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Q03137

- EPHA4_MOUSE

UniProt

Q03137 - EPHA4_MOUSE

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Protein
Ephrin type-A receptor 4
Gene
Epha4, Sek, Sek1
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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. Beside 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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei653 – 6531ATP By similarity
Active sitei746 – 7461Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi627 – 6359ATP By similarity

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 JUN kinase activity Source: BHF-UCL
  12. positive regulation of Rho guanyl-nucleotide exchange factor activity Source: UniProtKB
  13. positive regulation of dendrite morphogenesis Source: Ensembl
  14. protein autophosphorylation Source: UniProtKB
  15. regulation of Rac GTPase activity Source: UniProtKB
  16. regulation of Rap GTPase activity Source: UniProtKB
  17. regulation of astrocyte differentiation Source: UniProtKB
  18. regulation of axonogenesis Source: UniProtKB
  19. regulation of dendritic spine morphogenesis Source: UniProtKB
Complete GO annotation...

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini20 – 547528Extracellular Reviewed prediction
Add
BLAST
Transmembranei548 – 56922Helical; Reviewed prediction
Add
BLAST
Topological domaini570 – 986417Cytoplasmic Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. Golgi apparatus Source: Ensembl
  2. axon Source: UniProtKB
  3. axon terminus Source: Ensembl
  4. axonal growth cone Source: Ensembl
  5. cell junction Source: UniProtKB-KW
  6. cell surface Source: Ensembl
  7. cytoplasm Source: UniProtKB
  8. dendrite Source: UniProtKB
  9. dendritic spine Source: Ensembl
  10. early endosome membrane Source: UniProtKB
  11. endoplasmic reticulum Source: Ensembl
  12. filopodium 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
Complete GO annotation...

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 – 1919 Reviewed prediction
Add
BLAST
Chaini20 – 986967Ephrin type-A receptor 4
PRO_0000016808Add
BLAST

Amino acid modifications

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

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

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.

Miscellaneous databases

EvolutionaryTraceiQ03137.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini30 – 209180Eph LBD
Add
BLAST
Domaini328 – 439112Fibronectin type-III 1
Add
BLAST
Domaini440 – 53798Fibronectin type-III 2
Add
BLAST
Domaini621 – 882262Protein kinase
Add
BLAST
Domaini911 – 97565SAM
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi984 – 9863PDZ-binding Reviewed prediction

Compositional bias

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

Domaini

The protein kinase domain mediates interaction with NGEF.

Sequence similaritiesi

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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei783 – 83250Missing in isoform Short.
VSP_002998Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti145 – 1451I → T in CAA46268. 1 Publication
Sequence conflicti145 – 1451I → T in AAB25836. 1 Publication

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

« Hide 'large scale' publications
  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: July 9, 2014
This is version 162 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

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