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Protein

Ephrin type-A receptor 1

Gene

Epha1

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. 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)DescriptionActionsGraphical viewLength
Binding sitei657ATPPROSITE-ProRule annotation1
Active sitei750Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi631 – 639ATPPROSITE-ProRule annotation9

GO - Molecular functioni

GO - Biological processi

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

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 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
Proteomesi
  • UP000000589 Componenti: Chromosome 6

Organism-specific databases

MGIiMGI:107381. Epha1.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini27 – 548ExtracellularSequence analysisAdd BLAST522
Transmembranei549 – 569HelicalSequence analysisAdd BLAST21
Topological domaini570 – 977CytoplasmicSequence analysisAdd BLAST408

GO - Cellular componenti

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)DescriptionActionsGraphical viewLength
Signal peptidei1 – 26Sequence analysisAdd BLAST26
ChainiPRO_000001679927 – 977Ephrin type-A receptor 1By similarityAdd BLAST951

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi415N-linked (GlcNAc...)Sequence analysis1
Glycosylationi479N-linked (GlcNAc...)Sequence analysis1
Modified residuei600Phosphotyrosine; by autocatalysisSequence analysis1
Modified residuei606Phosphotyrosine; by autocatalysisSequence analysis1
Modified residuei782Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei907PhosphoserineBy similarity1
Modified residuei911PhosphoserineBy similarity1

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

MaxQBiQ60750.
PaxDbiQ60750.
PeptideAtlasiQ60750.
PRIDEiQ60750.

PTM databases

iPTMnetiQ60750.
PhosphoSitePlusiQ60750.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiENSMUSG00000029859.
CleanExiMM_EPHA1.
ExpressionAtlasiQ60750. baseline and differential.
GenevisibleiQ60750. MM.

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

GO - Molecular functioni

Protein-protein interaction databases

BioGridi199468. 1 interactor.
IntActiQ60750. 4 interactors.
MINTiMINT-7013408.
STRINGi10090.ENSMUSP00000073099.

Structurei

Secondary structure

1977
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi456 – 460Combined sources5
Beta strandi463 – 467Combined sources5
Beta strandi481 – 487Combined sources7
Beta strandi492 – 506Combined sources15
Beta strandi512 – 520Combined sources9
Beta strandi522 – 524Combined sources3
Beta strandi532 – 535Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1X5ANMR-A446-539[»]
ProteinModelPortaliQ60750.
SMRiQ60750.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ60750.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini28 – 210Eph LBDPROSITE-ProRule annotationAdd BLAST183
Domaini333 – 446Fibronectin type-III 1PROSITE-ProRule annotationAdd BLAST114
Domaini448 – 539Fibronectin type-III 2PROSITE-ProRule annotationAdd BLAST92
Domaini625 – 885Protein kinasePROSITE-ProRule annotationAdd BLAST261
Domaini914 – 977SAMPROSITE-ProRule annotationAdd BLAST64

Motif

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

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi192 – 330Cys-richAdd BLAST139

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.
InParanoidiQ60750.
KOiK05102.
OMAiQAYEDPA.
OrthoDBiEOG091G00W0.
PhylomeDBiQ60750.
TreeFamiTF315363.

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. 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)DescriptionActionsGraphical viewLength
Sequence conflicti163G → D in AAG12206 (PubMed:11519828).Curated1
Sequence conflicti422S → P in AAC52384 (PubMed:8552593).Curated1
Sequence conflicti504L → R in AAC52384 (PubMed:8552593).Curated1
Sequence conflicti521T → A in AAC52384 (PubMed:8552593).Curated1
Sequence conflicti590D → G in AAC52384 (PubMed:8552593).Curated1
Sequence conflicti636F → Y in AAC52384 (PubMed:8552593).Curated1
Sequence conflicti660K → R in AAC52384 (PubMed:8552593).Curated1
Sequence conflicti720D → G in AAC52384 (PubMed:8552593).Curated1
Sequence conflicti769F → L in AAC52384 (PubMed:8552593).Curated1
Sequence conflicti797E → G in AAC52384 (PubMed:8552593).Curated1
Sequence conflicti817M → T in AAG12206 (PubMed:11519828).Curated1

Sequence databases

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1X5ANMR-A446-539[»]
ProteinModelPortaliQ60750.
SMRiQ60750.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi199468. 1 interactor.
IntActiQ60750. 4 interactors.
MINTiMINT-7013408.
STRINGi10090.ENSMUSP00000073099.

PTM databases

iPTMnetiQ60750.
PhosphoSitePlusiQ60750.

Proteomic databases

MaxQBiQ60750.
PaxDbiQ60750.
PeptideAtlasiQ60750.
PRIDEiQ60750.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi2041.
MGIiMGI:107381. Epha1.

Phylogenomic databases

eggNOGiKOG0196. Eukaryota.
COG0515. LUCA.
GeneTreeiENSGT00760000118975.
HOGENOMiHOG000233856.
HOVERGENiHBG062180.
InParanoidiQ60750.
KOiK05102.
OMAiQAYEDPA.
OrthoDBiEOG091G00W0.
PhylomeDBiQ60750.
TreeFamiTF315363.

Enzyme and pathway databases

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

EvolutionaryTraceiQ60750.
PROiQ60750.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000029859.
CleanExiMM_EPHA1.
ExpressionAtlasiQ60750. baseline and differential.
GenevisibleiQ60750. 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. 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]
ProtoNetiSearch...

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: November 30, 2016
This is version 164 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

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.