: Brain.
[3]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.
[4]"Xeroderma pigmentosum group F caused by a defect in a structure-specific DNA repair endonuclease."
Sijbers A.M., de Laat W.L., Ariza R.R., Biggerstaff M., Wei Y.-F., Moggs J.G., Carter K.C., Shell B.K., Evans E., de Jong M.C., Rademakers S., de Rooij J., Jaspers N.G.J., Hoeijmakers J.H.J., Wood R.D.
Cell 86:811-822(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 7-916, VARIANT ASP-703, VARIANT XP-F TRP-799.
Tissue: Fibroblast.
[5]"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.
[6]"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.
[7]"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.
[8]"Coordination of structure-specific nucleases by human SLX4/BTBD12 is required for DNA repair."
Munoz I.M., Hain K., Declais A.-C., Gardiner M., Toh G.W., Sanchez-Pulido L., Heuckmann J.M., Toth R., Macartney T., Eppink B., Kanaar R., Ponting C.P., Lilley D.M.J., Rouse J.
Mol. Cell 35:116-127(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SLX4.
[9]"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.
[10]"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].
[11]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"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.
[14]"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.
[15]"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.
[16]"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.
[17]"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.
[18]"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.
[19]"A new progeroid syndrome reveals that genotoxic stress suppresses the somatotroph axis."
Niedernhofer L.J., Garinis G.A., Raams A., Lalai A.S., Robinson A.R., Appeldoorn E., Odijk H., Oostendorp R., Ahmad A., van Leeuwen W., Theil A.F., Vermeulen W., van der Horst G.T.J., Meinecke P., Kleijer W.J., Vijg J., Jaspers N.G.J., Hoeijmakers J.H.J.
Nature 444:1038-1043(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT XFEPS PRO-153.
[20]"Mutations in ERCC4, encoding the DNA-repair endonuclease XPF, cause Fanconi anemia."
Bogliolo M., Schuster B., Stoepker C., Derkunt B., Su Y., Raams A., Trujillo J.P., Minguillon J., Ramirez M.J., Pujol R., Casado J.A., Banos R., Rio P., Knies K., Zuniga S., Benitez J., Bueren J.A., Jaspers N.G. expand/collapse author list , Schaerer O.D., de Winter J.P., Schindler D., Surralles J.
Am. J. Hum. Genet. 92:800-806(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS FANCQ PRO-230 AND SER-689.
[21]"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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L77890 Genomic DNA. Translation: AAB50174.1.
AK289726 mRNA. Translation: BAF82415.1.
AF491814 Genomic DNA. Translation: AAL91593.1.
U64315 mRNA. Translation: AAB07689.1. Different initiation.
CCDSCCDS32390.1.
RefSeqNP_005227.1. NM_005236.2.
UniGeneHs.567265.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1Z00NMR-B834-916[»]
2A1JX-ray2.70A848-909[»]
2AQ0NMR-A/B834-916[»]
2KN7NMR-A/D842-908[»]
ProteinModelPortalQ92889.
SMRQ92889. Positions 679-916.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108384. 21 interactions.
DIPDIP-42006N.
IntActQ92889. 8 interactions.
MINTMINT-192303.
STRING9606.ENSP00000310520.

PTM databases

PhosphoSiteQ92889.

Polymorphism databases

DMDM229463004.

Proteomic databases

MaxQBQ92889.
PaxDbQ92889.
PRIDEQ92889.

Protocols and materials databases

DNASU2072.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000311895; ENSP00000310520; ENSG00000175595.
GeneID2072.
KEGGhsa:2072.
UCSCuc002dce.2. human.

Organism-specific databases

CTD2072.
GeneCardsGC16P014014.
GeneReviewsERCC4.
H-InvDBHIX0038603.
HIX0173284.
HGNCHGNC:3436. ERCC4.
HPACAB000156.
HPA045828.
MIM133520. gene.
278760. phenotype.
610965. phenotype.
615272. phenotype.
neXtProtNX_Q92889.
Orphanet90321. Cockayne syndrome type 1.
84. Fanconi anemia.
276264. Xeroderma pigmentosum complementation group F.
PharmGKBPA27850.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1948.
HOGENOMHOG000202204.
HOVERGENHBG051500.
InParanoidQ92889.
KOK10848.
OMARIIWSSS.
OrthoDBEOG7VTDM8.
PhylomeDBQ92889.
TreeFamTF101234.

Enzyme and pathway databases

ReactomeREACT_216. DNA Repair.

Gene expression databases

ArrayExpressQ92889.
BgeeQ92889.
CleanExHS_ERCC4.
GenevestigatorQ92889.

Family and domain databases

Gene3D3.40.50.10130. 1 hit.
InterProIPR020819. DNA_repair_nuc_XPF/helicase.
IPR006166. ERCC4_domain.
IPR006167. Rad1.
IPR011335. Restrct_endonuc-II-like.
IPR010994. RuvA_2-like.
[Graphical view]
PfamPF02732. ERCC4. 1 hit.
[Graphical view]
SMARTSM00891. ERCC4. 1 hit.
[Graphical view]
SUPFAMSSF47781. SSF47781. 1 hit.
SSF52980. SSF52980. 1 hit.
TIGRFAMsTIGR00596. rad1. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ92889.
GeneWikiERCC4.
GenomeRNAi2072.
NextBio8429.
PROQ92889.
SOURCESearch...

Entry information

Entry nameXPF_HUMAN
AccessionPrimary (citable) accession number: Q92889
Secondary accession number(s): A8K111, O00140, Q8TD83
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 5, 2009
Last modified: July 9, 2014
This is version 152 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM