Q92889 (XPF_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	ERCC4
Synonyms:	ERCC11, XPF

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	916 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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.7
Cofactor	Magnesium.
Subunit structure	Heterodimer composed of ERCC1 and XPF/ERCC4. Interacts with EME1. 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.10
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.14 Ref.15 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.17
Sequence similarities	Belongs to the XPF family. Contains 1 ERCC4 domain.
Sequence caution	The sequence AAB07689.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	DNA damage DNA repair
Cellular component	Nucleus
Coding sequence diversity	Polymorphism
Disease	Disease mutation Dwarfism Xeroderma pigmentosum
Domain	Repeat
Ligand	DNA-binding Magnesium
Molecular function	Endonuclease Hydrolase Nuclease
PTM	Acetylation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	UV protection Inferred from electronic annotation. Source: Compara double-strand break repair via homologous recombination Inferred from mutant phenotype PubMed 14728600. Source: UniProtKB meiotic mismatch repair Inferred from Biological aspect of Ancestor. Source: RefGenome negative regulation of telomere maintenance Inferred from mutant phenotype PubMed 17055345. Source: UniProtKB nucleotide-excision repair, DNA damage removal Traceable author statement. Source: Reactome 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 via telomere shortening Inferred from mutant phenotype PubMed 17055345. Source: BHF-UCL transcription-coupled nucleotide-excision repair Traceable author statement. Source: Reactome
Cellular_component	nuclear chromosome, telomeric region Inferred from direct assay PubMed 14690602. Source: UniProtKB nucleoplasm Traceable author statement. Source: Reactome nucleotide-excision repair factor 1 complex Inferred from direct assay PubMed 10413517. Source: UniProtKB
Molecular_function	damaged DNA binding Inferred from mutant phenotype PubMed 11790111. Source: UniProtKB single-stranded DNA binding Inferred from direct assay PubMed 10413517. Source: UniProtKB single-stranded DNA specific endodeoxyribonuclease activity Inferred from Biological aspect of Ancestor. Source: RefGenome
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
SLX4	Q8IY92	10	EBI-2370770,EBI-2370740

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 916

916

DNA repair endonuclease XPF

PRO_0000198853

Regions

Domain

683 – 763

81

ERCC4

Region

233 – 254

22

Leucine-zipper 1

Region

270 – 298

29

Leucine-zipper 2

Region

617 – 916

300

Interaction with EME1 and ERCC1

Motif

486 – 491

6

Nuclear localization signal Potential

Amino acid modifications

Modified residue

289

1

N6-acetyllysine Ref.11

Natural variations

Natural variant

33

1

V → L.
Corresponds to variant rs34205098 [ dbSNP | Ensembl ].

VAR_057477

Natural variant

153

1

R → P in XFEPS. Ref.17

VAR_034802

Natural variant

168

1

A → V. Ref.3
Corresponds to variant rs2020961 [ dbSNP | Ensembl ].

VAR_014769

Natural variant

225

1

I → M in XP-F. Ref.14

VAR_008200

Natural variant

379

1

P → S. Ref.3 Ref.13
Corresponds to variant rs1799802 [ dbSNP | Ensembl ].

VAR_013395

Natural variant

415

1

R → Q. Ref.2 Ref.3 Ref.16
Corresponds to variant rs1800067 [ dbSNP | Ensembl ].

VAR_013396

Natural variant

454

1

R → W in XP-F. Ref.14

VAR_008201

Natural variant

490

1

R → Q in XP-F. Ref.14

VAR_008202

Natural variant

502

1

E → K in XP-F. Ref.14

VAR_008203

Natural variant

513

1

G → R in XP-F. Ref.14

VAR_008204

Natural variant

529

1

I → T in XP-F. Ref.14

VAR_008205

Natural variant

567

1

T → A in XP-F. Ref.14

VAR_008206

Natural variant

576

1

R → T. Ref.16
Corresponds to variant rs1800068 [ dbSNP | Ensembl ].

VAR_013397

Natural variant

605 – 611

7

Missing in XP-F.

VAR_008207

Natural variant

608

1

L → P in XP-F. Ref.14

VAR_013398

Natural variant

662

1

S → P. Ref.3
Corresponds to variant rs2020955 [ dbSNP | Ensembl ].

VAR_014770

Natural variant

703

1

G → D. Ref.4

VAR_005849

Natural variant

706

1

I → T. Ref.3
Corresponds to variant rs1800069 [ dbSNP | Ensembl ].

VAR_014771

Natural variant

717

1

I → T. Ref.16

VAR_013399

Natural variant

768

1

S → F.
Corresponds to variant rs12928650 [ dbSNP | Ensembl ].

VAR_057478

Natural variant

799

1

R → W in XP-F; mild; significant residual repair activity. Ref.4 Ref.15

VAR_005850

Natural variant

860

1

A → D.
Corresponds to variant rs4986933 [ dbSNP | Ensembl ].

VAR_057479

Natural variant

873

1

I → V. Ref.3
Corresponds to variant rs2020957 [ dbSNP | Ensembl ].

VAR_019201

Natural variant

875

1

E → G. Ref.3 Ref.16
Corresponds to variant rs1800124 [ dbSNP | Ensembl ].

VAR_013408

Natural variant

912

1

G → E.
Corresponds to variant rs2020956 [ dbSNP | Ensembl ].

VAR_014772

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

916

Helix Strand Turn

Details...

Turn

835 – 837

3

Helix

839 – 842

4

Helix

850 – 853

4

Helix

860 – 869

10

Beta strand

870 – 872

3

Helix

873 – 877

5

Helix

881 – 888

8

Helix

891 – 902

12

Helix

905 – 908

4

Beta strand

911 – 913

3

Sequences

	Sequence		Length	Mass (Da)
	Q92889 [UniParc]. Last modified May 5, 2009. Version 3. Checksum: C58CDE900378CCA8	FASTA	916	104,486
	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

References

	« Hide 'large scale' referencesShow '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. , 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]	"Identification of FAAP24, a Fanconi anemia core complex protein that interacts with FANCM." Ciccia A., Ling C., Coulthard R., Yan Z., Xue Y., Meetei A.R., Laghmani el H., Joenje H., McDonald N., de Winter J.P., Wang W., West S.C. Mol. Cell 25:331-343(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH EME1 AND ERCC1.
[7]	"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.
[8]	"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.
[9]	"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.
[10]	"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.
[11]	"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, MASS SPECTROMETRY.
[12]	"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].
[13]	"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.
[14]	"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.
[15]	"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.
[16]	"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.
[17]	"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.
+	Additional computationally mapped references.

Web resources

Allelic variations of the XP genes

Atlas of Genetics and Cytogenetics in Oncology and Haematology

GeneReviews

NIEHS-SNPs

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.

IPI

IPI00219179.

RefSeq

NP_005227.1. NM_005236.2.

UniGene

Hs.567265.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1Z00	NMR	-	B	834-916	[»]
2A1J	X-ray	2.70	A	848-909	[»]
2AQ0	NMR	-	A/B	834-916	[»]
2KN7	NMR	-	A/D	842-908	[»]

ProteinModelPortal

Q92889.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-42006N.

IntAct

Q92889. 4 interactions.

STRING

9606.ENSP00000310520.

PTM databases

PhosphoSite

Q92889.

Polymorphism databases

DMDM

229463004.

Proteomic databases

PaxDb

Q92889.

PRIDE

Q92889.

Protocols and materials databases

DNASU

2072.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000311895; ENSP00000310520; ENSG00000175595.

GeneID

2072.

KEGG

hsa:2072.

UCSC

uc002dce.2. human.

Organism-specific databases

CTD

2072.

GeneCards

GC16P014014.

H-InvDB

HIX0038603.
HIX0173284.

HGNC

HGNC:3436. ERCC4.

HPA

CAB000156.

MIM

133520. gene.
278760. phenotype.
610965. phenotype.

neXtProt

NX_Q92889.

Orphanet

276264. Xeroderma pigmentosum complementation group F.

PharmGKB

PA27850.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG1948.

HOGENOM

HOG000202204.

HOVERGEN

HBG051500.

InParanoid

Q92889.

KO

K10848.

OMA

QQSIVVD.

Enzyme and pathway databases

Reactome

REACT_216. DNA Repair.

Gene expression databases

ArrayExpress

Q92889.

Bgee

Q92889.

CleanEx

HS_ERCC4.

Genevestigator

Q92889.

GermOnline

ENSG00000175595. Homo sapiens.

Family and domain databases

Gene3D

3.40.50.10130. 1 hit.

InterPro

IPR020819. DNA_repair_nuc_XPF/helicase.
IPR006166. ERCC4_domain.
IPR006167. Rad1.
IPR011335. Restrct_endonuc-II-like.
IPR010994. RuvA_2-like.
[Graphical view]

Pfam

PF02732. ERCC4. 1 hit.
[Graphical view]

SMART

SM00891. ERCC4. 1 hit.
[Graphical view]

SUPFAM

SSF52980. Restrict_endonuc_II-like_core. 1 hit.
SSF47781. RuvA_2_like. 1 hit.

TIGRFAMs

TIGR00596. rad1. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

Q92889.

GenomeRNAi

2072.

NextBio

8429.

SOURCE

Search...

Entry information

Entry name

XPF_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 139 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.