EFNA5_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: EFNA5_HUMAN
• UniProt AC: P52803
• Protein Name: Ephrin-A5
• Gene Name: EFNA5
• Organism: Homo sapiens (Human).
• Sequence Length: 228
• Subcellular Localization: Cell membrane ; Lipid-anchor, GPI-anchor . Membrane, caveola ; Lipid-anchor, GPI-anchor . Compartmentalized in discrete caveolae-like membrane microdomains.
• 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. 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. Induces compartmentalized signaling within a caveolae-like membrane microdomain when bound to the extracellular domain of its cognate receptor. This signaling event requires the activity of the Fyn tyrosine kinase. Activates the EPHA3 receptor to regulate cell-cell adhesion and cytoskeletal organization. With the receptor EPHA2 may regulate lens fiber cells shape and interactions and be important for lens transparency maintenance. May function actively to stimulate axon fasciculation. The interaction of EFNA5 with EPHA5 also mediates communication between pancreatic islet cells to regulate glucose-stimulated insulin secretion. Cognate/functional ligand for EPHA7, their interaction regulates brain development modulating cell-cell adhesion and repulsion..
• Protein Sequence: MLHVEMLTLVFLVLWMCVFSQDPGSKAVADRYAVYWNSSNPRFQRGDYHIDVCINDYLDVFCPHYEDSVPEDKTERYVLYMVNFDGYSACDHTSKGFKRWECNRPHSPNGPLKFSEKFQLFTPFSLGFEFRPGREYFYISSAIPDNGRRSCLKLKVFVRPTNSCMKTIGVHDRVFDVNDKVENSLEPADDTVHESAEPSRGENAAQTPRIPSRLLAILLFLLAMLLTL

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
8	Phosphorylation	MLHVEMLTLVFLVLW CCHHHHHHHHHHHHH	21.40	-
37	N-linked_Glycosylation	DRYAVYWNSSNPRFQ HEEEEEECCCCCCCC	20.20	17400922
115	Phosphorylation	PNGPLKFSEKFQLFT CCCCCCCCCEEEEEC	37.99	24719451
167	Phosphorylation	PTNSCMKTIGVHDRV CCCCHHHHHCCCCEE	8.97	22210691
184	Phosphorylation	VNDKVENSLEPADDT CCHHHHHCCCCCCCC	22.17	26471730
203	GPI-anchor	AEPSRGENAAQTPRI CCCCCCCCHHCCCCC	43.32	-

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

Oops, there are no upstream regulatory protein records of EFNA5_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of EFNA5_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 EFNA5_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
EPHA7_HUMAN	EPHA7	physical	10366629
EPHA3_HUMAN	EPHA3	physical	9245480
EPHB1_HUMAN	EPHB1	physical	9245480
SRC_HUMAN	SRC	physical	17631495
GRIP1_HUMAN	GRIP1	physical	17631495

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.

Related Literatures of Post-Translational Modification

N-linked Glycosylation

"Crystal structure of the human ephrin-A5 ectodomain.";
Nikolov D.B., Li C., Lackmann M., Jeffrey P., Himanen J.P.;
Protein Sci. 16:996-1000(2007).
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 27-189, AND GLYCOSYLATION ATASN-37.
PubMed: 17400922