GO_REF:0000002
Gene Ontology annotation through association of InterPro records with GO terms
GO_REF:0000003
Gene Ontology annotation based on Enzyme Commission mapping
GO_REF:0000024
Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity
GO_REF:0000033
Annotation inferences using phylogenetic trees
GO_REF:0000107
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
GO_REF:0000120
Combined Automated Annotation using Multiple IEA Methods
PMID:12734395
Forward EphB4 signaling in endothelial cells controls cellular repulsion and segregation from ephrinB2 positive cells.
PMID:15930280
EphB4 expression and biological significance in prostate cancer.
PMID:16867992
Structural and biophysical characterization of the EphB4*ephrinB2 protein-protein interaction and receptor specificity.
PMID:22555806
EphB4 promotes or suppresses Ras/MEK/ERK pathway in a context-dependent manner: Implications for EphB4 as a cancer target.
PMID:23533145
In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine.
PMID:26481148
Erythropoietin Stimulates Tumor Growth via EphB4.
PMID:28514442
Architecture of the human interactome defines protein communities and disease networks.
PMID:28687708
Germline Loss-of-Function Mutations in EPHB4 Cause a Second Form of Capillary Malformation-Arteriovenous Malformation (CM-AVM2) Deregulating RAS-MAPK Signaling.
PMID:30578106
Mutations in Chromatin Modifier and Ephrin Signaling Genes in Vein of Galen Malformation.
PMID:33961781
Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.
PMID:34431498
The intracellular domains of the EphB6 and EphA10 receptor tyrosine pseudokinases function as dynamic signalling hubs.
PMID:35384245
Physical and functional interactome atlas of human receptor tyrosine kinases.
PMID:40205054
Multimodal cell maps as a foundation for structural and functional genomics.
PMID:8188704
Cloning and characterization of HTK, a novel transmembrane tyrosine kinase of the EPH subfamily.
Reactome:R-HSA-3928578
EPH receptors autophosphorylate
Reactome:R-HSA-3928591
EPH:EFN tetramers oligomerise
Reactome:R-HSA-3928592
p190RhoGEF exchanges GTP for GDP on RHOA, activating it
Reactome:R-HSA-3928595
N-WASP binds ARP2/3 and G-actin
Reactome:R-HSA-3928597
EPH:EFN dimers tetramerise
Reactome:R-HSA-3928598
Recruitment of p190RhoGEF to p-FAK
Reactome:R-HSA-3928601
CDC42 and PIP2 bind WASL, activating it
Reactome:R-HSA-3928604
SFKs phosphorylate VAV2,3
Reactome:R-HSA-3928607
p-EPHs bind VAV2,3
Reactome:R-HSA-3928612
KALRN exchanges GTP for GDP on RAC1, activating it
Reactome:R-HSA-3928614
EFNB:GRB4 binds GIT1
Reactome:R-HSA-3928615
EFNBs bind SFKs
Reactome:R-HSA-3928617
EPHB2 binds KALRN
Reactome:R-HSA-3928624
EPHBs bind EFNBs
Reactome:R-HSA-3928625
PAKs autophosphorylate
Reactome:R-HSA-3928627
EPHB phosphorylates TIAM1
Reactome:R-HSA-3928628
VAV exchanges GTP for GDP on RAC1, activating it
Reactome:R-HSA-3928631
GIT1 binds bPIX
Reactome:R-HSA-3928633
bPIX exchanges GTP for GDP on RAC, activating it
Reactome:R-HSA-3928639
p-EFNB binds GRB4
Reactome:R-HSA-3928640
PAKs phosphorylate MLC
Reactome:R-HSA-3928641
PAK binds RAC and bPIX
Reactome:R-HSA-3928645
EPHB:NMDAR binds TIAM1
Reactome:R-HSA-3928654
Clathrin internalises EPH:EFN complexes
Reactome:R-HSA-3928656
gamma-secretase cleaves EPHB2
Reactome:R-HSA-3928657
MMP2,9 cleave EPHB
Reactome:R-HSA-4093329
EFNBs bind SDCBP
Reactome:R-HSA-4093331
Ras:GTP binds p120-RasGAP
Reactome:R-HSA-4093332
p-EPHB phosphorylates SDC2
Reactome:R-HSA-4093336
p-TIAM1 exchanges GTP for GDP on RAC1, activating it
Reactome:R-HSA-4093339
p120-RasGAP activates GTP hydrolysis on RAS, inactivating it
PMID:10518221
Symmetrical mutant phenotypes of the receptor EphB4 and its specific transmembrane ligand ephrin-B2 in cardiovascular development.
PMID:16424904
EphB4 controls blood vascular morphogenesis during postnatal angiogenesis.
PMID:17428795
Ligand binding and calcium influx induce distinct ectodomain/gamma-secretase-processing pathways of EphB2 receptor.
PMID:18593464
Novel splice variants derived from the receptor tyrosine kinase superfamily are potential therapeutics for rheumatoid arthritis.
PMID:18713744
Ephrin-B2-induced cleavage of EphB2 receptor is mediated by matrix metalloproteinases to trigger cell repulsion.
PMID:27400125
EPHB4 kinase-inactivating mutations cause autosomal dominant lymphatic-related hydrops fetalis.