P54756 (EPHA5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	EPHA5
Synonyms:	BSK, EHK1, HEK7, TYRO4

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1037 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 projection › axon By similarity. Cell projection › dendrite 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 process	Neurogenesis
Cellular component	Cell membrane Cell projection Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat Signal Transmembrane Transmembrane helix
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Receptor Transferase Tyrosine-protein kinase
PTM	Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	axon guidance Inferred from sequence or structural similarity. Source: UniProtKB cAMP-mediated signaling 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: Compara 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_component	axon 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 to 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 rough endoplasmic reticulum Inferred from direct assay Ref.7. Source: UniProtKB
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW GPI-linked 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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 24

24

Potential

Chain

25 – 1037

1013

Ephrin type-A receptor 5

PRO_0000016812

Regions

Topological domain

25 – 573

549

Extracellular Potential

Transmembrane

574 – 594

21

Helical; Potential

Topological domain

595 – 1037

443

Cytoplasmic Potential

Domain

60 – 238

179

Eph LBD

Domain

357 – 459

103

Fibronectin type-III 1

Domain

469 – 559

91

Fibronectin type-III 2

Domain

675 – 936

262

Protein kinase

Domain

965 – 1029

65

SAM

Nucleotide binding

681 – 689

9

ATP By similarity

Motif

1035 – 1037

3

PDZ-binding Potential

Compositional bias

220 – 354

135

Cys-rich

Sites

Active site

800

1

Proton acceptor By similarity

Binding site

707

1

ATP By similarity

Amino acid modifications

Modified residue

650

1

Phosphotyrosine; by autocatalysis By similarity

Modified residue

656

1

Phosphotyrosine; by autocatalysis By similarity

Modified residue

833

1

Phosphotyrosine; by autocatalysis Potential

Modified residue

982

1

Phosphotyrosine; by autocatalysis By similarity

Glycosylation

264

1

N-linked (GlcNAc...) Potential

Glycosylation

299

1

N-linked (GlcNAc...) Potential

Glycosylation

369

1

N-linked (GlcNAc...) Potential

Glycosylation

423

1

N-linked (GlcNAc...) Potential

Glycosylation

436

1

N-linked (GlcNAc...) Potential

Glycosylation

461

1

N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence

1 – 69

69

Missing in isoform 3.

VSP_039118

Alternative sequence

563

1

F → SV in isoform 3.

VSP_039119

Alternative sequence

597 – 619

23

SCCEC…PSLIW → R in isoform 2.

VSP_002999

Natural variant

81

1

N → T. Ref.8
Corresponds to variant rs33932471 [ dbSNP | Ensembl ].

VAR_042138

Natural variant

235

1

S → A. Ref.8
Corresponds to variant rs55710198 [ dbSNP | Ensembl ].

VAR_042139

Natural variant

330

1

E → Q. Ref.8
Corresponds to variant rs56205382 [ dbSNP | Ensembl ].

VAR_042140

Natural variant

417

1

R → Q in a lung adenocarcinoma sample; somatic mutation. Ref.8

VAR_042141

Natural variant

503

1

E → K in a lung large cell carcinoma sample; somatic mutation. Ref.8

VAR_042142

Natural variant

506

1

Y → C. Ref.8
Corresponds to variant rs56074660 [ dbSNP | Ensembl ].

VAR_045912

Natural variant

582

1

G → E in a lung adenocarcinoma sample; somatic mutation. Ref.8

VAR_042143

Natural variant

672

1

A → T. Ref.8
Corresponds to variant rs36050417 [ dbSNP | Ensembl ].

VAR_042144

Natural variant

673

1

S → T. Ref.8
Corresponds to variant rs56359290 [ dbSNP | Ensembl ].

VAR_042145

Natural variant

856

1

T → I in a lung squamous cell carcinoma sample; somatic mutation. Ref.8

VAR_042146

Natural variant

959

1

H → R. Ref.8
Corresponds to variant rs56312931 [ dbSNP | Ensembl ].

VAR_042147

Natural variant

1032

1

N → S in a lung large cell carcinoma sample; somatic mutation. Ref.8

VAR_042148

Experimental info

Sequence conflict

11

1

R → H in CAA64700. Ref.1

Sequence conflict

87

1

G → D in CAD97914. Ref.3

Sequence conflict

506

1

Y → H in CAA64700. Ref.1

Sequence conflict

611

1

A → V in CAD97914. Ref.3

Sequence conflict

616

1

S → I in CAA64700. Ref.1

Sequence conflict

820

1

G → E in CAD97914. Ref.3

Secondary structure

1

.

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1037

Helix Strand Turn

Details...

Helix

663 – 665

3

Helix

672 – 674

3

Beta strand

675 – 683

9

Beta strand

685 – 694

10

Beta strand

702 – 708

7

Helix

715 – 728

14

Beta strand

739 – 743

5

Beta strand

745 – 748

4

Beta strand

750 – 754

5

Helix

761 – 766

6

Turn

767 – 770

4

Helix

774 – 793

20

Helix

803 – 805

3

Beta strand

806 – 808

3

Beta strand

814 – 816

3

Helix

842 – 844

3

Helix

847 – 852

6

Helix

857 – 873

17

Turn

878 – 881

4

Helix

884 – 893

10

Helix

905 – 914

10

Helix

919 – 921

3

Helix

925 – 936

12

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified September 22, 2009. Version 3. Checksum: 578C2F4D950DE419	FASTA	1,037	114,803
	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
	Isoform 2 [UniParc]. Checksum: 0C0121184BCE631E	FASTA	1,015	112,624
	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 GVLLSGRRCG 610 620 630 640 650 660 YSKAKQDPEE EKMHFHNGHI KLPGVRTYID PHTYEDPNQA VHEFAKEIEA SCITIERVIG 670 680 690 700 710 720 AGEFGEVCSG RLKLPGKREL PVAIKTLKVG YTEKQRRDFL GEASIMGQFD HPNIIHLEGV 730 740 750 760 770 780 VTKSKPVMIV TEYMENGSLD TFLKKNDGQF TVIQLVGMLR GISAGMKYLS DMGYVHRDLA 790 800 810 820 830 840 ARNILINSNL VCKVSDFGLS RVLEDDPEAA YTTRGGKIPI RWTAPEAIAF RKFTSASDVW 850 860 870 880 890 900 SYGIVMWEVV SYGERPYWEM TNQDVIKAVE EGYRLPSPMD CPAALYQLML DCWQKERNSR 910 920 930 940 950 960 PKFDEIVNML DKLIRNPSSL KTLVNASCRV SNLLAEHSPL GSGAYRSVGE WLEAIKMGRY 970 980 990 1000 1010 TEIFMENGYS SMDAVAQVTL EDLRRLGVTL VGHQKKIMNS LQEMKVQLVN GMVPL
	Isoform 3 [UniParc]. Checksum: 3038A240682F6E84	FASTA	969	107,699
	10 20 30 40 50 60 MGDLGWIAFP KNGWEEIGEV DENYAPIHTY QVCKVMEQNQ NNWLLTSWIS NEGASRIFIE 70 80 90 100 110 120 LKFTLRDCNS LPGGLGTCKE TFNMYYFESD DQNGRNIKEN QYIKIDTIAA DESFTELDLG 130 140 150 160 170 180 DRVMKLNTEV RDVGPLSKKG FYLAFQDVGA CIALVSVRVY YKKCPSVVRH LAVFPDTITG 190 200 210 220 230 240 ADSSQLLEVS GSCVNHSVTD EPPKMHCSAE GEWLVPIGKC MCKAGYEEKN GTCQVCRPGF 250 260 270 280 290 300 FKASPHIQSC GKCPPHSYTH EEASTSCVCE KDYFRRESDP PTMACTRPPS APRNAISNVN 310 320 330 340 350 360 ETSVFLEWIP PADTGGRKDV SYYIACKKCN SHAGVCEECG GHVRYLPRQS GLKNTSVMMV 370 380 390 400 410 420 DLLAHTNYTF EIEAVNGVSD LSPGARQYVS VNVTTNQAAP SPVTNVKKGK IAKNSISLSW 430 440 450 460 470 480 QEPDRPNGII LEYEIKYFEK DQETSYTIIK SKETTITAEG LKPASVYVFQ IRARTAAGYG 490 500 510 520 530 540 VFSRRFEFET TPVSVAASSD QSQIPVIAVS VTVGVILLAV VIGVLLSGSC CECGCGRASS 550 560 570 580 590 600 LCAVAHPSLI WRCGYSKAKQ DPEEEKMHFH NGHIKLPGVR TYIDPHTYED PNQAVHEFAK 610 620 630 640 650 660 EIEASCITIE RVIGAGEFGE VCSGRLKLPG KRELPVAIKT LKVGYTEKQR RDFLGEASIM 670 680 690 700 710 720 GQFDHPNIIH LEGVVTKSKP VMIVTEYMEN GSLDTFLKKN DGQFTVIQLV GMLRGISAGM 730 740 750 760 770 780 KYLSDMGYVH RDLAARNILI NSNLVCKVSD FGLSRVLEDD PEAAYTTRGG KIPIRWTAPE 790 800 810 820 830 840 AIAFRKFTSA SDVWSYGIVM WEVVSYGERP YWEMTNQDVI KAVEEGYRLP SPMDCPAALY 850 860 870 880 890 900 QLMLDCWQKE RNSRPKFDEI VNMLDKLIRN PSSLKTLVNA SCRVSNLLAE HSPLGSGAYR 910 920 930 940 950 960 SVGEWLEAIK MGRYTEIFME NGYSSMDAVA QVTLEDLRRL GVTLVGHQKK IMNSLQEMKV QLVNGMVPL

References

	« Hide 'large scale' referencesShow '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. , 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. , 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.

IPI

IPI00008290.
IPI00215945.
IPI00964566.

RefSeq

NP_004430.4. NM_004439.5.
NP_872272.2. NM_182472.2.

UniGene

Hs.654492.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2R2P	X-ray	2.40	A	653-939	[»]

ProteinModelPortal

P54756.

ModBase

Search...

Protein-protein interaction databases

MINT

MINT-4722838.

STRING

9606.ENSP00000273854.

PTM databases

PhosphoSite

P54756.

Polymorphism databases

DMDM

259016353.

Proteomic databases

PaxDb

P54756.

PRIDE

P54756.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000273854; ENSP00000273854; ENSG00000145242.
ENST00000354839; ENSP00000346899; ENSG00000145242.

GeneID

2044.

KEGG

hsa:2044.

UCSC

uc003hcx.3. human.
uc003hcy.3. human.
uc003hcz.3. human.

Organism-specific databases

CTD

2044.

GeneCards

GC04M066193.

HGNC

HGNC:3389. EPHA5.

MIM

600004. gene.

neXtProt

NX_P54756.

PharmGKB

PA27821.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0515.

HOVERGEN

HBG062180.

InParanoid

P54756.

KO

K05106.

OMA

FHNGHIK.

OrthoDB

EOG4894KT.

PhylomeDB

P54756.

Enzyme and pathway databases

BRENDA

2.7.10.1. 2681.

Pathway_Interaction_DB

epha_fwdpathway. EPHA forward signaling.
ephrinarevpathway. Ephrin A reverse signaling.
ephrina_ephapathway. EphrinA-EPHA pathway.

SignaLink

P54756.

Gene expression databases

ArrayExpress

P54756.

Bgee

P54756.

CleanEx

HS_EPHA5.

Genevestigator

P54756.

GermOnline

ENSG00000145242. Homo sapiens.

Family and domain databases

Gene3D

1.10.150.50. 1 hit.
2.60.120.260. 1 hit.
2.60.40.10. 2 hits.

InterPro

IPR001090. Ephrin_rcpt_lig-bd_dom.
IPR003961. Fibronectin_type3.
IPR008979. Galactose-bd-like.
IPR013783. Ig-like_fold.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_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]

Pfam

PF01404. Ephrin_lbd. 1 hit.
PF00041. fn3. 2 hits.
PF07714. Pkinase_Tyr. 1 hit.
PF00536. SAM_1. 1 hit.
[Graphical view]

PIRSF

PIRSF000666. TyrPK_ephrin_receptor. 1 hit.

PRINTS

PR00109. TYRKINASE.

SMART

SM00615. EPH_lbd. 1 hit.
SM00060. FN3. 2 hits.
SM00454. SAM. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]

SUPFAM

SSF49265. FN_III-like. 2 hits.
SSF49785. Gal_bind_like. 1 hit.
SSF56112. Kinase_like. 1 hit.
SSF47769. SAM_homology. 1 hit.

PROSITE

PS01186. EGF_2. 1 hit. Uncertain.
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]

ProtoNet

Search...

Other

BindingDB

P54756.

ChEMBL

CHEMBL3987.

ChiTaRS

EPHA5. human.

EvolutionaryTrace

P54756.

GenomeRNAi

2044.

NextBio

8305.

SOURCE

Search...

Entry information

Entry name

EPHA5_HUMAN

Accession

Primary (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:	May 29, 2013
This is version 143 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.