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Protein Page:
EphA4 (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
EphA4 a tyrosine kinase receptor of the Eph family. Receptor for members of the ephrin-A family. Binds to ephrin-A1, -A4 and -A5. Binds more poorly to ephrin-A2 and -A3. May play a role in hindbrain pattern formation. 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. Note: This description may include information from UniProtKB.
Protein type: Membrane protein, integral; EC 2.7.1.112; EC 2.7.10.1; Protein kinase, tyrosine (receptor); Kinase, protein; Protein kinase, TK; TK group; Eph family
Cellular Component: Golgi apparatus; cell surface; endoplasmic reticulum; integral to plasma membrane; postsynaptic density; dendrite; dendritic spine; perikaryon; postsynaptic membrane; mitochondrial outer membrane; early endosome membrane; axon; cytoplasm; nerve terminal; neuromuscular junction; cell junction; filopodium
Molecular Function: identical protein binding; protein binding; transmembrane-ephrin receptor activity; ephrin receptor binding; GPI-linked ephrin receptor activity; PH domain binding; ATP binding; protein kinase activity
Biological Process: positive regulation of JNK activity; peptidyl-tyrosine phosphorylation; negative regulation of axon regeneration; protein amino acid autophosphorylation; regulation of astrocyte differentiation; motor axon guidance; positive regulation of dendrite morphogenesis; glial cell migration; regulation of axonogenesis; adult walking behavior; regulation of Rap GTPase activity; ephrin receptor signaling pathway; cell adhesion; corticospinal tract morphogenesis; regulation of Rac GTPase activity
Reference #:  P54764 (UniProtKB)
Alt. Names/Synonyms: EK8; EPH receptor A4; EPH-like kinase 8; EPHA4; ephrin receptor EphA4; Ephrin type-A receptor 4; HEK8; receptor protein-tyrosine kinase HEK8; SEK; TYRO1; TYRO1 protein tyrosine kinase; Tyrosine-protein kinase receptor SEK; Tyrosine-protein kinase TYRO1
Gene Symbols: EPHA4
Molecular weight: 109,860 Da
Basal Isoelectric point: 6.21  Predict pI for various phosphorylation states
CST Pathways:  Tyrosine Kinases & Substrates
Select Structure to View Below

EphA4

Protein Structure Not Found.


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Sites Implicated In
molecular association, regulation: Y602‑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 4 T117-p SLPGVMGtCKETFNL
0 1 T168-p DRIMKLNtEIRDVGP
0 1 S349-p TSVNLEWssPQNtGG
0 1 S350-p SVNLEWssPQNtGGR
0 1 T354-p EWssPQNtGGRQDIS
0 1 K587 KQEADEEKHLNQGVR
0 5 T595-p HLNQGVRtyVDPFTy
5 84 Y596-p LNQGVRtyVDPFTyE
0 2 T601 RtyVDPFTyEDPNQA
6 164 Y602-p tyVDPFTyEDPNQAV
0 1 S637-p GEFGEVCsGRLKVPG
0 1 K693-ac EGVVTKCkPVMIITE
0 2 K735-ub RGIGSGMkYLSDMsY
0 1 S741-p MkYLSDMsYVHRDLA
0 3 K761 VNSNLVCKVSDFGMS
3 707 Y779-p EDDPEAAyTtRGGKI
0 2 T780 DDPEAAyTtRGGKIP
0 2 T781-p DPEAAyTtRGGKIPI
0 5 Y798-p TAPEAIAyRKFTSAS
0 1 S887-p KLIRNPNsLKRTGTE
0 1 R890 RNPNsLKRTGTESSR
0 1 R897 RTGTESSRPNTALLD
1 0 Y928 QAIKMDRYKDNFTAA
0 1 T957-p DLARIGItAITHQNK
8793 : EphA3/A4/A5 (D2C11) Rabbit mAb
8862 : Phospho-EphA3 (Tyr779) (D10H1) Rabbit mAb
  mouse

 
T117 SLPGVMGTCKETFNL
T168 DRIMKLNTEIRDVGP
S349 TSVNLEWSSPQNTGG
S350 SVNLEWSSPQNTGGR
T354 EWSSPQNTGGRQDIS
K587-ub KQEADEEkHLNQGVR
T595-p HLNQGVRtyVDPFty
Y596-p LNQGVRtyVDPFtyE
T601-p RtyVDPFtyEDPNQA
Y602-p tyVDPFtyEDPNQAV
S637 GEFGEVCSGRLKVPG
K693 EGVVTKCKPVMIITE
K735-ub RGIGSGMkYLSDMSY
S741 MkYLSDMSYVHRDLA
K761-ac VNSNLVCkVSDFGMS
Y779-p EDDPEAAyttRGGKI
T780-p DDPEAAyttRGGKIP
T781-p DPEAAyttRGGKIPI
Y798 TAPEAIAYRKFTSAS
S887 KLIRNPNSLKRTGSE
R890 RNPNSLKRTGSESSR
R897 RTGSESSRPNTALLD
Y928-p QAIKMDRyKDNFTAA
T957 DLARIGITAITHQNK
8793 : EphA3/A4/A5 (D2C11) Rabbit mAb
8862 : Phospho-EphA3 (Tyr779) (D10H1) Rabbit mAb
  rat

 
T117 SLPGVMGTCKETFNL
T168 DRIMKLNTEIRDVGP
S349 TSVNLEWSSPQNTGG
S350 SVNLEWSSPQNTGGR
T354 EWSSPQNTGGRQDIS
K587 KQEADEEKHLNQGVR
T595-p HLNQGVRtyVDPFty
Y596-p LNQGVRtyVDPFtyE
T601-p RtyVDPFtyEDPNQA
Y602-p tyVDPFtyEDPNQAV
S637 GEFGEVCSGRLKVPG
K693 EGVVTKCKPVMIITE
K735 RGIGSGMKYLSDMSY
S741 MKYLSDMSYVHRDLA
K761 VNSNLVCKVSDFGMS
Y779-p EDDPEAAyTTRGGKI
T780 DDPEAAyTTRGGKIP
T781 DPEAAyTTRGGKIPI
Y798 TAPEAIAYRKFTSAS
S887 KLIRNPNSLKrTGPE
R890-m1 RNPNSLKrTGPESSr
R897-m1 rTGPESSrPNTALLD
Y928 QAIKMDRYKDNFTAA
T957 DLARIGITAITHQNK
8793 : EphA3/A4/A5 (D2C11) Rabbit mAb
8862 : Phospho-EphA3 (Tyr779) (D10H1) Rabbit mAb
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