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P54756

- EPHA5_HUMAN

UniProt

P54756 - EPHA5_HUMAN

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Protein

Ephrin type-A receptor 5

Gene

EPHA5

Organism
Homo sapiens (Human)
Status
Reviewed - 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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei707 – 7071ATPPROSITE-ProRule annotation
Active sitei800 – 8001Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi681 – 6899ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. ephrin receptor activity Source: UniProtKB
  3. GPI-linked ephrin receptor activity Source: UniProtKB
  4. transmembrane-ephrin receptor activity Source: UniProtKB

GO - Biological processi

  1. axon guidance Source: UniProtKB
  2. cAMP-mediated signaling Source: UniProtKB
  3. ephrin receptor signaling pathway Source: UniProtKB
  4. hippocampus development Source: UniProtKB
  5. negative regulation of synapse assembly Source: Ensembl
  6. neuron development Source: UniProtKB
  7. positive regulation of CREB transcription factor activity Source: UniProtKB
  8. regulation of actin cytoskeleton organization Source: UniProtKB
  9. regulation of insulin secretion involved in cellular response to glucose stimulus Source: UniProtKB
  10. regulation of Rac GTPase activity Source: UniProtKB
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

BRENDAi2.7.10.1. 2681.
SignaLinkiP54756.

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
ProteomesiUP000005640: Chromosome 4

Organism-specific databases

HGNCiHGNC:3389. EPHA5.

Subcellular locationi

Cell membrane By similarity; Single-pass type I membrane protein By similarity. Cell projectionaxon By similarity. Cell projectiondendrite 2 Publications

GO - Cellular componenti

  1. dendrite Source: UniProtKB
  2. external side of plasma membrane Source: UniProtKB
  3. integral component of plasma membrane Source: InterPro
  4. neuronal cell body Source: UniProtKB
  5. perinuclear region of cytoplasm Source: UniProtKB
  6. plasma membrane Source: UniProtKB
  7. rough endoplasmic reticulum Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27821.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424Sequence AnalysisAdd
BLAST
Chaini25 – 10371013Ephrin type-A receptor 5PRO_0000016812Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi264 – 2641N-linked (GlcNAc...)Sequence Analysis
Glycosylationi299 – 2991N-linked (GlcNAc...)Sequence Analysis
Glycosylationi369 – 3691N-linked (GlcNAc...)Sequence Analysis
Glycosylationi423 – 4231N-linked (GlcNAc...)Sequence Analysis
Glycosylationi436 – 4361N-linked (GlcNAc...)Sequence Analysis
Glycosylationi461 – 4611N-linked (GlcNAc...)Sequence Analysis
Modified residuei650 – 6501Phosphotyrosine; by autocatalysisBy similarity
Modified residuei656 – 6561Phosphotyrosine; by autocatalysisBy similarity
Modified residuei833 – 8331Phosphotyrosine; by autocatalysisSequence Analysis
Modified residuei982 – 9821Phosphotyrosine; by autocatalysisBy similarity

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

MaxQBiP54756.
PaxDbiP54756.
PRIDEiP54756.

PTM databases

PhosphoSiteiP54756.

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

BgeeiP54756.
CleanExiHS_EPHA5.
ExpressionAtlasiP54756. baseline and differential.
GenevestigatoriP54756.

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. 5 interactions.
IntActiP54756. 1 interaction.
MINTiMINT-4722838.
STRINGi9606.ENSP00000273854.

Structurei

Secondary structure

1
1037
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi61 – 655Combined sources
Turni66 – 683Combined sources
Beta strandi76 – 8914Combined sources
Beta strandi95 – 1017Combined sources
Beta strandi105 – 1073Combined sources
Beta strandi111 – 1144Combined sources
Beta strandi126 – 13510Combined sources
Helixi137 – 1393Combined sources
Beta strandi148 – 15710Combined sources
Helixi166 – 1683Combined sources
Beta strandi172 – 1787Combined sources
Beta strandi188 – 1925Combined sources
Beta strandi196 – 2027Combined sources
Beta strandi207 – 21913Combined sources
Beta strandi221 – 23010Combined sources
Helixi663 – 6653Combined sources
Helixi672 – 6743Combined sources
Beta strandi675 – 6839Combined sources
Beta strandi685 – 69410Combined sources
Beta strandi702 – 7087Combined sources
Helixi715 – 72814Combined sources
Beta strandi739 – 7435Combined sources
Beta strandi745 – 7484Combined sources
Beta strandi750 – 7545Combined sources
Helixi761 – 7666Combined sources
Turni767 – 7704Combined sources
Helixi774 – 79320Combined sources
Helixi803 – 8053Combined sources
Beta strandi806 – 8083Combined sources
Beta strandi814 – 8163Combined sources
Helixi842 – 8443Combined sources
Helixi847 – 8526Combined sources
Helixi857 – 87317Combined sources
Turni878 – 8814Combined sources
Helixi884 – 89310Combined sources
Helixi905 – 91410Combined sources
Helixi919 – 9213Combined sources
Helixi925 – 93612Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2R2PX-ray2.40A653-939[»]
4ET7X-ray2.60A59-235[»]
ProteinModelPortaliP54756.
SMRiP54756. Positions 57-562, 662-940, 966-1026.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP54756.

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini25 – 573549ExtracellularSequence AnalysisAdd
BLAST
Topological domaini595 – 1037443CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei574 – 59421HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini60 – 238179Eph LBDPROSITE-ProRule annotationAdd
BLAST
Domaini357 – 467111Fibronectin type-III 1PROSITE-ProRule annotationAdd
BLAST
Domaini468 – 56295Fibronectin type-III 2PROSITE-ProRule annotationAdd
BLAST
Domaini675 – 936262Protein kinasePROSITE-ProRule annotationAdd
BLAST
Domaini965 – 102965SAMPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi1035 – 10373PDZ-bindingSequence Analysis

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi220 – 354135Cys-richAdd
BLAST

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

eggNOGiCOG0515.
GeneTreeiENSGT00760000118975.
HOVERGENiHBG062180.
InParanoidiP54756.
KOiK05106.
OMAiPSLIWRC.
OrthoDBiEOG7VTDM6.
PhylomeDBiP54756.
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.
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]
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.
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. Align

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti11 – 111R → H in CAA64700. (PubMed:9191074)Curated
Sequence conflicti87 – 871G → D in CAD97914. (PubMed:17974005)Curated
Sequence conflicti506 – 5061Y → H in CAA64700. (PubMed:9191074)Curated
Sequence conflicti611 – 6111A → V in CAD97914. (PubMed:17974005)Curated
Sequence conflicti616 – 6161S → I in CAA64700. (PubMed:9191074)Curated
Sequence conflicti820 – 8201G → E in CAD97914. (PubMed:17974005)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti81 – 811N → T.1 Publication
Corresponds to variant rs33932471 [ dbSNP | Ensembl ].
VAR_042138
Natural varianti235 – 2351S → A.1 Publication
Corresponds to variant rs55710198 [ dbSNP | Ensembl ].
VAR_042139
Natural varianti330 – 3301E → Q.1 Publication
Corresponds to variant rs56205382 [ dbSNP | Ensembl ].
VAR_042140
Natural varianti417 – 4171R → Q in a lung adenocarcinoma sample; somatic mutation. 1 Publication
VAR_042141
Natural varianti503 – 5031E → K in a lung large cell carcinoma sample; somatic mutation. 1 Publication
VAR_042142
Natural varianti506 – 5061Y → C.1 Publication
Corresponds to variant rs56074660 [ dbSNP | Ensembl ].
VAR_045912
Natural varianti582 – 5821G → E in a lung adenocarcinoma sample; somatic mutation. 1 Publication
VAR_042143
Natural varianti672 – 6721A → T.1 Publication
Corresponds to variant rs36050417 [ dbSNP | Ensembl ].
VAR_042144
Natural varianti673 – 6731S → T.1 Publication
Corresponds to variant rs56359290 [ dbSNP | Ensembl ].
VAR_042145
Natural varianti856 – 8561T → I in a lung squamous cell carcinoma sample; somatic mutation. 1 Publication
VAR_042146
Natural varianti959 – 9591H → R.1 Publication
Corresponds to variant rs56312931 [ dbSNP | Ensembl ].
VAR_042147
Natural varianti1032 – 10321N → S in a lung large cell carcinoma sample; somatic mutation. 1 Publication
VAR_042148

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 6969Missing in isoform 3. 1 PublicationVSP_039118Add
BLAST
Alternative sequencei563 – 5631F → SV in isoform 3. 1 PublicationVSP_039119
Alternative sequencei597 – 61923SCCEC…PSLIW → R in isoform 2. CuratedVSP_002999Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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_004430.4. NM_004439.6. [P54756-1]
NP_872272.2. NM_182472.3. [P54756-2]
UniGeneiHs.654492.

Genome annotation databases

EnsembliENST00000273854; ENSP00000273854; ENSG00000145242. [P54756-1]
ENST00000354839; ENSP00000346899; ENSG00000145242. [P54756-2]
GeneIDi2044.
KEGGihsa:2044.
UCSCiuc003hcx.3. human. [P54756-3]
uc003hcy.3. human. [P54756-1]
uc003hcz.3. human. [P54756-2]

Polymorphism databases

DMDMi259016353.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS3513.1. [P54756-1 ]
CCDS3514.1. [P54756-2 ]
RefSeqi NP_004430.4. NM_004439.6. [P54756-1 ]
NP_872272.2. NM_182472.3. [P54756-2 ]
UniGenei Hs.654492.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2R2P X-ray 2.40 A 653-939 [» ]
4ET7 X-ray 2.60 A 59-235 [» ]
ProteinModelPortali P54756.
SMRi P54756. Positions 57-562, 662-940, 966-1026.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108358. 5 interactions.
IntActi P54756. 1 interaction.
MINTi MINT-4722838.
STRINGi 9606.ENSP00000273854.

Chemistry

BindingDBi P54756.
ChEMBLi CHEMBL2363043.
GuidetoPHARMACOLOGYi 1825.

PTM databases

PhosphoSitei P54756.

Polymorphism databases

DMDMi 259016353.

Proteomic databases

MaxQBi P54756.
PaxDbi P54756.
PRIDEi P54756.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000273854 ; ENSP00000273854 ; ENSG00000145242 . [P54756-1 ]
ENST00000354839 ; ENSP00000346899 ; ENSG00000145242 . [P54756-2 ]
GeneIDi 2044.
KEGGi hsa:2044.
UCSCi uc003hcx.3. human. [P54756-3 ]
uc003hcy.3. human. [P54756-1 ]
uc003hcz.3. human. [P54756-2 ]

Organism-specific databases

CTDi 2044.
GeneCardsi GC04M066193.
HGNCi HGNC:3389. EPHA5.
MIMi 600004. gene.
neXtProti NX_P54756.
PharmGKBi PA27821.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00760000118975.
HOVERGENi HBG062180.
InParanoidi P54756.
KOi K05106.
OMAi PSLIWRC.
OrthoDBi EOG7VTDM6.
PhylomeDBi P54756.
TreeFami TF315608.

Enzyme and pathway databases

BRENDAi 2.7.10.1. 2681.
SignaLinki P54756.

Miscellaneous databases

ChiTaRSi EPHA5. human.
EvolutionaryTracei P54756.
GeneWikii EPH_receptor_A5.
GenomeRNAii 2044.
NextBioi 8305.
PROi P54756.
SOURCEi Search...

Gene expression databases

Bgeei P54756.
CleanExi HS_EPHA5.
ExpressionAtlasi P54756. baseline and differential.
Genevestigatori P54756.

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.
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 ]
Pfami PF14575. 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 ]
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 PS01186. 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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.
    , 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.

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: October 29, 2014
This is version 156 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

External Data

Dasty 3