EPHB1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: EPHB1_MOUSE
• UniProt AC: Q8CBF3
• Protein Name: Ephrin type-B receptor 1
• Gene Name: Ephb1
• Organism: Mus musculus (Mouse).
• Sequence Length: 984
• Subcellular Localization: Cell membrane ; Single-pass type I membrane protein . Early endosome membrane . 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. Cognate/functional ephrin ligands for this receptor include EFNB1, EFNB2 and EFNB3. During nervous system development, regulates retinal axon guidance redirecting ipsilaterally ventrotemporal retinal ganglion cells axons at the optic chiasm midline. This probably requires repulsive interaction with EFNB2. In the adult nervous system together with EFNB3, regulates chemotaxis, proliferation and polarity of the hippocampus neural progenitors. 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 synapse formation. May also regulate angiogenesis. More generally, may play a role in targeted cell migration and adhesion. Upon activation by EFNB1 and probably other ephrin-B ligands activates the MAPK/ERK and the JNK signaling cascades to regulate cell migration and adhesion respectively. Involved in the maintenance of the pool of satellite cells (muscle stem cells) by promoting their self-renewal and reducing their activation and differentiation. [PubMed: 27446912]
• Protein Sequence: MALDCLLLFLLASAVAAMEETLMDTRTATAELGWTANPASGWEEVSGYDENLNTIRTYQVCNVFEPNQNNWLLTTFINRRGAHRIYTEMRFTVRDCSSLPNVPGSCKETFNLYYYETDSVIATKKSAFWSEAPYLKVDTIAADESFSQVDFGGRLMKVNTEVRSFGPLTRNGFYLAFQDYGACMSLLSVRVFFKKCPSIVQNFAVFPETMTGAESTSLVIARGTCIPNAEEVDVPIKLYCNGDGEWMVPIGRCTCKPGYEPENSVACKACPAGTFKASQEAEGCSHCPSNSRSPSEASPICTCRTGYYRADFDPPEVACTSVPSGPRNVISIVNETSIILEWHPPRETGGRDDVTYNIICKKCRADRRSCSRCDDNVEFVPRQLGLTECRVSISSLWAHTPYTFDIQAINGVSSKSPFPPQHVSVNITTNQAAPSTVPIMHQVSATMRSITLSWPQPEQPNGIILDYEIRYYEKEHNEFNSSMARSQTNTARIDGLRPGMVYVVQVRARTVAGYGKFSGKMCFQTLTDDDYKSELREQLPLIAGSAAAGVVFVVSLVAISIVCSRKRAYSKEAAYSDKLQHYSTGRGSPGMKIYIDPFTYEDPNEAVREFAKEIDVSFVKIEEVIGAGEFGEVYKGRLKLPGKREIYVAIKTLKAGYSEKQRRDFLSEASIMGQFDHPNIIRLEGVVTKSRPVMIITEFMENGALDSFLRQNDGQFTVIQLVGMLRGIAAGMKYLSEMNYVHRDLAARNILVNSNLVCKVSDFGLSRYLQDDTSDPTYTSSLGGKIPVRWTAPEAIAYRKFTSASDVWSYGIVMWEVMSFGERPYWDMSNQDVINAIEQDYRLPPPMDCPAALHQLMLDCWQKDRNSRPRFAEIVNTLDKMIRNPASLKTVATITAVPSQPLLDRSIPDFTAFTTVDDWLSAIKMVQYRDSFLTAGFTSLQLVTQMTSEDLLRIGVTLAGHQKKILSSIHSMRVQMNQSPSVMA

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
13	Phosphorylation	LLLFLLASAVAAMEE HHHHHHHHHHHHHHH	24.20	28059163
123	Phosphorylation	ETDSVIATKKSAFWS ECCCEEEECCCCCCC	28.07	-
293	Phosphorylation	HCPSNSRSPSEASPI CCCCCCCCHHHCCCC	32.38	22871156
295	Phosphorylation	PSNSRSPSEASPICT CCCCCCHHHCCCCEE	47.22	22871156
298	Phosphorylation	SRSPSEASPICTCRT CCCHHHCCCCEEECC	15.67	22871156
302	Phosphorylation	SEASPICTCRTGYYR HHCCCCEEECCCEEE	13.02	22871156
334	N-linked_Glycosylation	RNVISIVNETSIILE CCEEEEEECCEEEEE	45.20	-
426	N-linked_Glycosylation	PPQHVSVNITTNQAA CCCCEEEEEECCCCC	20.55	-
480	N-linked_Glycosylation	EKEHNEFNSSMARSQ HHHHCCCCHHHHHHH	27.31	-
575	Phosphorylation	AYSKEAAYSDKLQHY CCCCHHHHHHHCCCC	25.17	20139300
582	Phosphorylation	YSDKLQHYSTGRGSP HHHHCCCCCCCCCCC	8.58	-
588	Phosphorylation	HYSTGRGSPGMKIYI CCCCCCCCCCCEEEE	19.54	29899451
594	Phosphorylation	GSPGMKIYIDPFTYE CCCCCEEEECCCCCC	8.18	16512673
599	Phosphorylation	KIYIDPFTYEDPNEA EEEECCCCCCCHHHH	31.24	18515860
600	Phosphorylation	IYIDPFTYEDPNEAV EEECCCCCCCHHHHH	20.79	9233798
766	Phosphorylation	KVSDFGLSRYLQDDT EECCCCHHHHCCCCC	21.18	22817900
768	Phosphorylation	SDFGLSRYLQDDTSD CCCCHHHHCCCCCCC	12.82	29899451
773	Phosphorylation	SRYLQDDTSDPTYTS HHHCCCCCCCCCEEC	43.23	29899451
774	Phosphorylation	RYLQDDTSDPTYTSS HHCCCCCCCCCEECC	48.89	20415495
777	Phosphorylation	QDDTSDPTYTSSLGG CCCCCCCCEECCCCC	44.41	20415495
779	Phosphorylation	DTSDPTYTSSLGGKI CCCCCCEECCCCCCC	17.83	-
928	Phosphorylation	SAIKMVQYRDSFLTA HHHHHHHCHHHHHHC	12.65	-
948	Phosphorylation	QLVTQMTSEDLLRIG HHHEECCHHHHHHHC	24.62	-
957	Phosphorylation	DLLRIGVTLAGHQKK HHHHHCCEEHHHHHH	12.99	25338131
971	Phosphorylation	KILSSIHSMRVQMNQ HHHHHHHHHHCCCCC	13.45	-

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

Oops, there are no upstream regulatory protein records of EPHB1_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of EPHB1_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 EPHB1_MOUSE !!

Protein-Protein Interaction

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

Drug and Disease Associations

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