dbPTM

EYA4_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	EYA4_HUMAN
UniProt AC	O95677
Protein Name	Eyes absent homolog 4
Gene Name	EYA4
Organism	Homo sapiens (Human).
Sequence Length	639
Subcellular Localization	Cytoplasm . Nucleus .
Protein Description	Tyrosine phosphatase that specifically dephosphorylates 'Tyr-142' of histone H2AX (H2AXY142ph). 'Tyr-142' phosphorylation of histone H2AX plays a central role in DNA repair and acts as a mark that distinguishes between apoptotic and repair responses to genotoxic stress. Promotes efficient DNA repair by dephosphorylating H2AX, promoting the recruitment of DNA repair complexes containing MDC1. Its function as histone phosphatase probably explains its role in transcription regulation during organogenesis. May be involved in development of the eye (By similarity)..
Protein Sequence	MEDSQDLNEQSVKKTCTESDVSQSQNSRSMEMQDLASPHTLVGGGDTPGSSKLEKSNLSSTSVTTNGTGGENMTVLNTADWLLSCNTPSSATMSLLAVKTEPLNSSETTATTGDGALDTFTGSVITSSGYSPRSAHQYSPQLYPSKPYPHILSTPAAQTMSAYAGQTQYSGMQQPAVYTAYSQTGQPYSLPTYDLGVMLPAIKTESGLSQTQSPLQSGCLSYSPGFSTPQPGQTPYSYQMPGSSFAPSSTIYANNSVSNSTNFSGSQQDYPSYTAFGQNQYAQYYSASTYGAYMTSNNTADGTPSSTSTYQLQESLPGLTNQPGEFDTMQSPSTPIKDLDERTCRSSGSKSRGRGRKNNPSPPPDSDLERVFVWDLDETIIVFHSLLTGSYAQKYGKDPPMAVTLGLRMEEMIFNLADTHLFFNDLEECDQVHIDDVSSDDNGQDLSTYSFATDGFHAAASSANLCLPTGVRGGVDWMRKLAFRYRRVKELYNTYKNNVGGLLGPAKRDAWLQLRAEIEGLTDSWLTNALKSLSIISTRSNCINVLVTTTQLIPALAKVLLYSLGGAFPIENIYSATKIGKESCFERIMQRFGRKVVYVVIGDGVEEEQAAKKHNMPFWRISSHSDLLALHQALELEYL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MEDSQDLN -------CCCCHHHC	13.41	19413330
4	Phosphorylation	----MEDSQDLNEQS ----CCCCHHHCHHH	16.58	22167270
11	Phosphorylation	SQDLNEQSVKKTCTE CHHHCHHHHHHHHCH	29.71	22167270
14	Sumoylation	LNEQSVKKTCTESDV HCHHHHHHHHCHHHH	46.83	28112733
15	Phosphorylation	NEQSVKKTCTESDVS CHHHHHHHHCHHHHC	20.95	28509920
17	Phosphorylation	QSVKKTCTESDVSQS HHHHHHHCHHHHCHH	43.70	19690332
19	Phosphorylation	VKKTCTESDVSQSQN HHHHHCHHHHCHHHH	25.76	-
22	Phosphorylation	TCTESDVSQSQNSRS HHCHHHHCHHHHCCC	29.16	21815630
24	Phosphorylation	TESDVSQSQNSRSME CHHHHCHHHHCCCCH	24.67	21815630
27	Phosphorylation	DVSQSQNSRSMEMQD HHCHHHHCCCCHHHH	20.35	-
37	Phosphorylation	MEMQDLASPHTLVGG CHHHHHCCCCCEECC	25.22	21815630
40	Phosphorylation	QDLASPHTLVGGGDT HHHCCCCCEECCCCC	26.90	21815630
47	Phosphorylation	TLVGGGDTPGSSKLE CEECCCCCCCCCCCC	32.59	21815630
50	Phosphorylation	GGGDTPGSSKLEKSN CCCCCCCCCCCCCCC	26.04	29978859
51	Phosphorylation	GGDTPGSSKLEKSNL CCCCCCCCCCCCCCC	47.37	27732954
52	Sumoylation	GDTPGSSKLEKSNLS CCCCCCCCCCCCCCC	63.46	28112733
52	Acetylation	GDTPGSSKLEKSNLS CCCCCCCCCCCCCCC	63.46	26051181
99	Sumoylation	TMSLLAVKTEPLNSS EEEEEEEEEECCCCC	41.38	-
119	O-linked_Glycosylation	TGDGALDTFTGSVIT CCCCCCCEECCEEEE	24.77	30379171
126	Phosphorylation	TFTGSVITSSGYSPR EECCEEEECCCCCCC	18.06	29449344
127	Phosphorylation	FTGSVITSSGYSPRS ECCEEEECCCCCCCC	15.61	29449344
128	Phosphorylation	TGSVITSSGYSPRSA CCEEEECCCCCCCCH	32.85	21712546
130	Phosphorylation	SVITSSGYSPRSAHQ EEEECCCCCCCCHHC	19.90	30576142
131	Phosphorylation	VITSSGYSPRSAHQY EEECCCCCCCCHHCC	19.84	25159151
134	Phosphorylation	SSGYSPRSAHQYSPQ CCCCCCCCHHCCCCC	33.22	25159151
138	Phosphorylation	SPRSAHQYSPQLYPS CCCCHHCCCCCCCCC	16.67	29449344
139	Phosphorylation	PRSAHQYSPQLYPSK CCCHHCCCCCCCCCC	10.29	30576142
203	Sumoylation	GVMLPAIKTESGLSQ HCEECEEECCCCCCC	48.63	-
361	Phosphorylation	RGRKNNPSPPPDSDL CCCCCCCCCCCCCCC	52.76	29255136
366	Phosphorylation	NPSPPPDSDLERVFV CCCCCCCCCCCEEEE	50.28	23663014
507	Acetylation	GGLLGPAKRDAWLQL CCCCCCHHHHHHHHH	54.68	7851135
522	Phosphorylation	RAEIEGLTDSWLTNA HHHHCCCCHHHHHHH	38.55	-
540	Phosphorylation	LSIISTRSNCINVLV HHHHCCCCCCCCHHH	35.82	-
581	Ubiquitination	YSATKIGKESCFERI HHHCCCCHHHHHHHH	50.34	-

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
Oops, there are no upstream regulatory protein records of EYA4_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of EYA4_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of EYA4_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
DCTP1_HUMAN	DCTPP1	physical	27880917
RB6I2_HUMAN	ERC1	physical	27880917
RFA2_HUMAN	RPA2	physical	27880917
RFA3_HUMAN	RPA3	physical	27880917
SIX2_HUMAN	SIX2	physical	27880917
SIX4_HUMAN	SIX4	physical	27880917
SPT5H_HUMAN	SUPT5H	physical	27880917
EYA4_HUMAN	EYA4	physical	27432908
DCTP1_HUMAN	DCTPP1	physical	27432908
SCO1_HUMAN	SCO1	physical	27432908
EOGT_HUMAN	EOGT	physical	27432908
ORNT1_HUMAN	SLC25A15	physical	27432908
SCO2_HUMAN	SCO2	physical	27432908
BAG3_HUMAN	BAG3	physical	27432908
LGUL_HUMAN	GLO1	physical	27432908
PKP2_HUMAN	PKP2	physical	27432908
MISSL_HUMAN	MAPK1IP1L	physical	27432908
COQ5_HUMAN	COQ5	physical	27432908
DDI2_HUMAN	DDI2	physical	27432908
SOAT1_HUMAN	SOAT1	physical	27432908
PLEC_HUMAN	PLEC	physical	27173435
AAK1_HUMAN	AAK1	physical	27173435
SC24B_HUMAN	SEC24B	physical	27173435
GRDN_HUMAN	CCDC88A	physical	27173435
UB2D2_HUMAN	UBE2D2	physical	27173435
DVL3_HUMAN	DVL3	physical	27173435
VIP2_HUMAN	PPIP5K2	physical	27173435
LUZP1_HUMAN	LUZP1	physical	27173435
QSER1_HUMAN	QSER1	physical	27173435
URGCP_HUMAN	URGCP	physical	27173435

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
601316	Deafness, autosomal dominant, 10 (DFNA10)
605362	Cardiomyopathy, dilated 1J (CMD1J)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of EYA4_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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 MET-1, AND MASS SPECTROMETRY.	19413330 [Abstract]
Phosphorylation
Reference	PubMed
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-361, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-361, AND MASSSPECTROMETRY.	18691976 [Abstract]
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization."; Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; Nat. Biotechnol. 24:1285-1292(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-361, AND MASSSPECTROMETRY.	16964243 [Abstract]
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-15, AND MASSSPECTROMETRY.	19690332 [Abstract]