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Protein

Ephrin type-A receptor 5

Gene

EPHA5

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 promiscuously GPI-anchored ephrin-A 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. Among GPI-anchored ephrin-A ligands, EFNA5 most probably constitutes the cognate/functional ligand for EPHA5. Functions as an axon guidance molecule during development and may be involved in the development of the retinotectal, entorhino-hippocampal and hippocamposeptal pathways. Together with EFNA5 plays also a role in synaptic plasticity in adult brain through regulation of synaptogenesis. In addition to its function in the nervous system, the interaction of EPHA5 with EFNA5 mediates communication between pancreatic islet cells to regulate glucose-stimulated insulin secretion (By similarity).By similarity

Catalytic activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei707ATPPROSITE-ProRule annotation1
Active sitei800Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi681 – 689ATPPROSITE-ProRule annotation9

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Receptor, Transferase, Tyrosine-protein kinase

Keywords - Biological processi

Neurogenesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciZFISH:HS07237-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.
SignaLinkiP54756.
SIGNORiP54756.

Names & Taxonomyi

Protein namesi
Recommended name:
Ephrin type-A receptor 5 (EC:2.7.10.1)
Alternative name(s):
Brain-specific kinase
EPH homology kinase 1
Short name:
EHK-1
EPH-like kinase 7
Short name:
EK7
Short name:
hEK7
Gene namesi
Name:EPHA5
Synonyms:BSK, EHK1, HEK7, TYRO4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:3389. EPHA5.

Subcellular locationi

  • Cell membrane By similarity; Single-pass type I membrane protein Sequence analysis
  • Cell projectionaxon By similarity
  • Cell projectiondendrite By similarity

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini25 – 573ExtracellularSequence analysisAdd BLAST549
Transmembranei574 – 594HelicalSequence analysisAdd BLAST21
Topological domaini595 – 1037CytoplasmicSequence analysisAdd BLAST443

GO - Cellular componenti

  • axon Source: UniProtKB-SubCell
  • dendrite Source: UniProtKB
  • external side of plasma membrane Source: UniProtKB
  • integral component of plasma membrane Source: InterPro
  • neuronal cell body Source: UniProtKB
  • perinuclear region of cytoplasm Source: UniProtKB
  • plasma membrane Source: UniProtKB
  • rough endoplasmic reticulum Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Membrane

Pathology & Biotechi

Organism-specific databases

DisGeNETi2044.
OpenTargetsiENSG00000145242.
PharmGKBiPA27821.

Chemistry databases

ChEMBLiCHEMBL3987.
GuidetoPHARMACOLOGYi1825.

Polymorphism and mutation databases

BioMutaiEPHA5.
DMDMi259016353.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 24Sequence analysisAdd BLAST24
ChainiPRO_000001681225 – 1037Ephrin type-A receptor 5Add BLAST1013

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi264N-linked (GlcNAc...)Sequence analysis1
Glycosylationi299N-linked (GlcNAc...)Sequence analysis1
Glycosylationi369N-linked (GlcNAc...)Sequence analysis1
Glycosylationi423N-linked (GlcNAc...)Sequence analysis1
Glycosylationi436N-linked (GlcNAc...)Sequence analysis1
Glycosylationi461N-linked (GlcNAc...)Sequence analysis1
Modified residuei650Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei656Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei833Phosphotyrosine; by autocatalysisSequence analysis1
Modified residuei982Phosphotyrosine; by autocatalysisBy similarity1

Post-translational modificationi

Phosphorylated. Phosphorylation is stimulated by the ligand EFNA5. Dephosphorylation upon stimulation by glucose, inhibits EPHA5 forward signaling and results in insulin secretion (By similarity).By similarity

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

EPDiP54756.
MaxQBiP54756.
PaxDbiP54756.
PeptideAtlasiP54756.
PRIDEiP54756.
TopDownProteomicsiP54756-2. [P54756-2]

PTM databases

iPTMnetiP54756.
PhosphoSitePlusiP54756.

Expressioni

Tissue specificityi

Almost exclusively expressed in the nervous system in cortical neurons, cerebellar Purkinje cells and pyramidal neurons within the cortex and hippocampus. Display an increasing gradient of expression from the forebrain to hindbrain and spinal cord.2 Publications

Gene expression databases

BgeeiENSG00000145242.
CleanExiHS_EPHA5.
ExpressionAtlasiP54756. baseline and differential.
GenevisibleiP54756. HS.

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 (By similarity).By similarity

Protein-protein interaction databases

BioGridi108358. 4 interactors.
IntActiP54756. 2 interactors.
MINTiMINT-4722838.
STRINGi9606.ENSP00000273854.

Chemistry databases

BindingDBiP54756.

Structurei

Secondary structure

11037
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi61 – 65Combined sources5
Turni66 – 68Combined sources3
Beta strandi76 – 89Combined sources14
Beta strandi95 – 101Combined sources7
Beta strandi105 – 107Combined sources3
Beta strandi111 – 114Combined sources4
Beta strandi126 – 135Combined sources10
Helixi137 – 139Combined sources3
Beta strandi148 – 157Combined sources10
Helixi166 – 168Combined sources3
Beta strandi172 – 178Combined sources7
Beta strandi188 – 192Combined sources5
Beta strandi196 – 202Combined sources7
Beta strandi207 – 219Combined sources13
Beta strandi221 – 230Combined sources10
Helixi663 – 665Combined sources3
Helixi672 – 674Combined sources3
Beta strandi675 – 683Combined sources9
Beta strandi685 – 694Combined sources10
Beta strandi702 – 708Combined sources7
Helixi715 – 728Combined sources14
Beta strandi739 – 743Combined sources5
Beta strandi745 – 748Combined sources4
Beta strandi750 – 754Combined sources5
Helixi761 – 766Combined sources6
Turni767 – 770Combined sources4
Helixi774 – 793Combined sources20
Helixi803 – 805Combined sources3
Beta strandi806 – 808Combined sources3
Beta strandi814 – 816Combined sources3
Helixi842 – 844Combined sources3
Helixi847 – 852Combined sources6
Helixi857 – 873Combined sources17
Turni878 – 881Combined sources4
Helixi884 – 893Combined sources10
Helixi905 – 914Combined sources10
Helixi919 – 921Combined sources3
Helixi925 – 936Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2R2PX-ray2.40A653-939[»]
4ET7X-ray2.60A59-235[»]
ProteinModelPortaliP54756.
SMRiP54756.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP54756.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini60 – 238Eph LBDPROSITE-ProRule annotationAdd BLAST179
Domaini357 – 467Fibronectin type-III 1PROSITE-ProRule annotationAdd BLAST111
Domaini468 – 562Fibronectin type-III 2PROSITE-ProRule annotationAdd BLAST95
Domaini675 – 936Protein kinasePROSITE-ProRule annotationAdd BLAST262
Domaini965 – 1029SAMPROSITE-ProRule annotationAdd BLAST65

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi1035 – 1037PDZ-bindingSequence analysis3

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi220 – 354Cys-richAdd BLAST135

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.
HOVERGENiHBG062180.
InParanoidiP54756.
KOiK05106.
PhylomeDBiP54756.
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.
PF00536. SAM_1. 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.
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.
PROSITEiPS01186. EGF_2. 1 hit.
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]

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Note: Additional isoforms seem to exist.
Isoform 1 (identifier: P54756-1) [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
MRGSGPRGAG RRRPPSGGGD TPITPASLAG CYSAPRRAPL WTCLLLCAAL
60 70 80 90 100
RTLLASPSNE VNLLDSRTVM GDLGWIAFPK NGWEEIGEVD ENYAPIHTYQ
110 120 130 140 150
VCKVMEQNQN NWLLTSWISN EGASRIFIEL KFTLRDCNSL PGGLGTCKET
160 170 180 190 200
FNMYYFESDD QNGRNIKENQ YIKIDTIAAD ESFTELDLGD RVMKLNTEVR
210 220 230 240 250
DVGPLSKKGF YLAFQDVGAC IALVSVRVYY KKCPSVVRHL AVFPDTITGA
260 270 280 290 300
DSSQLLEVSG SCVNHSVTDE PPKMHCSAEG EWLVPIGKCM CKAGYEEKNG
310 320 330 340 350
TCQVCRPGFF KASPHIQSCG KCPPHSYTHE EASTSCVCEK DYFRRESDPP
360 370 380 390 400
TMACTRPPSA PRNAISNVNE TSVFLEWIPP ADTGGRKDVS YYIACKKCNS
410 420 430 440 450
HAGVCEECGG HVRYLPRQSG LKNTSVMMVD LLAHTNYTFE IEAVNGVSDL
460 470 480 490 500
SPGARQYVSV NVTTNQAAPS PVTNVKKGKI AKNSISLSWQ EPDRPNGIIL
510 520 530 540 550
EYEIKYFEKD QETSYTIIKS KETTITAEGL KPASVYVFQI RARTAAGYGV
560 570 580 590 600
FSRRFEFETT PVFAASSDQS QIPVIAVSVT VGVILLAVVI GVLLSGSCCE
610 620 630 640 650
CGCGRASSLC AVAHPSLIWR CGYSKAKQDP EEEKMHFHNG HIKLPGVRTY
660 670 680 690 700
IDPHTYEDPN QAVHEFAKEI EASCITIERV IGAGEFGEVC SGRLKLPGKR
710 720 730 740 750
ELPVAIKTLK VGYTEKQRRD FLGEASIMGQ FDHPNIIHLE GVVTKSKPVM
760 770 780 790 800
IVTEYMENGS LDTFLKKNDG QFTVIQLVGM LRGISAGMKY LSDMGYVHRD
810 820 830 840 850
LAARNILINS NLVCKVSDFG LSRVLEDDPE AAYTTRGGKI PIRWTAPEAI
860 870 880 890 900
AFRKFTSASD VWSYGIVMWE VVSYGERPYW EMTNQDVIKA VEEGYRLPSP
910 920 930 940 950
MDCPAALYQL MLDCWQKERN SRPKFDEIVN MLDKLIRNPS SLKTLVNASC
960 970 980 990 1000
RVSNLLAEHS PLGSGAYRSV GEWLEAIKMG RYTEIFMENG YSSMDAVAQV
1010 1020 1030
TLEDLRRLGV TLVGHQKKIM NSLQEMKVQL VNGMVPL
Length:1,037
Mass (Da):114,803
Last modified:September 22, 2009 - v3
Checksum:i578C2F4D950DE419
GO
Isoform 2 (identifier: P54756-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     597-619: SCCECGCGRASSLCAVAHPSLIW → R

Show »
Length:1,015
Mass (Da):112,624
Checksum:i0C0121184BCE631E
GO
Isoform 3 (identifier: P54756-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-69: Missing.
     563-563: F → SV

Show »
Length:969
Mass (Da):107,699
Checksum:i3038A240682F6E84
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti11R → H in CAA64700 (PubMed:9191074).Curated1
Sequence conflicti87G → D in CAD97914 (PubMed:17974005).Curated1
Sequence conflicti506Y → H in CAA64700 (PubMed:9191074).Curated1
Sequence conflicti611A → V in CAD97914 (PubMed:17974005).Curated1
Sequence conflicti616S → I in CAA64700 (PubMed:9191074).Curated1
Sequence conflicti820G → E in CAD97914 (PubMed:17974005).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_04213881N → T.1 PublicationCorresponds to variant rs33932471dbSNPEnsembl.1
Natural variantiVAR_042139235S → A.1 PublicationCorresponds to variant rs55710198dbSNPEnsembl.1
Natural variantiVAR_042140330E → Q.1 PublicationCorresponds to variant rs56205382dbSNPEnsembl.1
Natural variantiVAR_042141417R → Q in a lung adenocarcinoma sample; somatic mutation. 1 PublicationCorresponds to variant rs199614818dbSNPEnsembl.1
Natural variantiVAR_042142503E → K in a lung large cell carcinoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_045912506Y → C.1 PublicationCorresponds to variant rs56074660dbSNPEnsembl.1
Natural variantiVAR_042143582G → E in a lung adenocarcinoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_042144672A → T.1 PublicationCorresponds to variant rs36050417dbSNPEnsembl.1
Natural variantiVAR_042145673S → T.1 PublicationCorresponds to variant rs56359290dbSNPEnsembl.1
Natural variantiVAR_042146856T → I in a lung squamous cell carcinoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_042147959H → R.1 PublicationCorresponds to variant rs56312931dbSNPEnsembl.1
Natural variantiVAR_0421481032N → S in a lung large cell carcinoma sample; somatic mutation. 1 Publication1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0391181 – 69Missing in isoform 3. 1 PublicationAdd BLAST69
Alternative sequenceiVSP_039119563F → SV in isoform 3. 1 Publication1
Alternative sequenceiVSP_002999597 – 619SCCEC…PSLIW → R in isoform 2. CuratedAdd BLAST23

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X95425 mRNA. Translation: CAA64700.1.
AC018683 Genomic DNA. No translation available.
AC104137 Genomic DNA. No translation available.
AC105923 Genomic DNA. No translation available.
AC115223 Genomic DNA. No translation available.
BX537946 mRNA. Translation: CAD97914.1.
L36644 mRNA. Translation: AAA74245.1.
CCDSiCCDS3513.1. [P54756-1]
CCDS3514.1. [P54756-2]
RefSeqiNP_001268694.1. NM_001281765.2.
NP_001268695.1. NM_001281766.2.
NP_001305690.1. NM_001318761.1. [P54756-3]
NP_004430.4. NM_004439.7. [P54756-1]
NP_872272.2. NM_182472.4. [P54756-2]
UniGeneiHs.654492.

Genome annotation databases

EnsembliENST00000273854; ENSP00000273854; ENSG00000145242. [P54756-1]
ENST00000354839; ENSP00000346899; ENSG00000145242. [P54756-2]
GeneIDi2044.
KEGGihsa:2044.
UCSCiuc003hcy.5. human. [P54756-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X95425 mRNA. Translation: CAA64700.1.
AC018683 Genomic DNA. No translation available.
AC104137 Genomic DNA. No translation available.
AC105923 Genomic DNA. No translation available.
AC115223 Genomic DNA. No translation available.
BX537946 mRNA. Translation: CAD97914.1.
L36644 mRNA. Translation: AAA74245.1.
CCDSiCCDS3513.1. [P54756-1]
CCDS3514.1. [P54756-2]
RefSeqiNP_001268694.1. NM_001281765.2.
NP_001268695.1. NM_001281766.2.
NP_001305690.1. NM_001318761.1. [P54756-3]
NP_004430.4. NM_004439.7. [P54756-1]
NP_872272.2. NM_182472.4. [P54756-2]
UniGeneiHs.654492.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2R2PX-ray2.40A653-939[»]
4ET7X-ray2.60A59-235[»]
ProteinModelPortaliP54756.
SMRiP54756.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108358. 4 interactors.
IntActiP54756. 2 interactors.
MINTiMINT-4722838.
STRINGi9606.ENSP00000273854.

Chemistry databases

BindingDBiP54756.
ChEMBLiCHEMBL3987.
GuidetoPHARMACOLOGYi1825.

PTM databases

iPTMnetiP54756.
PhosphoSitePlusiP54756.

Polymorphism and mutation databases

BioMutaiEPHA5.
DMDMi259016353.

Proteomic databases

EPDiP54756.
MaxQBiP54756.
PaxDbiP54756.
PeptideAtlasiP54756.
PRIDEiP54756.
TopDownProteomicsiP54756-2. [P54756-2]

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000273854; ENSP00000273854; ENSG00000145242. [P54756-1]
ENST00000354839; ENSP00000346899; ENSG00000145242. [P54756-2]
GeneIDi2044.
KEGGihsa:2044.
UCSCiuc003hcy.5. human. [P54756-1]

Organism-specific databases

CTDi2044.
DisGeNETi2044.
GeneCardsiEPHA5.
HGNCiHGNC:3389. EPHA5.
MIMi600004. gene.
neXtProtiNX_P54756.
OpenTargetsiENSG00000145242.
PharmGKBiPA27821.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0196. Eukaryota.
COG0515. LUCA.
GeneTreeiENSGT00760000118975.
HOVERGENiHBG062180.
InParanoidiP54756.
KOiK05106.
PhylomeDBiP54756.
TreeFamiTF315608.

Enzyme and pathway databases

BioCyciZFISH:HS07237-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.
SignaLinkiP54756.
SIGNORiP54756.

Miscellaneous databases

ChiTaRSiEPHA5. human.
EvolutionaryTraceiP54756.
GeneWikiiEPH_receptor_A5.
GenomeRNAii2044.
PROiP54756.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000145242.
CleanExiHS_EPHA5.
ExpressionAtlasiP54756. baseline and differential.
GenevisibleiP54756. 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.
PF00536. SAM_1. 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.
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.
PROSITEiPS01186. EGF_2. 1 hit.
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]
ProtoNetiSearch...

Entry informationi

Entry nameiEPHA5_HUMAN
AccessioniPrimary (citable) accession number: P54756
Secondary accession number(s): Q7Z3F2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: September 22, 2009
Last modified: November 30, 2016
This is version 174 of the entry and version 3 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 4
    Human chromosome 4: 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.