Ephb6
entrez
13848
canonical
uniprot
O08644
canonical
ensembl
ENSMUSG00000029869
resolver
ensp
ENSMUSP00000110380
resolver
ensp
ENSMUSP00000235345
resolver
ensp
ENSMUSP00000235348
resolver
genesymbol
Ephb6
resolver
genesymbol_syn
Cekl
resolver
uniprot
Q3TQ77
resolver
uniprot
Q8BN76
resolver
uniprot
Q8K0A9
resolver
uniprot_entry
EPHB6_MOUSE
resolver
uniprot_sec
Q3TQ77
resolver
uniprot_sec
Q8BN76
resolver
uniprot_sec
Q8K0A9
resolver
amino_acid_sequence
MATEGTTGSGSRVVAGMVCSLWLLVLGSSVLALEEVLLDTTGETSEIGWLTYPPGGWDEVSVLDDQRRLTRTFEACHVAGLPPGSGQDNWLQTHFVERRGAQRAHIRLHFSVRACSSLGVSGGTCRETFTLYYRQADEPDGPDSIAAWHLKRWTKVDTIAADESFPASSSSSSWAVGPHRTGQRVGLQLNVKERSFGPLTQRGFYVAFQDTGACLALVAVKLFSYTCPSVLRAFASFPETQASGAGGASLVAAVGTCVAHAEPEEDGVGGQAGGSPPRLHCNGEGRWMVAVGGCRCQPGHQPARGDKLCQACPEGSYKALAGNVPCSPCPARSHSPDPAAPVCPCLQGFYRASSDPPEAPCTGPPSAPRELWFEVQGSALMLHWRLPQELGGRGDLLFNVVCKECGGHGEPSSGGMCRRCRDEVHFDPRQRGLTESRVLVGGLRAHVPYILEVQAVNGVSELSPDPPQAAAINVSTSHEVPSAVPVMHQVSRAANSITVSWPQPEQTNGNILDYQLRYYDQAEDESHSFTMTSETNTATVTRLSPGHIYGFQVRARTAAGHGPYGGKVYFQTLPQGELSSQLPEKLSLVIGSILGALAFLLLAAITVLAVIFQRKRRGTGYTEQLQQYSSPGLGVKYYIDPSTYDDPCQAIRELAREVDPTYIKIEEVIGAGSFGEVRRGRLQPRGRREQAVAIQALWAGGAESLKMTFLGRAALLGQFQHPNILRLEGVVTKSRPVMVLTELMELGPLDSFLRQREGQFSSLQLVAMQRGVAAAMQYLSSFAFVHRALSARSVLVNSHLVCKVARLGHSPQGSSSLLRWAAPEVITHGKYTTSSDVWSFGILMWEVMSYGERPYWDMNEQEVLNAIEQEFRLPPPPGCPPGLHLLMLDTWQKDRARRPHFDQLVAAFDKMIRKPDTLQAEGGSGDRPSQALLNPVALDFPCLDSPQAWLSAIGLECYQDNFSKFGLSTFSDVAQLSLEDLPGLGITLAGHQKKLLHNIQLLQQHLRQPGSVEV
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
110107
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
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
8761299
uniprot
proteins
sequence_length
1014
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Isoform 2]: Secreted {ECO:0000305}.; SUBCELLULAR LOCATION: [Isoform 3]: Secreted {ECO:0000305}.
uniprot
proteins
transmembrane_region
TRANSMEM 592..612; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins