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Protein

Ephrin type-A receptor 2

Gene

Epha2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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.PROSITE-ProRule annotation1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei647ATPPROSITE-ProRule annotation1
Active sitei740Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi620 – 628ATPPROSITE-ProRule annotation9

GO - Molecular functioni

GO - Biological processi

  • activation of GTPase activity Source: UniProtKB
  • axial mesoderm formation Source: MGI
  • blood vessel development Source: MGI
  • blood vessel endothelial cell proliferation involved in sprouting angiogenesis Source: MGI
  • blood vessel morphogenesis Source: MGI
  • bone remodeling Source: UniProtKB
  • branching involved in mammary gland duct morphogenesis Source: UniProtKB
  • cAMP metabolic process Source: UniProtKB
  • cell chemotaxis Source: UniProtKB
  • cell migration Source: UniProtKB
  • cell motility Source: UniProtKB
  • defense response to Gram-positive bacterium Source: MGI
  • ephrin receptor signaling pathway Source: UniProtKB
  • inflammatory response Source: MGI
  • intrinsic apoptotic signaling pathway in response to DNA damage Source: MGI
  • keratinocyte differentiation Source: MGI
  • lens fiber cell morphogenesis Source: UniProtKB
  • mammary gland epithelial cell proliferation Source: UniProtKB
  • negative regulation of angiogenesis Source: MGI
  • negative regulation of chemokine production Source: MGI
  • negative regulation of cytokine production Source: MGI
  • negative regulation of lymphangiogenesis Source: MGI
  • negative regulation of protein kinase B signaling Source: UniProtKB
  • neural tube development Source: MGI
  • neuron differentiation Source: MGI
  • notochord cell development Source: MGI
  • notochord formation Source: MGI
  • notochord morphogenesis Source: MGI
  • osteoblast differentiation Source: UniProtKB
  • osteoclast differentiation Source: UniProtKB
  • pericyte cell differentiation Source: MGI
  • positive regulation of establishment of protein localization to plasma membrane Source: UniProtKB
  • post-anal tail morphogenesis Source: MGI
  • protein kinase B signaling Source: UniProtKB
  • regulation of angiogenesis Source: UniProtKB
  • regulation of blood vessel endothelial cell migration Source: UniProtKB
  • regulation of cell adhesion mediated by integrin Source: UniProtKB
  • regulation of ERK1 and ERK2 cascade Source: MGI
  • regulation of lamellipodium assembly Source: UniProtKB
  • response to growth factor Source: UniProtKB
  • skeletal system development Source: MGI
  • 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.
ReactomeiR-MMU-2682334. EPH-Ephrin signaling.
R-MMU-3928663. EPHA-mediated growth cone collapse.
R-MMU-3928665. EPH-ephrin mediated repulsion of cells.

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
Proteomesi
  • UP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:95278. Epha2.

Subcellular locationi

  • Cell membrane By similarity; Single-pass type I membrane protein Sequence analysis
  • Cell projectionruffle membrane By similarity; Single-pass type I membrane protein Sequence analysis
  • Cell projectionlamellipodium membrane By similarity; Single-pass type I membrane protein Sequence analysis
  • Cell junctionfocal adhesion By similarity

  • Note: Present at regions of cell-cell contacts but also at the leading edge of migrating cells. Relocates from the plasma membrane to the cytoplasmic and perinuclear regions in cancer cells.By similarity

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini26 – 538ExtracellularSequence analysisAdd BLAST513
Transmembranei539 – 559HelicalSequence analysisAdd BLAST21
Topological domaini560 – 977CytoplasmicSequence analysisAdd BLAST418

GO - Cellular componenti

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)DescriptionActionsGraphical viewLength
Mutagenesisi589Y → 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 Publications1
Mutagenesisi589Y → F: Inhibits EFNA1-induced vascular assembly and kinase activity. 2 Publications1
Mutagenesisi595Y → 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 Publications1
Mutagenesisi595Y → F: Inhibits EFNA1-induced vascular assembly and abolishes kinase activity. 2 Publications1
Mutagenesisi736Y → 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 Publication1
Mutagenesisi740D → N: Loss of kinase activity and binding to VAV3. 1 Publication1
Mutagenesisi773Y → F: No significant effect on kinase activity. Significant reduction in phosphorylation. 1 Publication1
Mutagenesisi931Y → 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 Publication1

Chemistry databases

GuidetoPHARMACOLOGYi1822.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 25Sequence analysisAdd BLAST25
ChainiPRO_000001680126 – 977Ephrin type-A receptor 2Add BLAST952

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi69 ↔ 187By similarity
Disulfide bondi104 ↔ 114By similarity
Glycosylationi408N-linked (GlcNAc...)2 Publications1
Glycosylationi436N-linked (GlcNAc...)2 Publications1
Modified residuei571PhosphoserineBy similarity1
Modified residuei580PhosphoserineBy similarity1
Modified residuei589Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei595Phosphotyrosine; by autocatalysisCombined sources1 Publication1
Modified residuei629PhosphotyrosineBy similarity1
Modified residuei648PhosphothreonineBy similarity1
Modified residuei736Phosphotyrosine; by autocatalysis1 Publication1
Modified residuei773Phosphotyrosine; by autocatalysisCombined sources1 Publication1
Modified residuei870PhosphoserineBy similarity1
Modified residuei893PhosphoserineBy similarity1
Modified residuei898PhosphoserineBy similarity1
Modified residuei902PhosphoserineBy similarity1
Modified residuei922Phosphotyrosine; by autocatalysisSequence analysis1
Modified residuei931PhosphotyrosineBy similarity1

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. Phosphorylated at Ser-898 in response to TNF by RPS6KA1 and RPS6KA3; RPS6KA-EPHA2 signaling pathway controls cell migration. Phosphorylated at Ser-898 by PKA; blocks cell retraction induced by EPHA2 kinase activity. Dephosphorylated by ACP1.By similarity1 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

EPDiQ03145.
MaxQBiQ03145.
PaxDbiQ03145.
PeptideAtlasiQ03145.
PRIDEiQ03145.

PTM databases

iPTMnetiQ03145.
PhosphoSitePlusiQ03145.

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

BgeeiENSMUSG00000006445.
CleanExiMM_EPHA2.
GenevisibleiQ03145. MM.

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

GO - Molecular functioni

Protein-protein interaction databases

BioGridi199469. 3 interactors.
DIPiDIP-829N.
IntActiQ03145. 4 interactors.
MINTiMINT-3388286.
STRINGi10090.ENSMUSP00000006614.

Structurei

3D structure databases

ProteinModelPortaliQ03145.
SMRiQ03145.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini27 – 205Eph LBDPROSITE-ProRule annotationAdd BLAST179
Domaini329 – 433Fibronectin type-III 1PROSITE-ProRule annotationAdd BLAST105
Domaini439 – 530Fibronectin type-III 2PROSITE-ProRule annotationAdd BLAST92
Domaini614 – 876Protein kinasePROSITE-ProRule annotationAdd BLAST263
Domaini905 – 969SAMPROSITE-ProRule annotationAdd BLAST65

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 205Mediates interaction with CLDN4By similarityAdd BLAST205
Regioni607 – 907Mediates interaction with ARHGEF16By similarityAdd BLAST301
Regioni887 – 977Negatively regulates interaction with ARHGEF16By similarityAdd BLAST91

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi975 – 977PDZ-bindingSequence analysis3

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi187 – 326Cys-richAdd BLAST140

Sequence similaritiesi

Belongs to the protein kinase superfamily. Tyr protein kinase family. Ephrin receptor subfamily.PROSITE-ProRule annotation
Contains 1 Eph LBD (Eph ligand-binding) domain.PROSITE-ProRule annotation
Contains 2 fibronectin type-III domains.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation
Contains 1 SAM (sterile alpha motif) domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0196. Eukaryota.
COG0515. LUCA.
GeneTreeiENSGT00760000118975.
HOGENOMiHOG000233856.
HOVERGENiHBG062180.
InParanoidiQ03145.
KOiK05103.
OMAiCSPGFFK.
OrthoDBiEOG091G00W0.
TreeFamiTF315608.

Family and domain databases

CDDicd00063. FN3. 2 hits.
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. FN3_dom.
IPR008979. Galactose-bd-like.
IPR009030. Growth_fac_rcpt_.
IPR013783. Ig-like_fold.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001660. SAM.
IPR013761. SAM/pointed.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR011641. Tyr-kin_ephrin_A/B_rcpt-like.
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.
SM01411. Ephrin_rec_like. 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

« Hide

        10         20         30         40         50
MELRAVGFCL ALLWGCALAA AAAQGKEVVL LDFAAMKGEL GWLTHPYGKG
60 70 80 90 100
WDLMQNIMDD MPIYMYSVCN VVSGDQDNWL RTNWVYREEA ERIFIELKFT
110 120 130 140 150
VRDCNSFPGG ASSCKETFNL YYAESDVDYG TNFQKRQFTK IDTIAPDEIT
160 170 180 190 200
VSSDFEARNV KLNVEERMVG PLTRKGFYLA FQDIGACVAL LSVRVYYKKC
210 220 230 240 250
PEMLQSLARF PETIAVAVSD TQPLATVAGT CVDHAVVPYG GEGPLMHCTV
260 270 280 290 300
DGEWLVPIGQ CLCQEGYEKV EDACRACSPG FFKSEASESP CLECPEHTLP
310 320 330 340 350
STEGATSCQC EEGYFRAPED PLSMSCTRPP SAPNYLTAIG MGAKVELRWT
360 370 380 390 400
APKDTGGRQD IVYSVTCEQC WPESGECGPC EASVRYSEPP HALTRTSVTV
410 420 430 440 450
SDLEPHMNYT FAVEARNGVS GLVTSRSFRT ASVSINQTEP PKVRLEDRST
460 470 480 490 500
TSLSVTWSIP VSQQSRVWKY EVTYRKKGDA NSYNVRRTEG FSVTLDDLAP
510 520 530 540 550
DTTYLVQVQA LTQEGQGAGS KVHEFQTLST EGSANMAVIG GVAVGVVLLL
560 570 580 590 600
VLAGVGLFIH RRRRNLRARQ SSEDVRFSKS EQLKPLKTYV DPHTYEDPNQ
610 620 630 640 650
AVLKFTTEIH PSCVARQKVI GAGEFGEVYK GTLKASSGKK EIPVAIKTLK
660 670 680 690 700
AGYTEKQRVD FLSEASIMGQ FSHHNIIRLE GVVSKYKPMM IITEYMENGA
710 720 730 740 750
LDKFLREKDG EFSVLQLVGM LRGIASGMKY LANMNYVHRD LAARNILVNS
760 770 780 790 800
NLVCKVSDFG LSRVLEDDPE ATYTTSGGKI PIRWTAPEAI SYRKFTSASD
810 820 830 840 850
VWSYGIVMWE VMTYGERPYW ELSNHEVMKA INDGFRLPTP MDCPSAIYQL
860 870 880 890 900
MMQCWQQERS RRPKFADIVS ILDKLIRAPD SLKTLADFDP RVSIRLPSTS
910 920 930 940 950
GSEGVPFRTV SEWLESIKMQ QYTEHFMVAG YTAIEKVVQM SNEDIKRIGV
960 970
RLPGHQKRIA YSLLGLKDQV NTVGIPI
Length:977
Mass (Da):108,852
Last modified:July 27, 2011 - v3
Checksum:i66338CE7EF2DEE02
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti5A → T in CAA55135 (PubMed:8183555).Curated1
Sequence conflicti112 – 113SS → HA in AAA82113 (PubMed:7918100).Curated2
Sequence conflicti189A → R in AAA82113 (PubMed:7918100).Curated1
Sequence conflicti209R → C in AAA82113 (PubMed:7918100).Curated1
Sequence conflicti244P → A in AAA82113 (PubMed:7918100).Curated1
Sequence conflicti258 – 260IGQ → SE in AAA82113 (PubMed:7918100).Curated3
Sequence conflicti291C → S in AAA82113 (PubMed:7918100).Curated1
Sequence conflicti339 – 340IG → C in AAA82113 (PubMed:7918100).Curated2
Sequence conflicti371 – 372WP → CA in AAA82113 (PubMed:7918100).Curated2
Sequence conflicti383S → T in AAA82113 (PubMed:7918100).Curated1
Sequence conflicti457W → R in AAA82113 (PubMed:7918100).Curated1
Sequence conflicti485V → G in AAA82113 (PubMed:7918100).Curated1
Sequence conflicti511L → W in AAA82113 (PubMed:7918100).Curated1
Sequence conflicti534A → R in AAA82113 (PubMed:7918100).Curated1
Sequence conflicti678R → P in CAA55135 (PubMed:8183555).Curated1
Sequence conflicti681G → A in AAA82113 (PubMed:7918100).Curated1
Sequence conflicti819 – 820YW → LL in AAA82113 (PubMed:7918100).Curated2
Sequence conflicti878A → R in AAA82113 (PubMed:7918100).Curated1
Sequence conflicti919 – 920MQ → IE in AAA82113 (PubMed:7918100).Curated2

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ProteinModelPortaliQ03145.
SMRiQ03145.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi199469. 3 interactors.
DIPiDIP-829N.
IntActiQ03145. 4 interactors.
MINTiMINT-3388286.
STRINGi10090.ENSMUSP00000006614.

Chemistry databases

GuidetoPHARMACOLOGYi1822.

PTM databases

iPTMnetiQ03145.
PhosphoSitePlusiQ03145.

Proteomic databases

EPDiQ03145.
MaxQBiQ03145.
PaxDbiQ03145.
PeptideAtlasiQ03145.
PRIDEiQ03145.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi1969.
MGIiMGI:95278. Epha2.

Phylogenomic databases

eggNOGiKOG0196. Eukaryota.
COG0515. LUCA.
GeneTreeiENSGT00760000118975.
HOGENOMiHOG000233856.
HOVERGENiHBG062180.
InParanoidiQ03145.
KOiK05103.
OMAiCSPGFFK.
OrthoDBiEOG091G00W0.
TreeFamiTF315608.

Enzyme and pathway databases

BRENDAi2.7.10.1. 3474.
ReactomeiR-MMU-2682334. EPH-Ephrin signaling.
R-MMU-3928663. EPHA-mediated growth cone collapse.
R-MMU-3928665. EPH-ephrin mediated repulsion of cells.

Miscellaneous databases

PROiQ03145.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000006445.
CleanExiMM_EPHA2.
GenevisibleiQ03145. MM.

Family and domain databases

CDDicd00063. FN3. 2 hits.
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. FN3_dom.
IPR008979. Galactose-bd-like.
IPR009030. Growth_fac_rcpt_.
IPR013783. Ig-like_fold.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001660. SAM.
IPR013761. SAM/pointed.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR011641. Tyr-kin_ephrin_A/B_rcpt-like.
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.
SM01411. Ephrin_rec_like. 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]
ProtoNetiSearch...

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: November 30, 2016
This is version 176 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.