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P54764

- EPHA4_HUMAN

UniProt

P54764 - EPHA4_HUMAN

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Protein
Ephrin type-A receptor 4
Gene
EPHA4, HEK8, SEK, TYRO1
Organism
Homo sapiens (Human)
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.1 Publication

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. PH domain binding Source: UniProtKB
  5. ephrin receptor activity Source: InterPro
  6. protein binding Source: UniProtKB
  7. protein kinase activity Source: UniProtKB
  8. transmembrane-ephrin receptor activity Source: UniProtKB

GO - Biological processi

  1. adult walking behavior Source: Ensembl
  2. cell adhesion Source: UniProtKB-KW
  3. corticospinal tract morphogenesis Source: UniProtKB
  4. fasciculation of motor neuron axon Source: UniProtKB
  5. fasciculation of sensory neuron axon Source: UniProtKB
  6. glial cell migration Source: Ensembl
  7. motor neuron axon guidance Source: UniProtKB
  8. negative regulation of axon regeneration Source: UniProtKB
  9. peptidyl-tyrosine phosphorylation Source: UniProtKB
  10. positive regulation of JUN kinase activity Source: Ensembl
  11. positive regulation of Rho guanyl-nucleotide exchange factor activity Source: UniProtKB
  12. positive regulation of dendrite morphogenesis Source: Ensembl
  13. protein autophosphorylation Source: UniProtKB
  14. regulation of Rac GTPase activity Source: UniProtKB
  15. regulation of Rap GTPase activity Source: UniProtKB
  16. regulation of astrocyte differentiation Source: UniProtKB
  17. regulation of axonogenesis Source: UniProtKB
  18. 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. 2681.
SignaLinkiP54764.

Names & Taxonomyi

Protein namesi
Recommended name:
Ephrin type-A receptor 4 (EC:2.7.10.1)
Alternative name(s):
EPH-like kinase 8
Short name:
EK8
Short name:
hEK8
Tyrosine-protein kinase TYRO1
Tyrosine-protein kinase receptor SEK
Gene namesi
Name:EPHA4
Synonyms:HEK8, SEK, TYRO1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:3388. EPHA4.

Subcellular locationi

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

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: InterPro
  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

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi40 – 401Q → A: 10-fold reduced affinity for EFNB2; when associated with A-42. 1 Publication
Mutagenesisi42 – 421E → A: 10-fold reduced affinity for EFNB2; when associated with A-40. 1 Publication

Organism-specific databases

PharmGKBiPA27820.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919 Reviewed prediction
Add
BLAST
Chaini20 – 986967Ephrin type-A receptor 4
PRO_0000016807Add
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
Glycosylationi545 – 5451N-linked (GlcNAc...) Reviewed prediction
Modified residuei596 – 5961Phosphotyrosine; by autocatalysis By similarity
Modified residuei602 – 6021Phosphotyrosine; by autocatalysis By similarity
Modified residuei779 – 7791Phosphotyrosine; by autocatalysis Reviewed prediction
Modified residuei928 – 9281Phosphotyrosine; by autocatalysis Reviewed prediction

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiP54764.
PaxDbiP54764.
PeptideAtlasiP54764.
PRIDEiP54764.

PTM databases

PhosphoSiteiP54764.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

ArrayExpressiP54764.
BgeeiP54764.
CleanExiHS_EPHA4.
GenevestigatoriP54764.

Organism-specific databases

HPAiCAB004654.

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 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 By similarity. 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.1 Publication

Protein-protein interaction databases

BioGridi108357. 13 interactions.
DIPiDIP-48294N.
IntActiP54764. 2 interactions.
STRINGi9606.ENSP00000281821.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi30 – 356
Helixi36 – 383
Turni40 – 423
Beta strandi46 – 6116
Beta strandi65 – 739
Beta strandi76 – 783
Beta strandi82 – 854
Beta strandi93 – 964
Beta strandi97 – 1059
Helixi108 – 1103
Turni115 – 1173
Beta strandi120 – 13011
Beta strandi131 – 1333
Helixi139 – 1413
Beta strandi143 – 1497
Beta strandi154 – 1574
Turni159 – 1624
Beta strandi164 – 17310
Beta strandi178 – 18912
Beta strandi191 – 20212
Beta strandi207 – 2093
Beta strandi212 – 2143
Beta strandi226 – 2305
Beta strandi237 – 24812
Beta strandi257 – 2626
Beta strandi266 – 2694
Beta strandi272 – 2754
Beta strandi304 – 3063
Beta strandi333 – 3408
Beta strandi343 – 3497
Beta strandi361 – 3688
Turni373 – 3753
Beta strandi385 – 3884
Beta strandi390 – 3934
Beta strandi395 – 4017
Beta strandi405 – 41612
Beta strandi418 – 4236
Helixi426 – 4283
Beta strandi429 – 4357
Beta strandi447 – 4526
Beta strandi457 – 4615
Beta strandi473 – 48311
Beta strandi489 – 50012
Beta strandi508 – 51710
Beta strandi528 – 5314
Turni538 – 5403

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2LW8NMR-A29-209[»]
2WO1X-ray1.85A/B30-202[»]
2WO2X-ray2.45A30-202[»]
2WO3X-ray2.35A30-202[»]
3CKHX-ray2.80A/B29-209[»]
3GXUX-ray2.50A29-203[»]
4BK4X-ray3.65A/B20-547[»]
4BK5X-ray4.00A20-547[»]
4BKAX-ray5.30A20-547[»]
4BKFX-ray4.65A/B20-547[»]
4M4PX-ray2.08A27-543[»]
4M4RX-ray3.13A/C/E/G27-543[»]
ProteinModelPortaliP54764.
SMRiP54764. Positions 27-981.

Miscellaneous databases

EvolutionaryTraceiP54764.

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 By similarity.

Sequence similaritiesi

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0515.
HOGENOMiHOG000233856.
HOVERGENiHBG062180.
InParanoidiP54764.
KOiK05105.
OMAiDWIPREG.
PhylomeDBiP54764.
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]

Sequencei

Sequence statusi: Complete.

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

P54764-1 [UniParc]FASTAAdd to Basket

« Hide

MAGIFYFALF SCLFGICDAV TGSRVYPANE VTLLDSRSVQ GELGWIASPL    50
EGGWEEVSIM DEKNTPIRTY QVCNVMEPSQ NNWLRTDWIT REGAQRVYIE 100
IKFTLRDCNS LPGVMGTCKE TFNLYYYESD NDKERFIREN QFVKIDTIAA 150
DESFTQVDIG DRIMKLNTEI RDVGPLSKKG FYLAFQDVGA CIALVSVRVF 200
YKKCPLTVRN LAQFPDTITG ADTSSLVEVR GSCVNNSEEK DVPKMYCGAD 250
GEWLVPIGNC LCNAGHEERS GECQACKIGY YKALSTDATC AKCPPHSYSV 300
WEGATSCTCD RGFFRADNDA ASMPCTRPPS APLNLISNVN ETSVNLEWSS 350
PQNTGGRQDI SYNVVCKKCG AGDPSKCRPC GSGVHYTPQQ NGLKTTKVSI 400
TDLLAHTNYT FEIWAVNGVS KYNPNPDQSV 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 TGTESSRPNT 900
ALLDPSSPEF SAVVSVGDWL QAIKMDRYKD NFTAAGYTTL EAVVHVNQED 950
LARIGITAIT HQNKILSSVQ AMRTQMQQMH GRMVPV 986
Length:986
Mass (Da):109,860
Last modified:October 1, 1996 - v1
Checksum:i0C39C1152EDDD46F
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti269 – 2691R → Q.1 Publication
Corresponds to variant rs35084379 [ dbSNP | Ensembl ].
VAR_042135
Natural varianti370 – 3701G → E in a bladder carcinoma NOS sample; somatic mutation. 1 Publication
VAR_042136
Natural varianti399 – 3991S → F in a metastatic melanoma sample; somatic mutation. 1 Publication
VAR_042137
Natural varianti953 – 9531R → K.
Corresponds to variant rs35341687 [ dbSNP | Ensembl ].
VAR_049721

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti71 – 711Q → P in BAF82995. 1 Publication
Sequence conflicti102 – 1021K → R in BAF82995. 1 Publication
Sequence conflicti137 – 1371I → V in BAG35298. 1 Publication
Sequence conflicti362 – 3621Y → H in BAF82995. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L36645 mRNA. Translation: AAA74246.1.
AK290306 mRNA. Translation: BAF82995.1.
AK312380 mRNA. Translation: BAG35298.1.
BC105000 mRNA. Translation: AAI05001.1.
BC105002 mRNA. Translation: AAI05003.1.
CCDSiCCDS2447.1.
PIRiI78844.
RefSeqiNP_004429.1. NM_004438.3.
UniGeneiHs.371218.

Genome annotation databases

EnsembliENST00000281821; ENSP00000281821; ENSG00000116106.
ENST00000409938; ENSP00000386829; ENSG00000116106.
GeneIDi2043.
KEGGihsa:2043.
UCSCiuc002vmq.3. human.

Polymorphism databases

DMDMi1711371.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L36645 mRNA. Translation: AAA74246.1 .
AK290306 mRNA. Translation: BAF82995.1 .
AK312380 mRNA. Translation: BAG35298.1 .
BC105000 mRNA. Translation: AAI05001.1 .
BC105002 mRNA. Translation: AAI05003.1 .
CCDSi CCDS2447.1.
PIRi I78844.
RefSeqi NP_004429.1. NM_004438.3.
UniGenei Hs.371218.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2LW8 NMR - A 29-209 [» ]
2WO1 X-ray 1.85 A/B 30-202 [» ]
2WO2 X-ray 2.45 A 30-202 [» ]
2WO3 X-ray 2.35 A 30-202 [» ]
3CKH X-ray 2.80 A/B 29-209 [» ]
3GXU X-ray 2.50 A 29-203 [» ]
4BK4 X-ray 3.65 A/B 20-547 [» ]
4BK5 X-ray 4.00 A 20-547 [» ]
4BKA X-ray 5.30 A 20-547 [» ]
4BKF X-ray 4.65 A/B 20-547 [» ]
4M4P X-ray 2.08 A 27-543 [» ]
4M4R X-ray 3.13 A/C/E/G 27-543 [» ]
ProteinModelPortali P54764.
SMRi P54764. Positions 27-981.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108357. 13 interactions.
DIPi DIP-48294N.
IntActi P54764. 2 interactions.
STRINGi 9606.ENSP00000281821.

Chemistry

BindingDBi P54764.
ChEMBLi CHEMBL3988.
GuidetoPHARMACOLOGYi 1824.

PTM databases

PhosphoSitei P54764.

Polymorphism databases

DMDMi 1711371.

Proteomic databases

MaxQBi P54764.
PaxDbi P54764.
PeptideAtlasi P54764.
PRIDEi P54764.

Protocols and materials databases

DNASUi 2043.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000281821 ; ENSP00000281821 ; ENSG00000116106 .
ENST00000409938 ; ENSP00000386829 ; ENSG00000116106 .
GeneIDi 2043.
KEGGi hsa:2043.
UCSCi uc002vmq.3. human.

Organism-specific databases

CTDi 2043.
GeneCardsi GC02M222248.
HGNCi HGNC:3388. EPHA4.
HPAi CAB004654.
MIMi 602188. gene.
neXtProti NX_P54764.
PharmGKBi PA27820.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
HOGENOMi HOG000233856.
HOVERGENi HBG062180.
InParanoidi P54764.
KOi K05105.
OMAi DWIPREG.
PhylomeDBi P54764.
TreeFami TF315608.

Enzyme and pathway databases

BRENDAi 2.7.10.1. 2681.
SignaLinki P54764.

Miscellaneous databases

ChiTaRSi EPHA4. human.
EvolutionaryTracei P54764.
GeneWikii EPH_receptor_A4.
GenomeRNAii 2043.
NextBioi 35463929.
PROi P54764.
SOURCEi Search...

Gene expression databases

ArrayExpressi P54764.
Bgeei P54764.
CleanExi HS_EPHA4.
Genevestigatori P54764.

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. "cDNA cloning and tissue distribution of five human EPH-like receptor protein-tyrosine kinases."
    Fox G.M., Holst P.L., Chute H.T., Lindberg R.A., Janssen A.M., Basu R., Welcher A.A.
    Oncogene 10:897-905(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Fetal brain.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Amygdala and Tongue.
  3. "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].
    Tissue: Brain.
  4. "Unified nomenclature for Eph family receptors and their ligands, the ephrins."
    Eph nomenclature committee
    Cell 90:403-404(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NOMENCLATURE.
  5. "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: INTERACTION WITH SIPA1L1.
  6. "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 PHOSPHORYLATION OF CDK5, AUTOPHOSPHORYLATION.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "Crystal structure and NMR binding reveal that two small molecule antagonists target the high affinity ephrin-binding channel of the EphA4 receptor."
    Qin H., Shi J., Noberini R., Pasquale E.B., Song J.
    J. Biol. Chem. 283:29473-29484(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 29-209.
  9. "Structural plasticity of EPH receptor A4 facilitates cross-class ephrin signaling."
    Bowden T.A., Aricescu A.R., Nettleship J.E., Siebold C., Rahman-Huq N., Owens R.J., Stuart D.I., Jones E.Y.
    Structure 17:1386-1397(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 30-202 IN COMPLEX WITH EFNA2 OR EFNB2, LIGAND-BINDING.
  10. "Structural characterization of the EphA4-Ephrin-B2 complex reveals new features enabling Eph-ephrin binding promiscuity."
    Qin H., Noberini R., Huan X., Shi J., Pasquale E.B., Song J.
    J. Biol. Chem. 285:644-654(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 29-203 IN COMPLEX WITH EFNB2, MUTAGENESIS OF GLN-40 AND GLU-42.
  11. "Patterns of somatic mutation in human cancer genomes."
    Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
    , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
    Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS [LARGE SCALE ANALYSIS] GLN-269; GLU-370 AND PHE-399.

Entry informationi

Entry nameiEPHA4_HUMAN
AccessioniPrimary (citable) accession number: P54764
Secondary accession number(s): A8K2P1, B2R601, Q2M380
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: September 3, 2014
This is version 155 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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