EPHB2
entrez
2048
canonical
uniprot
P29323
canonical
ensembl
ENSG00000133216
resolver
ensp
ENSP00000363761
resolver
ensp
ENSP00000363763
resolver
ensp
ENSP00000383053
resolver
ensp
ENSP00000444174
resolver
enst
ENST00000544305
resolver
genesymbol
EPHB2
resolver
genesymbol_syn
DRT
resolver
genesymbol_syn
EPHT3
resolver
genesymbol_syn
EPTH3
resolver
genesymbol_syn
ERK
resolver
genesymbol_syn
HEK5
resolver
genesymbol_syn
TYRO5
resolver
hgnc
HGNC:3393
resolver
uniprot
B4DSE0
resolver
uniprot
F6TUL7
resolver
uniprot
O43477
resolver
uniprot
Q5T0U6
resolver
uniprot
Q5T0U7
resolver
uniprot
Q5T0U8
resolver
uniprot
Q6NVW1
resolver
uniprot_entry
B4DSE0_HUMAN
resolver
uniprot_entry
EPHB2_HUMAN
resolver
uniprot_entry
F6TUL7_HUMAN
resolver
uniprot_entry
Q6NVW1_HUMAN
resolver
uniprot_sec
O43477
resolver
uniprot_sec
Q5T0U6
resolver
uniprot_sec
Q5T0U7
resolver
uniprot_sec
Q5T0U8
resolver
amino_acid_sequence
MALRRLGAALLLLPLLAAVEETLMDSTTATAELGWMVHPPSGWEEVSGYDENMNTIRTYQVCNVFESSQNNWLRTKFIRRRGAHRIHVEMKFSVRDCSSIPSVPGSCKETFNLYYYEADFDSATKTFPNWMENPWVKVDTIAADESFSQVDLGGRVMKINTEVRSFGPVSRSGFYLAFQDYGGCMSLIAVRVFYRKCPRIIQNGAIFQETLSGAESTSLVAARGSCIANAEEVDVPIKLYCNGDGEWLVPIGRCMCKAGFEAVENGTVCRGCPSGTFKANQGDEACTHCPINSRTTSEGATNCVCRNGYYRADLDPLDMPCTTIPSAPQAVISSVNETSLMLEWTPPRDSGGREDLVYNIICKSCGSGRGACTRCGDNVQYAPRQLGLTEPRIYISDLLAHTQYTFEIQAVNGVTDQSPFSPQFASVNITTNQAAPSAVSIMHQVSRTVDSITLSWSQPDQPNGVILDYELQYYEKELSEYNATAIKSPTNTVTVQGLKAGAIYVFQVRARTVAGYGRYSGKMYFQTMTEAEYQTSIQEKLPLIIGSSAAGLVFLIAVVVIAIVCNRRGFERADSEYTDKLQHYTSGHMTPGMKIYIDPFTYEDPNEAVREFAKEIDISCVKIEQVIGAGEFGEVCSGHLKLPGKREIFVAIKTLKSGYTEKQRRDFLSEASIMGQFDHPNVIHLEGVVTKSTPVMIITEFMENGSLDSFLRQNDGQFTVIQLVGMLRGIAAGMKYLADMNYVHRDLAARNILVNSNLVCKVSDFGLSRFLEDDTSDPTYTSALGGKIPIRWTAPEAIQYRKFTSASDVWSYGIVMWEVMSYGERPYWDMTNQDVINAIEQDYRLPPPMDCPSALHQLMLDCWQKDRNHRPKFGQIVNTLDKMIRNPNSLKAMAPLSSGINLPLLDRTIPDYTSFNTVDEWLEAIKMGQYKESFANAGFTSFDVVSQMMMEDILRVGVTLAGHQKKILNSIQVMRAQMNQIQSVEGQPLARRPRATGRTKRCQPRDVTKKTCNSNDGKKKGMGKKKTDPGRGREIQGIFFKEDSHKESNDCSCGG
uniprot
proteins
disease_involvement
DISEASE: Prostate cancer (PC) [MIM:176807]: A malignancy originating in tissues of the prostate. Most prostate cancers are adenocarcinomas that develop in the acini of the prostatic ducts. Other rare histopathologic types of prostate cancer that occur in approximately 5% of patients include small cell carcinoma, mucinous carcinoma, prostatic ductal carcinoma, transitional cell carcinoma, squamous cell carcinoma, basal cell carcinoma, adenoid cystic carcinoma (basaloid), signet-ring cell carcinoma and neuroendocrine carcinoma. {ECO:0000269|PubMed:15300251, ECO:0000269|PubMed:16155194}. Note=The gene represented in this entry may be involved in disease pathogenesis. EPHB2 mutations have been found in a prostate cancer cell line derived from a brain metastasis.; DISEASE: Bleeding disorder, platelet-type, 22 (BDPLT22) [MIM:618462]: An autosomal recessive disorder characterized by increased bleeding tendency due to platelet dysfunction. Clinical features include epistaxis, hematomas, bleeding after minor injuries, and menorrhagia. {ECO:0000269|PubMed:30213874}. Note=The disease may be caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
2.7.10.1
uniprot
proteins
function
FUNCTION: 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. Functions in axon guidance during development. Involved in the guidance of commissural axons, that form a major interhemispheric connection between the 2 temporal lobes of the cerebral cortex. Also involved in guidance of contralateral inner ear efferent growth cones at the midline and of retinal ganglion cell axons to the optic disk. In addition to axon guidance, also regulates dendritic spines development and maturation and stimulates the formation of excitatory synapses. Upon activation by EFNB1, abolishes the ARHGEF15-mediated negative regulation on excitatory synapse formation. Controls other aspects of development including angiogenesis, palate development and in inner ear development through regulation of endolymph production. Forward and reverse signaling through the EFNB2/EPHB2 complex regulate movement and adhesion of cells that tubularize the urethra and septate the cloaca. May function as a tumor suppressor. May be involved in the regulation of platelet activation and blood coagulation (PubMed:30213874). {ECO:0000269|PubMed:15300251, ECO:0000269|PubMed:30213874}.
uniprot
proteins
mass_dalton
117493
uniprot
proteins
mutagenesis
MUTAGEN 787; /note="K->R: No loss of ubiquitination by RNF186."; /evidence="ECO:0000269|PubMed:33280498"; MUTAGEN 891; /note="K->R: Complete loss of ubiquitination by RNF186."; /evidence="ECO:0000269|PubMed:33280498
uniprot
proteins
post_translational_modification
PTM: Autophosphorylated; ligand binding stimulates autophosphorylation on tyrosine residues. {ECO:0000250|UniProtKB:P54763}.; PTM: (Microbial infection) Proteolytically cleaved at the cell membrane upon H.pylori infection. {ECO:0000269|PubMed:34742300}.; PTM: Polyubiquitinated; ligand binding stimulates ubiquitination (PubMed:28931592). Ubiquitinated by RNF186 at Lys-891, mainly through 'Lys-27'-linked polyubiquitin chains (PubMed:33280498). Ubiquitinated by CRL2(KLHDC2) E3 ligase complex (PubMed:36805027). {ECO:0000269|PubMed:28931592, ECO:0000269|PubMed:33280498, ECO:0000269|PubMed:36805027}.; PTM: Ligand binding induces cleavage by matrix metalloproteinases (MMPs) such as MMP7/MMP9, producing an EphB2/N-terminal fragment (NTF) and a C-terminal long fragment (EphB2-LF). EphB2-LF is further cleaved by MMPs, producing EphB2/CTF1 which is further cleaved by the PS1/gamma-secretase producing EphB2/CTF2. {ECO:0000250|UniProtKB:P54763}.
uniprot
proteins
protein_family
Ephrin receptor subfamily
uniprot
proteins
protein_family
Protein kinase superfamily
uniprot
proteins
protein_family
Tyr protein kinase family
uniprot
proteins
pubmed
10508479
uniprot
proteins
pubmed
15300251
uniprot
proteins
pubmed
16155194
uniprot
proteins
pubmed
1648701
uniprot
proteins
pubmed
16710414
uniprot
proteins
pubmed
17344846
uniprot
proteins
pubmed
17897949
uniprot
proteins
pubmed
18691976
uniprot
proteins
pubmed
19369195
uniprot
proteins
pubmed
28931592
uniprot
proteins
pubmed
30213874
uniprot
proteins
pubmed
33280498
uniprot
proteins
pubmed
34742300
uniprot
proteins
pubmed
36805027
uniprot
proteins
pubmed
7601466
uniprot
proteins
pubmed
7688222
uniprot
proteins
pubmed
7898931
uniprot
proteins
pubmed
8033077
uniprot
proteins
pubmed
8589679
uniprot
proteins
pubmed
9267020
uniprot
proteins
pubmed
9696046
uniprot
proteins
pubmed
9933164
uniprot
proteins
sequence_length
1055
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. Cell projection, axon {ECO:0000250}. Cell projection, dendrite {ECO:0000250}.; SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:34742300}. Note=(Microbial infection) Proteolytically cleaved at the cell membrane upon H.pylori infection. {ECO:0000269|PubMed:34742300}.
uniprot
proteins
transmembrane_region
TRANSMEM 544..564; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins