产品描述
*The optimal dilutions should be determined by the end user.
*Tips:
WB: 适用于变性蛋白样本的免疫印迹检测. IHC: 适用于组织样本的石蜡(IHC-p)或冰冻(IHC-f)切片样本的免疫组化/荧光检测. IF/ICC: 适用于细胞样本的荧光检测. ELISA(peptide): 适用于抗原肽的ELISA检测.
引用格式: Affinity Biosciences Cat# AF0028, RRID:AB_2833511.
展开/折叠
ARCC2; AW545284; CTPA; CTPP1; CTRCT6; EC 2.7.10.1; Eck; Eph receptor A2; EPHA2; EPHA2_HUMAN; Ephrin receptor; Ephrin receptor EphA2; Ephrin type A receptor 2; Ephrin type-A receptor 2; Epithelial cell kinase; Epithelial cell receptor protein tyrosine kinase; Myk 2; Myk2; Sek 2; Sek2; Soluble EPHA2 variant 1; Tyrosine protein kinase receptor ECK; Tyrosine-protein kinase receptor ECK; Tyrosine-protein kinase receptor MPK-5; Tyrosine-protein kinase receptor SEK-2; AW492086; Cek4; EC 2.7.10.1; EK4; End3; Eph receptor A3; EPH-like kinase 4; EPH-like tyrosine kinase 1; EPHA3; EPHA3_HUMAN; Ephrin receptor EphA3; Ephrin type-A receptor 3; ETK 1; ETK; ETK1; HEK 4; HEK; HEK4; Human embryo kinase 1; Human embryo kinase; Mek4; MGC109882; Receptor tyrosine kinase HEK; Testicular tissue protein Li 64; Tyro 4; Tyro4; TYRO4 protein tyrosine kinase; Tyrosine protein kinase receptor ETK 1; Tyrosine-protein kinase receptor ETK1; Tyrosine-protein kinase TYRO4; Cek 8; CEK8; EK8; eph receptor a4; EPH-like kinase 8; EPHA4; EPHA4_HUMAN; Ephrin type-A receptor 4; HEK 8; hEK8; Receptor protein-tyrosine kinase HEK8; Sek 1; SEK; TYRO 1 protein tyrosine kinase; TYRO1; Tyrosine-protein kinase receptor SEK; Tyrosine-protein kinase TYRO1;
抗原和靶标
Expressed in brain and glioma tissue and glioma cell lines (at protein level). Expressed most highly in tissues that contain a high proportion of epithelial cells, e.g. skin, intestine, lung, and ovary.
P29320 EPHA3_HUMAN:Widely expressed. Highest level in placenta.
P54764 EPHA4_HUMAN:Ubiquitous.
- P29317 EPHA2_HUMAN:
- Protein BLAST With
- NCBI/
- ExPASy/
- Uniprot
MELQAARACFALLWGCALAAAAAAQGKEVVLLDFAAAGGELGWLTHPYGKGWDLMQNIMNDMPIYMYSVCNVMSGDQDNWLRTNWVYRGEAERIFIELKFTVRDCNSFPGGASSCKETFNLYYAESDLDYGTNFQKRLFTKIDTIAPDEITVSSDFEARHVKLNVEERSVGPLTRKGFYLAFQDIGACVALLSVRVYYKKCPELLQGLAHFPETIAGSDAPSLATVAGTCVDHAVVPPGGEEPRMHCAVDGEWLVPIGQCLCQAGYEKVEDACQACSPGFFKFEASESPCLECPEHTLPSPEGATSCECEEGFFRAPQDPASMPCTRPPSAPHYLTAVGMGAKVELRWTPPQDSGGREDIVYSVTCEQCWPESGECGPCEASVRYSEPPHGLTRTSVTVSDLEPHMNYTFTVEARNGVSGLVTSRSFRTASVSINQTEPPKVRLEGRSTTSLSVSWSIPPPQQSRVWKYEVTYRKKGDSNSYNVRRTEGFSVTLDDLAPDTTYLVQVQALTQEGQGAGSKVHEFQTLSPEGSGNLAVIGGVAVGVVLLLVLAGVGFFIHRRRKNQRARQSPEDVYFSKSEQLKPLKTYVDPHTYEDPNQAVLKFTTEIHPSCVTRQKVIGAGEFGEVYKGMLKTSSGKKEVPVAIKTLKAGYTEKQRVDFLGEAGIMGQFSHHNIIRLEGVISKYKPMMIITEYMENGALDKFLREKDGEFSVLQLVGMLRGIAAGMKYLANMNYVHRDLAARNILVNSNLVCKVSDFGLSRVLEDDPEATYTTSGGKIPIRWTAPEAISYRKFTSASDVWSFGIVMWEVMTYGERPYWELSNHEVMKAINDGFRLPTPMDCPSAIYQLMMQCWQQERARRPKFADIVSILDKLIRAPDSLKTLADFDPRVSIRLPSTSGSEGVPFRTVSEWLESIKMQQYTEHFMAAGYTAIEKVVQMTNDDIKRIGVRLPGHQKRIAYSLLGLKDQVNTVGIPI
- P29320 EPHA3_HUMAN:
- Protein BLAST With
- NCBI/
- ExPASy/
- Uniprot
MDCQLSILLLLSCSVLDSFGELIPQPSNEVNLLDSKTIQGELGWISYPSHGWEEISGVDEHYTPIRTYQVCNVMDHSQNNWLRTNWVPRNSAQKIYVELKFTLRDCNSIPLVLGTCKETFNLYYMESDDDHGVKFREHQFTKIDTIAADESFTQMDLGDRILKLNTEIREVGPVNKKGFYLAFQDVGACVALVSVRVYFKKCPFTVKNLAMFPDTVPMDSQSLVEVRGSCVNNSKEEDPPRMYCSTEGEWLVPIGKCSCNAGYEERGFMCQACRPGFYKALDGNMKCAKCPPHSSTQEDGSMNCRCENNYFRADKDPPSMACTRPPSSPRNVISNINETSVILDWSWPLDTGGRKDVTFNIICKKCGWNIKQCEPCSPNVRFLPRQFGLTNTTVTVTDLLAHTNYTFEIDAVNGVSELSSPPRQFAAVSITTNQAAPSPVLTIKKDRTSRNSISLSWQEPEHPNGIILDYEVKYYEKQEQETSYTILRARGTNVTISSLKPDTIYVFQIRARTAAGYGTNSRKFEFETSPDSFSISGESSQVVMIAISAAVAIILLTVVIYVLIGRFCGYKSKHGADEKRLHFGNGHLKLPGLRTYVDPHTYEDPTQAVHEFAKELDATNISIDKVVGAGEFGEVCSGRLKLPSKKEISVAIKTLKVGYTEKQRRDFLGEASIMGQFDHPNIIRLEGVVTKSKPVMIVTEYMENGSLDSFLRKHDAQFTVIQLVGMLRGIASGMKYLSDMGYVHRDLAARNILINSNLVCKVSDFGLSRVLEDDPEAAYTTRGGKIPIRWTSPEAIAYRKFTSASDVWSYGIVLWEVMSYGERPYWEMSNQDVIKAVDEGYRLPPPMDCPAALYQLMLDCWQKDRNNRPKFEQIVSILDKLIRNPGSLKIITSAAARPSNLLLDQSNVDITTFRTTGDWLNGVWTAHCKEIFTGVEYSSCDTIAKISTDDMKKVGVTVVGPQKKIISSIKALETQSKNGPVPV
- P54764 EPHA4_HUMAN:
- Protein BLAST With
- NCBI/
- ExPASy/
- Uniprot
MAGIFYFALFSCLFGICDAVTGSRVYPANEVTLLDSRSVQGELGWIASPLEGGWEEVSIMDEKNTPIRTYQVCNVMEPSQNNWLRTDWITREGAQRVYIEIKFTLRDCNSLPGVMGTCKETFNLYYYESDNDKERFIRENQFVKIDTIAADESFTQVDIGDRIMKLNTEIRDVGPLSKKGFYLAFQDVGACIALVSVRVFYKKCPLTVRNLAQFPDTITGADTSSLVEVRGSCVNNSEEKDVPKMYCGADGEWLVPIGNCLCNAGHEERSGECQACKIGYYKALSTDATCAKCPPHSYSVWEGATSCTCDRGFFRADNDAASMPCTRPPSAPLNLISNVNETSVNLEWSSPQNTGGRQDISYNVVCKKCGAGDPSKCRPCGSGVHYTPQQNGLKTTKVSITDLLAHTNYTFEIWAVNGVSKYNPNPDQSVSVTVTTNQAAPSSIALVQAKEVTRYSVALAWLEPDRPNGVILEYEVKYYEKDQNERSYRIVRTAARNTDIKGLNPLTSYVFHVRARTAAGYGDFSEPLEVTTNTVPSRIIGDGANSTVLLVSVSGSVVLVVILIAAFVISRRRSKYSKAKQEADEEKHLNQGVRTYVDPFTYEDPNQAVREFAKEIDASCIKIEKVIGVGEFGEVCSGRLKVPGKREICVAIKTLKAGYTDKQRRDFLSEASIMGQFDHPNIIHLEGVVTKCKPVMIITEYMENGSLDAFLRKNDGRFTVIQLVGMLRGIGSGMKYLSDMSYVHRDLAARNILVNSNLVCKVSDFGMSRVLEDDPEAAYTTRGGKIPIRWTAPEAIAYRKFTSASDVWSYGIVMWEVMSYGERPYWDMSNQDVIKAIEEGYRLPPPMDCPIALHQLMLDCWQKERSDRPKFGQIVNMLDKLIRNPNSLKRTGTESSRPNTALLDPSSPEFSAVVSVGDWLQAIKMDRYKDNFTAAGYTTLEAVVHVNQEDLARIGITAITHQNKILSSVQAMRTQMQQMHGRMVPV
种属预测
score>80的预测可信度较高,可尝试用于WB检测。*预测模型主要基于免疫原序列比对,结果仅作参考,不作为质保凭据。
High(score>80) Medium(80>score>50) Low(score<50) No confidence
翻译修饰 - P29317/P29320/P54764 作为底物
Site | PTM Type | Enzyme | Source |
---|---|---|---|
Y67 | Phosphorylation | Uniprot | |
K136 | Ubiquitination | Uniprot | |
K141 | Ubiquitination | Uniprot | |
S153 | Phosphorylation | Uniprot | |
S154 | Phosphorylation | Uniprot | |
K162 | Ubiquitination | Uniprot | |
S373 | Phosphorylation | Uniprot | |
S426 | Phosphorylation | Uniprot | |
S433 | Phosphorylation | Uniprot | |
N435 | N-Glycosylation | Uniprot | |
T437 | Phosphorylation | Uniprot | |
S570 | Phosphorylation | Uniprot | |
Y575 | Phosphorylation | P29317 (EPHA2) | Uniprot |
S577 | Phosphorylation | Uniprot | |
K578 | Ubiquitination | Uniprot | |
S579 | Phosphorylation | Uniprot | |
K583 | Ubiquitination | Uniprot | |
K586 | Ubiquitination | Uniprot | |
T587 | Phosphorylation | Uniprot | |
Y588 | Phosphorylation | P29317 (EPHA2) | Uniprot |
T593 | Phosphorylation | Uniprot | |
Y594 | Phosphorylation | P12931 (SRC) , P29317 (EPHA2) | Uniprot |
K603 | Ubiquitination | Uniprot | |
C612 | S-Nitrosylation | Uniprot | |
K617 | Ubiquitination | Uniprot | |
Y628 | Phosphorylation | P29317 (EPHA2) | Uniprot |
K629 | Ubiquitination | Uniprot | |
K639 | Ubiquitination | Uniprot | |
K646 | Ubiquitination | Uniprot | |
T647 | Phosphorylation | Uniprot | |
K649 | Ubiquitination | Uniprot | |
K655 | Ubiquitination | Uniprot | |
Y685 | Phosphorylation | Uniprot | |
K686 | Ubiquitination | Uniprot | |
T692 | Phosphorylation | Uniprot | |
Y694 | Phosphorylation | P29317 (EPHA2) | Uniprot |
S712 | Phosphorylation | Uniprot | |
K728 | Ubiquitination | Uniprot | |
Y735 | Phosphorylation | P29317 (EPHA2) | Uniprot |
S749 | Phosphorylation | Uniprot | |
S756 | Phosphorylation | Uniprot | |
S761 | Phosphorylation | Uniprot | |
T771 | Phosphorylation | Uniprot | |
Y772 | Phosphorylation | P29317 (EPHA2) | Uniprot |
T773 | Phosphorylation | Uniprot | |
T774 | Phosphorylation | Uniprot | |
S775 | Phosphorylation | Uniprot | |
K778 | Ubiquitination | Uniprot | |
S790 | Phosphorylation | Uniprot | |
Y791 | Phosphorylation | Uniprot | |
K828 | Sumoylation | Uniprot | |
S869 | Phosphorylation | Uniprot | |
K873 | Ubiquitination | Uniprot | |
S880 | Phosphorylation | Uniprot | |
K882 | Ubiquitination | Uniprot | |
T883 | Phosphorylation | Uniprot | |
S892 | Phosphorylation | Uniprot | |
S897 | Phosphorylation | P51812 (RPS6KA3) , P31749 (AKT1) , Q15418 (RPS6KA1) | Uniprot |
T898 | Phosphorylation | Uniprot | |
S899 | Phosphorylation | Uniprot | |
S901 | Phosphorylation | Uniprot | |
S910 | Phosphorylation | Uniprot | |
Y921 | Phosphorylation | P29317 (EPHA2) | Uniprot |
T922 | Phosphorylation | Uniprot | |
Y930 | Phosphorylation | Uniprot | |
K935 | Ubiquitination | Uniprot | |
T940 | Phosphorylation | Uniprot | |
K945 | Ubiquitination | Uniprot | |
Y960 | Phosphorylation | P29317 (EPHA2) | Uniprot |
S961 | Phosphorylation | Uniprot |
Site | PTM Type | Enzyme | Source |
---|---|---|---|
S294 | Phosphorylation | Uniprot | |
T432 | Phosphorylation | Uniprot | |
T442 | Phosphorylation | Uniprot | |
T485 | Phosphorylation | Uniprot | |
S497 | Phosphorylation | Uniprot | |
S498 | Phosphorylation | Uniprot | |
Y561 | Phosphorylation | Uniprot | |
Y570 | Phosphorylation | Uniprot | |
T595 | Phosphorylation | Uniprot | |
Y596 | Phosphorylation | P29320 (EPHA3) | Uniprot |
T601 | Phosphorylation | Uniprot | |
Y602 | Phosphorylation | P29320 (EPHA3) | Uniprot |
K625 | Ubiquitination | Uniprot | |
T654 | Phosphorylation | Uniprot | |
K656 | Ubiquitination | Uniprot | |
Y659 | Phosphorylation | Uniprot | |
Y701 | Phosphorylation | P29320 (EPHA3) | Uniprot |
Y736 | Phosphorylation | Uniprot | |
Y742 | Phosphorylation | Uniprot | |
S768 | Phosphorylation | Uniprot | |
Y779 | Phosphorylation | P29320 (EPHA3) | Uniprot |
T781 | Phosphorylation | Uniprot | |
Y937 | Phosphorylation | Uniprot | |
T974 | Phosphorylation | Uniprot | |
S976 | Phosphorylation | Uniprot |
Site | PTM Type | Enzyme | Source |
---|---|---|---|
T117 | Phosphorylation | Uniprot | |
T168 | Phosphorylation | Uniprot | |
S349 | Phosphorylation | Uniprot | |
S350 | Phosphorylation | Uniprot | |
T354 | Phosphorylation | Uniprot | |
T595 | Phosphorylation | Uniprot | |
Y596 | Phosphorylation | P54764 (EPHA4) | Uniprot |
T601 | Phosphorylation | Uniprot | |
Y602 | Phosphorylation | P54764 (EPHA4) | Uniprot |
S637 | Phosphorylation | Uniprot | |
K693 | Acetylation | Uniprot | |
K735 | Ubiquitination | Uniprot | |
S741 | Phosphorylation | Uniprot | |
Y779 | Phosphorylation | Uniprot | |
T781 | Phosphorylation | Uniprot | |
Y798 | Phosphorylation | Uniprot | |
S887 | Phosphorylation | Uniprot | |
T957 | Phosphorylation | Uniprot |
翻译修饰 - P29317/P29320/P54764 作为激酶
Substrate | Site | Source |
---|---|---|
O14493 (CLDN4) | Y208 | Uniprot |
P29317-1 (EPHA2) | S570 | Uniprot |
P29317 (EPHA2) | Y575 | Uniprot |
P29317 (EPHA2) | Y588 | Uniprot |
P29317 (EPHA2) | Y594 | Uniprot |
P29317 (EPHA2) | Y628 | Uniprot |
P29317 (EPHA2) | Y694 | Uniprot |
P29317 (EPHA2) | Y735 | Uniprot |
P29317 (EPHA2) | Y772 | Uniprot |
P29317-1 (EPHA2) | S897 | Uniprot |
P29317-1 (EPHA2) | T898 | Uniprot |
P29317-1 (EPHA2) | S899 | Uniprot |
P29317-1 (EPHA2) | S901 | Uniprot |
P29317 (EPHA2) | Y921 | Uniprot |
P29317 (EPHA2) | Y960 | Uniprot |
研究背景
Receptor tyrosine kinase which binds promiscuously membrane-bound ephrin-A family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Activated by the ligand ephrin-A1/EFNA1 regulates migration, integrin-mediated adhesion, proliferation and differentiation of cells. Regulates cell adhesion and differentiation through DSG1/desmoglein-1 and inhibition of the ERK1/ERK2 (MAPK3/MAPK1, respectively) signaling pathway. May also participate in UV radiation-induced apoptosis and have a ligand-independent stimulatory effect on chemotactic cell migration. During development, may function in distinctive aspects of pattern formation and subsequently in development of several fetal tissues. Involved for instance in angiogenesis, in early hindbrain development and epithelial proliferation and branching morphogenesis during mammary gland development. Engaged by the ligand ephrin-A5/EFNA5 may regulate lens fiber cells shape and interactions and be important for lens transparency development and maintenance. With ephrin-A2/EFNA2 may play a role in bone remodeling through regulation of osteoclastogenesis and osteoblastogenesis.
(Microbial infection) Acts as a receptor for hepatitis C virus (HCV) in hepatocytes and facilitates its cell entry. Mediates HCV entry by promoting the formation of the CD81-CLDN1 receptor complexes that are essential for HCV entry and by enhancing membrane fusion of cells expressing HCV envelope glycoproteins.
Autophosphorylates. Phosphorylated on tyrosine upon binding and activation by EFNA1. Phosphorylated residues Tyr-588 and Tyr-594 are required for binding VAV2 and VAV3 while phosphorylated residues Tyr-735 and Tyr-930 are required for binding PI3-kinase p85 subunit (PIK3R1, PIK3R2 or PIK3R3). These phosphorylated residues are critical for recruitment of VAV2 and VAV3 and PI3-kinase p85 subunit which transduce downstream signaling to activate RAC1 GTPase and cell migration. Dephosphorylation of Tyr-930 by PTPRF prevents the interaction of EPHA2 with NCK1. Phosphorylated at Ser-897 by PKB; serum-induced phosphorylation which targets EPHA2 to the cell leading edge and stimulates cell migration. Phosphorylation by PKB is inhibited by EFNA1-activated EPHA2 which regulates PKB activity via a reciprocal regulatory loop. Phosphorylated at Ser-897 in response to TNF by RPS6KA1 and RPS6KA3; RPS6KA-EPHA2 signaling pathway controls cell migration. Phosphorylated at Ser-897 by PKA; blocks cell retraction induced by EPHA2 kinase activity. Dephosphorylated by ACP1.
Ubiquitinated by CHIP/STUB1. Ubiquitination is regulated by the HSP90 chaperone and regulates the receptor stability and activity through proteasomal degradation. ANKS1A prevents ubiquitination and degradation (By similarity).
Cell membrane>Single-pass type I membrane protein. Cell projection>Ruffle membrane>Single-pass type I membrane protein. Cell projection>Lamellipodium membrane>Single-pass type I membrane protein. Cell junction>Focal adhesion.
Note: Present at regions of cell-cell contacts but also at the leading edge of migrating cells (PubMed:19573808, PubMed:20861311). Relocates from the plasma membrane to the cytoplasmic and perinuclear regions in cancer cells (PubMed:18794797).
Expressed in brain and glioma tissue and glioma cell lines (at protein level). Expressed most highly in tissues that contain a high proportion of epithelial cells, e.g. skin, intestine, lung, and ovary.
Homodimer. Interacts with SLA. Interacts (phosphorylated form) with VAV2, VAV3 and PI3-kinase p85 subunit (PIK3R1, PIK3R2 or PIK3R3); critical for the EFNA1-induced activation of RAC1 which stimulates cell migration (By similarity). Interacts with INPPL1; regulates activated EPHA2 endocytosis and degradation. Interacts (inactivated form) with PTK2/FAK1 and interacts (EFNA1 ligand-activated form) with PTPN11; regulates integrin-mediated adhesion. Interacts with ARHGEF16, DOCK4 and ELMO2; mediates ligand-independent activation of RAC1 which stimulates cell migration. Interacts with CLDN4; phosphorylates CLDN4 and may regulate tight junctions. Interacts with ACP1. Interacts (via SAM domain) with ANKS1A (via SAM domain). Interacts with CEMIP. Interacts with NCK1; may regulate EPHA2 activity in cell migration and adhesion.
(Microbial infection) Interacts with human herpes virus 8/HHV-8 glycoprotein L/gL and glycoprotein H/gH heterodimer; this interaction triggers EPHA2 phosphorylation and endocytosis, allowing virus entry.
(Microbial infection) Interacts with Epstein-Barr virus/HHV-4 glycoprotein L/gL and glycoprotein H/gH heterodimer; this interaction facilitates virus internalization and fusion.
Belongs to the protein kinase superfamily. Tyr protein kinase family. Ephrin receptor subfamily.
Receptor tyrosine kinase which binds promiscuously membrane-bound ephrin family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Highly promiscuous for ephrin-A ligands it binds preferentially EFNA5. Upon activation by EFNA5 regulates cell-cell adhesion, cytoskeletal organization and cell migration. Plays a role in cardiac cells migration and differentiation and regulates the formation of the atrioventricular canal and septum during development probably through activation by EFNA1. Involved in the retinotectal mapping of neurons. May also control the segregation but not the guidance of motor and sensory axons during neuromuscular circuit development.
Autophosphorylates upon activation by EFNA5. Phosphorylation on Tyr-602 mediates interaction with NCK1. Dephosphorylated by PTPN1.
Cell membrane>Single-pass type I membrane protein.
Secreted.
Widely expressed. Highest level in placenta.
Heterotetramer upon binding of the ligand. The heterotetramer is composed of an ephrin dimer and a receptor dimer. Oligomerization is probably required to induce biological responses. Forms a ternary EFNA5-EPHA3-ADAM10 complex mediating EFNA5 extracellular domain shedding by ADAM10 which regulates the EFNA5-EPHA3 complex internalization and function. Interacts with NCK1 (via SH2 domain); mediates EFNA5-EPHA3 signaling (By similarity). Interacts (phosphorylated) with PTPN1; dephosphorylates EPHA3 and may regulate its trafficking and function. Interacts (phosphorylated) with CRK; mediates EFNA5-EPHA3 signaling through RHOA GTPase activation.
Belongs to the protein kinase superfamily. Tyr protein kinase family. Ephrin receptor subfamily.
Receptor tyrosine kinase which binds membrane-bound ephrin family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Highly promiscuous, it has the unique property among Eph receptors to bind and to be physiologically activated by both GPI-anchored ephrin-A and transmembrane ephrin-B ligands including EFNA1 and EFNB3. Upon activation by ephrin ligands, modulates cell morphology and integrin-dependent cell adhesion through regulation of the Rac, Rap and Rho GTPases activity. Plays an important role in the development of the nervous system controlling different steps of axonal guidance including the establishment of the corticospinal projections. May also control the segregation of motor and sensory axons during neuromuscular circuit development. In addition to its role in axonal guidance plays a role in synaptic plasticity. Activated by EFNA1 phosphorylates CDK5 at 'Tyr-15' which in turn phosphorylates NGEF regulating RHOA and dendritic spine morphogenesis. In the nervous system, plays also a role in repair after injury preventing axonal regeneration and in angiogenesis playing a role in central nervous system vascular formation. Additionally, its promiscuity makes it available to participate in a variety of cell-cell signaling regulating for instance the development of the thymic epithelium. During development of the cochlear organ of Corti, regulates pillar cell separation by forming a ternary complex with ADAM10 and CADH1 which facilitates the cleavage of CADH1 by ADAM10 and disruption of adherens junctions (By similarity).
Cell membrane>Single-pass type I membrane protein. Cell projection>Axon. Cell projection>Dendrite. Cell junction>Synapse>Postsynaptic density membrane. Early endosome. Cell junction>Adherens junction.
Note: Clustered upon activation and targeted to early endosome.
Ubiquitous.
Heterotetramer upon binding of the ligand. The heterotetramer is composed of an ephrin dimer and a receptor dimer. Oligomerization is probably required to induce biological responses. Interacts (phosphorylated at position Tyr-602) with FYN. Interacts with CDK5, CDK5R1 and NGEF; upon activation by EFNA1 induces NGEF phosphorylation by the kinase CDK5. Interacts with CHN1; effector of EPHA4 in axon guidance linking EPHA4 activation to RAC1 regulation (By similarity). Interacts (via PDZ motif) with SIPA1L1 (via PDZ domain); controls neuronal morphology through regulation of the RAP1 (RAP1A or RAP1B) and RAP2 (RAP2A, RAP2B or RAP2C) GTPases. Forms a ternary complex composed of ADAM10, CADH1 and EPHA4; within the complex, CADH1 is cleaved by ADAM10 which disrupts adherens junctions (By similarity).
The protein kinase domain mediates interaction with NGEF.
Belongs to the protein kinase superfamily. Tyr protein kinase family. Ephrin receptor subfamily.
研究领域
· Environmental Information Processing > Signal transduction > MAPK signaling pathway. (View pathway)
· Environmental Information Processing > Signal transduction > Ras signaling pathway. (View pathway)
· Environmental Information Processing > Signal transduction > Rap1 signaling pathway. (View pathway)
· Environmental Information Processing > Signal transduction > PI3K-Akt signaling pathway. (View pathway)
· Organismal Systems > Development > Axon guidance. (View pathway)
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