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Q60750

- EPHA1_MOUSE

UniProt

Q60750 - EPHA1_MOUSE

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Protein

Ephrin type-A receptor 1

Gene

Epha1

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. Binds with a low affinity EFNA3 and EFNA4 and with a high affinity to EFNA1 which most probably constitutes its cognate/functional ligand. Upon activation by EFNA1 induces cell attachment to the extracellular matrix inhibiting cell spreading and motility through regulation of ILK and downstream RHOA and RAC. Plays also a role in angiogenesis and regulates cell proliferation. May play a role in apoptosis.1 Publication

Catalytic activityi

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.PROSITE-ProRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei657 – 6571ATPPROSITE-ProRule annotation
Active sitei750 – 7501Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi631 – 6399ATPPROSITE-ProRule annotation

GO - Molecular functioni

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

GO - Biological processi

  1. activation of Rho GTPase activity Source: UniProtKB
  2. angiogenesis Source: UniProtKB-KW
  3. cell surface receptor signaling pathway Source: UniProtKB
  4. negative regulation of cell migration Source: UniProtKB
  5. negative regulation of protein kinase activity Source: UniProtKB
  6. peptidyl-tyrosine phosphorylation Source: UniProtKB
  7. positive regulation of angiogenesis Source: UniProtKB
  8. positive regulation of cell-matrix adhesion Source: UniProtKB
  9. positive regulation of cell migration Source: UniProtKB
  10. positive regulation of cell proliferation Source: UniProtKB
  11. positive regulation of stress fiber assembly Source: UniProtKB
  12. protein autophosphorylation Source: UniProtKB
  13. regulation of Rac GTPase activity Source: UniProtKB
  14. substrate adhesion-dependent cell spreading Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Receptor, Transferase, Tyrosine-protein kinase

Keywords - Biological processi

Angiogenesis, Cell adhesion

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_220962. POU5F1 (OCT4), SOX2, NANOG activate genes related to proliferation.

Names & Taxonomyi

Protein namesi
Recommended name:
Ephrin type-A receptor 1 (EC:2.7.10.1)
Short name:
mEpha1
Alternative name(s):
Embryonic stem cell kinase
Tyrosine-protein kinase receptor ESK
Gene namesi
Name:Epha1
Synonyms:Esk
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 6

Organism-specific databases

MGIiMGI:107381. Epha1.

Subcellular locationi

GO - Cellular componenti

  1. integral component of plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Disruption phenotypei

Mice display a partially-penetrant uterovaginal and tail development defects. The uterovaginal defect is due to a defect in apoptosis during development.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2626Sequence AnalysisAdd
BLAST
Chaini27 – 977951Ephrin type-A receptor 1By similarityPRO_0000016799Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi415 – 4151N-linked (GlcNAc...)Sequence Analysis
Glycosylationi479 – 4791N-linked (GlcNAc...)Sequence Analysis
Modified residuei600 – 6001Phosphotyrosine; by autocatalysisSequence Analysis
Modified residuei606 – 6061Phosphotyrosine; by autocatalysisSequence Analysis
Modified residuei782 – 7821Phosphotyrosine; by autocatalysisBy similarity
Modified residuei907 – 9071PhosphoserineBy similarity
Modified residuei911 – 9111PhosphoserineBy similarity

Post-translational modificationi

Phosphorylated. Autophosphorylation is stimulated by its ligand EFNA1 By similarity.By similarity
Ubiquitinated.By similarity

Keywords - PTMi

Glycoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ60750.
PRIDEiQ60750.

PTM databases

PhosphoSiteiQ60750.

Expressioni

Tissue specificityi

Preferentially expressed in epithelial cells including skin, kidney, liver and thymus.2 Publications

Gene expression databases

BgeeiQ60750.
CleanExiMM_EPHA1.
GenevestigatoriQ60750.

Interactioni

Subunit structurei

Homodimer. Forms a signaling complex with LCK; PTK2B/PYK2 and PI3-kinase upon activation by EFNA1; regulates T-lymphocytes migration. Interacts (via SAM domain) with ILK (via ANK repeats); stimulated by EFNA1 but independent of the kinase activity of EPHA1. Interacts (kinase activity-dependent) with PTK2/FAK1 By similarity.By similarity

Protein-protein interaction databases

BioGridi199468. 1 interaction.
IntActiQ60750. 4 interactions.
MINTiMINT-7013408.

Structurei

Secondary structure

1
977
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi456 – 4605
Beta strandi463 – 4675
Beta strandi481 – 4877
Beta strandi492 – 50615
Beta strandi512 – 5209
Beta strandi522 – 5243
Beta strandi532 – 5354

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1X5ANMR-A446-539[»]
ProteinModelPortaliQ60750.
SMRiQ60750. Positions 25-539, 611-909, 912-975.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ60750.

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini27 – 548522ExtracellularSequence AnalysisAdd
BLAST
Topological domaini570 – 977408CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei549 – 56921HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini28 – 210183Eph LBDPROSITE-ProRule annotationAdd
BLAST
Domaini333 – 446114Fibronectin type-III 1PROSITE-ProRule annotationAdd
BLAST
Domaini448 – 53992Fibronectin type-III 2PROSITE-ProRule annotationAdd
BLAST
Domaini625 – 885261Protein kinasePROSITE-ProRule annotationAdd
BLAST
Domaini914 – 97764SAMPROSITE-ProRule annotationAdd
BLAST

Motif

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

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi192 – 330139Cys-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.
InParanoidiQ60750.
KOiK05102.
OMAiQAYEDPA.
OrthoDBiEOG7VTDM6.
PhylomeDBiQ60750.
TreeFamiTF315363.

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. 1 hit.
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.

Q60750-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MERRWPLGLA LLLLLLCAPL PPGARAEEVT LMDTSTAQGE LGWLLDPPET
60 70 80 90 100
GWSEVQQMLN GTPLYMYQDC PIQEGGDTDH WLRSNWIYRG EEASRIYVEL
110 120 130 140 150
QFTVRDCKSF PGGAGPLGCK ETFNLFYMES DQDVGIQLRR PLFQKVTTVA
160 170 180 190 200
ADQSFTIRDL ASGSVKLNVE RCSLGHLTRR GLYLAFHNPG SCVALVSVRV
210 220 230 240 250
FYQRCAETVH GLAHFPDTLP GPGGLVEVAG TCLSHAQISL GSSGTPRMHC
260 270 280 290 300
SPDGEWLVPV GQCQCEPGYE ESSGNVGCTA CPTGFYRVDM NTLRCLKCPQ
310 320 330 340 350
HSIAESEGST ICTCENGHYR APGEGPQVAC TRPPSAPQNL SFSTSGTQLS
360 370 380 390 400
LRWEPPRDTG GRHDIRYSVE CLQCRGIAQD GGPCQPCGKG VHFSPAASGL
410 420 430 440 450
TTSTVQVQGL EPYANYTFTV KSQNRVSGLD SSSPSSASLS INMGHAESLS
460 470 480 490 500
GLSLKLVKKE PRQLELTWAG SRPRNPGGNL SYELHVLNQD EEWHQMVLEP
510 520 530 540 550
RVLLTKLQPD TTYIVRVRTL TPLGPGPFSP DHEFRTSPPV SRSLTGGEIV
560 570 580 590 600
AVIFGLLLGI ALLIGIYVFR SRRGQRQRQQ RQRERTTNVD REDKLWLKPY
610 620 630 640 650
VDLQAYEDPA QGALDFAQEL DPAWLIVDTV IGEGEFGEVY RGALRLPSQD
660 670 680 690 700
CKTVAIKTLK DTSPDGYWWN FLREATIMGQ FNHPHILRLE GVITKRKPIM
710 720 730 740 750
IITEFMENGA LDAFLKERED QLAPGQLVAM LLGIASGMNC LSGHNYVHRD
760 770 780 790 800
LAARNILVNQ NLCCKVSDFG LTRLLDDFDG TYETQGGKIP IRWTAPEAIA
810 820 830 840 850
HRIFTTASDV WSFGIVMWEV LSFGDKPYGE MSNQEVMKSI EDGYRLPPPV
860 870 880 890 900
DCPAPLYELM KNCWAYDRAR RPHFLQLQAH LEQLLTDPHS LRTIANFDPR
910 920 930 940 950
VTLRLPSLSG SDGIPYRSVS EWLESIRMKR YILHFRSAGL DTMECVLELT
960 970
AEDLTQMGIT LPGHQKRILC SIQGFKD
Length:977
Mass (Da):108,578
Last modified:May 10, 2004 - v2
Checksum:iAB78D6E6C8B2E7F4
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti163 – 1631G → D in AAG12206. (PubMed:11519828)Curated
Sequence conflicti422 – 4221S → P in AAC52384. (PubMed:8552593)Curated
Sequence conflicti504 – 5041L → R in AAC52384. (PubMed:8552593)Curated
Sequence conflicti521 – 5211T → A in AAC52384. (PubMed:8552593)Curated
Sequence conflicti590 – 5901D → G in AAC52384. (PubMed:8552593)Curated
Sequence conflicti636 – 6361F → Y in AAC52384. (PubMed:8552593)Curated
Sequence conflicti660 – 6601K → R in AAC52384. (PubMed:8552593)Curated
Sequence conflicti720 – 7201D → G in AAC52384. (PubMed:8552593)Curated
Sequence conflicti769 – 7691F → L in AAC52384. (PubMed:8552593)Curated
Sequence conflicti797 – 7971E → G in AAC52384. (PubMed:8552593)Curated
Sequence conflicti817 – 8171M → T in AAG12206. (PubMed:11519828)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF131197 mRNA. Translation: AAG12206.1.
AK028478 mRNA. Translation: BAC25971.1.
U18084 mRNA. Translation: AAC52384.1.
CCDSiCCDS20067.1.
RefSeqiNP_076069.2. NM_023580.4.
UniGeneiMm.133330.

Genome annotation databases

EnsembliENSMUST00000073387; ENSMUSP00000073099; ENSMUSG00000029859.
GeneIDi13835.
KEGGimmu:13835.
UCSCiuc009brc.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF131197 mRNA. Translation: AAG12206.1 .
AK028478 mRNA. Translation: BAC25971.1 .
U18084 mRNA. Translation: AAC52384.1 .
CCDSi CCDS20067.1.
RefSeqi NP_076069.2. NM_023580.4.
UniGenei Mm.133330.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1X5A NMR - A 446-539 [» ]
ProteinModelPortali Q60750.
SMRi Q60750. Positions 25-539, 611-909, 912-975.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 199468. 1 interaction.
IntActi Q60750. 4 interactions.
MINTi MINT-7013408.

PTM databases

PhosphoSitei Q60750.

Proteomic databases

PaxDbi Q60750.
PRIDEi Q60750.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000073387 ; ENSMUSP00000073099 ; ENSMUSG00000029859 .
GeneIDi 13835.
KEGGi mmu:13835.
UCSCi uc009brc.1. mouse.

Organism-specific databases

CTDi 2041.
MGIi MGI:107381. Epha1.

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00760000118975.
HOGENOMi HOG000233856.
HOVERGENi HBG062180.
InParanoidi Q60750.
KOi K05102.
OMAi QAYEDPA.
OrthoDBi EOG7VTDM6.
PhylomeDBi Q60750.
TreeFami TF315363.

Enzyme and pathway databases

Reactomei REACT_220962. POU5F1 (OCT4), SOX2, NANOG activate genes related to proliferation.

Miscellaneous databases

EvolutionaryTracei Q60750.
NextBioi 284652.
PROi Q60750.
SOURCEi Search...

Gene expression databases

Bgeei Q60750.
CleanExi MM_EPHA1.
Genevestigatori Q60750.

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. 1 hit.
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. "Characterization of the Epha1 receptor tyrosine kinase: expression in epithelial tissues."
    Coulthard M.G., Lickliter J.D., Subanesan N., Chen K., Webb G.C., Lowry A.J., Koblar S., Bottema C.D., Boyd A.W.
    Growth Factors 18:303-317(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, EFNA1 LIGAND-BINDING.
  2. "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: Skin.
  3. "Embryonic stem cells express multiple Eph-subfamily receptor tyrosine kinases."
    Lickliter J.D., Smith F.M., Olsson J.E., Mackwell K.L., Boyd A.W.
    Proc. Natl. Acad. Sci. U.S.A. 93:145-150(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 281-814.
    Strain: 129/Sv.
  4. "Generation and characterization of EphA1 receptor tyrosine kinase reporter knockout mice."
    Duffy S.L., Coulthard M.G., Spanevello M.D., Herath N.I., Yeadon T.M., McCarron J.K., Carter J.C., Tonks I.D., Kay G.F., Phillips G.E., Boyd A.W.
    Genesis 46:553-561(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION IN APOPTOSIS, TISSUE SPECIFICITY.
  5. "The solution structure of the second fibronectin type III domain of mouse ephrin type-A receptor 1."
    RIKEN structural genomics initiative (RSGI)
    Submitted (NOV-2005) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 446-539.

Entry informationi

Entry nameiEPHA1_MOUSE
AccessioniPrimary (citable) accession number: Q60750
Secondary accession number(s): Q8CED9, Q9ESJ2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 10, 2004
Last modified: October 29, 2014
This is version 147 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3