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Q15375 (EPHA7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 152. 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·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ephrin type-A receptor 7

EC=2.7.10.1
Alternative name(s):
EPH homology kinase 3
Short name=EHK-3
EPH-like kinase 11
Short name=EK11
Short name=hEK11
Gene names
Name:EPHA7
Synonyms:EHK3, HEK11
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length998 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 is a cognate/functional ligand for EPHA7 and their interaction regulates brain development modulating cell-cell adhesion and repulsion. Has a repellent activity on axons and is for instance involved in the guidance of corticothalamic axons and in the proper topographic mapping of retinal axons to the colliculus. May also regulate brain development through a caspase(CASP3)-dependent proapoptotic activity. Forward signaling may result in activation of components of the ERK signaling pathway including MAP2K1, MAP2K2, MAPK1 AND MAPK3 which are phosphorylated upon activation of EPHA7. Ref.8

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. Interacts (via PDZ-binding motif) with GRIP1 and PICK1 (via PDZ domain) By similarity.

Subcellular location

Cell membrane Probable; Single-pass type I membrane protein Probable.

Tissue specificity

Widely expressed.

Post-translational modification

Phosphorylated By similarity.

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.

Sequence caution

The sequence BAD92506.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processApoptosis
Neurogenesis
   Cellular componentCell membrane
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
Signal
Transmembrane
Transmembrane helix
   LigandATP-binding
Nucleotide-binding
   Molecular functionDevelopmental protein
Kinase
Receptor
Transferase
Tyrosine-protein kinase
   PTMGlycoprotein
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processbrain development

Inferred from sequence or structural similarity. Source: UniProtKB

branching morphogenesis of a nerve

Inferred from sequence or structural similarity. Source: UniProtKB

ephrin receptor signaling pathway

Inferred from direct assay Ref.8. Source: UniProtKB

negative chemotaxis

Inferred from sequence or structural similarity. Source: UniProtKB

peptidyl-tyrosine phosphorylation

Inferred from sequence or structural similarity. Source: GOC

phosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of neuron apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of ERK1 and ERK2 cascade

Inferred from direct assay Ref.8. Source: UniProtKB

regulation of cell-cell adhesion

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of cysteine-type endopeptidase activity involved in apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of peptidyl-tyrosine phosphorylation

Inferred from direct assay Ref.8. Source: UniProtKB

regulation of protein autophosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

retinal ganglion cell axon guidance

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentdendrite

Inferred from electronic annotation. Source: Ensembl

integral component of plasma membrane

Inferred from electronic annotation. Source: InterPro

neuromuscular junction

Inferred from electronic annotation. Source: Ensembl

neuronal cell body

Inferred from electronic annotation. Source: Ensembl

postsynaptic membrane

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

GPI-linked ephrin receptor activity

Inferred from sequence or structural similarity. Source: UniProtKB

axon guidance receptor activity

Inferred from sequence or structural similarity. Source: UniProtKB

chemorepellent activity

Inferred from sequence or structural similarity. Source: UniProtKB

protein tyrosine kinase activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Efna1P527932EBI-1383428,EBI-5241529From a different organism.
EPHA2P293173EBI-1383428,EBI-702104

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q15375-1)

Also known as: EPHA7-FL;

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: Q15375-2)

The sequence of this isoform differs from the canonical sequence as follows:
     540-544: Missing.
Note: May be due to a competing donor splice site.
Isoform 3 (identifier: Q15375-3)

The sequence of this isoform differs from the canonical sequence as follows:
     278-279: PC → RK
     280-998: Missing.
Note: No experimental confirmation available.
Isoform 4 (identifier: Q15375-4)

The sequence of this isoform differs from the canonical sequence as follows:
     600-604: FKFPG → C
Note: No experimental confirmation available.
Isoform 5 (identifier: Q15375-5)

Also known as: EPHA7-S;

The sequence of this isoform differs from the canonical sequence as follows:
     442-450: APSQVSGVM → GMFCVYLH
     451-998: Missing.
Note: Expressed in lung cancer cells, lacks the kinase domain and is most probably secreted.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727 Potential
Chain28 – 998971Ephrin type-A receptor 7
PRO_0000016818

Regions

Topological domain28 – 555528Extracellular Potential
Transmembrane556 – 57621Helical; Potential
Topological domain577 – 998422Cytoplasmic Potential
Domain32 – 210179Eph LBD
Domain331 – 441111Fibronectin type-III 1
Domain442 – 53796Fibronectin type-III 2
Domain633 – 894262Protein kinase
Domain923 – 98765SAM
Nucleotide binding639 – 6479ATP By similarity
Motif996 – 9983PDZ-binding Potential
Compositional bias192 – 328137Cys-rich

Sites

Active site7581Proton acceptor By similarity
Binding site6651ATP By similarity

Amino acid modifications

Modified residue6081Phosphotyrosine; by autocatalysis Potential
Modified residue6141Phosphotyrosine; by autocatalysis Potential
Modified residue7911Phosphotyrosine; by autocatalysis Potential
Modified residue9401Phosphotyrosine; by autocatalysis Potential
Glycosylation3431N-linked (GlcNAc...) Potential
Glycosylation4101N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence278 – 2792PC → RK in isoform 3.
VSP_014380
Alternative sequence280 – 998719Missing in isoform 3.
VSP_014381
Alternative sequence442 – 4509APSQVSGVM → GMFCVYLH in isoform 5.
VSP_041943
Alternative sequence451 – 998548Missing in isoform 5.
VSP_041944
Alternative sequence540 – 5445Missing in isoform 2.
VSP_014382
Alternative sequence600 – 6045FKFPG → C in isoform 4.
VSP_041945
Natural variant1381I → V. Ref.6 Ref.12
Corresponds to variant rs2278107 [ dbSNP | Ensembl ].
VAR_022105
Natural variant1701E → K in a colorectal adenocarcinoma sample; somatic mutation. Ref.12
VAR_042150
Natural variant2321G → R in a metastatic melanoma sample; somatic mutation. Ref.12
VAR_042151
Natural variant2781P → S. Ref.12
Corresponds to variant rs2278106 [ dbSNP | Ensembl ].
VAR_022106
Natural variant3711R → W in a colorectal cancer sample; somatic mutation. Ref.11
VAR_036090
Natural variant9031P → S in a metastatic melanoma sample; somatic mutation. Ref.12
VAR_042152

Experimental info

Isoform 3:
Sequence conflict2781R → C in AAH27940. Ref.6

Secondary structure

......................................................................................... 998
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (EPHA7-FL) [UniParc].

Last modified May 1, 2007. Version 3.
Checksum: 479B9CA0D2BB06EB

FASTA998112,097
        10         20         30         40         50         60 
MVFQTRYPSW IILCYIWLLR FAHTGEAQAA KEVLLLDSKA QQTELEWISS PPNGWEEISG 

        70         80         90        100        110        120 
LDENYTPIRT YQVCQVMEPN QNNWLRTNWI SKGNAQRIFV ELKFTLRDCN SLPGVLGTCK 

       130        140        150        160        170        180 
ETFNLYYYET DYDTGRNIRE NLYVKIDTIA ADESFTQGDL GERKMKLNTE VREIGPLSKK 

       190        200        210        220        230        240 
GFYLAFQDVG ACIALVSVKV YYKKCWSIIE NLAIFPDTVT GSEFSSLVEV RGTCVSSAEE 

       250        260        270        280        290        300 
EAENAPRMHC SAEGEWLVPI GKCICKAGYQ QKGDTCEPCG RGFYKSSSQD LQCSRCPTHS 

       310        320        330        340        350        360 
FSDKEGSSRC ECEDGYYRAP SDPPYVACTR PPSAPQNLIF NINQTTVSLE WSPPADNGGR 

       370        380        390        400        410        420 
NDVTYRILCK RCSWEQGECV PCGSNIGYMP QQTGLEDNYV TVMDLLAHAN YTFEVEAVNG 

       430        440        450        460        470        480 
VSDLSRSQRL FAAVSITTGQ AAPSQVSGVM KERVLQRSVE LSWQEPEHPN GVITEYEIKY 

       490        500        510        520        530        540 
YEKDQRERTY STVKTKSTSA SINNLKPGTV YVFQIRAFTA AGYGNYSPRL DVATLEEATG 

       550        560        570        580        590        600 
KMFEATAVSS EQNPVIIIAV VAVAGTIILV FMVFGFIIGR RHCGYSKADQ EGDEELYFHF 

       610        620        630        640        650        660 
KFPGTKTYID PETYEDPNRA VHQFAKELDA SCIKIERVIG AGEFGEVCSG RLKLPGKRDV 

       670        680        690        700        710        720 
AVAIKTLKVG YTEKQRRDFL CEASIMGQFD HPNVVHLEGV VTRGKPVMIV IEFMENGALD 

       730        740        750        760        770        780 
AFLRKHDGQF TVIQLVGMLR GIAAGMRYLA DMGYVHRDLA ARNILVNSNL VCKVSDFGLS 

       790        800        810        820        830        840 
RVIEDDPEAV YTTTGGKIPV RWTAPEAIQY RKFTSASDVW SYGIVMWEVM SYGERPYWDM 

       850        860        870        880        890        900 
SNQDVIKAIE EGYRLPAPMD CPAGLHQLML DCWQKERAER PKFEQIVGIL DKMIRNPNSL 

       910        920        930        940        950        960 
KTPLGTCSRP ISPLLDQNTP DFTTFCSVGE WLQAIKMERY KDNFTAAGYN SLESVARMTI 

       970        980        990 
EDVMSLGITL VGHQKKIMSS IQTMRAQMLH LHGTGIQV 

« Hide

Isoform 2 [UniParc].

Checksum: 4DEE43AD86F2CA11
Show »

FASTA993111,504
Isoform 3 [UniParc].

Checksum: 54A2687994762500
Show »

FASTA27931,833
Isoform 4 [UniParc].

Checksum: E35ED97999DBF944
Show »

FASTA994111,623
Isoform 5 (EPHA7-S) [UniParc].

Checksum: 4E15BF1881AC175A
Show »

FASTA44950,521

References

« Hide 'large scale' references
[1]"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] (ISOFORM 1).
Tissue: Fetal brain.
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[3]Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Brain.
[4]"The DNA sequence and analysis of human chromosome 6."
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4), VARIANT VAL-138.
Tissue: Brain.
[7]"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.
[8]"ALL1 fusion proteins induce deregulation of EphA7 and ERK phosphorylation in human acute leukemias."
Nakanishi H., Nakamura T., Canaani E., Croce C.M.
Proc. Natl. Acad. Sci. U.S.A. 104:14442-14447(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN MAP2K1; MAP2K2; MAPK1 AND MAPK3 PHOSPHORYLATION.
[9]"Secreted form of EphA7 in lung cancer."
Tsuboi M., Mori H., Bunai T., Kageyama S., Suzuki M., Okudela K., Takamochi K., Ogawa H., Niwa H., Shinmura K., Sugimura H.
Int. J. Oncol. 36:635-640(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING (ISOFORM 5).
[10]"Ephrin A7 ligand binding domain."
Walker J.R., Yermekbayeva L., Seitova A., Kania J., Bountra C., Weigelt J., Arrowsmith C.H., Edwards A.M., Bochkarev A., Dhe-Paganon S.
Submitted (JUN-2010) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 32-204.
[11]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] TRP-371.
[12]"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] VAL-138; LYS-170; ARG-232; SER-278 AND SER-903.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L36642 mRNA. Translation: AAA74243.1.
AK313529 mRNA. Translation: BAG36308.1.
AB209269 mRNA. Translation: BAD92506.1. Different initiation.
AL121966 Genomic DNA. Translation: CAC19520.2.
AL354857, AL121966, AL591036 Genomic DNA. Translation: CAH72780.1.
AL591036, AL121966, AL354857 Genomic DNA. Translation: CAH73650.1.
AL121966, AL354857, AL591036 Genomic DNA. Translation: CAI19722.1.
CH471051 Genomic DNA. Translation: EAW48518.1.
BC027940 mRNA. Translation: AAH27940.1.
BC126125 mRNA. Translation: AAI26126.1.
BC126151 mRNA. Translation: AAI26152.1.
BC143857 mRNA. Translation: AAI43858.1.
BC143858 mRNA. Translation: AAI43859.1.
PIRI58351.
RefSeqNP_001275558.1. NM_001288629.1.
NP_001275559.1. NM_001288630.1.
NP_004431.1. NM_004440.3.
XP_005248726.1. XM_005248669.1.
UniGeneHs.73962.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2REIX-ray1.60A590-899[»]
3DKOX-ray2.00A590-899[»]
3H8MX-ray2.10A/B919-990[»]
3NRUX-ray2.30A/B/C/D/E/F/G/H/I/J/K/L32-204[»]
ProteinModelPortalQ15375.
SMRQ15375. Positions 30-899, 919-989.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108359. 8 interactions.
IntActQ15375. 9 interactions.
MINTMINT-1538326.
STRING9606.ENSP00000358309.

Chemistry

BindingDBQ15375.
ChEMBLCHEMBL4602.
GuidetoPHARMACOLOGY1827.

PTM databases

PhosphoSiteQ15375.

Polymorphism databases

DMDM146345416.

Proteomic databases

PaxDbQ15375.
PRIDEQ15375.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000369297; ENSP00000358303; ENSG00000135333. [Q15375-3]
ENST00000369303; ENSP00000358309; ENSG00000135333. [Q15375-1]
GeneID2045.
KEGGhsa:2045.
UCSCuc003poe.3. human. [Q15375-1]
uc003pof.3. human. [Q15375-2]
uc003pog.4. human. [Q15375-3]
uc011eac.2. human. [Q15375-4]

Organism-specific databases

CTD2045.
GeneCardsGC06M094007.
HGNCHGNC:3390. EPHA7.
HPACAB010496.
MIM602190. gene.
neXtProtNX_Q15375.
PharmGKBPA27822.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOVERGENHBG062180.
InParanoidQ15375.
KOK05108.
OMAPSGWEEI.
OrthoDBEOG7VTDM6.
PhylomeDBQ15375.
TreeFamTF315608.

Enzyme and pathway databases

BRENDA2.7.10.1. 2681.
SignaLinkQ15375.

Gene expression databases

BgeeQ15375.
CleanExHS_EPHA7.
GenevestigatorQ15375.

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.
IPR009030. Growth_fac_rcpt_N_dom.
IPR013783. Ig-like_fold.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001660. SAM.
IPR013761. SAM/pointed.
IPR011510. SAM_2.
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]
PfamPF14575. EphA2_TM. 1 hit.
PF01404. Ephrin_lbd. 1 hit.
PF00041. fn3. 2 hits.
PF07699. GCC2_GCC3. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
PF07647. SAM_2. 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.
SSF57184. SSF57184. 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

EvolutionaryTraceQ15375.
GeneWikiEPHA7.
GenomeRNAi2045.
NextBio8311.
PROQ15375.
SOURCESearch...

Entry information

Entry nameEPHA7_HUMAN
AccessionPrimary (citable) accession number: Q15375
Secondary accession number(s): A0AUX7 expand/collapse secondary AC list , B2R8W1, B7ZLJ9, B7ZLK0, Q59G40, Q5VTU0, Q8N368, Q9H124
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 1, 2007
Last modified: April 16, 2014
This is version 152 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 6

Human chromosome 6: entries, gene names and cross-references to MIM