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Protein Page:
EphB1 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
EphB1 a receptor tyrosine kinase of the Eph family. Receptor for members of the ephrin-B family: ephrin-B1, -B2 and -B3. The Eph receptor tyrosine kinase family, the largest in the tyrosine kinase group, has fourteen members. They bind membrane-anchored ligands, ephrins, at sites of cell-cell contact, regulating the repulsion and adhesion of cells that underlie the establishment, maintenance, and remodeling of patterns of cellular organization. Eph signals are particularly important in regulating cell adhesion and cell migration during development, axon guidance, homeostasis and disease. EphA receptors bind to GPI-anchored ephrin-A ligands, while EphB receptors bind to ephrin-B proteins that have a transmembrane and cytoplasmic domain. Interactions between EphB receptor kinases and ephrin-B proteins transduce signals bidirectionally, signaling to both interacting cell types. Eph receptors and ephrins also regulate the adhesion of endothelial cells and are required for the remodeling of blood vessels. The ligand-activated form of EphB1 interacts with GRB2, GRB10 and NCK through their respective SH2 domains. Four alternatively spliced isoforms are known. Note: This description may include information from UniProtKB.
Protein type: EC 2.7.10.1; Membrane protein, integral; Protein kinase, TK; Kinase, protein; Protein kinase, tyrosine (receptor); TK group; Eph family
Chromosomal Location of Human Ortholog: 3q21-q23
Cellular Component: early endosome membrane; integral to plasma membrane; axon; dendrite; lipid raft
Molecular Function: protein binding; transmembrane-ephrin receptor activity; axon guidance receptor activity; ATP binding
Biological Process: axon guidance; peptidyl-tyrosine phosphorylation; protein amino acid autophosphorylation; central nervous system projection neuron axonogenesis; optic nerve morphogenesis; regulation of JNK cascade; cell-substrate adhesion; positive regulation of synaptogenesis; camera-type eye morphogenesis; neurogenesis; establishment of cell polarity; ephrin receptor signaling pathway; angiogenesis; detection of temperature stimulus involved in sensory perception of pain; retinal ganglion cell axon guidance
Reference #:  P54762 (UniProtKB)
Alt. Names/Synonyms: EK6; ELK; EPH receptor B1; eph tyrosine kinase 2; EPH-like kinase 6; EPHB1; Ephrin type-B receptor 1; EPHT2; FLJ37986; hEK6; NET; soluble EPHB1 variant 1; Tyrosine-protein kinase receptor EPH-2
Gene Symbols: EPHB1
Molecular weight: 109,885 Da
Basal Isoelectric point: 6.03  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

EphB1

Protein Structure Not Found.


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Sites Implicated In
cell adhesion, altered: Y594‑p
cell motility, altered: Y594‑p, Y928‑p
molecular association, regulation: Y594‑p, Y600‑p, Y778‑p, Y928‑p
phosphorylation: Y594‑p, Y928‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 1 T123 ETDSVIATKKSAFWS
0 1 S164-p KVNTEVRsFGPLTRN
0 1 S395-p ECRVSISsLWAHTPY
0 12 Y575-p AYSKEAVySDKLQHy
0 1 S576 YSKEAVySDKLQHys
0 7 Y582-p ySDKLQHysTGRGsP
0 1 S583-p SDKLQHysTGRGsPG
0 1 T584 DKLQHysTGRGsPGM
0 2 S588-p HysTGRGsPGMkIyI
0 5 K592-ub GRGsPGMkIyIDPFt
5 127 Y594-p GsPGMkIyIDPFtyE
0 7 T599-p kIyIDPFtyEDPNEA
1 130 Y600-p IyIDPFtyEDPNEAV
0 19 Y634-p AGEFGEVyKGRLKLP
0 5 Y740-p KYLAEMNyVHRDLAA
0 3 S766-p KVSDFGLsRYLQDDT
0 1 S774-p RYLQDDTsDPtyTSS
0 1 T777-p QDDTsDPtyTSSLGG
2 20 Y778-p DDTsDPtyTSSLGGK
0 1 T779 DTsDPtyTSSLGGKI
0 5 Y798-p TAPEAIAyRKFTSAS
2 0 Y928-p SAIKMVQyRDSFLTA
0 1 S948 QLVTQMTSEDLLRIG
0 1 S968-p HQKKILNsIHSMRVQ
0 1 S971 KILNsIHSMRVQISQ
  mouse

 
T123-p ETDSVIAtKKSAFWS
S164 KVNTEVRSFGPLTRN
S395 ECRVSISSLWAHTPY
Y575-p AYSKEAAySDKLQHy
S576 YSKEAAySDKLQHyS
Y582-p ySDKLQHySTGRGsP
S583 SDKLQHySTGRGsPG
T584 DKLQHySTGRGsPGM
S588-p HySTGRGsPGMKIyI
K592 GRGsPGMKIyIDPFt
Y594-p GsPGMKIyIDPFtyE
T599-p KIyIDPFtyEDPNEA
Y600-p IyIDPFtyEDPNEAV
Y634 AGEFGEVYKGRLKLP
Y740 KYLSEMNYVHRDLAA
S766-p KVSDFGLsRYLQDDT
S774 RYLQDDTSDPTYtSS
T777 QDDTSDPTYtSSLGG
Y778 DDTSDPTYtSSLGGK
T779-p DTSDPTYtSSLGGKI
Y798 TAPEAIAYRKFTSAS
Y928 SAIKMVQYRDSFLTA
S948-p QLVTQMTsEDLLRIG
S968 HQKKILSSIHsMRVQ
S971-p KILSSIHsMRVQMNQ
  rat

 
T123 ETDSVIATKKSAFWS
S164 KVNTEVRSFGPLTRN
S395 ECRVSISSLWAHTPY
Y575-p AYSKEAVysDKLQHy
S576-p YSKEAVysDKLQHyS
Y582-p ysDKLQHyStGRGSP
S583 sDKLQHyStGRGSPG
T584-p DKLQHyStGRGSPGM
S588 HyStGRGSPGMKIyI
K592 GRGSPGMKIyIDPFt
Y594-p GSPGMKIyIDPFtyE
T599-p KIyIDPFtyEDPNEA
Y600-p IyIDPFtyEDPNEAV
Y634 AGEFGEVYKGRLKLP
Y740-p KYLSEMNyVHRDLAA
S766 KVSDFGLSRYLQDDT
S774 RYLQDDTSDPTyTSS
T777 QDDTSDPTyTSSLGG
Y778-p DDTSDPTyTSSLGGK
T779 DTSDPTyTSSLGGKI
Y798 TAPEAIAYRKFTSAS
Y928 SAIKMVQYRDSFLTA
S948 QLVTQMTSEDLLRIG
S968 HQKKILSSIHSMRVQ
S971 KILSSIHSMRVQMNQ
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