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Protein

Ephrin type-A receptor 4

Gene

EPHA4

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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. 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.1 Publication

Catalytic activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei653ATPPROSITE-ProRule annotation1
Active sitei746Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi627 – 635ATPPROSITE-ProRule annotation9

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • DH domain binding Source: UniProtKB
  • GPI-linked ephrin receptor activity Source: UniProtKB
  • PH domain binding Source: UniProtKB
  • protein kinase activity Source: UniProtKB
  • transmembrane-ephrin receptor activity Source: UniProtKB

GO - Biological processi

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

BioCyciZFISH:HS03980-MONOMER.
BRENDAi2.7.10.1. 2681.
ReactomeiR-HSA-2682334. EPH-Ephrin signaling.
R-HSA-3928663. EPHA-mediated growth cone collapse.
R-HSA-3928665. EPH-ephrin mediated repulsion of cells.
SignaLinkiP54764.
SIGNORiP54764.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:3388. EPHA4.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini20 – 547ExtracellularSequence analysisAdd BLAST528
Transmembranei548 – 569HelicalSequence analysisAdd BLAST22
Topological domaini570 – 986CytoplasmicSequence analysisAdd BLAST417

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi40Q → A: 10-fold reduced affinity for EFNB2; when associated with A-42. 1 Publication1
Mutagenesisi42E → A: 10-fold reduced affinity for EFNB2; when associated with A-40. 1 Publication1

Organism-specific databases

DisGeNETi2043.
OpenTargetsiENSG00000116106.
PharmGKBiPA27820.

Chemistry databases

ChEMBLiCHEMBL3988.
GuidetoPHARMACOLOGYi1824.

Polymorphism and mutation databases

BioMutaiEPHA4.
DMDMi1711371.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 19Sequence analysisAdd BLAST19
ChainiPRO_000001680720 – 986Ephrin type-A receptor 4Add BLAST967

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi235N-linked (GlcNAc...)Sequence analysis1
Glycosylationi340N-linked (GlcNAc...)Sequence analysis1
Glycosylationi408N-linked (GlcNAc...)Sequence analysis1
Glycosylationi545N-linked (GlcNAc...)Sequence analysis1
Modified residuei596Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei602Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei779Phosphotyrosine; by autocatalysisSequence analysis1
Modified residuei928Phosphotyrosine; by autocatalysisSequence analysis1

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

EPDiP54764.
MaxQBiP54764.
PaxDbiP54764.
PeptideAtlasiP54764.
PRIDEiP54764.
TopDownProteomicsiP54764-1. [P54764-1]

PTM databases

iPTMnetiP54764.
PhosphoSitePlusiP54764.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

BgeeiENSG00000116106.
CleanExiHS_EPHA4.
ExpressionAtlasiP54764. baseline and differential.
GenevisibleiP54764. HS.

Organism-specific databases

HPAiCAB028368.

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.By similarity3 Publications

GO - Molecular functioni

  • DH domain binding Source: UniProtKB
  • PH domain binding Source: UniProtKB

Protein-protein interaction databases

BioGridi108357. 38 interactors.
DIPiDIP-48294N.
IntActiP54764. 2 interactors.
STRINGi9606.ENSP00000281821.

Chemistry databases

BindingDBiP54764.

Structurei

Secondary structure

1986
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi30 – 35Combined sources6
Helixi36 – 38Combined sources3
Turni40 – 42Combined sources3
Beta strandi46 – 60Combined sources15
Beta strandi62 – 65Combined sources4
Beta strandi66 – 73Combined sources8
Beta strandi77 – 79Combined sources3
Beta strandi82 – 85Combined sources4
Beta strandi93 – 96Combined sources4
Beta strandi97 – 105Combined sources9
Helixi108 – 110Combined sources3
Turni115 – 117Combined sources3
Beta strandi120 – 130Combined sources11
Beta strandi131 – 133Combined sources3
Helixi139 – 141Combined sources3
Beta strandi143 – 149Combined sources7
Beta strandi154 – 158Combined sources5
Turni159 – 162Combined sources4
Beta strandi163 – 173Combined sources11
Beta strandi178 – 189Combined sources12
Beta strandi191 – 202Combined sources12
Beta strandi207 – 209Combined sources3
Beta strandi212 – 214Combined sources3
Beta strandi226 – 230Combined sources5
Beta strandi237 – 248Combined sources12
Beta strandi257 – 262Combined sources6
Beta strandi266 – 269Combined sources4
Beta strandi272 – 275Combined sources4
Beta strandi304 – 306Combined sources3
Beta strandi333 – 340Combined sources8
Beta strandi343 – 349Combined sources7
Beta strandi361 – 368Combined sources8
Turni373 – 375Combined sources3
Beta strandi385 – 388Combined sources4
Beta strandi390 – 393Combined sources4
Beta strandi395 – 401Combined sources7
Beta strandi405 – 416Combined sources12
Beta strandi418 – 423Combined sources6
Helixi426 – 428Combined sources3
Beta strandi429 – 435Combined sources7
Beta strandi447 – 452Combined sources6
Beta strandi457 – 461Combined sources5
Beta strandi473 – 483Combined sources11
Beta strandi489 – 500Combined sources12
Beta strandi508 – 517Combined sources10
Beta strandi528 – 531Combined sources4
Turni538 – 540Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4W4ZX-ray2.41A/B/C/D29-204[»]
4W50X-ray2.42A/B/C/D29-204[»]
5JR2X-ray1.75A/B/C/D29-204[»]
ProteinModelPortaliP54764.
SMRiP54764.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP54764.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini30 – 209Eph LBDPROSITE-ProRule annotationAdd BLAST180
Domaini328 – 439Fibronectin type-III 1PROSITE-ProRule annotationAdd BLAST112
Domaini440 – 537Fibronectin type-III 2PROSITE-ProRule annotationAdd BLAST98
Domaini621 – 882Protein kinasePROSITE-ProRule annotationAdd BLAST262
Domaini911 – 975SAMPROSITE-ProRule annotationAdd BLAST65

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi984 – 986PDZ-bindingSequence analysis3

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi191 – 325Cys-richAdd BLAST135

Domaini

The protein kinase domain mediates interaction with NGEF.By similarity

Sequence similaritiesi

Belongs to the protein kinase superfamily. Tyr protein kinase family. Ephrin receptor subfamily.PROSITE-ProRule annotation
Contains 1 Eph LBD (Eph ligand-binding) domain.PROSITE-ProRule annotation
Contains 2 fibronectin type-III domains.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation
Contains 1 SAM (sterile alpha motif) domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0196. Eukaryota.
COG0515. LUCA.
GeneTreeiENSGT00760000118975.
HOGENOMiHOG000233856.
HOVERGENiHBG062180.
InParanoidiP54764.
KOiK05105.
OMAiDWIPREG.
OrthoDBiEOG091G00W0.
PhylomeDBiP54764.
TreeFamiTF315608.

Family and domain databases

CDDicd00063. FN3. 2 hits.
Gene3Di1.10.150.50. 1 hit.
2.60.120.260. 1 hit.
2.60.40.10. 2 hits.
InterProiIPR027936. Eph_TM.
IPR001090. Ephrin_rcpt_lig-bd_dom.
IPR003961. FN3_dom.
IPR008979. Galactose-bd-like.
IPR013783. Ig-like_fold.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001660. SAM.
IPR013761. SAM/pointed.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR011641. Tyr-kin_ephrin_A/B_rcpt-like.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
IPR016257. Tyr_kinase_ephrin_rcpt.
IPR001426. Tyr_kinase_rcpt_V_CS.
[Graphical view]
PfamiPF14575. EphA2_TM. 1 hit.
PF01404. Ephrin_lbd. 1 hit.
PF00041. fn3. 2 hits.
PF07714. Pkinase_Tyr. 1 hit.
PF07647. SAM_2. 1 hit.
[Graphical view]
PIRSFiPIRSF000666. TyrPK_ephrin_receptor. 1 hit.
PRINTSiPR00109. TYRKINASE.
SMARTiSM00615. EPH_lbd. 1 hit.
SM01411. Ephrin_rec_like. 1 hit.
SM00060. FN3. 2 hits.
SM00220. S_TKc. 1 hit.
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. AlignAdd to basket

Isoform 1 (identifier: P54764-1) [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

        10         20         30         40         50
MAGIFYFALF SCLFGICDAV TGSRVYPANE VTLLDSRSVQ GELGWIASPL
60 70 80 90 100
EGGWEEVSIM DEKNTPIRTY QVCNVMEPSQ NNWLRTDWIT REGAQRVYIE
110 120 130 140 150
IKFTLRDCNS LPGVMGTCKE TFNLYYYESD NDKERFIREN QFVKIDTIAA
160 170 180 190 200
DESFTQVDIG DRIMKLNTEI RDVGPLSKKG FYLAFQDVGA CIALVSVRVF
210 220 230 240 250
YKKCPLTVRN LAQFPDTITG ADTSSLVEVR GSCVNNSEEK DVPKMYCGAD
260 270 280 290 300
GEWLVPIGNC LCNAGHEERS GECQACKIGY YKALSTDATC AKCPPHSYSV
310 320 330 340 350
WEGATSCTCD RGFFRADNDA ASMPCTRPPS APLNLISNVN ETSVNLEWSS
360 370 380 390 400
PQNTGGRQDI SYNVVCKKCG AGDPSKCRPC GSGVHYTPQQ NGLKTTKVSI
410 420 430 440 450
TDLLAHTNYT FEIWAVNGVS KYNPNPDQSV SVTVTTNQAA PSSIALVQAK
460 470 480 490 500
EVTRYSVALA WLEPDRPNGV ILEYEVKYYE KDQNERSYRI VRTAARNTDI
510 520 530 540 550
KGLNPLTSYV FHVRARTAAG YGDFSEPLEV TTNTVPSRII GDGANSTVLL
560 570 580 590 600
VSVSGSVVLV VILIAAFVIS RRRSKYSKAK QEADEEKHLN QGVRTYVDPF
610 620 630 640 650
TYEDPNQAVR EFAKEIDASC IKIEKVIGVG EFGEVCSGRL KVPGKREICV
660 670 680 690 700
AIKTLKAGYT DKQRRDFLSE ASIMGQFDHP NIIHLEGVVT KCKPVMIITE
710 720 730 740 750
YMENGSLDAF LRKNDGRFTV IQLVGMLRGI GSGMKYLSDM SYVHRDLAAR
760 770 780 790 800
NILVNSNLVC KVSDFGMSRV LEDDPEAAYT TRGGKIPIRW TAPEAIAYRK
810 820 830 840 850
FTSASDVWSY GIVMWEVMSY GERPYWDMSN QDVIKAIEEG YRLPPPMDCP
860 870 880 890 900
IALHQLMLDC WQKERSDRPK FGQIVNMLDK LIRNPNSLKR TGTESSRPNT
910 920 930 940 950
ALLDPSSPEF SAVVSVGDWL QAIKMDRYKD NFTAAGYTTL EAVVHVNQED
960 970 980
LARIGITAIT HQNKILSSVQ AMRTQMQQMH GRMVPV
Length:986
Mass (Da):109,860
Last modified:October 1, 1996 - v1
Checksum:i0C39C1152EDDD46F
GO
Isoform 2 (identifier: P54764-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-53: MAGIFYFALFSCLFGICDAVTGSRVYPANEVTLLDSRSVQGELGWIASPLEGG → MK

Note: No experimental confirmation available.
Show »
Length:935
Mass (Da):104,507
Checksum:i588D6FDA5FCCDCE4
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti71Q → P in BAF82995 (PubMed:14702039).Curated1
Sequence conflicti102K → R in BAF82995 (PubMed:14702039).Curated1
Sequence conflicti137I → V in BAG35298 (PubMed:14702039).Curated1
Sequence conflicti362Y → H in BAF82995 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_042135269R → Q.1 PublicationCorresponds to variant rs35084379dbSNPEnsembl.1
Natural variantiVAR_042136370G → E in a bladder carcinoma NOS sample; somatic mutation. 1 PublicationCorresponds to variant rs756952113dbSNPEnsembl.1
Natural variantiVAR_042137399S → F in a metastatic melanoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_049721953R → K.Corresponds to variant rs35341687dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0560161 – 53MAGIF…PLEGG → MK in isoform 2. 1 PublicationAdd BLAST53

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L36645 mRNA. Translation: AAA74246.1.
AK290306 mRNA. Translation: BAF82995.1.
AK300772 mRNA. Translation: BAH13344.1.
AK312380 mRNA. Translation: BAG35298.1.
AC010899 Genomic DNA. No translation available.
AC079834 Genomic DNA. No translation available.
BC105000 mRNA. Translation: AAI05001.1.
BC105002 mRNA. Translation: AAI05003.1.
CCDSiCCDS2447.1. [P54764-1]
PIRiI78844.
RefSeqiNP_001291465.1. NM_001304536.1. [P54764-1]
NP_001291466.1. NM_001304537.1. [P54764-2]
NP_004429.1. NM_004438.4. [P54764-1]
UniGeneiHs.371218.

Genome annotation databases

EnsembliENST00000281821; ENSP00000281821; ENSG00000116106. [P54764-1]
ENST00000409938; ENSP00000386829; ENSG00000116106. [P54764-1]
GeneIDi2043.
KEGGihsa:2043.
UCSCiuc002vmq.4. human. [P54764-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L36645 mRNA. Translation: AAA74246.1.
AK290306 mRNA. Translation: BAF82995.1.
AK300772 mRNA. Translation: BAH13344.1.
AK312380 mRNA. Translation: BAG35298.1.
AC010899 Genomic DNA. No translation available.
AC079834 Genomic DNA. No translation available.
BC105000 mRNA. Translation: AAI05001.1.
BC105002 mRNA. Translation: AAI05003.1.
CCDSiCCDS2447.1. [P54764-1]
PIRiI78844.
RefSeqiNP_001291465.1. NM_001304536.1. [P54764-1]
NP_001291466.1. NM_001304537.1. [P54764-2]
NP_004429.1. NM_004438.4. [P54764-1]
UniGeneiHs.371218.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4W4ZX-ray2.41A/B/C/D29-204[»]
4W50X-ray2.42A/B/C/D29-204[»]
5JR2X-ray1.75A/B/C/D29-204[»]
ProteinModelPortaliP54764.
SMRiP54764.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108357. 38 interactors.
DIPiDIP-48294N.
IntActiP54764. 2 interactors.
STRINGi9606.ENSP00000281821.

Chemistry databases

BindingDBiP54764.
ChEMBLiCHEMBL3988.
GuidetoPHARMACOLOGYi1824.

PTM databases

iPTMnetiP54764.
PhosphoSitePlusiP54764.

Polymorphism and mutation databases

BioMutaiEPHA4.
DMDMi1711371.

Proteomic databases

EPDiP54764.
MaxQBiP54764.
PaxDbiP54764.
PeptideAtlasiP54764.
PRIDEiP54764.
TopDownProteomicsiP54764-1. [P54764-1]

Protocols and materials databases

DNASUi2043.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000281821; ENSP00000281821; ENSG00000116106. [P54764-1]
ENST00000409938; ENSP00000386829; ENSG00000116106. [P54764-1]
GeneIDi2043.
KEGGihsa:2043.
UCSCiuc002vmq.4. human. [P54764-1]

Organism-specific databases

CTDi2043.
DisGeNETi2043.
GeneCardsiEPHA4.
HGNCiHGNC:3388. EPHA4.
HPAiCAB028368.
MIMi602188. gene.
neXtProtiNX_P54764.
OpenTargetsiENSG00000116106.
PharmGKBiPA27820.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0196. Eukaryota.
COG0515. LUCA.
GeneTreeiENSGT00760000118975.
HOGENOMiHOG000233856.
HOVERGENiHBG062180.
InParanoidiP54764.
KOiK05105.
OMAiDWIPREG.
OrthoDBiEOG091G00W0.
PhylomeDBiP54764.
TreeFamiTF315608.

Enzyme and pathway databases

BioCyciZFISH:HS03980-MONOMER.
BRENDAi2.7.10.1. 2681.
ReactomeiR-HSA-2682334. EPH-Ephrin signaling.
R-HSA-3928663. EPHA-mediated growth cone collapse.
R-HSA-3928665. EPH-ephrin mediated repulsion of cells.
SignaLinkiP54764.
SIGNORiP54764.

Miscellaneous databases

ChiTaRSiEPHA4. human.
EvolutionaryTraceiP54764.
GeneWikiiEPH_receptor_A4.
GenomeRNAii2043.
PROiP54764.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000116106.
CleanExiHS_EPHA4.
ExpressionAtlasiP54764. baseline and differential.
GenevisibleiP54764. HS.

Family and domain databases

CDDicd00063. FN3. 2 hits.
Gene3Di1.10.150.50. 1 hit.
2.60.120.260. 1 hit.
2.60.40.10. 2 hits.
InterProiIPR027936. Eph_TM.
IPR001090. Ephrin_rcpt_lig-bd_dom.
IPR003961. FN3_dom.
IPR008979. Galactose-bd-like.
IPR013783. Ig-like_fold.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001660. SAM.
IPR013761. SAM/pointed.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR011641. Tyr-kin_ephrin_A/B_rcpt-like.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
IPR016257. Tyr_kinase_ephrin_rcpt.
IPR001426. Tyr_kinase_rcpt_V_CS.
[Graphical view]
PfamiPF14575. EphA2_TM. 1 hit.
PF01404. Ephrin_lbd. 1 hit.
PF00041. fn3. 2 hits.
PF07714. Pkinase_Tyr. 1 hit.
PF07647. SAM_2. 1 hit.
[Graphical view]
PIRSFiPIRSF000666. TyrPK_ephrin_receptor. 1 hit.
PRINTSiPR00109. TYRKINASE.
SMARTiSM00615. EPH_lbd. 1 hit.
SM01411. Ephrin_rec_like. 1 hit.
SM00060. FN3. 2 hits.
SM00220. S_TKc. 1 hit.
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]
ProtoNetiSearch...

Entry informationi

Entry nameiEPHA4_HUMAN
AccessioniPrimary (citable) accession number: P54764
Secondary accession number(s): A8K2P1
, B2R601, B7Z6Q8, Q2M380
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: November 30, 2016
This is version 177 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.