XPA_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: XPA_HUMAN
• UniProt AC: P23025
• Protein Name: DNA repair protein complementing XP-A cells
• Gene Name: XPA
• Organism: Homo sapiens (Human).
• Sequence Length: 273
• Subcellular Localization: Nucleus .
• Protein Description: Involved in DNA excision repair. Initiates repair by binding to damaged sites with various affinities, depending on the photoproduct and the transcriptional state of the region. Required for UV-induced CHEK1 phosphorylation and the recruitment of CEP164 to cyclobutane pyrimidine dimmers (CPD), sites of DNA damage after UV irradiation..
• Protein Sequence: MAAADGALPEAAALEQPAELPASVRASIERKRQRALMLRQARLAARPYSATAAAATGGMANVKAAPKIIDTGGGFILEEEEEEEQKIGKVVHQPGPVMEFDYVICEECGKEFMDSYLMNHFDLPTCDNCRDADDKHKLITKTEAKQEYLLKDCDLEKREPPLKFIVKKNPHHSQWGDMKLYLKLQIVKRSLEVWGSQEALEEAKEVRQENREKMKQKKFDKKVKELRRAVRSSVWKRETIVHQHEYGPEENLEDDMYRKTCTMCGHELTYEKM

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAAADGALP ------CCCCCCCCC	16.03	22814378
48	Phosphorylation	ARLAARPYSATAAAA HHHHCCCCCHHHHHH	12.84	26552605
49	Phosphorylation	RLAARPYSATAAAAT HHHCCCCCHHHHHHH	23.09	26552605
51	Phosphorylation	AARPYSATAAAATGG HCCCCCHHHHHHHCC	15.76	26552605
56	Phosphorylation	SATAAAATGGMANVK CHHHHHHHCCCCCCC	29.55	26552605
63	Sumoylation	TGGMANVKAAPKIID HCCCCCCCCCCEEEE	38.34	-
63	Sumoylation	TGGMANVKAAPKIID HCCCCCCCCCCEEEE	38.34	28112733
63	Acetylation	TGGMANVKAAPKIID HCCCCCCCCCCEEEE	38.34	20670893
67	Ubiquitination	ANVKAAPKIIDTGGG CCCCCCCEEEECCCC	47.79	29967540
67	Acetylation	ANVKAAPKIIDTGGG CCCCCCCEEEECCCC	47.79	20670893
86	Sumoylation	EEEEEEQKIGKVVHQ CHHHHHHHHCCCCCC	57.62	28112733
141	Ubiquitination	DKHKLITKTEAKQEY CCCCEECHHHHHHHH	37.06	29967540
141	Sumoylation	DKHKLITKTEAKQEY CCCCEECHHHHHHHH	37.06	-
141	Sumoylation	DKHKLITKTEAKQEY CCCCEECHHHHHHHH	37.06	-
145	Sumoylation	LITKTEAKQEYLLKD EECHHHHHHHHHHHC	37.11	25218447
145	Ubiquitination	LITKTEAKQEYLLKD EECHHHHHHHHHHHC	37.11	29967540
145	Sumoylation	LITKTEAKQEYLLKD EECHHHHHHHHHHHC	37.11	-
151	Ubiquitination	AKQEYLLKDCDLEKR HHHHHHHHCCCHHHC	54.43	29967540
157	Acetylation	LKDCDLEKREPPLKF HHCCCHHHCCCCCEE	70.16	23749302
168	Ubiquitination	PLKFIVKKNPHHSQW CCEEEEECCCCCCCC	65.89	29967540
173	Phosphorylation	VKKNPHHSQWGDMKL EECCCCCCCCCCHHH	25.29	22817900
196	Phosphorylation	RSLEVWGSQEALEEA HHHHHHCCHHHHHHH	14.77	17525332
204	Ubiquitination	QEALEEAKEVRQENR HHHHHHHHHHHHHHH	61.08	29967540
215	Acetylation	QENREKMKQKKFDKK HHHHHHHHHHHHHHH	70.77	-
239	Phosphorylation	SSVWKRETIVHQHEY HCHHHHCCCCCCCCC	32.12	-
257	Phosphorylation	ENLEDDMYRKTCTMC CCCCCHHHHHHHHHC	18.89	-
259	Ubiquitination	LEDDMYRKTCTMCGH CCCHHHHHHHHHCCC	30.39	29967540

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
173	S	Phosphorylation	Kinase	ATM	Q13315	PSP
173	S	Phosphorylation	Kinase	ATR	Q13535	PSP
173	S	Phosphorylation	Kinase	PRKDC	P78527	GPS
196	S	Phosphorylation	Kinase	ATM	Q13315	PSP
196	S	Phosphorylation	Kinase	ATR	Q13535	PSP
196	S	Phosphorylation	Kinase	PRKDC	P78527	GPS
-	K	Ubiquitination	E3 ubiquitin ligase	HERC2	O95714	PMID:21193487

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
196	S	Phosphorylation	ATR-dependent phosphorylation of XPA at Ser-196 is important for cell survival in response to UV damage.	16540648

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of XPA_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RFA4_HUMAN	RPA4	physical	7565690
GPN1_HUMAN	GPN1	physical	11058119
ERCC1_HUMAN	ERCC1	physical	8197174
RFA2_HUMAN	RPA2	physical	11081631
SYF1_HUMAN	XAB2	physical	10944529
T2EB_HUMAN	GTF2E2	physical	7876263
RFA1_HUMAN	RPA1	physical	7565690
RFA2_HUMAN	RPA2	physical	20670893
ORF73_HHV8P	HHV8GK18_gp81	physical	22379092
DDB1_HUMAN	DDB1	physical	19056823
DDB2_HUMAN	DDB2	physical	19056823
ERCC1_HUMAN	ERCC1	physical	19056823
HMGB1_HUMAN	HMGB1	physical	19446504
RFA1_HUMAN	RPA1	physical	19446504
ATR_HUMAN	ATR	physical	16540648
ATR_HUMAN	ATR	physical	23178497
HERC2_HUMAN	HERC2	physical	23178497
NDEL1_HUMAN	NDEL1	physical	25416956
XPF_HUMAN	ERCC4	physical	26186194
ERCC1_HUMAN	ERCC1	physical	26186194
NUP43_HUMAN	NUP43	physical	26186194
Z518A_HUMAN	ZNF518A	physical	26186194
ERCC1_HUMAN	ERCC1	physical	28514442
XPF_HUMAN	ERCC4	physical	28514442
NUP43_HUMAN	NUP43	physical	28514442
Z518A_HUMAN	ZNF518A	physical	28514442
SPTA1_HUMAN	SPTA1	physical	16889989

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• 278700: Xeroderma pigmentosum complementation group A (XP-A)
• Kegg Drug
• There are no disease associations of PTM sites.
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Acetylation

"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
PubMed: 19413330

Phosphorylation

"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-196, AND MASSSPECTROMETRY.
PubMed: 17525332