EFNB3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: EFNB3_HUMAN
• UniProt AC: Q15768
• Protein Name: Ephrin-B3
• Gene Name: EFNB3
• Organism: Homo sapiens (Human).
• Sequence Length: 340
• Subcellular Localization: Membrane; Single-pass type I membrane protein.
• Protein Description: Cell surface transmembrane 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. May play a pivotal role in forebrain function. Binds to, and induce the collapse of, commissural axons/growth cones in vitro. May play a role in constraining the orientation of longitudinally projecting axons (By similarity).; (Microbial infection) Acts as a receptor for nipah virus and hendra virus..
• Protein Sequence: MGPPHSGPGGVRVGALLLLGVLGLVSGLSLEPVYWNSANKRFQAEGGYVLYPQIGDRLDLLCPRARPPGPHSSPNYEFYKLYLVGGAQGRRCEAPPAPNLLLTCDRPDLDLRFTIKFQEYSPNLWGHEFRSHHDYYIIATSDGTREGLESLQGGVCLTRGMKVLLRVGQSPRGGAVPRKPVSEMPMERDRGAAHSLEPGKENLPGDPTSNATSRGAEGPLPPPSMPAVAGAAGGLALLLLGVAGAGGAMCWRRRRAKPSESRHPGPGSFGRGGSLGLGGGGGMGPREAEPGELGIALRGGGAADPPFCPHYEKVSGDYGHPVYIVQDGPPQSPPNIYYKV

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
210	N-linked_Glycosylation	LPGDPTSNATSRGAE CCCCCCCCCCCCCCC	50.11	UniProtKB CARBOHYD
259	Phosphorylation	RRRRAKPSESRHPGP HHHCCCCCCCCCCCC	47.71	23312004
261	Phosphorylation	RRAKPSESRHPGPGS HCCCCCCCCCCCCCC	39.98	23312004
268	Phosphorylation	SRHPGPGSFGRGGSL CCCCCCCCCCCCCCC	27.88	20363803
271	Methylation	PGPGSFGRGGSLGLG CCCCCCCCCCCCCCC	44.27	-
274	Phosphorylation	GSFGRGGSLGLGGGG CCCCCCCCCCCCCCC	23.30	30266825
311	Phosphorylation	DPPFCPHYEKVSGDY CCCCCCCCEECCCCC	11.55	25884760
315	Phosphorylation	CPHYEKVSGDYGHPV CCCCEECCCCCCCCE	36.69	26356563
318	Phosphorylation	YEKVSGDYGHPVYIV CEECCCCCCCCEEEE	22.36	25884760
323	Phosphorylation	GDYGHPVYIVQDGPP CCCCCCEEEEECCCC	10.38	25884760
332	Phosphorylation	VQDGPPQSPPNIYYK EECCCCCCCCCCEEE	48.36	27732954
337	Phosphorylation	PQSPPNIYYKV---- CCCCCCCEEEC----	12.13	25884760
338	Phosphorylation	QSPPNIYYKV----- CCCCCCEEEC-----	11.07	26356563
339	Ubiquitination	SPPNIYYKV------ CCCCCEEEC------	25.21	-

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

Oops, there are no upstream regulatory protein records of EFNB3_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of EFNB3_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 EFNB3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
P2RX7_HUMAN	P2RX7	physical	21988832
ELOC_HUMAN	TCEB1	physical	21988832
1433Z_HUMAN	YWHAZ	physical	21988832
MPP7_HUMAN	MPP7	physical	28514442
DLG1_HUMAN	DLG1	physical	28514442
PKN3_HUMAN	PKN3	physical	28514442
TCAF2_HUMAN	FAM115C	physical	28514442
RTEL1_HUMAN	RTEL1	physical	28514442
PLCD3_HUMAN	PLCD3	physical	28514442
CDYL_HUMAN	CDYL	physical	28514442
LCHN_HUMAN	KIAA1147	physical	28514442
TBB8_HUMAN	TUBB8	physical	28514442
TBB3_HUMAN	TUBB3	physical	28514442
TRI11_HUMAN	TRIM11	physical	28514442
DEN6A_HUMAN	DENND6A	physical	28514442
RA51C_HUMAN	RAD51C	physical	28514442
EPHA4_HUMAN	EPHA4	physical	28514442
LEG1_HUMAN	LGALS1	physical	28514442
EVI5L_HUMAN	EVI5L	physical	28514442
THUM3_HUMAN	THUMPD3	physical	28514442
TBA4A_HUMAN	TUBA4A	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.