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Q03145

- EPHA2_MOUSE

UniProt

Q03145 - EPHA2_MOUSE

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Protein

Ephrin type-A receptor 2

Gene

Epha2

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 PublicationPROSITE-ProRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei647 – 6471ATPPROSITE-ProRule annotation
Active sitei740 – 7401Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi620 – 6289ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. ephrin receptor activity Source: InterPro
  3. 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.
ReactomeiREACT_243590. EPH-ephrin mediated repulsion of cells.
REACT_243939. EPHA-mediated growth cone collapse.
REACT_258158. EPH-Ephrin signaling.

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 By similarity; Single-pass type I membrane protein By similarity. Cell projectionruffle membrane By similarity; Single-pass type I membrane protein By similarity. Cell projectionlamellipodium membrane By similarity; 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 – 538513ExtracellularSequence AnalysisAdd
BLAST
Transmembranei539 – 55921HelicalSequence AnalysisAdd
BLAST
Topological domaini560 – 977418CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. cell projection Source: UniProtKB-KW
  2. focal adhesion Source: UniProtKB
  3. integral component of plasma membrane Source: UniProtKB
  4. leading edge membrane Source: UniProtKB
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 – 2525Sequence AnalysisAdd
BLAST
Chaini26 – 977952Ephrin type-A receptor 2PRO_0000016801Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi69 ↔ 187By similarity
Disulfide bondi104 ↔ 114By similarity
Modified residuei152 – 1521PhosphoserineBy similarity
Modified residuei374 – 3741PhosphoserineBy similarity
Glycosylationi408 – 4081N-linked (GlcNAc...)2 Publications
Glycosylationi436 – 4361N-linked (GlcNAc...)2 Publications
Modified residuei571 – 5711PhosphoserineBy similarity
Modified residuei580 – 5801PhosphoserineBy similarity
Modified residuei588 – 5881PhosphothreonineBy similarity
Modified residuei589 – 5891Phosphotyrosine; by autocatalysisBy similarity
Modified residuei594 – 5941PhosphothreonineBy similarity
Modified residuei595 – 5951Phosphotyrosine; by autocatalysis2 Publications
Modified residuei629 – 6291PhosphotyrosineBy similarity
Modified residuei648 – 6481PhosphothreonineBy similarity
Modified residuei736 – 7361Phosphotyrosine; by autocatalysis1 Publication
Modified residuei772 – 7721PhosphothreonineBy similarity
Modified residuei773 – 7731Phosphotyrosine; by autocatalysis2 Publications
Modified residuei791 – 7911PhosphoserineBy similarity
Modified residuei792 – 7921PhosphotyrosineBy similarity
Modified residuei870 – 8701PhosphoserineBy similarity
Modified residuei881 – 8811PhosphoserineBy similarity
Modified residuei893 – 8931PhosphoserineBy similarity
Modified residuei898 – 8981PhosphoserineBy similarity
Modified residuei899 – 8991PhosphothreonineBy similarity
Modified residuei900 – 9001PhosphoserineBy similarity
Modified residuei902 – 9021PhosphoserineBy similarity
Modified residuei911 – 9111PhosphoserineBy similarity
Modified residuei922 – 9221Phosphotyrosine; by autocatalysisSequence Analysis
Modified residuei931 – 9311PhosphotyrosineBy similarity
Modified residuei961 – 9611PhosphotyrosineBy 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 ACP1.2 Publications
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

MaxQBiQ03145.
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, 566-971.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini27 – 205179Eph LBDPROSITE-ProRule annotationAdd
BLAST
Domaini329 – 433105Fibronectin type-III 1PROSITE-ProRule annotationAdd
BLAST
Domaini439 – 53092Fibronectin type-III 2PROSITE-ProRule annotationAdd
BLAST
Domaini614 – 876263Protein kinasePROSITE-ProRule annotationAdd
BLAST
Domaini905 – 96965SAMPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 205205Mediates interaction with CLDN4By similarityAdd
BLAST
Regioni607 – 907301Mediates interaction with ARHGEF16By similarityAdd
BLAST
Regioni887 – 97791Negatively regulates interaction with ARHGEF16By similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi975 – 9773PDZ-bindingSequence Analysis

Compositional bias

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

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

eggNOGiCOG0515.
GeneTreeiENSGT00760000118975.
HOGENOMiHOG000233856.
HOVERGENiHBG062180.
InParanoidiQ03145.
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

« 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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti5 – 51A → T in CAA55135. (PubMed:8183555)Curated
Sequence conflicti112 – 1132SS → HA in AAA82113. (PubMed:7918100)Curated
Sequence conflicti189 – 1891A → R in AAA82113. (PubMed:7918100)Curated
Sequence conflicti209 – 2091R → C in AAA82113. (PubMed:7918100)Curated
Sequence conflicti244 – 2441P → A in AAA82113. (PubMed:7918100)Curated
Sequence conflicti258 – 2603IGQ → SE in AAA82113. (PubMed:7918100)Curated
Sequence conflicti291 – 2911C → S in AAA82113. (PubMed:7918100)Curated
Sequence conflicti339 – 3402IG → C in AAA82113. (PubMed:7918100)Curated
Sequence conflicti371 – 3722WP → CA in AAA82113. (PubMed:7918100)Curated
Sequence conflicti383 – 3831S → T in AAA82113. (PubMed:7918100)Curated
Sequence conflicti457 – 4571W → R in AAA82113. (PubMed:7918100)Curated
Sequence conflicti485 – 4851V → G in AAA82113. (PubMed:7918100)Curated
Sequence conflicti511 – 5111L → W in AAA82113. (PubMed:7918100)Curated
Sequence conflicti534 – 5341A → R in AAA82113. (PubMed:7918100)Curated
Sequence conflicti678 – 6781R → P in CAA55135. (PubMed:8183555)Curated
Sequence conflicti681 – 6811G → A in AAA82113. (PubMed:7918100)Curated
Sequence conflicti819 – 8202YW → LL in AAA82113. (PubMed:7918100)Curated
Sequence conflicti878 – 8781A → R in AAA82113. (PubMed:7918100)Curated
Sequence conflicti919 – 9202MQ → IE in AAA82113. (PubMed:7918100)Curated

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 .
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, 566-971.
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

MaxQBi Q03145.
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 ENSGT00760000118975.
HOGENOMi HOG000233856.
HOVERGENi HBG062180.
InParanoidi Q03145.
KOi K05103.
OMAi LVPIGQC.
OrthoDBi EOG7VTDM6.
TreeFami TF315608.

Enzyme and pathway databases

BRENDAi 2.7.10.1. 3474.
Reactomei REACT_243590. EPH-ephrin mediated repulsion of cells.
REACT_243939. EPHA-mediated growth cone collapse.
REACT_258158. EPH-Ephrin signaling.

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: November 26, 2014
This is version 157 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

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