EFNA1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: EFNA1_HUMAN
• UniProt AC: P20827
• Protein Name: Ephrin-A1
• Gene Name: EFNA1
• Organism: Homo sapiens (Human).
• Sequence Length: 205
• Subcellular Localization: Cell membrane ; Lipid-anchor, GPI-anchor .; Ephrin-A1, secreted form: Secreted .
• Protein Description: Cell surface GPI-bound ligand for Eph receptors, a family of receptor tyrosine kinases which are crucial for migration, repulsion and adhesion during neuronal, vascular and epithelial development. Binds promiscuously Eph receptors residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. Plays an important role in angiogenesis and tumor neovascularization. The recruitment of VAV2, VAV3 and PI3-kinase p85 subunit by phosphorylated EPHA2 is critical for EFNA1-induced RAC1 GTPase activation and vascular endothelial cell migration and assembly. Exerts anti-oncogenic effects in tumor cells through activation and down-regulation of EPHA2. Activates EPHA2 by inducing tyrosine phosphorylation which leads to its internalization and degradation. Acts as a negative regulator in the tumorigenesis of gliomas by down-regulating EPHA2 and FAK. Can evoke collapse of embryonic neuronal growth cone and regulates dendritic spine morphogenesis..
• Protein Sequence: MEFLWAPLLGLCCSLAAADRHTVFWNSSNPKFRNEDYTIHVQLNDYVDIICPHYEDHSVADAAMEQYILYLVEHEEYQLCQPQSKDQVRWQCNRPSAKHGPEKLSEKFQRFTPFTLGKEFKEGHSYYYISKPIHQHEDRCLRLKVTVSGKITHSPQAHDNPQEKRLAADDPEVRVLHSIGHSAAPRLFPLAWTVLLLPLLLLQTP

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
26	N-linked_Glycosylation	DRHTVFWNSSNPKFR HCCEEECCCCCCCCC	24.89	23661698
96	Phosphorylation	RWQCNRPSAKHGPEK CHHCCCCHHHHCHHH	46.87	22964224
98	Ubiquitination	QCNRPSAKHGPEKLS HCCCCHHHHCHHHHH	54.13	29967540
103	Ubiquitination	SAKHGPEKLSEKFQR HHHHCHHHHHHHHHH	61.52	29967540
107	Ubiquitination	GPEKLSEKFQRFTPF CHHHHHHHHHHCCCC	43.34	29967540
115	O-linked_Glycosylation	FQRFTPFTLGKEFKE HHHCCCCCCCCHHCC	35.49	OGP
118	Acetylation	FTPFTLGKEFKEGHS CCCCCCCCHHCCCCC	64.19	30588357
118	Ubiquitination	FTPFTLGKEFKEGHS CCCCCCCCHHCCCCC	64.19	29967540
126	Phosphorylation	EFKEGHSYYYISKPI HHCCCCCEEEECCCC	8.46	-
128	Phosphorylation	KEGHSYYYISKPIHQ CCCCCEEEECCCCCC	7.18	-
131	Ubiquitination	HSYYYISKPIHQHED CCEEEECCCCCCCCC	38.13	29967540
146	Phosphorylation	RCLRLKVTVSGKITH CEEEEEEEEECEECC	13.84	-
146	O-linked_Glycosylation	RCLRLKVTVSGKITH CEEEEEEEEECEECC	13.84	29237092
150	Ubiquitination	LKVTVSGKITHSPQA EEEEEECEECCCCCC	36.60	29967540
152	Phosphorylation	VTVSGKITHSPQAHD EEEECEECCCCCCCC	21.56	29396449
152	O-linked_Glycosylation	VTVSGKITHSPQAHD EEEECEECCCCCCCC	21.56	55834111
154	Phosphorylation	VSGKITHSPQAHDNP EECEECCCCCCCCCH	15.28	25159151
154	O-linked_Glycosylation	VSGKITHSPQAHDNP EECEECCCCCCCCCH	15.28	OGP
182	GPI-anchor	VLHSIGHSAAPRLFP HHHHCCCCCCCCHHH	22.40	-

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

Oops, there are no upstream regulatory protein records of EFNA1_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of EFNA1_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 EFNA1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CXCL7_HUMAN	PPBP	physical	16169070
EF1G_HUMAN	EEF1G	physical	16169070
KAT5_HUMAN	KAT5	physical	16169070
EPHA4_HUMAN	EPHA4	physical	10366629
XRCC6_HUMAN	XRCC6	physical	21900206
CXCL7_HUMAN	PPBP	physical	21900206
GARE1_HUMAN	GAREM	physical	28514442

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• There are no disease associations of PTM sites.
• Kegg Drug
• There are no disease associations of PTM sites.
• DrugBank
• There are no disease associations of PTM sites.