HUMAN:XPA

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	XPA (synonyms: XPAC)
Protein Name(s)	DNA repair protein complementing XP-A cells Xeroderma pigmentosum group A-complementing protein
External Links
UniProt	P23025
EMBL	D14533 BT019518 AF503166 AL445531 CH471105 BC014965 U16815 U10347 U10343 U10344 U10345 U10346
CCDS	CCDS6729.1
PIR	I38886 JG0190
RefSeq	NP_000371.1
UniGene	Hs.654364
PDB	1D4U 1XPA 2JNW
PDBsum	1D4U 1XPA 2JNW
DisProt	DP00243
ProteinModelPortal	P23025
SMR	P23025
BioGrid	113344
DIP	DIP-24191N
IntAct	P23025
MINT	MINT-192332
STRING	9606.ENSP00000364270
PhosphoSite	P23025
DMDM	139816
MaxQB	P23025
PaxDb	P23025
PRIDE	P23025
DNASU	7507
Ensembl	ENST00000375128
GeneID	7507
KEGG	hsa:7507
UCSC	uc004axr.4
CTD	7507
GeneCards	GC09M100437
GeneReviews	XPA
HGNC	HGNC:12814
HPA	CAB000155 HPA030997 HPA056856
MIM	278700 611153
neXtProt	NX_P23025
Orphanet	276249
PharmGKB	PA368
eggNOG	COG5145
GeneTree	ENSGT00390000002721
HOGENOM	HOG000045820
HOVERGEN	HBG009053
InParanoid	P23025
KO	K10847
OMA	MKLYLHL
PhylomeDB	P23025
TreeFam	TF101241
Reactome	REACT_257 REACT_311
EvolutionaryTrace	P23025
GeneWiki	XPA
GenomeRNAi	7507
NextBio	29387
PRO	PR:P23025
Proteomes	UP000005640
Bgee	P23025
CleanEx	HS_XPA
ExpressionAtlas	P23025
Genevestigator	P23025
GO	GO:0005737 GO:0005794 GO:0045171 GO:0005654 GO:0005634 GO:0003684 GO:0046872 GO:0019904 GO:0042803 GO:0006281 GO:0008630 GO:0035264 GO:0006289 GO:0000718 GO:0006979 GO:0009636 GO:0009411
Gene3D	3.90.530.10
InterPro	IPR009061 IPR000465 IPR022656 IPR022658 IPR022652
PANTHER	PTHR10142
Pfam	PF05181 PF01286
SUPFAM	SSF46955
TIGRFAMs	TIGR00598
PROSITE	PS00752 PS00753

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
	GO:0033683	nucleotide-excision repair, DNA incision	PMID:21148310^[1]	ECO:0000315			P		In Fig.6, XPA nucleotide-excision repair activity is shown through mutant phenotype.	complete CACAO 6331
Colocalizes with	GO:0005730	nucleolus	PMID:28416769^[2]	ECO:0000314			C		UniProt’s Protein Name: DNA repair protein complementing XP-A cells. Paper’s Protein Name: XPA. Organism: Homo sapiens. Notes: Figure 1C is used. According to the paper, the researchers “observed a distinct enrichment of XPA, a critical NER protein [1] in the nucleolus of pre-extracted U2OS and MRC5 cells, starting at 1 hour after UV irradiation.” This can indeed be seen in the cell visualization for Figure 1C. As this only occur after one hour of UV irradiation, the relationship between this protein and the nucleolus is quite clearly transient, and the Colocalizes with qualifier is necessary. U2OS and MRC5 cells are human cells, so the protein is human as well.	complete CACAO 12679
involved_in	GO:0009650	UV protection	PMID:1601884^[3]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0009650	UV protection	PMID:1601884^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0034504	protein localization to nucleus	PMID:1601884^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	has_input:(UniProtKB:P23025)	Seeded From UniProt	complete
involved_in	GO:0006281	DNA repair	PMID:1601884^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0033683	nucleotide-excision repair, DNA incision	PMID:21148310^[1]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006281	DNA repair	PMID:1601884^[3]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:1601884^[3]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0042803	protein homodimerization activity	PMID:8197175^[4]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P23025	F		Seeded From UniProt	complete
enables	GO:0019904	protein domain specific binding	PMID:17720715^[5]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P07992	F		Seeded From UniProt	complete
colocalizes_with	GO:0005662	DNA replication factor A complex	PMID:7700386^[6]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0003684	damaged DNA binding	PMID:7700386^[6]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:1901255	nucleotide-excision repair involved in interstrand cross-link repair	PMID:21873635^[7]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000015717 PomBase:SPBC649.03	P		Seeded From UniProt	complete
involved_in	GO:0070914	UV-damage excision repair	PMID:21873635^[7]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000015717 PomBase:SPBC649.03 WB:WBGene00006963	P		Seeded From UniProt	complete
involved_in	GO:0033683	nucleotide-excision repair, DNA incision	PMID:21873635^[7]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000015717 UniProtKB:P23025	P		Seeded From UniProt	complete
involved_in	GO:0006284	base-excision repair	PMID:21873635^[7]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000015717 WB:WBGene00006963	P		Seeded From UniProt	complete
enables	GO:0003684	damaged DNA binding	PMID:21873635^[7]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000015717 SGD:S000004814 UniProtKB:P23025	F		Seeded From UniProt	complete
involved_in	GO:0000715	nucleotide-excision repair, DNA damage recognition	PMID:21873635^[7]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000015717 SGD:S000004814	P		Seeded From UniProt	complete
part_of	GO:0000110	nucleotide-excision repair factor 1 complex	PMID:21873635^[7]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000015717 SGD:S000004814	C		Seeded From UniProt	complete
part_of	GO:0045171	intercellular bridge	GO_REF:0000052	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000052	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0010996	response to auditory stimulus	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:D4A981 ensembl:ENSRNOP00000059280	P		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:D4A981 ensembl:ENSRNOP00000059280	C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:D4A981 ensembl:ENSRNOP00000059280	C		Seeded From UniProt	complete
involved_in	GO:0035264	multicellular organism growth	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q64267 ensembl:ENSMUSP00000030013	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:Q64267 ensembl:ENSMUSP00000030013	P		Seeded From UniProt	complete
involved_in	GO:0009636	response to toxic substance	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q64267 ensembl:ENSMUSP00000030013	P		Seeded From UniProt	complete
involved_in	GO:0009411	response to UV	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q64267 ensembl:ENSMUSP00000030013	P		Seeded From UniProt	complete
involved_in	GO:0008630	intrinsic apoptotic signaling pathway in response to DNA damage	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q64267 ensembl:ENSMUSP00000030013	P		Seeded From UniProt	complete
involved_in	GO:0006979	response to oxidative stress	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q64267 ensembl:ENSMUSP00000030013	P		Seeded From UniProt	complete
involved_in	GO:0006289	nucleotide-excision repair	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q64267 ensembl:ENSMUSP00000030013	P		Seeded From UniProt	complete
involved_in	GO:0006281	DNA repair	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q64267 ensembl:ENSMUSP00000030013	P		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q64267 ensembl:ENSMUSP00000030013	C		Seeded From UniProt	complete
enables	GO:0003684	damaged DNA binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000465	F		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000465	C		Seeded From UniProt	complete
involved_in	GO:0006289	nucleotide-excision repair	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000465	P		Seeded From UniProt	complete
enables	GO:0003684	damaged DNA binding	PMID:10946233^[8]	ECO:0000304	author statement supported by traceable reference used in manual assertion		F		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: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:0006294	nucleotide-excision repair, preincision complex assembly	Reactome:R-HSA-5689861 Reactome:R-HSA-5689317	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-6790487 Reactome:R-HSA-6790454 Reactome:R-HSA-6782224 Reactome:R-HSA-6782211 Reactome:R-HSA-6782204 Reactome:R-HSA-6782141 Reactome:R-HSA-6782138 Reactome:R-HSA-6782131 Reactome:R-HSA-6782069 Reactome:R-HSA-6782004 Reactome:R-HSA-5696670 Reactome:R-HSA-5690996 Reactome:R-HSA-5690991 Reactome:R-HSA-5690990 Reactome:R-HSA-5690988 Reactome:R-HSA-5690213 Reactome:R-HSA-5689861 Reactome:R-HSA-5689317	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0000717	nucleotide-excision repair, DNA duplex unwinding	Reactome:R-HSA-5690996	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		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: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
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
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
enables	GO:0046872	metal ion binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0479	F		Seeded From UniProt	complete
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Notes

References

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

↑ ^1.0 ^1.1 Saijo, M et al. (2011) Nucleotide excision repair by mutant xeroderma pigmentosum group A (XPA) proteins with deficiency in interaction with RPA. J. Biol. Chem. 286 5476-83 PubMed GONUTS page
↑ Chitale, S & Richly, H (2017) Nuclear organization of nucleotide excision repair is mediated by RING1B dependent H2A-ubiquitylation. Oncotarget PubMed GONUTS page
↑ ^3.0 ^3.1 ^3.2 ^3.3 ^3.4 ^3.5 Miyamoto, I et al. (1992) Mutational analysis of the structure and function of the xeroderma pigmentosum group A complementing protein. Identification of essential domains for nuclear localization and DNA excision repair. J. Biol. Chem. 267 12182-7 PubMed GONUTS page
↑ Park, CH & Sancar, A (1994) Formation of a ternary complex by human XPA, ERCC1, and ERCC4(XPF) excision repair proteins. Proc. Natl. Acad. Sci. U.S.A. 91 5017-21 PubMed GONUTS page
↑ Tripsianes, K et al. (2007) Analysis of the XPA and ssDNA-binding surfaces on the central domain of human ERCC1 reveals evidence for subfunctionalization. Nucleic Acids Res. 35 5789-98 PubMed GONUTS page
↑ ^6.0 ^6.1 He, Z et al. (1995) RPA involvement in the damage-recognition and incision steps of nucleotide excision repair. Nature 374 566-9 PubMed GONUTS page
↑ ^7.0 ^7.1 ^7.2 ^7.3 ^7.4 ^7.5 ^7.6 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ Morikawa, K & Shirakawa, M (2000) Three-dimensional structural views of damaged-DNA recognition: T4 endonuclease V, E. coli Vsr protein, and human nucleotide excision repair factor XPA. Mutat. Res. 460 257-75 PubMed GONUTS page

[PMID:21148310-1] 1.0 ^1.1 Saijo, M et al. (2011) Nucleotide excision repair by mutant xeroderma pigmentosum group A (XPA) proteins with deficiency in interaction with RPA. J. Biol. Chem. 286 5476-83 PubMed GONUTS page

[PMID:28416769-2] Chitale, S & Richly, H (2017) Nuclear organization of nucleotide excision repair is mediated by RING1B dependent H2A-ubiquitylation. Oncotarget PubMed GONUTS page

[PMID:1601884-3] 3.0 ^3.1 ^3.2 ^3.3 ^3.4 ^3.5 Miyamoto, I et al. (1992) Mutational analysis of the structure and function of the xeroderma pigmentosum group A complementing protein. Identification of essential domains for nuclear localization and DNA excision repair. J. Biol. Chem. 267 12182-7 PubMed GONUTS page

[PMID:8197175-4] Park, CH & Sancar, A (1994) Formation of a ternary complex by human XPA, ERCC1, and ERCC4(XPF) excision repair proteins. Proc. Natl. Acad. Sci. U.S.A. 91 5017-21 PubMed GONUTS page

[PMID:17720715-5] Tripsianes, K et al. (2007) Analysis of the XPA and ssDNA-binding surfaces on the central domain of human ERCC1 reveals evidence for subfunctionalization. Nucleic Acids Res. 35 5789-98 PubMed GONUTS page

[PMID:7700386-6] 6.0 ^6.1 He, Z et al. (1995) RPA involvement in the damage-recognition and incision steps of nucleotide excision repair. Nature 374 566-9 PubMed GONUTS page

[PMID:21873635-7] 7.0 ^7.1 ^7.2 ^7.3 ^7.4 ^7.5 ^7.6 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:10946233-8] Morikawa, K & Shirakawa, M (2000) Three-dimensional structural views of damaged-DNA recognition: T4 endonuclease V, E. coli Vsr protein, and human nucleotide excision repair factor XPA. Mutat. Res. 460 257-75 PubMed GONUTS page

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HUMAN:XPA

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