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Q03137 (EPHA4_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 162. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Epha4
Synonyms:Sek, Sek1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length986 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.7 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.18

Catalytic activity

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

Subunit structure

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. Ref.6 Ref.8 Ref.13 Ref.14 Ref.15 Ref.16

Subcellular location

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. Ref.15

Tissue specificity

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 stage

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. Ref.9

Domain

The protein kinase domain mediates interaction with NGEF.

Disruption phenotype

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. Ref.7 Ref.10 Ref.12

Sequence similarities

Belongs to the protein kinase superfamily. Tyr protein kinase family. Ephrin receptor subfamily.

Contains 1 Eph LBD (Eph ligand-binding) domain.

Contains 2 fibronectin type-III domains.

Contains 1 protein kinase domain.

Contains 1 SAM (sterile alpha motif) domain.

Ontologies

Keywords
   Biological processCell adhesion
Neurogenesis
   Cellular componentCell junction
Cell membrane
Cell projection
Endosome
Membrane
Postsynaptic cell membrane
Synapse
   Coding sequence diversityAlternative splicing
   DomainRepeat
Signal
Transmembrane
Transmembrane helix
   LigandATP-binding
Nucleotide-binding
   Molecular functionDevelopmental protein
Kinase
Receptor
Transferase
Tyrosine-protein kinase
   PTMGlycoprotein
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processadult walking behavior

Inferred from mutant phenotype PubMed 12649481. Source: MGI

axon guidance

Inferred from mutant phenotype PubMed 12649481. Source: MGI

cell adhesion

Inferred from electronic annotation. Source: UniProtKB-KW

corticospinal tract morphogenesis

Inferred from mutant phenotype Ref.7. Source: UniProtKB

fasciculation of motor neuron axon

Inferred from mutant phenotype Ref.18. Source: UniProtKB

fasciculation of sensory neuron axon

Inferred from mutant phenotype Ref.18. Source: UniProtKB

glial cell migration

Inferred from electronic annotation. Source: Ensembl

motor neuron axon guidance

Inferred from mutant phenotype Ref.16. Source: UniProtKB

negative regulation of axon regeneration

Inferred from mutant phenotype Ref.10. Source: UniProtKB

peptidyl-tyrosine phosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of JUN kinase activity

Inferred from direct assay PubMed 10523642. Source: BHF-UCL

positive regulation of Rho guanyl-nucleotide exchange factor activity

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of dendrite morphogenesis

Inferred from electronic annotation. Source: Ensembl

protein autophosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of Rac GTPase activity

Inferred from direct assay Ref.13. Source: UniProtKB

regulation of Rap GTPase activity

Inferred from mutant phenotype Ref.14. Source: UniProtKB

regulation of astrocyte differentiation

Inferred from mutant phenotype Ref.10. Source: UniProtKB

regulation of axonogenesis

Inferred from mutant phenotype Ref.10. Source: UniProtKB

regulation of dendritic spine morphogenesis

Inferred from mutant phenotype Ref.15. Source: UniProtKB

   Cellular_componentGolgi apparatus

Inferred from electronic annotation. Source: Ensembl

axon

Inferred from direct assay Ref.15. Source: UniProtKB

axon terminus

Inferred from electronic annotation. Source: Ensembl

axonal growth cone

Inferred from electronic annotation. Source: Ensembl

cell junction

Inferred from electronic annotation. Source: UniProtKB-KW

cell surface

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

dendrite

Inferred from direct assay Ref.15. Source: UniProtKB

dendritic spine

Inferred from electronic annotation. Source: Ensembl

early endosome membrane

Inferred from direct assay Ref.15. Source: UniProtKB

endoplasmic reticulum

Inferred from electronic annotation. Source: Ensembl

filopodium

Inferred from electronic annotation. Source: Ensembl

integral component of plasma membrane

Inferred from direct assay Ref.15. Source: UniProtKB

mitochondrial outer membrane

Inferred from electronic annotation. Source: Ensembl

neuromuscular junction

Inferred from electronic annotation. Source: Ensembl

perikaryon

Inferred from electronic annotation. Source: Ensembl

postsynaptic density

Inferred from electronic annotation. Source: UniProtKB-SubCell

postsynaptic membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

DH domain binding

Inferred from sequence or structural similarity. Source: UniProtKB

GPI-linked ephrin receptor activity

Inferred from mutant phenotype Ref.15Ref.14. Source: UniProtKB

identical protein binding

Inferred from physical interaction PubMed 16977320. Source: IntAct

protein binding

Inferred from physical interaction Ref.15Ref.13Ref.16Ref.14. Source: UniProtKB

protein kinase activity

Inferred from sequence or structural similarity. Source: UniProtKB

transmembrane-ephrin receptor activity

Inferred from direct assay Ref.13. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform Long (identifier: Q03137-1)

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.
Isoform Short (identifier: Q03137-2)

The sequence of this isoform differs from the canonical sequence as follows:
     783-832: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Potential
Chain20 – 986967Ephrin type-A receptor 4
PRO_0000016808

Regions

Topological domain20 – 547528Extracellular Potential
Transmembrane548 – 56922Helical; Potential
Topological domain570 – 986417Cytoplasmic Potential
Domain30 – 209180Eph LBD
Domain328 – 439112Fibronectin type-III 1
Domain440 – 53798Fibronectin type-III 2
Domain621 – 882262Protein kinase
Domain911 – 97565SAM
Nucleotide binding627 – 6359ATP By similarity
Motif984 – 9863PDZ-binding Potential
Compositional bias191 – 325135Cys-rich

Sites

Active site7461Proton acceptor By similarity
Binding site6531ATP By similarity

Amino acid modifications

Modified residue5961Phosphotyrosine; by autocatalysis Ref.6
Modified residue6021Phosphotyrosine; by autocatalysis Ref.6 Ref.17
Modified residue7791Phosphotyrosine; by autocatalysis Potential
Modified residue9281Phosphotyrosine; by autocatalysis Potential
Glycosylation2351N-linked (GlcNAc...) Potential
Glycosylation3401N-linked (GlcNAc...) Potential
Glycosylation4081N-linked (GlcNAc...) Potential
Glycosylation4231N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence783 – 83250Missing in isoform Short.
VSP_002998

Experimental info

Mutagenesis6351V → M: Kinase dead; loss of autophosphorylation and loss of CHN1 phosphorylation. No effect on interaction with NGEF. Ref.8 Ref.16
Sequence conflict1451I → T in CAA46268. Ref.1
Sequence conflict1451I → T in AAB25836. Ref.1

Secondary structure

........................................................ 986
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform Long [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 89BEB2C7CDB54A55

FASTA986109,814
        10         20         30         40         50         60 
MAGIFYFILF SFLFGICDAV TGSRVYPANE VTLLDSRSVQ GELGWIASPL EGGWEEVSIM 

        70         80         90        100        110        120 
DEKNTPIRTY QVCNVMEASQ NNWLRTDWIT REGAQRVYIE IKFTLRDCNS LPGVMGTCKE 

       130        140        150        160        170        180 
TFNLYYYESD NDKERFIRES QFGKIDTIAA DESFTQVDIG DRIMKLNTEI RDVGPLSKKG 

       190        200        210        220        230        240 
FYLAFQDVGA CIALVSVRVF YKKCPLTVRN LAQFPDTITG ADTSSLVEVR GSCVNNSEEK 

       250        260        270        280        290        300 
DVPKMYCGAD GEWLVPIGNC LCNAGHEEQN GECQACKIGY YKALSTDASC AKCPPHSYSV 

       310        320        330        340        350        360 
WEGATSCTCD RGFFRADNDA ASMPCTRPPS APLNLISNVN ETSVNLEWSS PQNTGGRQDI 

       370        380        390        400        410        420 
SYNVVCKKCG AGDPSKCRPC GSGVHYTPQQ NGLKTTRVSI TDLLAHTNYT FEIWAVNGVS 

       430        440        450        460        470        480 
KYNPSPDQSV SVTVTTNQAA PSSIALVQAK EVTRYSVALA WLEPDRPNGV ILEYEVKYYE 

       490        500        510        520        530        540 
KDQNERSYRI VRTAARNTDI KGLNPLTSYV FHVRARTAAG YGDFSEPLEV TTNTVPSRII 

       550        560        570        580        590        600 
GDGANSTVLL VSVSGSVVLV VILIAAFVIS RRRSKYSKAK QEADEEKHLN QGVRTYVDPF 

       610        620        630        640        650        660 
TYEDPNQAVR EFAKEIDASC IKIEKVIGVG EFGEVCSGRL KVPGKREICV AIKTLKAGYT 

       670        680        690        700        710        720 
DKQRRDFLSE ASIMGQFDHP NIIHLEGVVT KCKPVMIITE YMENGSLDAF LRKNDGRFTV 

       730        740        750        760        770        780 
IQLVGMLRGI GSGMKYLSDM SYVHRDLAAR NILVNSNLVC KVSDFGMSRV LEDDPEAAYT 

       790        800        810        820        830        840 
TRGGKIPIRW TAPEAIAYRK FTSASDVWSY GIVMWEVMSY GERPYWDMSN QDVIKAIEEG 

       850        860        870        880        890        900 
YRLPPPMDCP IALHQLMLDC WQKERSDRPK FGQIVNMLDK LIRNPNSLKR TGSESSRPNT 

       910        920        930        940        950        960 
ALLDPSSPEF SAVVSVGDWL QAIKMDRYKD NFTAAGYTTL EAVVHMSQDD LARIGITAIT 

       970        980 
HQNKILSSVQ AMRTQMQQMH GRMVPV 

« Hide

Isoform Short [UniParc].

Checksum: 3C3EFE4620316DB2
Show »

FASTA936103,984

References

« Hide 'large scale' references
[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]Erratum
Gilardi-Hebenstreit P., Nieto M.A., Frain M., Mattei M.-G., Chestier A., Wilkinson D.G., Charnay P.
Oncogene 8:1103-1103(1993) [PubMed] [Europe PMC] [Abstract]
[3]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , 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.
[4]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].
[5]"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.
[6]"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.
[7]"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.
[8]"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.
[9]"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.
[10]"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.
[11]"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.
[12]"Thymic alterations in EphA4-deficient mice."
Munoz J.J., Alfaro D., Garcia-Ceca J., Alonso-C L.M., Jimenez E., Zapata A.
J. Immunol. 177:804-813(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE, FUNCTION IN THYMUS DEVELOPMENT.
[13]"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.
[14]"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.
[15]"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.
[16]"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.
[17]"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.
[18]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS35627.1. [Q03137-1]
PIRS78059.
RefSeqNP_031962.2. NM_007936.3. [Q03137-1]
UniGeneMm.400747.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalQ03137.
SMRQ03137. Positions 27-981.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid199471. 2 interactions.
DIPDIP-1019N.
IntActQ03137. 7 interactions.
MINTMINT-3381444.

Chemistry

BindingDBQ03137.
ChEMBLCHEMBL1293259.

PTM databases

PhosphoSiteQ03137.

Proteomic databases

MaxQBQ03137.
PaxDbQ03137.
PRIDEQ03137.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000027451; ENSMUSP00000027451; ENSMUSG00000026235. [Q03137-1]
GeneID13838.
KEGGmmu:13838.
UCSCuc007bpz.1. mouse. [Q03137-1]

Organism-specific databases

CTD2043.
MGIMGI:98277. Epha4.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00750000117255.
HOGENOMHOG000233856.
HOVERGENHBG062180.
InParanoidQ80VZ2.
KOK05105.
OMADWIPREG.
OrthoDBEOG7VTDM6.
TreeFamTF315608.

Enzyme and pathway databases

BRENDA2.7.10.1. 3474.

Gene expression databases

ArrayExpressQ03137.
BgeeQ03137.
CleanExMM_EPHA4.
GenevestigatorQ03137.

Family and domain databases

Gene3D1.10.150.50. 1 hit.
2.60.120.260. 1 hit.
2.60.40.10. 2 hits.
InterProIPR027936. 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]
PfamPF14575. 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]
PIRSFPIRSF000666. TyrPK_ephrin_receptor. 1 hit.
PRINTSPR00109. TYRKINASE.
SMARTSM00615. EPH_lbd. 1 hit.
SM00060. FN3. 2 hits.
SM00454. SAM. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMSSF47769. SSF47769. 1 hit.
SSF49265. SSF49265. 1 hit.
SSF49785. SSF49785. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEPS51550. 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]
ProtoNetSearch...

Other

EvolutionaryTraceQ03137.
NextBio284664.
PROQ03137.
SOURCESearch...

Entry information

Entry nameEPHA4_MOUSE
AccessionPrimary (citable) accession number: Q03137
Secondary accession number(s): Q80VZ2
Entry history
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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot