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Q03145

- EPHA2_MOUSE

UniProt

Q03145 - EPHA2_MOUSE

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Protein

Ephrin type-A receptor 2

Gene
Epha2, Eck, Myk2, Sek2
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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 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.7 Publications

Catalytic activityi

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei647 – 6471ATP By similarity
Active sitei740 – 7401Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi620 – 6289ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. ephrin receptor activity Source: InterPro
  3. protein binding Source: UniProtKB
  4. transmembrane receptor protein tyrosine kinase activity Source: UniProtKB

GO - Biological processi

  1. activation of Rac GTPase activity Source: UniProtKB
  2. angiogenesis Source: UniProtKB-KW
  3. axial mesoderm formation Source: MGI
  4. blood vessel development Source: MGI
  5. bone remodeling Source: UniProtKB
  6. branching involved in mammary gland duct morphogenesis Source: UniProtKB
  7. cell adhesion Source: UniProtKB-KW
  8. cell chemotaxis Source: UniProtKB
  9. cell migration Source: UniProtKB
  10. ephrin receptor signaling pathway Source: UniProtKB
  11. intrinsic apoptotic signaling pathway in response to DNA damage Source: Ensembl
  12. keratinocyte differentiation Source: Ensembl
  13. lens fiber cell morphogenesis Source: UniProtKB
  14. mammary gland epithelial cell proliferation Source: UniProtKB
  15. negative regulation of protein kinase B signaling Source: UniProtKB
  16. neural tube development Source: MGI
  17. neuron differentiation Source: MGI
  18. notochord cell development Source: MGI
  19. notochord formation Source: MGI
  20. notochord morphogenesis Source: MGI
  21. osteoblast differentiation Source: UniProtKB
  22. osteoclast differentiation Source: UniProtKB
  23. peptidyl-tyrosine phosphorylation Source: GOC
  24. positive regulation of establishment of protein localization to plasma membrane Source: UniProtKB
  25. post-anal tail morphogenesis Source: MGI
  26. protein kinase B signaling Source: UniProtKB
  27. regulation of angiogenesis Source: UniProtKB
  28. regulation of blood vessel endothelial cell migration Source: UniProtKB
  29. regulation of cell adhesion mediated by integrin Source: UniProtKB
  30. regulation of ERK1 and ERK2 cascade Source: Ensembl
  31. regulation of lamellipodium assembly Source: UniProtKB
  32. response to growth factor Source: UniProtKB
  33. skeletal system development Source: MGI
  34. vasculogenesis Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Receptor, Transferase, Tyrosine-protein kinase

Keywords - Biological processi

Angiogenesis, Apoptosis, Cell adhesion, Differentiation

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.10.1. 3474.

Names & Taxonomyi

Protein namesi
Recommended name:
Ephrin type-A receptor 2 (EC:2.7.10.1)
Alternative name(s):
Epithelial cell kinase
Tyrosine-protein kinase receptor ECK
Tyrosine-protein kinase receptor MPK-5
Tyrosine-protein kinase receptor SEK-2
Gene namesi
Name:Epha2
Synonyms:Eck, Myk2, Sek2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 4

Organism-specific databases

MGIiMGI:95278. Epha2.

Subcellular locationi

Cell membrane; Single-pass type I membrane protein By similarity. Cell projectionruffle membrane; Single-pass type I membrane protein By similarity. Cell projectionlamellipodium membrane; Single-pass type I membrane protein By similarity. Cell junctionfocal adhesion By similarity
Note: Present at regions of cell-cell contacts but also at the leading edge of migrating cells By similarity.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini26 – 538513Extracellular Reviewed predictionAdd
BLAST
Transmembranei539 – 55921Helical; Reviewed predictionAdd
BLAST
Topological domaini560 – 977418Cytoplasmic Reviewed predictionAdd
BLAST

GO - Cellular componenti

  1. focal adhesion Source: UniProtKB
  2. integral component of plasma membrane Source: UniProtKB
  3. lamellipodium membrane Source: UniProtKB-SubCell
  4. leading edge membrane Source: UniProtKB
  5. ruffle membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Membrane

Pathology & Biotechi

Disruption phenotypei

Mice are viable, fertile but exhibit aberrant development of tail vertebra and susceptibility to carcinogenesis.3 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi589 – 5891Y → E: No significant effect on kinase activity and loss of binding to VAV2 and VAV3. Inhibits EFNA1-induced vascular assembly and RAC1 activation in endothelial cells, no significant effect on kinase activity, significant reduction in phosphorylation and binding to VAV3; when associated with E-595. 2 Publications
Mutagenesisi589 – 5891Y → F: Inhibits EFNA1-induced vascular assembly and kinase activity. 2 Publications
Mutagenesisi595 – 5951Y → E: No significant effect on kinase activity and loss of binding to VAV2 and VAV3. Inhibits EFNA1-induced vascular assembly and RAC1 activation in endothelial cells, no significant effect on kinase activity, significant reduction in phosphorylation and binding to VAV3; when associated with E-589. 2 Publications
Mutagenesisi595 – 5951Y → F: Inhibits EFNA1-induced vascular assembly and abolishes kinase activity. 2 Publications
Mutagenesisi736 – 7361Y → F: Inhibits EFNA1-induced vascular assembly and RAC1 activation in endothelial cells. No significant effect on kinase activity. Loss of binding to PI3-kinase p85 subunit. 1 Publication
Mutagenesisi740 – 7401D → N: Loss of kinase activity and binding to VAV3. 1 Publication
Mutagenesisi773 – 7731Y → F: No significant effect on kinase activity. Significant reduction in phosphorylation. 1 Publication
Mutagenesisi931 – 9311Y → F: Inhibits EFNA1-induced vascular assembly and RAC1 activation in endothelial cells. Inhibits kinase activity. Loss of binding to VAV3 and PI3-kinase p85 subunit. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2525 Reviewed predictionAdd
BLAST
Chaini26 – 977952Ephrin type-A receptor 2PRO_0000016801Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi69 ↔ 187 By similarity
Disulfide bondi104 ↔ 114 By similarity
Modified residuei152 – 1521Phosphoserine By similarity
Modified residuei374 – 3741Phosphoserine By similarity
Glycosylationi408 – 4081N-linked (GlcNAc...)2 Publications
Glycosylationi436 – 4361N-linked (GlcNAc...)2 Publications
Modified residuei571 – 5711Phosphoserine By similarity
Modified residuei580 – 5801Phosphoserine By similarity
Modified residuei588 – 5881Phosphothreonine By similarity
Modified residuei589 – 5891Phosphotyrosine; by autocatalysis By similarity
Modified residuei594 – 5941Phosphothreonine By similarity
Modified residuei595 – 5951Phosphotyrosine; by autocatalysis2 Publications
Modified residuei629 – 6291Phosphotyrosine By similarity
Modified residuei648 – 6481Phosphothreonine By similarity
Modified residuei736 – 7361Phosphotyrosine; by autocatalysis1 Publication
Modified residuei772 – 7721Phosphothreonine By similarity
Modified residuei773 – 7731Phosphotyrosine; by autocatalysis2 Publications
Modified residuei791 – 7911Phosphoserine By similarity
Modified residuei792 – 7921Phosphotyrosine By similarity
Modified residuei870 – 8701Phosphoserine By similarity
Modified residuei881 – 8811Phosphoserine By similarity
Modified residuei893 – 8931Phosphoserine By similarity
Modified residuei898 – 8981Phosphoserine By similarity
Modified residuei899 – 8991Phosphothreonine By similarity
Modified residuei900 – 9001Phosphoserine By similarity
Modified residuei902 – 9021Phosphoserine By similarity
Modified residuei911 – 9111Phosphoserine By similarity
Modified residuei922 – 9221Phosphotyrosine; by autocatalysis Reviewed prediction
Modified residuei931 – 9311Phosphotyrosine By similarity
Modified residuei961 – 9611Phosphotyrosine By similarity

Post-translational modificationi

Autophosphorylates. Phosphorylated at Ser-898 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 on tyrosine upon binding and activation by EFNA1. Phosphorylated residues Tyr-589 and Tyr-595 are required for binding VAV2 and VAV3 while phosphorylated residues Tyr-736 and Tyr-931 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-931 by PTPRF prevents the interaction of EPHA2 with NCK1. Dephosphorylated by ACP1.1 Publication
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.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ03145.
PRIDEiQ03145.

PTM databases

PhosphoSiteiQ03145.

Expressioni

Tissue specificityi

Expressed in the lung, intestine and liver.1 Publication

Developmental stagei

First detected in gastrulation stage embryos (6.5-7.5 dpc) in ectodermal cells adjacent to the distal region of the primitive streak. By the neural plate stage (approximately 7.5 dpc), EPHA2 expression becomes restricted to the extreme distal end or node of the primitive streak. After the beginning of somitogenesis (approximately 8.0 dpc), expression persists in the node as this structure regresses toward the caudal end of the embryo. In addition, beginning at the mid head fold stage (approximately 7.75 dpc), we observe that EPHA2 exhibits a dynamic and spatially restricted expression pattern in the prospective hindbrain region. EPHA2 transcripts are initially detected in a 5-cell wide strip of mesodermal cells underlying prospective rhombomere 4 (R4). Subsequently at the beginning of somitogenesis, expression is observed in prospective R4. At the 4-8-somite stage, EPHA2 transcripts are observed in R4, mesenchymal cells underlying R4, and surface ectoderm in the vicinity of the developing second branchial arch. By the 10-somite stage, expression in these cells is down-regulated. Additionally, at the 5-8-somite stage, EPHA2 transcripts are detected initially in the lateral mesenchyme immediately underlying the surface ectoderm adjacent to R5 and R6, and subsequently in surface ectoderm overlying the developing third branchial arch.4 Publications

Gene expression databases

BgeeiQ03145.
CleanExiMM_EPHA2.
GenevestigatoriQ03145.

Interactioni

Subunit structurei

Homodimer. 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 with CEMIP. Interacts with NCK1; may regulate EPHA2 activity in cell migration and adhesion. 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. Interacts with ANKS1A.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Epha4Q031373EBI-529701,EBI-1539152

Protein-protein interaction databases

BioGridi199469. 2 interactions.
DIPiDIP-829N.
IntActiQ03145. 4 interactions.
MINTiMINT-3388286.

Structurei

3D structure databases

ProteinModelPortaliQ03145.
SMRiQ03145. Positions 24-529, 603-971.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini27 – 205179Eph LBDAdd
BLAST
Domaini329 – 433105Fibronectin type-III 1Add
BLAST
Domaini439 – 53092Fibronectin type-III 2Add
BLAST
Domaini614 – 876263Protein kinaseAdd
BLAST
Domaini905 – 96965SAMAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 205205Mediates interaction with CLDN4 By similarityAdd
BLAST
Regioni607 – 907301Mediates interaction with ARHGEF16 By similarityAdd
BLAST
Regioni887 – 97791Negatively regulates interaction with ARHGEF16 By similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi975 – 9773PDZ-binding Reviewed prediction

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi187 – 326140Cys-richAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00740000115081.
HOGENOMiHOG000233856.
HOVERGENiHBG062180.
InParanoidiQ3UNI2.
KOiK05103.
OMAiLVPIGQC.
OrthoDBiEOG7VTDM6.
TreeFamiTF315608.

Family and domain databases

Gene3Di1.10.150.50. 1 hit.
2.60.120.260. 1 hit.
2.60.40.10. 2 hits.
InterProiIPR027936. Eph_TM.
IPR001090. Ephrin_rcpt_lig-bd_dom.
IPR003961. Fibronectin_type3.
IPR008979. Galactose-bd-like.
IPR009030. Growth_fac_rcpt_N_dom.
IPR013783. Ig-like_fold.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001660. SAM.
IPR013761. SAM/pointed.
IPR021129. SAM_type1.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
IPR016257. Tyr_kinase_ephrin_rcpt.
IPR001426. Tyr_kinase_rcpt_V_CS.
[Graphical view]
PfamiPF14575. EphA2_TM. 1 hit.
PF01404. Ephrin_lbd. 1 hit.
PF00041. fn3. 2 hits.
PF07714. Pkinase_Tyr. 1 hit.
PF00536. SAM_1. 1 hit.
[Graphical view]
PIRSFiPIRSF000666. TyrPK_ephrin_receptor. 1 hit.
PRINTSiPR00109. TYRKINASE.
SMARTiSM00615. EPH_lbd. 1 hit.
SM00060. FN3. 2 hits.
SM00454. SAM. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF47769. SSF47769. 1 hit.
SSF49265. SSF49265. 1 hit.
SSF49785. SSF49785. 1 hit.
SSF56112. SSF56112. 1 hit.
SSF57184. SSF57184. 2 hits.
PROSITEiPS01186. EGF_2. 1 hit.
PS51550. EPH_LBD. 1 hit.
PS50853. FN3. 2 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS00790. RECEPTOR_TYR_KIN_V_1. 1 hit.
PS00791. RECEPTOR_TYR_KIN_V_2. 1 hit.
PS50105. SAM_DOMAIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q03145-1 [UniParc]FASTAAdd to Basket

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MELRAVGFCL ALLWGCALAA AAAQGKEVVL LDFAAMKGEL GWLTHPYGKG    50
WDLMQNIMDD MPIYMYSVCN VVSGDQDNWL RTNWVYREEA ERIFIELKFT 100
VRDCNSFPGG ASSCKETFNL YYAESDVDYG TNFQKRQFTK IDTIAPDEIT 150
VSSDFEARNV KLNVEERMVG PLTRKGFYLA FQDIGACVAL LSVRVYYKKC 200
PEMLQSLARF PETIAVAVSD TQPLATVAGT CVDHAVVPYG GEGPLMHCTV 250
DGEWLVPIGQ CLCQEGYEKV EDACRACSPG FFKSEASESP CLECPEHTLP 300
STEGATSCQC EEGYFRAPED PLSMSCTRPP SAPNYLTAIG MGAKVELRWT 350
APKDTGGRQD IVYSVTCEQC WPESGECGPC EASVRYSEPP HALTRTSVTV 400
SDLEPHMNYT FAVEARNGVS GLVTSRSFRT ASVSINQTEP PKVRLEDRST 450
TSLSVTWSIP VSQQSRVWKY EVTYRKKGDA NSYNVRRTEG FSVTLDDLAP 500
DTTYLVQVQA LTQEGQGAGS KVHEFQTLST EGSANMAVIG GVAVGVVLLL 550
VLAGVGLFIH RRRRNLRARQ SSEDVRFSKS EQLKPLKTYV DPHTYEDPNQ 600
AVLKFTTEIH PSCVARQKVI GAGEFGEVYK GTLKASSGKK EIPVAIKTLK 650
AGYTEKQRVD FLSEASIMGQ FSHHNIIRLE GVVSKYKPMM IITEYMENGA 700
LDKFLREKDG EFSVLQLVGM LRGIASGMKY LANMNYVHRD LAARNILVNS 750
NLVCKVSDFG LSRVLEDDPE ATYTTSGGKI PIRWTAPEAI SYRKFTSASD 800
VWSYGIVMWE VMTYGERPYW ELSNHEVMKA INDGFRLPTP MDCPSAIYQL 850
MMQCWQQERS RRPKFADIVS ILDKLIRAPD SLKTLADFDP RVSIRLPSTS 900
GSEGVPFRTV SEWLESIKMQ QYTEHFMVAG YTAIEKVVQM SNEDIKRIGV 950
RLPGHQKRIA YSLLGLKDQV NTVGIPI 977
Length:977
Mass (Da):108,852
Last modified:July 27, 2011 - v3
Checksum:i66338CE7EF2DEE02
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti5 – 51A → T in CAA55135. 1 Publication
Sequence conflicti112 – 1132SS → HA in AAA82113. 1 Publication
Sequence conflicti189 – 1891A → R in AAA82113. 1 Publication
Sequence conflicti209 – 2091R → C in AAA82113. 1 Publication
Sequence conflicti244 – 2441P → A in AAA82113. 1 Publication
Sequence conflicti258 – 2603IGQ → SE in AAA82113. 1 Publication
Sequence conflicti291 – 2911C → S in AAA82113. 1 Publication
Sequence conflicti339 – 3402IG → C in AAA82113. 1 Publication
Sequence conflicti371 – 3722WP → CA in AAA82113. 1 Publication
Sequence conflicti383 – 3831S → T in AAA82113. 1 Publication
Sequence conflicti457 – 4571W → R in AAA82113. 1 Publication
Sequence conflicti485 – 4851V → G in AAA82113. 1 Publication
Sequence conflicti511 – 5111L → W in AAA82113. 1 Publication
Sequence conflicti534 – 5341A → R in AAA82113. 1 Publication
Sequence conflicti678 – 6781R → P in CAA55135. 1 Publication
Sequence conflicti681 – 6811G → A in AAA82113. 1 Publication
Sequence conflicti819 – 8202YW → LL in AAA82113. 1 Publication
Sequence conflicti878 – 8781A → R in AAA82113. 1 Publication
Sequence conflicti919 – 9202MQ → IE in AAA82113. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X78339 mRNA. Translation: CAA55135.1.
U07634 mRNA. Translation: AAA82113.1.
AK137704 mRNA. Translation: BAE23470.1.
AK144202 mRNA. Translation: BAE25765.1.
AL607087, AL670285 Genomic DNA. Translation: CAM17000.1.
AL670285, AL607087 Genomic DNA. Translation: CAM20402.1.
CH466615 Genomic DNA. Translation: EDL13361.1.
BC140960 mRNA. Translation: AAI40961.1.
X76010 mRNA. Translation: CAA53597.1.
X57243 mRNA. Translation: CAA40519.1.
CCDSiCCDS18869.1.
PIRiI48759.
I48974.
S49004.
RefSeqiNP_034269.2. NM_010139.3.
UniGeneiMm.2581.

Genome annotation databases

EnsembliENSMUST00000006614; ENSMUSP00000006614; ENSMUSG00000006445.
GeneIDi13836.
KEGGimmu:13836.
UCSCiuc008voc.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X78339 mRNA. Translation: CAA55135.1 .
U07634 mRNA. Translation: AAA82113.1 .
AK137704 mRNA. Translation: BAE23470.1 .
AK144202 mRNA. Translation: BAE25765.1 .
AL607087 , AL670285 Genomic DNA. Translation: CAM17000.1 .
AL670285 , AL607087 Genomic DNA. Translation: CAM20402.1 .
CH466615 Genomic DNA. Translation: EDL13361.1 .
BC140960 mRNA. Translation: AAI40961.1 .
X76010 mRNA. Translation: CAA53597.1 .
X57243 mRNA. Translation: CAA40519.1 .
CCDSi CCDS18869.1.
PIRi I48759.
I48974.
S49004.
RefSeqi NP_034269.2. NM_010139.3.
UniGenei Mm.2581.

3D structure databases

ProteinModelPortali Q03145.
SMRi Q03145. Positions 24-529, 603-971.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 199469. 2 interactions.
DIPi DIP-829N.
IntActi Q03145. 4 interactions.
MINTi MINT-3388286.

PTM databases

PhosphoSitei Q03145.

Proteomic databases

PaxDbi Q03145.
PRIDEi Q03145.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000006614 ; ENSMUSP00000006614 ; ENSMUSG00000006445 .
GeneIDi 13836.
KEGGi mmu:13836.
UCSCi uc008voc.2. mouse.

Organism-specific databases

CTDi 1969.
MGIi MGI:95278. Epha2.

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00740000115081.
HOGENOMi HOG000233856.
HOVERGENi HBG062180.
InParanoidi Q3UNI2.
KOi K05103.
OMAi LVPIGQC.
OrthoDBi EOG7VTDM6.
TreeFami TF315608.

Enzyme and pathway databases

BRENDAi 2.7.10.1. 3474.

Miscellaneous databases

NextBioi 284656.
PROi Q03145.
SOURCEi Search...

Gene expression databases

Bgeei Q03145.
CleanExi MM_EPHA2.
Genevestigatori Q03145.

Family and domain databases

Gene3Di 1.10.150.50. 1 hit.
2.60.120.260. 1 hit.
2.60.40.10. 2 hits.
InterProi IPR027936. Eph_TM.
IPR001090. Ephrin_rcpt_lig-bd_dom.
IPR003961. Fibronectin_type3.
IPR008979. Galactose-bd-like.
IPR009030. Growth_fac_rcpt_N_dom.
IPR013783. Ig-like_fold.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001660. SAM.
IPR013761. SAM/pointed.
IPR021129. SAM_type1.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
IPR016257. Tyr_kinase_ephrin_rcpt.
IPR001426. Tyr_kinase_rcpt_V_CS.
[Graphical view ]
Pfami PF14575. EphA2_TM. 1 hit.
PF01404. Ephrin_lbd. 1 hit.
PF00041. fn3. 2 hits.
PF07714. Pkinase_Tyr. 1 hit.
PF00536. SAM_1. 1 hit.
[Graphical view ]
PIRSFi PIRSF000666. TyrPK_ephrin_receptor. 1 hit.
PRINTSi PR00109. TYRKINASE.
SMARTi SM00615. EPH_lbd. 1 hit.
SM00060. FN3. 2 hits.
SM00454. SAM. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view ]
SUPFAMi SSF47769. SSF47769. 1 hit.
SSF49265. SSF49265. 1 hit.
SSF49785. SSF49785. 1 hit.
SSF56112. SSF56112. 1 hit.
SSF57184. SSF57184. 2 hits.
PROSITEi PS01186. EGF_2. 1 hit.
PS51550. EPH_LBD. 1 hit.
PS50853. FN3. 2 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS00790. RECEPTOR_TYR_KIN_V_1. 1 hit.
PS00791. RECEPTOR_TYR_KIN_V_2. 1 hit.
PS50105. SAM_DOMAIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The Eck receptor tyrosine kinase is implicated in pattern formation during gastrulation, hindbrain segmentation and limb development."
    Ganju P., Shigemoto K., Brennan J., Entwistle A., Reith A.D.
    Oncogene 9:1613-1624(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], GLYCOSYLATION, CATALYTIC ACTIVITY, DEVELOPMENTAL STAGE.
  2. "The expression of the receptor-protein tyrosine kinase gene, eck, is highly restricted during early mouse development."
    Ruiz J.C., Robertson E.J.
    Mech. Dev. 46:87-100(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Bone marrow and Vagina.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  5. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  7. "Several receptor tyrosine kinase genes of the Eph family are segmentally expressed in the developing hindbrain."
    Becker N., Seitanidou T., Murphy P., Mattei M.-G., Topilko P., Nieto A., Wilkinson D.G., Charnay P., Gilardi P.
    Mech. Dev. 47:3-17(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 552-977, DEVELOPMENTAL STAGE.
    Strain: C57BL/6.
    Tissue: Embryo.
  8. "An Eph-related receptor protein tyrosine kinase gene segmentally expressed in the developing mouse hindbrain."
    Gilardi-Hebenstreit P., Nieto M.A., Frain M., Mattei M.-G., Chestier A., Wilkinson D.G., Charnay P.
    Oncogene 7:2499-2506(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 742-799.
    Tissue: Embryonic brain.
  9. "Characterization of a novel Src-like adapter protein that associates with the Eck receptor tyrosine kinase."
    Pandey A., Duan H., Dixit V.M.
    J. Biol. Chem. 270:19201-19204(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SLA.
    Tissue: Embryonic brain.
  10. "Involvement of EphA2 in the formation of the tail notochord via interaction with ephrinA1."
    Naruse-Nakajima C., Asano M., Iwakura Y.
    Mech. Dev. 102:95-105(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY.
  11. "EphA2 receptor tyrosine kinase regulates endothelial cell migration and vascular assembly through phosphoinositide 3-kinase-mediated Rac1 GTPase activation."
    Brantley-Sieders D.M., Caughron J., Hicks D., Pozzi A., Ruiz J.C., Chen J.
    J. Cell Sci. 117:2037-2049(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN ANGIOGENESIS, DISRUPTION PHENOTYPE.
  12. "Disruption of EphA2 receptor tyrosine kinase leads to increased susceptibility to carcinogenesis in mouse skin."
    Guo H., Miao H., Gerber L., Singh J., Denning M.F., Gilliam A.C., Wang B.
    Cancer Res. 66:7050-7058(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CELL PROLIFERATION, DISRUPTION PHENOTYPE.
  13. "Essential role of Vav family guanine nucleotide exchange factors in EphA receptor-mediated angiogenesis."
    Hunter S.G., Zhuang G., Brantley-Sieders D.M., Swat W., Cowan C.W., Chen J.
    Mol. Cell. Biol. 26:4830-4842(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN ANGIOGENESIS, INTERACTION WITH VAV2 AND VAV3, MUTAGENESIS OF TYR-589; TYR-595 AND ASP-740.
  14. "Identification and functional analysis of phosphorylated tyrosine residues within EphA2 receptor tyrosine kinase."
    Fang W.B., Brantley-Sieders D.M., Hwang Y., Ham A.-J.L., Chen J.
    J. Biol. Chem. 283:16017-16026(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, INTERACTION WITH VAV2; VAV3 AND PI3-KINASE P85 SUBUNIT, PHOSPHORYLATION AT TYR-589; TYR-595; TYR-736 AND TYR-773, MUTAGENESIS OF TYR-589; TYR-595; TYR-736; TYR-773 AND TYR-931.
  15. "Loss of ephrin-A5 function disrupts lens fiber cell packing and leads to cataract."
    Cooper M.A., Son A.I., Komlos D., Sun Y., Kleiman N.J., Zhou R.
    Proc. Natl. Acad. Sci. U.S.A. 105:16620-16625(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN LENS FIBER CELLS MORPHOGENESIS.
  16. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
    Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
    Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-595 AND TYR-773, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  17. "Bidirectional signaling through ephrinA2-EphA2 enhances osteoclastogenesis and suppresses osteoblastogenesis."
    Irie N., Takada Y., Watanabe Y., Matsuzaki Y., Naruse C., Asano M., Iwakura Y., Suda T., Matsuo K.
    J. Biol. Chem. 284:14637-14644(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN BONE IN REMODELING.
  18. "Regulation of mammary gland branching morphogenesis by EphA2 receptor tyrosine kinase."
    Vaught D., Chen J., Brantley-Sieders D.M.
    Mol. Biol. Cell 20:2572-2581(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN MAMMARY GLAND DEVELOPMENT.
  19. "The mouse C2C12 myoblast cell surface N-linked glycoproteome: identification, glycosite occupancy, and membrane orientation."
    Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B.
    Mol. Cell. Proteomics 8:2555-2569(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-408 AND ASN-436.
    Tissue: Myoblast.
  20. "Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
    Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
    Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-408 AND ASN-436.
  21. "The SAM domains of Anks family proteins are critically involved in modulating the degradation of EphA receptors."
    Kim J., Lee H., Kim Y., Yoo S., Park E., Park S.
    Mol. Cell. Biol. 30:1582-1592(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION, INTERACTION WITH ANKS1A.

Entry informationi

Entry nameiEPHA2_MOUSE
AccessioniPrimary (citable) accession number: Q03145
Secondary accession number(s): Q3UNI2, Q60633, Q62212
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: July 27, 2011
Last modified: September 3, 2014
This is version 154 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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