EPHA3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: EPHA3_HUMAN
• UniProt AC: P29320
• Protein Name: Ephrin type-A receptor 3
• Gene Name: EPHA3
• Organism: Homo sapiens (Human).
• Sequence Length: 983
• Subcellular Localization: Isoform 1: Cell membrane ; Single-pass type I membrane protein .; Isoform 2: Secreted .
• Protein Description: Receptor tyrosine kinase which binds promiscuously membrane-bound ephrin family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Highly promiscuous for ephrin-A ligands it binds preferentially EFNA5. Upon activation by EFNA5 regulates cell-cell adhesion, cytoskeletal organization and cell migration. Plays a role in cardiac cells migration and differentiation and regulates the formation of the atrioventricular canal and septum during development probably through activation by EFNA1. Involved in the retinotectal mapping of neurons. May also control the segregation but not the guidance of motor and sensory axons during neuromuscular circuit development..
• Protein Sequence: MDCQLSILLLLSCSVLDSFGELIPQPSNEVNLLDSKTIQGELGWISYPSHGWEEISGVDEHYTPIRTYQVCNVMDHSQNNWLRTNWVPRNSAQKIYVELKFTLRDCNSIPLVLGTCKETFNLYYMESDDDHGVKFREHQFTKIDTIAADESFTQMDLGDRILKLNTEIREVGPVNKKGFYLAFQDVGACVALVSVRVYFKKCPFTVKNLAMFPDTVPMDSQSLVEVRGSCVNNSKEEDPPRMYCSTEGEWLVPIGKCSCNAGYEERGFMCQACRPGFYKALDGNMKCAKCPPHSSTQEDGSMNCRCENNYFRADKDPPSMACTRPPSSPRNVISNINETSVILDWSWPLDTGGRKDVTFNIICKKCGWNIKQCEPCSPNVRFLPRQFGLTNTTVTVTDLLAHTNYTFEIDAVNGVSELSSPPRQFAAVSITTNQAAPSPVLTIKKDRTSRNSISLSWQEPEHPNGIILDYEVKYYEKQEQETSYTILRARGTNVTISSLKPDTIYVFQIRARTAAGYGTNSRKFEFETSPDSFSISGESSQVVMIAISAAVAIILLTVVIYVLIGRFCGYKSKHGADEKRLHFGNGHLKLPGLRTYVDPHTYEDPTQAVHEFAKELDATNISIDKVVGAGEFGEVCSGRLKLPSKKEISVAIKTLKVGYTEKQRRDFLGEASIMGQFDHPNIIRLEGVVTKSKPVMIVTEYMENGSLDSFLRKHDAQFTVIQLVGMLRGIASGMKYLSDMGYVHRDLAARNILINSNLVCKVSDFGLSRVLEDDPEAAYTTRGGKIPIRWTSPEAIAYRKFTSASDVWSYGIVLWEVMSYGERPYWEMSNQDVIKAVDEGYRLPPPMDCPAALYQLMLDCWQKDRNNRPKFEQIVSILDKLIRNPGSLKIITSAAARPSNLLLDQSNVDITTFRTTGDWLNGVWTAHCKEIFTGVEYSSCDTIAKISTDDMKKVGVTVVGPQKKIISSIKALETQSKNGPVPV

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
102	Phosphorylation	IYVELKFTLRDCNSI EEEEEEEEECCCCCC	21.21	24719451
123	Phosphorylation	CKETFNLYYMESDDD CCCEEEEEEEECCCC	11.23	22817900
124	Phosphorylation	KETFNLYYMESDDDH CCEEEEEEEECCCCC	9.51	22817900
155	Sulfoxidation	ADESFTQMDLGDRIL CCCCCCCCCHHHHHH	4.11	21406390
194	Phosphorylation	GACVALVSVRVYFKK HHEEEEEEEEEEECC	12.69	24719451
232	N-linked_Glycosylation	EVRGSCVNNSKEEDP EEECCCCCCCCCCCC	51.92	UniProtKB CARBOHYD
243	Phosphorylation	EEDPPRMYCSTEGEW CCCCCCEEEECCCCE	5.64	23917254
245	Phosphorylation	DPPRMYCSTEGEWLV CCCCEEEECCCCEEE	16.41	23917254
246	Phosphorylation	PPRMYCSTEGEWLVP CCCEEEECCCCEEEE	44.44	23917254
294	Phosphorylation	CAKCPPHSSTQEDGS ECCCCCCCCCCCCCC	40.63	-
337	N-linked_Glycosylation	RNVISNINETSVILD CCHHCCCCCCEEEEE	51.23	UniProtKB CARBOHYD
358	Phosphorylation	TGGRKDVTFNIICKK CCCCCCEEEEEEECC	22.54	24702127
391	N-linked_Glycosylation	PRQFGLTNTTVTVTD CCHHCCCCCEEEHHH	38.50	UniProtKB CARBOHYD
404	N-linked_Glycosylation	TDLLAHTNYTFEIDA HHHHCCCCEEEEEEE	24.79	UniProtKB CARBOHYD
432	Phosphorylation	FAAVSITTNQAAPSP EEEEEEECCCCCCCC	24.54	-
442	Phosphorylation	AAPSPVLTIKKDRTS CCCCCEEEEEECCCC	30.86	-
485	Phosphorylation	QEQETSYTILRARGT CCCCCEEEEEEECCC	17.19	-
493	N-linked_Glycosylation	ILRARGTNVTISSLK EEEECCCEEEEEECC	31.58	19349973
493	N-linked_Glycosylation	ILRARGTNVTISSLK EEEECCCEEEEEECC	31.58	UniProtKB CARBOHYD
497	Phosphorylation	RGTNVTISSLKPDTI CCCEEEEEECCCCEE	21.91	23403867
498	Phosphorylation	GTNVTISSLKPDTIY CCEEEEEECCCCEEE	36.24	23403867
528	Phosphorylation	SRKFEFETSPDSFSI CCEEEEECCCCCEEC	51.37	24400094
532	Phosphorylation	EFETSPDSFSISGES EEECCCCCEECCCCC	25.03	24400094
548	Phosphorylation	QVVMIAISAAVAIIL HHHHHHHHHHHHHHH	10.93	24400094
561	Phosphorylation	ILLTVVIYVLIGRFC HHHHHHHHHHHHHHC	4.24	-
570	Phosphorylation	LIGRFCGYKSKHGAD HHHHHCCCCCCCCCC	17.17	-
595	Phosphorylation	LKLPGLRTYVDPHTY CCCCCCCCCCCCCCC	32.70	26356563
596	Phosphorylation	KLPGLRTYVDPHTYE CCCCCCCCCCCCCCC	9.09	25159151
601	Phosphorylation	RTYVDPHTYEDPTQA CCCCCCCCCCCHHHH	33.71	26356563
602	Phosphorylation	TYVDPHTYEDPTQAV CCCCCCCCCCHHHHH	18.46	20007894
606	Phosphorylation	PHTYEDPTQAVHEFA CCCCCCHHHHHHHHH	41.29	26356563
625	Ubiquitination	ATNISIDKVVGAGEF CCCCEEEEEECCCCC	36.83	-
644	Phosphorylation	SGRLKLPSKKEISVA CCCCCCCCHHHEEEE	67.79	24719451
654	Phosphorylation	EISVAIKTLKVGYTE HEEEEEEEECCCCCH	26.21	22461510
656	Ubiquitination	SVAIKTLKVGYTEKQ EEEEEEECCCCCHHH	38.55	-
659	Phosphorylation	IKTLKVGYTEKQRRD EEEECCCCCHHHCCC	18.08	22461510
701	Phosphorylation	PVMIVTEYMENGSLD CEEEEEEECCCCCHH	10.60	19060867
719	Phosphorylation	RKHDAQFTVIQLVGM HHHCHHHHHHHHHHH	12.48	29438985
736	Phosphorylation	GIASGMKYLSDMGYV HHHHHCHHHHHCCCC	11.53	22817900
742	Phosphorylation	KYLSDMGYVHRDLAA HHHHHCCCCCHHHHH	6.09	29438985
763	Phosphorylation	SNLVCKVSDFGLSRV CCEEEEECHHCCHHH	16.83	-
768	Phosphorylation	KVSDFGLSRVLEDDP EECHHCCHHHCCCCC	22.26	19369195
779	Phosphorylation	EDDPEAAYTTRGGKI CCCCCHHCCCCCCCC	18.72	27273156
780	Phosphorylation	DDPEAAYTTRGGKIP CCCCHHCCCCCCCCC	12.80	25159151
781	Phosphorylation	DPEAAYTTRGGKIPI CCCHHCCCCCCCCCC	18.03	25159151
798	Phosphorylation	TSPEAIAYRKFTSAS CCHHHHHCCCCCCHH	14.28	22817900
825	Phosphorylation	MSYGERPYWEMSNQD HHCCCCCCEECCCHH	21.88	26074081
829	Phosphorylation	ERPYWEMSNQDVIKA CCCCEECCCHHHHHH	21.59	26074081
906	Phosphorylation	SNLLLDQSNVDITTF CCEEECCCCCEEEEE	38.19	28122231
933	Phosphorylation	AHCKEIFTGVEYSSC HHHHHHHCCCCCCCC	46.08	29978859
937	Phosphorylation	EIFTGVEYSSCDTIA HHHCCCCCCCCCEEE	11.95	29978859
938	Phosphorylation	IFTGVEYSSCDTIAK HHCCCCCCCCCEEEE	15.81	29978859
939	Phosphorylation	FTGVEYSSCDTIAKI HCCCCCCCCCEEEEE	18.34	29978859
942	Phosphorylation	VEYSSCDTIAKISTD CCCCCCCEEEEECHH	27.45	29978859
968	Phosphorylation	PQKKIISSIKALETQ CCHHHHHHHHHHHHH	20.07	28857561
974	Phosphorylation	SSIKALETQSKNGPV HHHHHHHHHCCCCCC	38.71	-
976	Phosphorylation	IKALETQSKNGPVPV HHHHHHHCCCCCCCC	35.19	-

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
596	Y	Phosphorylation	Kinase	EPHA3	P29320	GPS
602	Y	Phosphorylation	Kinase	EPHA3	P29320	PhosphoELM
701	Y	Phosphorylation	Kinase	EPHA3	P29320	GPS
779	Y	Phosphorylation	Kinase	EPHA3	P29320	PhosphoELM

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of EPHA3_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of EPHA3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
P53_HUMAN	TP53	physical	15355990
EFNB2_HUMAN	EFNB2	physical	8559144
EFNA1_HUMAN	EFNA1	physical	9195962
EFNB1_HUMAN	EFNB1	physical	9195962
EFNA3_HUMAN	EFNA3	physical	9195962
EFNA4_HUMAN	EFNA4	physical	9195962
EFNB2_HUMAN	EFNB2	physical	9195962
EFNA5_HUMAN	EFNA5	physical	9195962
RBM18_HUMAN	RBM18	physical	21988832
ILKAP_HUMAN	ILKAP	physical	28065597
CTDS2_HUMAN	CTDSP2	physical	28065597
DUS18_HUMAN	DUSP18	physical	28065597
DUS21_HUMAN	DUSP21	physical	28065597
STYX_HUMAN	STYX	physical	28065597
TPTE_HUMAN	TPTE	physical	28065597
MTMRB_HUMAN	MTMR11	physical	28065597

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• 114500: Colorectal cancer (CRC)
• 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

Phosphorylation

"Autoregulation by the juxtamembrane region of the human ephrinreceptor tyrosine kinase A3 (EphA3).";
Davis T.L., Walker J.R., Loppnau P., Butler-Cole C.,Allali-Hassani A., Dhe-Paganon S.;
Structure 16:873-884(2008).
Cited for: X-RAY CRYSTALLOGRAPHY (1.07 ANGSTROMS) OF 577-947 IN COMPLEX WITH ATPANALOG, IDENTIFICATION BY MASS SPECTROMETRY, AUTOPHOSPHORYLATION ATTYR-596; TYR-602 AND TYR-701, AND MUTAGENESIS OF TYR-596; TYR-602;TYR-742 AND SER-768.
PubMed: 18547520

"Proteomics analysis of protein kinases by target class-selectiveprefractionation and tandem mass spectrometry.";
Wissing J., Jaensch L., Nimtz M., Dieterich G., Hornberger R.,Keri G., Wehland J., Daub H.;
Mol. Cell. Proteomics 6:537-547(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-779, AND MASSSPECTROMETRY.
PubMed: 17192257

"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-779, AND MASSSPECTROMETRY.
PubMed: 18083107