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Q03137

- EPHA4_MOUSE

UniProt

Q03137 - EPHA4_MOUSE

Protein

Ephrin type-A receptor 4

Gene

Epha4

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 163 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    Receptor tyrosine kinase which binds membrane-bound ephrin 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. Highly promiscuous, it has the unique property among Eph receptors to bind and to be physiologically activated by both GPI-anchored ephrin-A and transmembrane ephrin-B ligands including EFNA1 and EFNB3. Upon activation by ephrin ligands, modulates cell morphology and integrin-dependent cell adhesion through regulation of the Rac, Rap and Rho GTPases activity. Plays an important role in the development of the nervous system controlling different steps of axonal guidance including the establishment of the corticospinal projections. May also control the segregation of motor and sensory axons during neuromuscular circuit development. In addition to its role in axonal guidance plays a role in synaptic plasticity. Activated by EFNA1 phosphorylates CDK5 at 'Tyr-15' which in turn phosphorylates NGEF regulating RHOA and dendritic spine morphogenesis. In the nervous system, plays also a role in repair after injury preventing axonal regeneration and in angiogenesis playing a role in central nervous system vascular formation. Additionally, its promiscuity makes it available to participate in a variety of cell-cell signaling regulating for instance the development of the thymic epithelium.9 Publications

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei653 – 6531ATPPROSITE-ProRule annotation
    Active sitei746 – 7461Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi627 – 6359ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. DH domain binding Source: UniProtKB
    3. GPI-linked ephrin receptor activity Source: UniProtKB
    4. identical protein binding Source: IntAct
    5. protein binding Source: UniProtKB
    6. protein kinase activity Source: UniProtKB
    7. transmembrane-ephrin receptor activity Source: UniProtKB

    GO - Biological processi

    1. adult walking behavior Source: MGI
    2. axon guidance Source: MGI
    3. cell adhesion Source: UniProtKB-KW
    4. corticospinal tract morphogenesis Source: UniProtKB
    5. fasciculation of motor neuron axon Source: UniProtKB
    6. fasciculation of sensory neuron axon Source: UniProtKB
    7. glial cell migration Source: Ensembl
    8. motor neuron axon guidance Source: UniProtKB
    9. negative regulation of axon regeneration Source: UniProtKB
    10. peptidyl-tyrosine phosphorylation Source: UniProtKB
    11. positive regulation of dendrite morphogenesis Source: Ensembl
    12. positive regulation of JUN kinase activity Source: BHF-UCL
    13. positive regulation of Rho guanyl-nucleotide exchange factor activity Source: UniProtKB
    14. protein autophosphorylation Source: UniProtKB
    15. regulation of astrocyte differentiation Source: UniProtKB
    16. regulation of axonogenesis Source: UniProtKB
    17. regulation of dendritic spine morphogenesis Source: UniProtKB
    18. regulation of Rac GTPase activity Source: UniProtKB
    19. regulation of Rap GTPase activity Source: UniProtKB

    Keywords - Molecular functioni

    Developmental protein, Kinase, Receptor, Transferase, Tyrosine-protein kinase

    Keywords - Biological processi

    Cell adhesion, Neurogenesis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.10.1. 3474.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ephrin type-A receptor 4 (EC:2.7.10.1)
    Alternative name(s):
    Tyrosine-protein kinase receptor MPK-3
    Tyrosine-protein kinase receptor SEK-1
    Gene namesi
    Name:Epha4
    Synonyms:Sek, Sek1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 1

    Organism-specific databases

    MGIiMGI:98277. Epha4.

    Subcellular locationi

    Cell membrane 1 Publication; Single-pass type I membrane protein 1 Publication. Cell projectionaxon 1 Publication. Cell projectiondendrite 1 Publication. Cell junctionsynapsepostsynaptic cell membranepostsynaptic density By similarity. Early endosome 1 Publication
    Note: Clustered upon activation and targeted to early endosome.

    GO - Cellular componenti

    1. axon Source: UniProtKB
    2. axonal growth cone Source: Ensembl
    3. axon terminus Source: Ensembl
    4. cell junction Source: UniProtKB-KW
    5. cell surface Source: Ensembl
    6. cytoplasm Source: UniProtKB
    7. dendrite Source: UniProtKB
    8. dendritic spine Source: Ensembl
    9. early endosome membrane Source: UniProtKB
    10. endoplasmic reticulum Source: Ensembl
    11. filopodium Source: Ensembl
    12. Golgi apparatus Source: Ensembl
    13. integral component of plasma membrane Source: UniProtKB
    14. mitochondrial outer membrane Source: Ensembl
    15. neuromuscular junction Source: Ensembl
    16. perikaryon Source: Ensembl
    17. postsynaptic density Source: UniProtKB-SubCell
    18. postsynaptic membrane Source: UniProtKB-KW

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Cell projection, Endosome, Membrane, Postsynaptic cell membrane, Synapse

    Pathology & Biotechi

    Disruption phenotypei

    Mice are viable and fertile but display a loss of coordination of limb movement associated with disruptions of cortico-spinal tract. They also display altered development of the thymic epithelium which leads to a defective T-cells development.3 Publications

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi635 – 6351V → M: Kinase dead; loss of autophosphorylation and loss of CHN1 phosphorylation. No effect on interaction with NGEF. 2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1919Sequence AnalysisAdd
    BLAST
    Chaini20 – 986967Ephrin type-A receptor 4PRO_0000016808Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi235 – 2351N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi340 – 3401N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi408 – 4081N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi423 – 4231N-linked (GlcNAc...)Sequence Analysis
    Modified residuei596 – 5961Phosphotyrosine; by autocatalysis1 Publication
    Modified residuei602 – 6021Phosphotyrosine; by autocatalysis2 Publications
    Modified residuei779 – 7791Phosphotyrosine; by autocatalysisSequence Analysis
    Modified residuei928 – 9281Phosphotyrosine; by autocatalysisSequence Analysis

    Keywords - PTMi

    Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiQ03137.
    PaxDbiQ03137.
    PRIDEiQ03137.

    PTM databases

    PhosphoSiteiQ03137.

    Expressioni

    Tissue specificityi

    Highest expression in the adult brain and retina and also detectable in kidney, lung, skeletal muscle and thymus. Not detected in heart and liver.

    Developmental stagei

    Found in both the 10-day embryonic brain and body tissues. In the embryonic brain, expressed in the developing cortex of the telencephalon and major cortical tracts. Also expressed in the hippocampus, fornix and striatal cells and tracts. In the diencephalon, strongly expressed in thalamus, hypothalamus and thalamo-cortical projection. Also expressed in red nuclei of the mesencephalon and in the cerebellum. In the spinal cord, persistent expression occurs in the dorsal funiculus and ventral gray matter.1 Publication

    Gene expression databases

    ArrayExpressiQ03137.
    BgeeiQ03137.
    CleanExiMM_EPHA4.
    GenevestigatoriQ03137.

    Interactioni

    Subunit structurei

    Heterotetramer upon binding of the ligand. The heterotetramer is composed of an ephrin dimer and a receptor dimer. Oligomerization is probably required to induce biological responses. Interacts (phosphorylated at position Tyr-602) with FYN. Interacts (via PDZ motif) with SIPA1L1 (via PDZ domain); controls neuronal morphology through regulation of the RAP1 (RAP1A or RAP1B) and RAP2 (RAP2A, RAP2B or RAP2C) GTPases. Interacts with CDK5, CDK5R1 and NGEF; upon activation by EFNA1 induces NGEF phosphorylation by the kinase CDK5. Interacts with CHN1; effector of EPHA4 in axon guidance linking EPHA4 activation to RAC1 regulation.6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself2EBI-1539152,EBI-1539152
    Chn1Q91V57-12EBI-1539152,EBI-1539203
    Efnb2P528002EBI-1539152,EBI-1032676
    Epha2Q031453EBI-1539152,EBI-529701
    Ephb2P547633EBI-1539152,EBI-537711
    VAPBO952922EBI-1539152,EBI-1188298From a different organism.

    Protein-protein interaction databases

    BioGridi199471. 2 interactions.
    DIPiDIP-1019N.
    IntActiQ03137. 7 interactions.
    MINTiMINT-3381444.

    Structurei

    Secondary structure

    1
    986
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi618 – 6203
    Beta strandi621 – 6299
    Beta strandi631 – 64010
    Beta strandi648 – 6558
    Helixi661 – 67414
    Beta strandi685 – 6895
    Beta strandi691 – 6944
    Beta strandi696 – 7005
    Helixi707 – 7126
    Turni713 – 7164
    Helixi720 – 73920
    Helixi749 – 7513
    Beta strandi752 – 7543
    Beta strandi760 – 7623
    Helixi788 – 7903
    Helixi793 – 7986
    Helixi803 – 81816
    Turni824 – 8274
    Helixi830 – 8389
    Helixi851 – 86010
    Helixi865 – 8673
    Helixi871 – 88313
    Helixi885 – 8884
    Helixi916 – 9227
    Helixi926 – 9283
    Helixi929 – 9346
    Helixi940 – 9434
    Helixi948 – 9547
    Helixi959 – 97719
    Helixi978 – 9803

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1B0XX-ray2.00A890-981[»]
    2HELX-ray2.35A591-896[»]
    2I8Jmodel-@594-888[»]
    2XYUX-ray2.12A612-896[»]
    2Y6MX-ray1.70A606-896[»]
    2Y6OX-ray1.54A606-896[»]
    ProteinModelPortaliQ03137.
    SMRiQ03137. Positions 27-981.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ03137.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini20 – 547528ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini570 – 986417CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei548 – 56922HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini30 – 209180Eph LBDPROSITE-ProRule annotationAdd
    BLAST
    Domaini328 – 439112Fibronectin type-III 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini440 – 53798Fibronectin type-III 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini621 – 882262Protein kinasePROSITE-ProRule annotationAdd
    BLAST
    Domaini911 – 97565SAMPROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi984 – 9863PDZ-bindingSequence Analysis

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi191 – 325135Cys-richAdd
    BLAST

    Domaini

    The protein kinase domain mediates interaction with NGEF.

    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.
    GeneTreeiENSGT00750000117255.
    HOGENOMiHOG000233856.
    HOVERGENiHBG062180.
    InParanoidiQ80VZ2.
    KOiK05105.
    OMAiDWIPREG.
    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.
    IPR013783. Ig-like_fold.
    IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR001660. SAM.
    IPR013761. SAM/pointed.
    IPR011510. SAM_2.
    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.
    PF07647. SAM_2. 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.
    PROSITEiPS51550. 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]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform Long (identifier: Q03137-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MAGIFYFILF SFLFGICDAV TGSRVYPANE VTLLDSRSVQ GELGWIASPL    50
    EGGWEEVSIM DEKNTPIRTY QVCNVMEASQ NNWLRTDWIT REGAQRVYIE 100
    IKFTLRDCNS LPGVMGTCKE TFNLYYYESD NDKERFIRES QFGKIDTIAA 150
    DESFTQVDIG DRIMKLNTEI RDVGPLSKKG FYLAFQDVGA CIALVSVRVF 200
    YKKCPLTVRN LAQFPDTITG ADTSSLVEVR GSCVNNSEEK DVPKMYCGAD 250
    GEWLVPIGNC LCNAGHEEQN GECQACKIGY YKALSTDASC AKCPPHSYSV 300
    WEGATSCTCD RGFFRADNDA ASMPCTRPPS APLNLISNVN ETSVNLEWSS 350
    PQNTGGRQDI SYNVVCKKCG AGDPSKCRPC GSGVHYTPQQ NGLKTTRVSI 400
    TDLLAHTNYT FEIWAVNGVS KYNPSPDQSV SVTVTTNQAA PSSIALVQAK 450
    EVTRYSVALA WLEPDRPNGV ILEYEVKYYE KDQNERSYRI VRTAARNTDI 500
    KGLNPLTSYV FHVRARTAAG YGDFSEPLEV TTNTVPSRII GDGANSTVLL 550
    VSVSGSVVLV VILIAAFVIS RRRSKYSKAK QEADEEKHLN QGVRTYVDPF 600
    TYEDPNQAVR EFAKEIDASC IKIEKVIGVG EFGEVCSGRL KVPGKREICV 650
    AIKTLKAGYT DKQRRDFLSE ASIMGQFDHP NIIHLEGVVT KCKPVMIITE 700
    YMENGSLDAF LRKNDGRFTV IQLVGMLRGI GSGMKYLSDM SYVHRDLAAR 750
    NILVNSNLVC KVSDFGMSRV LEDDPEAAYT TRGGKIPIRW TAPEAIAYRK 800
    FTSASDVWSY GIVMWEVMSY GERPYWDMSN QDVIKAIEEG YRLPPPMDCP 850
    IALHQLMLDC WQKERSDRPK FGQIVNMLDK LIRNPNSLKR TGSESSRPNT 900
    ALLDPSSPEF SAVVSVGDWL QAIKMDRYKD NFTAAGYTTL EAVVHMSQDD 950
    LARIGITAIT HQNKILSSVQ AMRTQMQQMH GRMVPV 986
    Length:986
    Mass (Da):109,814
    Last modified:July 27, 2011 - v2
    Checksum:i89BEB2C7CDB54A55
    GO
    Isoform Short (identifier: Q03137-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         783-832: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:936
    Mass (Da):103,984
    Checksum:i3C3EFE4620316DB2
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti145 – 1451I → T in CAA46268. (PubMed:1281307)Curated
    Sequence conflicti145 – 1451I → T in AAB25836. (PubMed:1281307)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei783 – 83250Missing in isoform Short. CuratedVSP_002998Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X65138 mRNA. Translation: CAA46268.1.
    X57241 mRNA. Translation: CAA40517.1.
    S57168 mRNA. Translation: AAB25836.1.
    AK147698 mRNA. Translation: BAE28081.1.
    CH466548 Genomic DNA. Translation: EDL00429.1.
    BC052164 mRNA. Translation: AAH52164.1.
    CCDSiCCDS35627.1. [Q03137-1]
    PIRiS78059.
    RefSeqiNP_031962.2. NM_007936.3. [Q03137-1]
    UniGeneiMm.400747.

    Genome annotation databases

    EnsembliENSMUST00000027451; ENSMUSP00000027451; ENSMUSG00000026235. [Q03137-1]
    GeneIDi13838.
    KEGGimmu:13838.
    UCSCiuc007bpz.1. mouse. [Q03137-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X65138 mRNA. Translation: CAA46268.1 .
    X57241 mRNA. Translation: CAA40517.1 .
    S57168 mRNA. Translation: AAB25836.1 .
    AK147698 mRNA. Translation: BAE28081.1 .
    CH466548 Genomic DNA. Translation: EDL00429.1 .
    BC052164 mRNA. Translation: AAH52164.1 .
    CCDSi CCDS35627.1. [Q03137-1 ]
    PIRi S78059.
    RefSeqi NP_031962.2. NM_007936.3. [Q03137-1 ]
    UniGenei Mm.400747.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1B0X X-ray 2.00 A 890-981 [» ]
    2HEL X-ray 2.35 A 591-896 [» ]
    2I8J model - @ 594-888 [» ]
    2XYU X-ray 2.12 A 612-896 [» ]
    2Y6M X-ray 1.70 A 606-896 [» ]
    2Y6O X-ray 1.54 A 606-896 [» ]
    ProteinModelPortali Q03137.
    SMRi Q03137. Positions 27-981.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 199471. 2 interactions.
    DIPi DIP-1019N.
    IntActi Q03137. 7 interactions.
    MINTi MINT-3381444.

    Chemistry

    BindingDBi Q03137.
    ChEMBLi CHEMBL1293259.

    PTM databases

    PhosphoSitei Q03137.

    Proteomic databases

    MaxQBi Q03137.
    PaxDbi Q03137.
    PRIDEi Q03137.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000027451 ; ENSMUSP00000027451 ; ENSMUSG00000026235 . [Q03137-1 ]
    GeneIDi 13838.
    KEGGi mmu:13838.
    UCSCi uc007bpz.1. mouse. [Q03137-1 ]

    Organism-specific databases

    CTDi 2043.
    MGIi MGI:98277. Epha4.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00750000117255.
    HOGENOMi HOG000233856.
    HOVERGENi HBG062180.
    InParanoidi Q80VZ2.
    KOi K05105.
    OMAi DWIPREG.
    OrthoDBi EOG7VTDM6.
    TreeFami TF315608.

    Enzyme and pathway databases

    BRENDAi 2.7.10.1. 3474.

    Miscellaneous databases

    EvolutionaryTracei Q03137.
    NextBioi 284664.
    PROi Q03137.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q03137.
    Bgeei Q03137.
    CleanExi MM_EPHA4.
    Genevestigatori Q03137.

    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.
    IPR013783. Ig-like_fold.
    IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR001660. SAM.
    IPR013761. SAM/pointed.
    IPR011510. SAM_2.
    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.
    PF07647. SAM_2. 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.
    PROSITEi 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

    1. "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] (ISOFORM LONG).
      Strain: C57BL/6.
      Tissue: Embryonic brain.
    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] (ISOFORM LONG).
      Strain: C57BL/6J.
    3. 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].
    4. "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] (ISOFORM LONG).
      Tissue: Limb.
    5. "A juxtamembrane autophosphorylation site in the Eph family receptor tyrosine kinase, Sek, mediates high affinity interaction with p59fyn."
      Ellis C., Kasmi F., Ganju P., Walls E., Panayotou G., Reith A.D.
      Oncogene 12:1727-1736(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-596 AND TYR-602, INTERACTION WITH FYN.
    6. "EphA4 (Sek1) receptor tyrosine kinase is required for the development of the corticospinal tract."
      Dottori M., Hartley L., Galea M., Paxinos G., Polizzotto M., Kilpatrick T., Bartlett P.F., Murphy M., Koentgen F., Boyd A.W.
      Proc. Natl. Acad. Sci. U.S.A. 95:13248-13253(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE, FUNCTION IN AXON GUIDANCE.
    7. "EphA receptors regulate growth cone dynamics through the novel guanine nucleotide exchange factor ephexin."
      Shamah S.M., Lin M.Z., Goldberg J.L., Estrach S., Sahin M., Hu L., Bazalakova M., Neve R.L., Corfas G., Debant A., Greenberg M.E.
      Cell 105:233-244(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NGEF, MUTAGENESIS OF VAL-635.
    8. "Developmental expression of EphA4-tyrosine kinase receptor in the mouse brain and spinal cord."
      Greferath U., Canty A.J., Messenger J., Murphy M.
      Mech. Dev. 119:S231-S238(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: DEVELOPMENTAL STAGE.
    9. "Axonal regeneration and lack of astrocytic gliosis in EphA4-deficient mice."
      Goldshmit Y., Galea M.P., Wise G., Bartlett P.F., Turnley A.M.
      J. Neurosci. 24:10064-10073(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE, FUNCTION IN AXONAL REGENERATION.
    10. "EphA4 regulates central nervous system vascular formation."
      Goldshmit Y., Galea M.P., Bartlett P.F., Turnley A.M.
      J. Comp. Neurol. 497:864-875(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN ANGIOGENESIS.
    11. Cited for: DISRUPTION PHENOTYPE, FUNCTION IN THYMUS DEVELOPMENT.
    12. "Rac-GAP alpha-chimerin regulates motor-circuit formation as a key mediator of EphrinB3/EphA4 forward signaling."
      Iwasato T., Katoh H., Nishimaru H., Ishikawa Y., Inoue H., Saito Y.M., Ando R., Iwama M., Takahashi R., Negishi M., Itohara S.
      Cell 130:742-753(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN RAC1 REGULATION, FUNCTION IN AXON GUIDANCE, INTERACTION WITH CHN1.
    13. "The EphA4 receptor regulates neuronal morphology through SPAR-mediated inactivation of Rap GTPases."
      Richter M., Murai K.K., Bourgin C., Pak D.T., Pasquale E.B.
      J. Neurosci. 27:14205-14215(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN NEURON MORPHOLOGY, INTERACTION WITH SIPA1L1.
    14. "Cdk5 regulates EphA4-mediated dendritic spine retraction through an ephexin1-dependent mechanism."
      Fu W.Y., Chen Y., Sahin M., Zhao X.S., Shi L., Bikoff J.B., Lai K.O., Yung W.H., Fu A.K., Greenberg M.E., Ip N.Y.
      Nat. Neurosci. 10:67-76(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN DENDRITIC SPINE MORPHOGENESIS, TOPOLOGY, SUBCELLULAR LOCATION, INTERACTION WITH NGEF.
    15. "alpha2-Chimaerin is an essential EphA4 effector in the assembly of neuronal locomotor circuits."
      Beg A.A., Sommer J.E., Martin J.H., Scheiffele P.
      Neuron 55:768-778(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN AXON GUIDANCE, INTERACTION WITH CHN1, MUTAGENESIS OF VAL-635.
    16. "Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
      Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
      J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-602, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Brain.
    17. "Segregation of axial motor and sensory pathways via heterotypic trans-axonal signaling."
      Gallarda B.W., Bonanomi D., Mueller D., Brown A., Alaynick W.A., Andrews S.E., Lemke G., Pfaff S.L., Marquardt T.
      Science 320:233-236(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN MOTOR AND SENSORY AXONS SEGREGATION.

    Entry informationi

    Entry nameiEPHA4_MOUSE
    AccessioniPrimary (citable) accession number: Q03137
    Secondary accession number(s): Q80VZ2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1994
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 163 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