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P54756 (EPHA5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 154. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:EPHA5
Synonyms:BSK, EHK1, HEK7, TYRO4
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1037 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 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. Beside 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.

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 By similarity.

Subcellular location

Cell membrane By similarity; Single-pass type I membrane protein By similarity. Cell projectionaxon By similarity. Cell projectiondendrite Ref.1 Ref.7.

Tissue specificity

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. Ref.1 Ref.7

Post-translational modification

Phosphorylated. Phosphorylation is stimulated by the ligand EFNA5. Dephosphorylation upon stimulation by glucose, inhibits EPHA5 forward signaling and results in insulin secretion By similarity. Ref.5

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 processNeurogenesis
   Cellular componentCell membrane
Cell projection
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
Signal
Transmembrane
Transmembrane helix
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Receptor
Transferase
Tyrosine-protein kinase
   PTMGlycoprotein
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processaxon guidance

Inferred from sequence or structural similarity. Source: UniProtKB

cAMP-mediated signaling

Inferred from sequence or structural similarity. Source: UniProtKB

ephrin receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

hippocampus development

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of synapse assembly

Inferred from electronic annotation. Source: Ensembl

neuron development

Inferred from expression pattern Ref.7. Source: UniProtKB

positive regulation of CREB transcription factor activity

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of Rac GTPase activity

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of actin cytoskeleton organization

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of insulin secretion involved in cellular response to glucose stimulus

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentaxon

Inferred from electronic annotation. Source: UniProtKB-SubCell

dendrite

Inferred from direct assay Ref.7. Source: UniProtKB

external side of plasma membrane

Inferred from direct assay PubMed 10064801. Source: UniProtKB

integral component of plasma membrane

Inferred from electronic annotation. Source: InterPro

neuronal cell body

Inferred from direct assay Ref.7. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from direct assay Ref.7. Source: UniProtKB

plasma membrane

Inferred from direct assay Ref.7. Source: UniProtKB

rough endoplasmic reticulum

Inferred from direct assay Ref.7. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

GPI-linked ephrin receptor activity

Inferred from sequence or structural similarity. Source: UniProtKB

ephrin receptor activity

Inferred from sequence or structural similarity. Source: UniProtKB

transmembrane-ephrin receptor activity

Non-traceable author statement Ref.4. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform 1 (identifier: P54756-1)

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 2 (identifier: P54756-2)

The sequence of this isoform differs from the canonical sequence as follows:
     597-619: SCCECGCGRASSLCAVAHPSLIW → R
Isoform 3 (identifier: P54756-3)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Potential
Chain25 – 10371013Ephrin type-A receptor 5
PRO_0000016812

Regions

Topological domain25 – 573549Extracellular Potential
Transmembrane574 – 59421Helical; Potential
Topological domain595 – 1037443Cytoplasmic Potential
Domain60 – 238179Eph LBD
Domain357 – 467111Fibronectin type-III 1
Domain468 – 56295Fibronectin type-III 2
Domain675 – 936262Protein kinase
Domain965 – 102965SAM
Nucleotide binding681 – 6899ATP By similarity
Motif1035 – 10373PDZ-binding Potential
Compositional bias220 – 354135Cys-rich

Sites

Active site8001Proton acceptor By similarity
Binding site7071ATP By similarity

Amino acid modifications

Modified residue6501Phosphotyrosine; by autocatalysis By similarity
Modified residue6561Phosphotyrosine; by autocatalysis By similarity
Modified residue8331Phosphotyrosine; by autocatalysis Potential
Modified residue9821Phosphotyrosine; by autocatalysis By similarity
Glycosylation2641N-linked (GlcNAc...) Potential
Glycosylation2991N-linked (GlcNAc...) Potential
Glycosylation3691N-linked (GlcNAc...) Potential
Glycosylation4231N-linked (GlcNAc...) Potential
Glycosylation4361N-linked (GlcNAc...) Potential
Glycosylation4611N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence1 – 6969Missing in isoform 3.
VSP_039118
Alternative sequence5631F → SV in isoform 3.
VSP_039119
Alternative sequence597 – 61923SCCEC…PSLIW → R in isoform 2.
VSP_002999
Natural variant811N → T. Ref.8
Corresponds to variant rs33932471 [ dbSNP | Ensembl ].
VAR_042138
Natural variant2351S → A. Ref.8
Corresponds to variant rs55710198 [ dbSNP | Ensembl ].
VAR_042139
Natural variant3301E → Q. Ref.8
Corresponds to variant rs56205382 [ dbSNP | Ensembl ].
VAR_042140
Natural variant4171R → Q in a lung adenocarcinoma sample; somatic mutation. Ref.8
VAR_042141
Natural variant5031E → K in a lung large cell carcinoma sample; somatic mutation. Ref.8
VAR_042142
Natural variant5061Y → C. Ref.8
Corresponds to variant rs56074660 [ dbSNP | Ensembl ].
VAR_045912
Natural variant5821G → E in a lung adenocarcinoma sample; somatic mutation. Ref.8
VAR_042143
Natural variant6721A → T. Ref.8
Corresponds to variant rs36050417 [ dbSNP | Ensembl ].
VAR_042144
Natural variant6731S → T. Ref.8
Corresponds to variant rs56359290 [ dbSNP | Ensembl ].
VAR_042145
Natural variant8561T → I in a lung squamous cell carcinoma sample; somatic mutation. Ref.8
VAR_042146
Natural variant9591H → R. Ref.8
Corresponds to variant rs56312931 [ dbSNP | Ensembl ].
VAR_042147
Natural variant10321N → S in a lung large cell carcinoma sample; somatic mutation. Ref.8
VAR_042148

Experimental info

Sequence conflict111R → H in CAA64700. Ref.1
Sequence conflict871G → D in CAD97914. Ref.3
Sequence conflict5061Y → H in CAA64700. Ref.1
Sequence conflict6111A → V in CAD97914. Ref.3
Sequence conflict6161S → I in CAA64700. Ref.1
Sequence conflict8201G → E in CAD97914. Ref.3

Secondary structure

......................................................................... 1037
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified September 22, 2009. Version 3.
Checksum: 578C2F4D950DE419

FASTA1,037114,803
        10         20         30         40         50         60 
MRGSGPRGAG RRRPPSGGGD TPITPASLAG CYSAPRRAPL WTCLLLCAAL RTLLASPSNE 

        70         80         90        100        110        120 
VNLLDSRTVM GDLGWIAFPK NGWEEIGEVD ENYAPIHTYQ VCKVMEQNQN NWLLTSWISN 

       130        140        150        160        170        180 
EGASRIFIEL KFTLRDCNSL PGGLGTCKET FNMYYFESDD QNGRNIKENQ YIKIDTIAAD 

       190        200        210        220        230        240 
ESFTELDLGD RVMKLNTEVR DVGPLSKKGF YLAFQDVGAC IALVSVRVYY KKCPSVVRHL 

       250        260        270        280        290        300 
AVFPDTITGA DSSQLLEVSG SCVNHSVTDE PPKMHCSAEG EWLVPIGKCM CKAGYEEKNG 

       310        320        330        340        350        360 
TCQVCRPGFF KASPHIQSCG KCPPHSYTHE EASTSCVCEK DYFRRESDPP TMACTRPPSA 

       370        380        390        400        410        420 
PRNAISNVNE TSVFLEWIPP ADTGGRKDVS YYIACKKCNS HAGVCEECGG HVRYLPRQSG 

       430        440        450        460        470        480 
LKNTSVMMVD LLAHTNYTFE IEAVNGVSDL SPGARQYVSV NVTTNQAAPS PVTNVKKGKI 

       490        500        510        520        530        540 
AKNSISLSWQ EPDRPNGIIL EYEIKYFEKD QETSYTIIKS KETTITAEGL KPASVYVFQI 

       550        560        570        580        590        600 
RARTAAGYGV FSRRFEFETT PVFAASSDQS QIPVIAVSVT VGVILLAVVI GVLLSGSCCE 

       610        620        630        640        650        660 
CGCGRASSLC AVAHPSLIWR CGYSKAKQDP EEEKMHFHNG HIKLPGVRTY IDPHTYEDPN 

       670        680        690        700        710        720 
QAVHEFAKEI EASCITIERV IGAGEFGEVC SGRLKLPGKR ELPVAIKTLK VGYTEKQRRD 

       730        740        750        760        770        780 
FLGEASIMGQ FDHPNIIHLE GVVTKSKPVM IVTEYMENGS LDTFLKKNDG QFTVIQLVGM 

       790        800        810        820        830        840 
LRGISAGMKY LSDMGYVHRD LAARNILINS NLVCKVSDFG LSRVLEDDPE AAYTTRGGKI 

       850        860        870        880        890        900 
PIRWTAPEAI AFRKFTSASD VWSYGIVMWE VVSYGERPYW EMTNQDVIKA VEEGYRLPSP 

       910        920        930        940        950        960 
MDCPAALYQL MLDCWQKERN SRPKFDEIVN MLDKLIRNPS SLKTLVNASC RVSNLLAEHS 

       970        980        990       1000       1010       1020 
PLGSGAYRSV GEWLEAIKMG RYTEIFMENG YSSMDAVAQV TLEDLRRLGV TLVGHQKKIM 

      1030 
NSLQEMKVQL VNGMVPL 

« Hide

Isoform 2 [UniParc].

Checksum: 0C0121184BCE631E
Show »

FASTA1,015112,624
Isoform 3 [UniParc].

Checksum: 3038A240682F6E84
Show »

FASTA969107,699

References

« Hide 'large scale' references
[1]"Extensive splice variation and localization of the EHK-1 receptor tyrosine kinase in adult human brain and glial tumors."
Miescher G.C., Taylor V., Olivieri G., Mindermann T., Shrock E., Steck A.J.
Brain Res. Mol. Brain Res. 46:17-24(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
Tissue: Brain.
[2]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
Tissue: Retina.
[4]"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] OF 25-1037.
Tissue: Brain.
[5]"Cloning of AL-1, a ligand for an Eph-related tyrosine kinase receptor involved in axon bundle formation."
Winslow J.W., Moran P., Valverde J., Shih A., Yuan J.Q., Wong S.C., Tsai S.P., Goddard A., Henzel W.J., Hefti F., Beck K.D., Caras I.W.
Neuron 14:973-981(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION OF EFNA5 AS LIGAND, PHOSPHORYLATION.
[6]"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.
[7]"Immunohistochemical localization of EphA5 in the adult human central nervous system."
Olivieri G., Miescher G.C.
J. Histochem. Cytochem. 47:855-861(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[8]"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. expand/collapse author list , 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] THR-81; ALA-235; GLN-330; GLN-417; LYS-503; CYS-506; GLU-582; THR-672; THR-673; ILE-856; ARG-959 AND SER-1032.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS3513.1. [P54756-1]
CCDS3514.1. [P54756-2]
RefSeqNP_004430.4. NM_004439.6. [P54756-1]
NP_872272.2. NM_182472.3. [P54756-2]
UniGeneHs.654492.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2R2PX-ray2.40A653-939[»]
4ET7X-ray2.60A59-235[»]
ProteinModelPortalP54756.
SMRP54756. Positions 57-562, 662-940, 966-1026.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108358. 3 interactions.
MINTMINT-4722838.
STRING9606.ENSP00000273854.

Chemistry

BindingDBP54756.
ChEMBLCHEMBL2363043.
GuidetoPHARMACOLOGY1825.

PTM databases

PhosphoSiteP54756.

Polymorphism databases

DMDM259016353.

Proteomic databases

MaxQBP54756.
PaxDbP54756.
PRIDEP54756.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000273854; ENSP00000273854; ENSG00000145242. [P54756-1]
ENST00000354839; ENSP00000346899; ENSG00000145242. [P54756-2]
GeneID2044.
KEGGhsa:2044.
UCSCuc003hcx.3. human. [P54756-3]
uc003hcy.3. human. [P54756-1]
uc003hcz.3. human. [P54756-2]

Organism-specific databases

CTD2044.
GeneCardsGC04M066193.
HGNCHGNC:3389. EPHA5.
MIM600004. gene.
neXtProtNX_P54756.
PharmGKBPA27821.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOVERGENHBG062180.
InParanoidP54756.
KOK05106.
OMAPSLIWRC.
OrthoDBEOG7VTDM6.
PhylomeDBP54756.
TreeFamTF315608.

Enzyme and pathway databases

BRENDA2.7.10.1. 2681.
SignaLinkP54756.

Gene expression databases

ArrayExpressP54756.
BgeeP54756.
CleanExHS_EPHA5.
GenevestigatorP54756.

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.
IPR021129. SAM_type1.
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.
PF00536. SAM_1. 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.
PROSITEPS01186. 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]
ProtoNetSearch...

Other

ChiTaRSEPHA5. human.
EvolutionaryTraceP54756.
GeneWikiEPH_receptor_A5.
GenomeRNAi2044.
NextBio8305.
PROP54756.
SOURCESearch...

Entry information

Entry nameEPHA5_HUMAN
AccessionPrimary (citable) accession number: P54756
Secondary accession number(s): Q7Z3F2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: September 22, 2009
Last modified: July 9, 2014
This is version 154 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

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

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM