EPHB3_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: EPHB3_MOUSE
• UniProt AC: P54754
• Protein Name: Ephrin type-B receptor 3
• Gene Name: Ephb3
• Organism: Mus musculus (Mouse).
• Sequence Length: 993
• Subcellular Localization: Cell membrane ; Single-pass type I membrane protein . Cell projection, dendrite .
• Protein Description: Receptor tyrosine kinase which binds promiscuously transmembrane ephrin-B 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. Generally has an overlapping and redundant function with EPHB2. Like EPHB2, functions in axon guidance during development regulating for instance the neurons forming the corpus callosum and the anterior commissure, 2 major interhemispheric connections between the temporal lobes of the cerebral cortex. In addition to its role in axon guidance plays also an important redundant role with other ephrin-B receptors in development and maturation of dendritic spines and the formation of excitatory synapses. Controls other aspects of development through regulation of cell migration and positioning. This includes angiogenesis, palate development and thymic epithelium development for instance. Forward and reverse signaling through the EFNB2/EPHB3 complex also regulate migration and adhesion of cells that tubularize the urethra and septate the cloaca. Finally, plays an important role in intestinal epithelium differentiation segregating progenitor from differentiated cells in the crypt..
• Protein Sequence: MAGARPPPGLLPLLAPLLLPLLLPAGCWALEETLMDTKWVTSELAWTSHPESGWEEVSGYDEAMNPIRTYQVCNVRESSQNNWLRTGFIWRREVQRVYVELKFTVRDCNSIPNIPGSCKETFNLFYYEADSDVASASSPFWMENPYVKVDTIAPDESFSRLDAGRVNTKVRSFGPLSKAGFYLAFQDQGACMSLISVRAFYKKCASTTAGFALFPETLTGAEPTSLVIAPGTCIANAVEVSVPLKLYCNGDGEWMVPVGACTCATGHEPAAKESQCRACPPGSYKAKQGEGPCLPCPPNSRTTSPAASICTCHNNFYRADSDSADSACTTVPSPPRGVISNVNETSLILEWSEPRDLGGRDDLLYNVICKKCRGSSGAGGPATCSRCDDNVEFVPRQLGLTERRVHISHLLAHTRYTFEVQAVNGVSGKSPLPPRYAAVNITTNQAAPSEVPTLHLHSSSGSSLTLSWAPPERPNGVILDYEMKYFEKSKGIASTVTSQKNSVQLDGLQPDARYVVQVRARTVAGYGQYSHPAEFETTSERGSGAQQLQEQLPLIVGSTVAGFVFMVVVVVIALVCLRKQRHGPDAEYTEKLQQYIAPGMKVYIDPFTYEDPNEAVREFAKEIDVSCVKIEEVIGAGEFGEVCRGRLKLPGRREVFVAIKTLKVGYTERQRRDFLSEASIMGQFDHPNIIRLEGVVTKSRPVMILTEFMENCALDSFLRLNDGQFTVIQLVGMLRGIAAGMKYLSEMNYVHRDLAARNILVNSNLVCKVSDFGLSRFLEDDPSDPTYTSSLGGKIPIRWTAPEAIAYRKFTSASDVWSYGIVMWEVMSYGERPYWDMSNQDVINAVEQDYRLPPPMDCPTALHQLMLDCWVRDRNLRPKFSQIVNTLDKLIRNAASLKVTASAPSGMSQPLLDRTVPDYTTFTTVGDWLDAIKMGRYKESFVGAGFASFDLVAQMTAEDLLRIGVTLAGHQKKILCSIQDMRLQMNQTLPVQV

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
343	N-linked_Glycosylation	RGVISNVNETSLILE CCCCCCCCCCEEEEE	51.59	-
376	Phosphorylation	CKKCRGSSGAGGPAT CHHCCCCCCCCCCCC	35.17	22871156
385	Phosphorylation	AGGPATCSRCDDNVE CCCCCCCCCCCCCCE	31.43	22871156
440	N-linked_Glycosylation	PPRYAAVNITTNQAA CCCEEEEEEECCCCC	22.59	-
494	Phosphorylation	EKSKGIASTVTSQKN HHCCCCCCCCCCCCC	22.84	-
588	Phosphorylation	RHGPDAEYTEKLQQY HCCCCHHHHHHHHHH	23.17	26824392
589	Phosphorylation	HGPDAEYTEKLQQYI CCCCHHHHHHHHHHH	20.39	-
595	Phosphorylation	YTEKLQQYIAPGMKV HHHHHHHHHCCCCEE	6.01	20116462
603	Phosphorylation	IAPGMKVYIDPFTYE HCCCCEEEECCCCCC	8.29	26824392
608	Phosphorylation	KVYIDPFTYEDPNEA EEEECCCCCCCHHHH	31.24	22499769
609	Phosphorylation	VYIDPFTYEDPNEAV EEECCCCCCCHHHHH	20.79	26824392
742	Acetylation	RGIAAGMKYLSEMNY HHHHHHHHHHHHCCC	41.96	19856645
775	Phosphorylation	KVSDFGLSRFLEDDP EECHHCHHHHCCCCC	22.74	22817900
783	Phosphorylation	RFLEDDPSDPTYTSS HHCCCCCCCCCEECC	64.32	22499769
786	Phosphorylation	EDDPSDPTYTSSLGG CCCCCCCCEECCCCC	44.41	22499769
787	Phosphorylation	DDPSDPTYTSSLGGK CCCCCCCEECCCCCC	15.26	20116462
788	Phosphorylation	DPSDPTYTSSLGGKI CCCCCCEECCCCCCC	17.83	22499769
789	Phosphorylation	PSDPTYTSSLGGKIP CCCCCEECCCCCCCC	17.10	22499769
790	Phosphorylation	SDPTYTSSLGGKIPI CCCCEECCCCCCCCE	24.19	22499769
889	Ubiquitination	QIVNTLDKLIRNAAS HHHHHHHHHHHHHHC	49.26	22790023
896	Phosphorylation	KLIRNAASLKVTASA HHHHHHHCCCEEECC	26.72	29514104
902	Phosphorylation	ASLKVTASAPSGMSQ HCCCEEECCCCCCCC	31.20	29514104
919	Phosphorylation	LDRTVPDYTTFTTVG CCCCCCCCCEEEEHH	11.12	22817900
966	Phosphorylation	DLLRIGVTLAGHQKK HHHHHCCEECCCCCE	12.99	25338131
988	Phosphorylation	MRLQMNQTLPVQV-- HCCHHCCCCCCCC--	28.20	29514104

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

Oops, there are no upstream regulatory protein records of EPHB3_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of EPHB3_MOUSE !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of EPHB3_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
EFNB1_MOUSE	Efnb1	physical	8954633
ELF2_MOUSE	Elf2	physical	8954633
HUWE1_MOUSE	Huwe1	physical	27184401

Drug and Disease Associations

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