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Protein Page:
EphA1 (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
EphA1 a receptor tyrosine kinase. Receptor for members of the ephrin-A family. Binds with a low affinity to ephrin-A1. 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. Misexpressed in several cancers, including upregulation in head and neck cancer, and downregulation in invasive breast cancer cell lines and glioblastoma Note: This description may include information from UniProtKB.
Protein type: Kinase, protein; Protein kinase, tyrosine (receptor); Protein kinase, TK; EC 2.7.10.1; Membrane protein, integral; TK group; Eph family
Chromosomal Location of Human Ortholog: 7q34
Cellular Component: integral to plasma membrane
Molecular Function: transmembrane-ephrin receptor activity; protein kinase binding; ATP binding; protein kinase activity
Biological Process: peptidyl-tyrosine phosphorylation; protein amino acid autophosphorylation; activation of Rho GTPase; positive regulation of angiogenesis; cell surface receptor linked signal transduction; positive regulation of cell proliferation; positive regulation of stress fiber formation; ephrin receptor signaling pathway; negative regulation of protein kinase activity; angiogenesis; positive regulation of cell-matrix adhesion; negative regulation of cell migration; regulation of Rac GTPase activity; positive regulation of cell migration
Reference #:  P21709 (UniProtKB)
Alt. Names/Synonyms: EPH; EPH receptor A1; eph tyrosine kinase 1; EPHA1; ephrin receptor EphA1; Ephrin type-A receptor 1; EPHT; EPHT1; erythropoietin-producing hepatoma amplified sequence; MGC163163; oncogene EPH; soluble EPHA1 variant 1; soluble EPHA1 variant 2; Tyrosine-protein kinase receptor EPH
Gene Symbols: EPHA1
Molecular weight: 108,127 Da
Basal Isoelectric point: 6.2  Predict pI for various phosphorylation states
Select Structure to View Below

EphA1

Protein Structure Not Found.


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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 T33-p KEVTLMDtsKAQGEL
0 1 S34-p EVTLMDtsKAQGELG
0 1 S93 IYRGEEASRVHVELQ
0 1 H96 GEEASRVHVELQFTV
0 1 T102 VHVELQFTVRDCKSF
0 1 S153-p TTVAADQsFtIRDLV
0 1 T155-p VAADQsFtIRDLVSG
0 1 K593-ub TDVDREDkLWLkPyV
0 1 K597-ub REDkLWLkPyVDLQA
0 35 Y599-p DkLWLkPyVDLQAyE
0 33 Y605-p PyVDLQAyEDPAQGA
0 4 T780-p LLDDFDGtyEtQGGk
0 253 Y781-p LDDFDGtyEtQGGkI
0 1 T783-p DFDGtyEtQGGkIPI
0 3 K787-ub tyEtQGGkIPIRWTA
0 1 T805-p IAHRIFTtASDVWsF
0 1 S811-p TtASDVWsFGIVMWE
0 2 T892-p ANPHSLRtIANFDPR
0 16 S906-p RMTLRLPsLsGsDGI
0 2 S908-p TLRLPsLsGsDGIPY
0 14 S910-p RLPsLsGsDGIPYRT
0 1 S919-p GIPYRTVsEWLESIR
  mouse

 
T34 EEVTLMDTSTAQGEL
S35 EVTLMDTSTAQGELG
S94-p IYRGEEAsRIyVELQ
Y97-p GEEAsRIyVELQFtV
T103-p IyVELQFtVRDCKSF
S154 TTVAADQSFTIRDLA
T156 VAADQSFTIRDLASG
K594 TNVDREDKLWLKPYV
K598 REDKLWLKPYVDLQA
Y600 DKLWLKPYVDLQAYE
Y606 PYVDLQAYEDPAQGA
T781 LLDDFDGTyETQGGk
Y782-p LDDFDGTyETQGGkI
T784 DFDGTyETQGGkIPI
K788-ub TyETQGGkIPIRWTA
T806 IAHRIFTTASDVWSF
S812 TTASDVWSFGIVMWE
T893 TDPHSLRTIANFDPR
S907-p RVTLRLPsLsGsDGI
S909-p TLRLPsLsGsDGIPY
S911-p RLPsLsGsDGIPYRS
S920 GIPYRSVSEWLESIR
  rat

 
T34 EEVTLMDTSTAQGEL
S35 EVTLMDTSTAQGELG
S94 IYRGEEASRVHVELQ
H97 GEEASRVHVELQFTV
T103 VHVELQFTVRDCKSF
S154 TTVAADQSFTIRDLA
T156 VAADQSFTIRDLASG
K594 TNVDREDKLWLKPYV
K598 REDKLWLKPYVDLQA
Y600 DKLWLKPYVDLQAYE
Y606 PYVDLQAYEDPAQGA
T781 LLDDFDGTYETQGGK
Y782 LDDFDGTYETQGGKI
T784 DFDGTYETQGGKIPI
K788 TYETQGGKIPIRWTA
T806 IAHRIFTTASDVWSF
S812 TTASDVWSFGIVMWE
T893 TDPHSLRTIANFDPR
S907-p RVTLRLPsLSGSDGI
S909 TLRLPsLSGSDGIPY
S911 RLPsLSGSDGIPYRS
S920 GIPYRSVSEWLESIR
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