HUMAN:XPF

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	ERCC4 (synonyms: ERCC11, XPF)
Protein Name(s)	DNA repair endonuclease XPF DNA excision repair protein ERCC-4 DNA repair protein complementing XP-F cells Xeroderma pigmentosum group F-complementing protein
External Links
UniProt	Q92889
EMBL	L77890 AF491814 AK289726 AC010401 BC142631 U64315
CCDS	CCDS32390.1
RefSeq	NP_005227.1
UniGene	Hs.567265
PDB	1Z00 2A1J 2AQ0 2KN7
PDBsum	1Z00 2A1J 2AQ0 2KN7
ProteinModelPortal	Q92889
SMR	Q92889
BioGrid	108384
DIP	DIP-42006N
IntAct	Q92889
MINT	MINT-192303
STRING	9606.ENSP00000310520
PhosphoSite	Q92889
DMDM	229463004
MaxQB	Q92889
PaxDb	Q92889
PRIDE	Q92889
DNASU	2072
Ensembl	ENST00000311895 ENST00000575156
GeneID	2072
KEGG	hsa:2072
UCSC	uc002dce.2 uc010bva.3
CTD	2072
GeneCards	GC16P014014
GeneReviews	ERCC4
H-InvDB	HIX0038603 HIX0173284
HGNC	HGNC:3436
HPA	CAB000156 HPA045828
MIM	133520 278760 610965 615272
neXtProt	NX_Q92889
Orphanet	90321 84 276264
PharmGKB	PA27850
eggNOG	COG1948
GeneTree	ENSGT00390000004394
HOGENOM	HOG000202204
HOVERGEN	HBG051500
InParanoid	Q92889
KO	K10848
OMA	QQSIVVD
OrthoDB	EOG7VTDM8
PhylomeDB	Q92889
TreeFam	TF101234
Reactome	REACT_1941 REACT_2222 REACT_257 REACT_311
EvolutionaryTrace	Q92889
GeneWiki	ERCC4
GenomeRNAi	2072
NextBio	35462247
PRO	PR:Q92889
Proteomes	UP000005640
Bgee	Q92889
CleanEx	HS_ERCC4
ExpressionAtlas	Q92889
Genevestigator	Q92889
GO	GO:0000781 GO:0000784 GO:0005654 GO:0000109 GO:0000110 GO:0005634 GO:0005669 GO:0003684 GO:0004520 GO:0008022 GO:0047485 GO:0003697 GO:0000014 GO:0000737 GO:0006281 GO:0000724 GO:0032205 GO:0006289 GO:1901255 GO:0000718 GO:0033683 GO:0006295 GO:0006296 GO:0000712 GO:0009411 GO:0000723 GO:0010834 GO:0006283 GO:0009650
Gene3D	3.40.50.10130
InterPro	IPR020819 IPR006166 IPR006167 IPR011335 IPR010994
Pfam	PF02732
SMART	SM00891
SUPFAM	SSF47781 SSF52980
TIGRFAMs	TIGR00596

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
involved_in	GO:1905768	negative regulation of double-stranded telomeric DNA binding	PMID:18812185^[1]	ECO:0000314	direct assay evidence used in manual assertion		P	regulates_activity_of:(UniProtKB:Q15554)	Seeded From UniProt	complete
NOT\|involved_in	GO:0051974	negative regulation of telomerase activity	PMID:18812185^[1]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
NOT\|enables	GO:0010521	telomerase inhibitor activity	PMID:18812185^[1]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:1904357	negative regulation of telomere maintenance via telomere lengthening	PMID:18812185^[1]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0070522	ERCC4-ERCC1 complex	PMID:17055345^[2]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0004520	endodeoxyribonuclease activity	PMID:17055345^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0034644	cellular response to UV	PMID:17055345^[2]	ECO:0000316	genetic interaction evidence used in manual assertion	UniProtKB:Q15554	P		Seeded From UniProt	complete
involved_in	GO:0006281	DNA repair	PMID:17055345^[2]	ECO:0000316	genetic interaction evidence used in manual assertion	UniProtKB:Q15554	P		Seeded From UniProt	complete
involved_in	GO:0000723	telomere maintenance	PMID:17055345^[2]	ECO:0000316	genetic interaction evidence used in manual assertion	UniProtKB:Q15554	P		Seeded From UniProt	complete
involved_in	GO:0061819	telomeric DNA-containing double minutes formation	PMID:14690602^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:1905765	negative regulation of protection from non-homologous end joining at telomere	PMID:14690602^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006303	double-strand break repair via nonhomologous end joining	PMID:14690602^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	occurs_at:(GO:0000784)	Seeded From UniProt	complete
part_of	GO:0070522	ERCC4-ERCC1 complex	PMID:14690602^[3]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
contributes_to	GO:1990599	3' overhang single-stranded DNA endodeoxyribonuclease activity	PMID:14690602^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		F	occurs_at:(GO:0000784) part_of:(GO:0006303)	Seeded From UniProt	complete
part_of	GO:0000781	chromosome, telomeric region	PMID:14690602^[3]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0000723	telomere maintenance	PMID:14690602^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0047485	protein N-terminus binding	PMID:14734547^[4]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P43351	F		Seeded From UniProt	complete
contributes_to	GO:0003677	DNA binding	PMID:14734547^[4]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0033683	nucleotide-excision repair, DNA incision	PMID:10413517^[5]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0032205	negative regulation of telomere maintenance	PMID:17055345^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0009411	response to UV	PMID:16678501^[6]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0008022	protein C-terminus binding	PMID:9722633^[7]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P07992	F		Seeded From UniProt	complete
involved_in	GO:0006296	nucleotide-excision repair, DNA incision, 5'-to lesion	PMID:14728600^[8]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006296	nucleotide-excision repair, DNA incision, 5'-to lesion	PMID:11790111^[9]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006295	nucleotide-excision repair, DNA incision, 3'-to lesion	PMID:11790111^[9]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006289	nucleotide-excision repair	PMID:8797827^[10]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006281	DNA repair	PMID:19596235^[11]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:12571280^[12]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0004520	endodeoxyribonuclease activity	PMID:10413517^[5]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0004520	endodeoxyribonuclease activity	PMID:14734547^[4]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
contributes_to	GO:0004520	endodeoxyribonuclease activity	PMID:8797827^[10]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0003697	single-stranded DNA binding	PMID:10413517^[5]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0003684	damaged DNA binding	PMID:11790111^[9]	ECO:0000315	mutant phenotype evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0000784	nuclear chromosome, telomeric region	PMID:14690602^[3]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0000724	double-strand break repair via homologous recombination	PMID:14728600^[8]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0000110	nucleotide-excision repair factor 1 complex	PMID:10413517^[5]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:1901255	nucleotide-excision repair involved in interstrand cross-link repair	PMID:21873635^[13]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000015911 PomBase:SPCC970.01	P		Seeded From UniProt	complete
involved_in	GO:0006296	nucleotide-excision repair, DNA incision, 5'-to lesion	PMID:21873635^[13]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000015911 SGD:S000005943 UniProtKB:Q92889	P		Seeded From UniProt	complete
enables	GO:0003697	single-stranded DNA binding	PMID:21873635^[13]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000015911 SGD:S000005943 UniProtKB:Q92889	F		Seeded From UniProt	complete
enables	GO:0003684	damaged DNA binding	PMID:21873635^[13]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000015911 UniProtKB:Q92889	F		Seeded From UniProt	complete
involved_in	GO:0000724	double-strand break repair via homologous recombination	PMID:21873635^[13]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000015911 PomBase:SPCC970.01 UniProtKB:Q92889 UniProtKB:Q9LKI5 dictyBase:DDB_G0284419	P		Seeded From UniProt	complete
involved_in	GO:0000712	resolution of meiotic recombination intermediates	PMID:21873635^[13]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0002707 PANTHER:PTN000015911 WB:WBGene00008140	P		Seeded From UniProt	complete
part_of	GO:0000110	nucleotide-excision repair factor 1 complex	PMID:21873635^[13]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000015911 PomBase:SPCC970.01 SGD:S000005943 UniProtKB:Q92889	C		Seeded From UniProt	complete
enables	GO:0000014	single-stranded DNA endodeoxyribonuclease activity	PMID:21873635^[13]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000015911 SGD:S000005943 UniProtKB:Q9LKI5	F		Seeded From UniProt	complete
involved_in	GO:0006289	nucleotide-excision repair	PMID:10644440^[14]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0000109	nucleotide-excision repair complex	PMID:10644440^[14]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:22483113^[15]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q92889	F		Seeded From UniProt	complete
involved_in	GO:0051974	negative regulation of telomerase activity	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0010521	P		Seeded From UniProt	complete
involved_in	GO:0010506	regulation of autophagy	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9QZD4 ensembl:ENSMUSP00000023206	P		Seeded From UniProt	complete
involved_in	GO:0009650	UV protection	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9QZD4 ensembl:ENSMUSP00000023206	P		Seeded From UniProt	complete
involved_in	GO:0006281	DNA repair	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9QZD4 ensembl:ENSMUSP00000023206	P		Seeded From UniProt	complete
part_of	GO:0005669	transcription factor TFIID complex	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9QZD4 ensembl:ENSMUSP00000023206	C		Seeded From UniProt	complete
enables	GO:0001094	TFIID-class transcription factor complex binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9QZD4 ensembl:ENSMUSP00000023206	F		Seeded From UniProt	complete
enables	GO:0003677	DNA binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR006166	F		Seeded From UniProt	complete
enables	GO:0003697	single-stranded DNA binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR006167	F		Seeded From UniProt	complete
enables	GO:0004518	nuclease activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR006166	F		Seeded From UniProt	complete
enables	GO:0004520	endodeoxyribonuclease activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR006167	F		Seeded From UniProt	complete
involved_in	GO:0006281	DNA repair	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR006167	P		Seeded From UniProt	complete
involved_in	GO:0070911	global genome nucleotide-excision repair	Reactome:R-HSA-5696399	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0036297	interstrand cross-link repair	Reactome:R-HSA-6783310	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0033683	nucleotide-excision repair, DNA incision	Reactome:R-HSA-5696400	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006296	nucleotide-excision repair, DNA incision, 5'-to lesion	Reactome:R-HSA-5690988	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006295	nucleotide-excision repair, DNA incision, 3'-to lesion	Reactome:R-HSA-5690990	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006293	nucleotide-excision repair, preincision complex stabilization	Reactome:R-HSA-5690991	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006283	transcription-coupled nucleotide-excision repair	Reactome:R-HSA-6781827	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005654	nucleoplasm	Reactome:R-HSA-6785986 Reactome:R-HSA-6785732 Reactome:R-HSA-6782224 Reactome:R-HSA-6782211 Reactome:R-HSA-6782204 Reactome:R-HSA-6782141 Reactome:R-HSA-5690991 Reactome:R-HSA-5690990 Reactome:R-HSA-5690988 Reactome:R-HSA-5690213 Reactome:R-HSA-5686657 Reactome:R-HSA-109955	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0003677	DNA binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0238	F		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0539 UniProtKB-SubCell:SL-0191	C		Seeded From UniProt	complete
involved_in	GO:0006974	cellular response to DNA damage stimulus	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0227	P		Seeded From UniProt	complete
enables	GO:0016787	hydrolase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0378	F		Seeded From UniProt	complete
involved_in	GO:0006281	DNA repair	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0234	P		Seeded From UniProt	complete
enables	GO:0004518	nuclease activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0540	F		Seeded From UniProt	complete
enables	GO:0004519	endonuclease activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0255	F		Seeded From UniProt	complete
edit table

Notes

References

See Help:References for how to manage references in GONUTS.

↑ ^1.0 ^1.1 ^1.2 ^1.3 Wu, Y et al. (2008) Human XPF controls TRF2 and telomere length maintenance through distinctive mechanisms. Mech. Ageing Dev. 129 602-10 PubMed GONUTS page
↑ ^2.0 ^2.1 ^2.2 ^2.3 ^2.4 ^2.5 Wu, Y et al. (2007) XPF with mutations in its conserved nuclease domain is defective in DNA repair but functions in TRF2-mediated telomere shortening. DNA Repair (Amst.) 6 157-66 PubMed GONUTS page
↑ ^3.0 ^3.1 ^3.2 ^3.3 ^3.4 ^3.5 ^3.6 ^3.7 Zhu, XD et al. (2003) ERCC1/XPF removes the 3' overhang from uncapped telomeres and represses formation of telomeric DNA-containing double minute chromosomes. Mol. Cell 12 1489-98 PubMed GONUTS page
↑ ^4.0 ^4.1 ^4.2 Motycka, TA et al. (2004) Physical and functional interaction between the XPF/ERCC1 endonuclease and hRad52. J. Biol. Chem. 279 13634-9 PubMed GONUTS page
↑ ^5.0 ^5.1 ^5.2 ^5.3 McCutchen-Maloney, SL et al. (1999) Domain mapping of the DNA binding, endonuclease, and ERCC1 binding properties of the human DNA repair protein XPF. Biochemistry 38 9417-25 PubMed GONUTS page
↑ Mogi, S & Oh, DH (2006) gamma-H2AX formation in response to interstrand crosslinks requires XPF in human cells. DNA Repair (Amst.) 5 731-40 PubMed GONUTS page
↑ de Laat, WL et al. (1998) Mapping of interaction domains between human repair proteins ERCC1 and XPF. Nucleic Acids Res. 26 4146-52 PubMed GONUTS page
↑ ^8.0 ^8.1 Chen, Z et al. (2004) Defining the function of xeroderma pigmentosum group F protein in psoralen interstrand cross-link-mediated DNA repair and mutagenesis. Biochem. J. 379 71-8 PubMed GONUTS page
↑ ^9.0 ^9.1 ^9.2 Kumaresan, KR et al. (2002) Contribution of XPF functional domains to the 5' and 3' incisions produced at the site of a psoralen interstrand cross-link. Biochemistry 41 890-6 PubMed GONUTS page
↑ ^10.0 ^10.1 Sijbers, AM et al. (1996) Xeroderma pigmentosum group F caused by a defect in a structure-specific DNA repair endonuclease. Cell 86 811-22 PubMed GONUTS page
↑ Svendsen, JM et al. (2009) Mammalian BTBD12/SLX4 assembles a Holliday junction resolvase and is required for DNA repair. Cell 138 63-77 PubMed GONUTS page
↑ Sridharan, D et al. (2003) Nonerythroid alphaII spectrin is required for recruitment of FANCA and XPF to nuclear foci induced by DNA interstrand cross-links. J. Cell. Sci. 116 823-35 PubMed GONUTS page
↑ ^13.0 ^13.1 ^13.2 ^13.3 ^13.4 ^13.5 ^13.6 ^13.7 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ ^14.0 ^14.1 Shannon, M et al. (1999) Characterization of the mouse Xpf DNA repair gene and differential expression during spermatogenesis. Genomics 62 427-35 PubMed GONUTS page
↑ Das, D et al. (2012) The structure of the XPF-ssDNA complex underscores the distinct roles of the XPF and ERCC1 helix- hairpin-helix domains in ss/ds DNA recognition. Structure 20 667-75 PubMed GONUTS page

[PMID:18812185-1] 1.0 ^1.1 ^1.2 ^1.3 Wu, Y et al. (2008) Human XPF controls TRF2 and telomere length maintenance through distinctive mechanisms. Mech. Ageing Dev. 129 602-10 PubMed GONUTS page

[PMID:17055345-2] 2.0 ^2.1 ^2.2 ^2.3 ^2.4 ^2.5 Wu, Y et al. (2007) XPF with mutations in its conserved nuclease domain is defective in DNA repair but functions in TRF2-mediated telomere shortening. DNA Repair (Amst.) 6 157-66 PubMed GONUTS page

[PMID:14690602-3] 3.0 ^3.1 ^3.2 ^3.3 ^3.4 ^3.5 ^3.6 ^3.7 Zhu, XD et al. (2003) ERCC1/XPF removes the 3' overhang from uncapped telomeres and represses formation of telomeric DNA-containing double minute chromosomes. Mol. Cell 12 1489-98 PubMed GONUTS page

[PMID:14734547-4] 4.0 ^4.1 ^4.2 Motycka, TA et al. (2004) Physical and functional interaction between the XPF/ERCC1 endonuclease and hRad52. J. Biol. Chem. 279 13634-9 PubMed GONUTS page

[PMID:10413517-5] 5.0 ^5.1 ^5.2 ^5.3 McCutchen-Maloney, SL et al. (1999) Domain mapping of the DNA binding, endonuclease, and ERCC1 binding properties of the human DNA repair protein XPF. Biochemistry 38 9417-25 PubMed GONUTS page

[PMID:16678501-6] Mogi, S & Oh, DH (2006) gamma-H2AX formation in response to interstrand crosslinks requires XPF in human cells. DNA Repair (Amst.) 5 731-40 PubMed GONUTS page

[PMID:9722633-7] Laat, WL et al. (1998) Mapping of interaction domains between human repair proteins ERCC1 and XPF. Nucleic Acids Res. 26 4146-52 PubMed GONUTS page

[PMID:14728600-8] 8.0 ^8.1 Chen, Z et al. (2004) Defining the function of xeroderma pigmentosum group F protein in psoralen interstrand cross-link-mediated DNA repair and mutagenesis. Biochem. J. 379 71-8 PubMed GONUTS page

[PMID:11790111-9] 9.0 ^9.1 ^9.2 Kumaresan, KR et al. (2002) Contribution of XPF functional domains to the 5' and 3' incisions produced at the site of a psoralen interstrand cross-link. Biochemistry 41 890-6 PubMed GONUTS page

[PMID:8797827-10] 10.0 ^10.1 Sijbers, AM et al. (1996) Xeroderma pigmentosum group F caused by a defect in a structure-specific DNA repair endonuclease. Cell 86 811-22 PubMed GONUTS page

[PMID:19596235-11] Svendsen, JM et al. (2009) Mammalian BTBD12/SLX4 assembles a Holliday junction resolvase and is required for DNA repair. Cell 138 63-77 PubMed GONUTS page

[PMID:12571280-12] Sridharan, D et al. (2003) Nonerythroid alphaII spectrin is required for recruitment of FANCA and XPF to nuclear foci induced by DNA interstrand cross-links. J. Cell. Sci. 116 823-35 PubMed GONUTS page

[PMID:21873635-13] 13.0 ^13.1 ^13.2 ^13.3 ^13.4 ^13.5 ^13.6 ^13.7 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

[PMID:10644440-14] 14.0 ^14.1 Shannon, M et al. (1999) Characterization of the mouse Xpf DNA repair gene and differential expression during spermatogenesis. Genomics 62 427-35 PubMed GONUTS page

[PMID:22483113-15] Das, D et al. (2012) The structure of the XPF-ssDNA complex underscores the distinct roles of the XPF and ERCC1 helix- hairpin-helix domains in ss/ds DNA recognition. Structure 20 667-75 PubMed GONUTS page

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HUMAN:XPF

Contents

Annotations

Notes

References

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