dbPTM

EFNB1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	EFNB1_MOUSE
UniProt AC	P52795
Protein Name	Ephrin-B1
Gene Name	Efnb1
Organism	Mus musculus (Mouse).
Sequence Length	345
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. Binds to the receptor tyrosine kinases EPHB3 (preferred), EPHB1 and EPHA1. 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..
Protein Sequence	MARPGQRWLSKWLVAMVVLTLCRLATPLAKNLEPVSWSSLNPKFLSGKGLVIYPKIGDKLDIICPRAEAGRPYEYYKLYLVRPEQAAACSTVLDPNVLVTCNKPHQEIRFTIKFQEFSPNYMGLEFKKYHDYYITSTSNGSLEGLENREGGVCRTRTMKIVMKVGQDPNAVTPEQLTTSRPSKESDNTVKTATQAPGRGSQGDSDGKHETVNQEEKSGPGAGGGGSGDSDSFFNSKVALFAAVGAGCVIFLLIIIFLTVLLLKLRKRHRKHTQQRAAALSLSTLASPKGGSGTAGTEPSDIIIPLRTTENNYCPHYEKVSGDYGHPVYIVQEMPPQSPANIYYKV

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
46	Phosphorylation	SLNPKFLSGKGLVIY HCCHHHHCCCCEEEE	41.41	22871156
53	Phosphorylation	SGKGLVIYPKIGDKL CCCCEEEECCCCCCE	7.32	22871156
139	N-linked_Glycosylation	YYITSTSNGSLEGLE EEEEECCCCCCCCCC	44.13	-
280	Phosphorylation	QQRAAALSLSTLASP HHHHHHHHHHHHCCC	18.62	26824392
282	Phosphorylation	RAAALSLSTLASPKG HHHHHHHHHHCCCCC	20.28	22324799
283	Phosphorylation	AAALSLSTLASPKGG HHHHHHHHHCCCCCC	31.47	24068923
286	Phosphorylation	LSLSTLASPKGGSGT HHHHHHCCCCCCCCC	30.20	25521595
288	Ubiquitination	LSTLASPKGGSGTAG HHHHCCCCCCCCCCC	73.70	22790023
291	Phosphorylation	LASPKGGSGTAGTEP HCCCCCCCCCCCCCC	41.46	27180971
293	Phosphorylation	SPKGGSGTAGTEPSD CCCCCCCCCCCCCCC	24.50	24759943
296	Phosphorylation	GGSGTAGTEPSDIII CCCCCCCCCCCCEEE	42.11	26643407
312	Phosphorylation	LRTTENNYCPHYEKV CEECCCCCCCCCEEC	20.95	22817900
316	Phosphorylation	ENNYCPHYEKVSGDY CCCCCCCCEECCCCC	11.55	22499769
318	Ubiquitination	NYCPHYEKVSGDYGH CCCCCCEECCCCCCC	34.24	-
320	Phosphorylation	CPHYEKVSGDYGHPV CCCCEECCCCCCCCE	36.69	22499769
323	Phosphorylation	YEKVSGDYGHPVYIV CEECCCCCCCCEEEE	22.36	22499769
328	Phosphorylation	GDYGHPVYIVQEMPP CCCCCCEEEEEECCC	10.38	22499769
337	Phosphorylation	VQEMPPQSPANIYYK EEECCCCCCCCCEEE	31.58	22499769
342	Phosphorylation	PQSPANIYYKV---- CCCCCCCEEEC----	9.31	20116462
343	Phosphorylation	QSPANIYYKV----- CCCCCCEEEC-----	11.07	22499769

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
323	Y	Phosphorylation	Kinase	SRC	P05480	PSP
328	Y	Phosphorylation	Kinase	SRC	P05480	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of EFNB1_MOUSE !!

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 EFNB1_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
NCK2_MOUSE	Nck2	physical	11557983
EPHB3_MOUSE	Ephb3	physical	8954633
EPHB1_MOUSE	Ephb1	physical	8954633

Drug and Disease Associations

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

Regulatory Network of EFNB1_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations."; Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.; Mol. Cell. Proteomics 6:283-293(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-286, AND MASSSPECTROMETRY.	17114649 [Abstract]