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Protein Page:
EphA3 (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
EphA3 a receptor tyrosine kinase of the Eph family. Receptor for members of the ephrin-A family: binds to ephrin-A2, -A3, -A4 and -A5The 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. Two point mutations seen in a survey of colorectal tumors. Soluble receptors reduce tumor growth and angiogenesis in mouse models. Two alternatively spliced isoforms of EphA3 have been described. Note: This description may include information from UniProtKB.
Protein type: Kinase, protein; EC 2.7.10.1; Membrane protein, integral; Protein kinase, TK; Protein kinase, tyrosine (receptor); TK group; Eph family
Cellular Component: integral to plasma membrane; early endosome; extracellular region
Molecular Function: protein binding; GPI-linked ephrin receptor activity; ATP binding
Biological Process: cell migration; peptidyl-tyrosine phosphorylation; regulation of Rho GTPase activity; regulation of actin cytoskeleton organization and biogenesis; regulation of focal adhesion formation; ephrin receptor signaling pathway; cell adhesion
Reference #:  P29320 (UniProtKB)
Alt. Names/Synonyms: EK4; EPH receptor A3; EPH-like kinase 4; eph-like tyrosine kinase 1; EPHA3; ephrin receptor EphA3; Ephrin type-A receptor 3; ETK; ETK1; HEK; hEK4; human embryo kinase 1; TYRO4; TYRO4 protein tyrosine kinase; Tyrosine-protein kinase receptor ETK1; Tyrosine-protein kinase TYRO4
Gene Symbols: EPHA3
Molecular weight: 110,131 Da
Basal Isoelectric point: 6.33  Predict pI for various phosphorylation states
CST Pathways:  Tyrosine Kinases & Substrates
Select Structure to View Below

EphA3

Protein Structure Not Found.


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Sites Implicated In
cell adhesion, altered: Y596‑p, Y602‑p, Y779‑p
cytoskeletal reorganization: Y596‑p, Y602‑p, Y779‑p
enzymatic activity, induced: Y596‑p, Y602‑p, Y742‑p, Y779‑p
molecular association, regulation: Y596‑p, Y602‑p, Y779‑p
protein conformation: Y596‑p, Y742‑p, S768‑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 Y123-p CKETFNLyyMESDDD
0 1 Y124-p KETFNLyyMESDDDH
0 1 S294-p CAKCPPHsSTQEDGS
0 1 T432-p FAAVSITtNQAAPSP
0 1 T442-p AAPSPVLtIKKDRTS
0 1 T485-p QEQETSYtILRARGT
0 1 S497-p RGTNVTIssLKPDTI
0 1 S498-p GTNVTIssLKPDTIY
0 1 T513 VFQIRARTAAGYGTN
0 1 S521 AAGYGTNSRKFEFET
0 1 Y561-p ILLTVVIyVLIGRFC
0 1 Y570-p LIGRFCGyKSKHGAD
0 1 T595-p LKLPGLRtyVDPHty
3 31 Y596-p KLPGLRtyVDPHtyE
0 5 T601-p RtyVDPHtyEDPTQA
3 36 Y602-p tyVDPHtyEDPTQAV
0 1 K625-ub ATNISIDkVVGAGEF
0 3 K656-ub SVAIKTLkVGYTEKQ
1 1 Y701-p PVMIVTEyMENGSLD
0 1 Y736-p GIASGMKyLSDMGyV
1 2 Y742-p KyLSDMGyVHRDLAA
1 3 S768-p KVSDFGLsRVLEDDP
3 695 Y779-p EDDPEAAyTtRGGKI
0 2 T780 DDPEAAyTtRGGKIP
0 2 T781-p DPEAAyTtRGGKIPI
0 5 Y937-p EIFTGVEySSCDTIA
0 1 T974-p SSIKALEtQsKNGPV
0 1 S976-p IKALEtQsKNGPVPV
8793 : EphA3/A4/A5 (D2C11) Rabbit mAb
8862 : Phospho-EphA3 (Tyr779) (D10H1) Rabbit mAb
  mouse

 
Y123 CKETFNLYYMESDDH
Y124 KETFNLYYMESDDHG
S293 CAKCPPHSSTQEDGS
T431 YAAVSITTNQAAPSP
T441 AAPSPVMTIKKDRTS
T484 QEQETSYTILRARGT
S496 RGTNVTISSLKPDTT
S497 GTNVTISSLKPDTTY
T512-p VFQIRARtAAGYGTN
S520-p AAGYGTNsRKFEFET
Y560 IVLTVVTYVLVGRFC
Y569 LVGRFCGYHKSKHSA
T595 LKLPGLRTyVDPHTy
Y596-p KLPGLRTyVDPHTyE
T601 RTyVDPHTyEDPTQA
Y602-p TyVDPHTyEDPTQAV
K625 ATNISIDKVVGAGEF
K656 SVAIKTLKVGYTEKQ
Y701 PEMIVTEYMENGSLD
Y736 GIASGMKYLSDMGYV
Y742 KYLSDMGYVHRDLAA
S768-p KVSDFGLsRVLEDDP
Y779-p EDDPEAAyttRGGKI
T780-p DDPEAAyttRGGKIP
T781-p DPEAAyttRGGKIPI
Y937-p EIFTGVEySSCDTIA
T974 STIKALETQSKNGPV
S976 IKALETQSKNGPVPV
8793 : EphA3/A4/A5 (D2C11) Rabbit mAb
8862 : Phospho-EphA3 (Tyr779) (D10H1) Rabbit mAb
  rat

 
Y123 CKETFNLYYMESDDD
Y124 KETFNLYYMESDDDH
S294 CTKCPPHSSTQEDGS
T432 FAAVSITTNQAAPSP
T442 AAPSPVMTIKKDRTS
T485 QEQETSYTILRARGT
S497 RGTNVTISSLKPDTT
S498 GTNVTISSLKPDTTY
T513 VFQIRARTAAGYGTN
S521 AAGYGTNSRKFEFEN
Y561 IVLTVVTYVLVGRFC
Y570 LVGRFCGYHKSKHSS
T596 LRLPGLRTYVDPHTY
Y597 RLPGLRTYVDPHTYE
T602 RTYVDPHTYEDPTQA
Y603 TYVDPHTYEDPTQAV
K626 ATNIAIDKVVGAGEF
K657 SVAIKTLKVGYTEKQ
Y702 PVMIVTEYMENGSLD
Y737 GIASGMKYLSDMGYV
Y743 KYLSDMGYVHRDLAA
S769 KVSDFGLSRVLEDDP
Y780-p EDDPEAAyTTRGGKI
T781 DDPEAAyTTRGGKIP
T782 DPEAAyTTRGGKIPV
Y938 EIFTGVEYSSCDTIA
T975 SSIKALETQSKNGPV
S977 IKALETQSKNGPVPV
8793 : EphA3/A4/A5 (D2C11) Rabbit mAb
8862 : Phospho-EphA3 (Tyr779) (D10H1) Rabbit mAb
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