Ephb6
entrez
312275
canonical
uniprot
P0C0K7
canonical
ensembl
ENSRNOG00000014367
resolver
ensembl
ENSRNOG00055030905
resolver
ensembl
ENSRNOG00060007548
resolver
ensembl
ENSRNOG00065015942
resolver
ensp
ENSRNOP00000019720
resolver
ensp
ENSRNOP00055044339
resolver
ensp
ENSRNOP00060009409
resolver
ensp
ENSRNOP00065020775
resolver
enst
ENSRNOT00000019720
resolver
enst
ENSRNOT00055053615
resolver
enst
ENSRNOT00060012439
resolver
enst
ENSRNOT00065026489
resolver
genesymbol
Ephb6
resolver
uniprot_entry
EPHB6_RAT
resolver
amino_acid_sequence
MASENTAGSGSRVAGMVYSLWLLVLGPSVLALEEVLLDTTGETSEIGWLTYPPGGWDEVSVLDDQRRLTRTFEACHVAGLPPGSGQDNWLQTHFVERRGAQRAHIRLHFSVRACSSLGVSGGTCRETFTLYYRQADEPDSPDSISAWHLKRWTKVDTIAADESFPASSSSSSWAVGPHRTDQRVGLQLNVKERSFGPLTQRGFYVAFQDTGACLALVAVKLFSYTCPSVLRAFASFPETQASGAGGASLVAAVGTCVAHAEPEEDGVGGQAGGSPPRLHCNGEGRWMVAVGGCRCQPGHQPARGDKLCQACPEGSYKALPGNVPCSPCPARSHSPDPAAPVCPCLQGFYRASSDPPEAPCTGPPSAPRELWFEVQGSALMLHWRLPQELGGRGDLLFNVVCKECGGHKEPSSGGMCRRCRDEVHFDPRQRGLTESRVLVGGLRAHVPYILEVQAVNGVSELSPDPPQAAAINVSTSHEVPSAVPVMHQVSRAANSITVSWPQPEQTNGNILDYQLRYYDQAEDESHSFTMTSETNTATVTRLSPGHIYGFQVRARTAAGHGPYGGKVYFQTLPQGELSSQLPEKLSLVIGSILGALAFLLLAAITVLAVIFQRKRRGTGYTEQLQQYSSPGLGVKYYIDPSTYDDPCQAIRELAREVDPTYIKIEEVIGAGSFGEVRRGRLQPRGRREQAVAIQALWAGGAESLKMTFLGRAALLGQFQHPNILRLEGVVTRSRPVMVLTELMELGPLDSFLRQREGQFSSLQLVAMQRGVAAAMQYLSSFAFVHRALSARSVLVNSHLVCKVARLGHSPQGSSSLLRWAAPEVITHGKYTTSSDVWSFGILMWEVMSYGERPYWDMSDQEVLNAIEQEFRLPPPPGCPTGLHLLMLDTWQKDRARRPHFDQLVAAFDKMIRKPDTLQAEGSSGDRPSQALLNPVALDFPCLDSPQAWLSAIGLECYQDNFSKFGLSTFSDVAQLSLEDLPGLGITLAGHQKKLLHNIQLLQQHLRQPGSVEV
uniprot
proteins
function
FUNCTION: Kinase-defective receptor for members of the ephrin-B family. Binds to ephrin-B1 and ephrin-B2. Modulates cell adhesion and migration by exerting both positive and negative effects upon stimulation with ephrin-B2. Inhibits JNK activation, T-cell receptor-induced IL-2 secretion and CD25 expression upon stimulation with ephrin-B2. Can recruit SH2 domain-containing signaling adapters following phosphorylation by EPHB4. {ECO:0000250|UniProtKB:O15197}.
uniprot
proteins
mass_dalton
110313
uniprot
proteins
post_translational_modification
PTM: Ligand-binding increases phosphorylation on tyrosine residues. Phosphorylation on tyrosine residues is mediated by transphosphorylation by the catalytically active EPHB1 in a ligand-independent manner. Tyrosine phosphorylation of the receptor may act as a switch on the functional transition from cell adhesion/attraction to de-adhesion/repulsion. Also phosphorylated by EPHB4 which promotes binding of EPHB6 to SH2 domains, allowing it to interact with downstream SH2 domain-containing signaling adapters. {ECO:0000250|UniProtKB:O15197}.
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
15057822
uniprot
proteins
sequence_length
1013
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000255}.
uniprot
proteins
transmembrane_region
TRANSMEM 591..611; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins