Q15375 (EPHA7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

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	998 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 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 process	Apoptosis Neurogenesis
Cellular component	Cell membrane Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat Signal Transmembrane Transmembrane helix
Ligand	ATP-binding Nucleotide-binding
Molecular function	Developmental protein Kinase Receptor Transferase Tyrosine-protein kinase
PTM	Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	brain development Inferred from sequence or structural similarity. Source: UniProtKB branching morphogenesis of a nerve 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: Compara
Cellular_component	dendrite Inferred from electronic annotation. Source: Compara integral to plasma membrane Inferred from electronic annotation. Source: InterPro neuromuscular junction Inferred from electronic annotation. Source: Compara neuronal cell body Inferred from electronic annotation. Source: Compara postsynaptic membrane Inferred from electronic annotation. Source: Compara
Molecular_function	ATP 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
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Efna1	P52793	2	EBI-1383428,EBI-5241529	From a different organism.
EPHA2	P29317	3	EBI-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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 27

27

Potential

Chain

28 – 998

971

Ephrin type-A receptor 7

PRO_0000016818

Regions

Topological domain

28 – 555

528

Extracellular Potential

Transmembrane

556 – 576

21

Helical; Potential

Topological domain

577 – 998

422

Cytoplasmic Potential

Domain

32 – 210

179

Eph LBD

Domain

331 – 433

103

Fibronectin type-III 1

Domain

443 – 535

93

Fibronectin type-III 2

Domain

633 – 894

262

Protein kinase

Domain

923 – 987

65

SAM

Nucleotide binding

639 – 647

9

ATP By similarity

Motif

996 – 998

3

PDZ-binding Potential

Compositional bias

192 – 328

137

Cys-rich

Sites

Active site

758

1

Proton acceptor By similarity

Binding site

665

1

ATP By similarity

Amino acid modifications

Modified residue

608

1

Phosphotyrosine; by autocatalysis Potential

Modified residue

614

1

Phosphotyrosine; by autocatalysis Potential

Modified residue

791

1

Phosphotyrosine; by autocatalysis Potential

Modified residue

940

1

Phosphotyrosine; by autocatalysis Potential

Glycosylation

343

1

N-linked (GlcNAc...) Potential

Glycosylation

410

1

N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence

278 – 279

2

PC → RK in isoform 3.

VSP_014380

Alternative sequence

280 – 998

719

Missing in isoform 3.

VSP_014381

Alternative sequence

442 – 450

9

APSQVSGVM → GMFCVYLH in isoform 5.

VSP_041943

Alternative sequence

451 – 998

548

Missing in isoform 5.

VSP_041944

Alternative sequence

540 – 544

5

Missing in isoform 2.

VSP_014382

Alternative sequence

600 – 604

5

FKFPG → C in isoform 4.

VSP_041945

Natural variant

138

1

I → V. Ref.6 Ref.12
Corresponds to variant rs2278107 [ dbSNP | Ensembl ].

VAR_022105

Natural variant

170

1

E → K in a colorectal adenocarcinoma sample; somatic mutation. Ref.12

VAR_042150

Natural variant

232

1

G → R in a metastatic melanoma sample; somatic mutation. Ref.12

VAR_042151

Natural variant

278

1

P → S. Ref.12
Corresponds to variant rs2278106 [ dbSNP | Ensembl ].

VAR_022106

Natural variant

371

1

R → W in a colorectal cancer sample; somatic mutation. Ref.11

VAR_036090

Natural variant

903

1

P → S in a metastatic melanoma sample; somatic mutation. Ref.12

VAR_042152

Experimental info

Isoform 3:

Sequence conflict

278

1

R → C in AAH27940. Ref.6

Secondary structure

1

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998

Helix Strand Turn

Details...

Beta strand

33 – 37

5

Beta strand

48 – 51

4

Beta strand

54 – 61

8

Beta strand

67 – 74

8

Beta strand

78 – 80

3

Beta strand

83 – 86

4

Beta strand

96 – 106

11

Turn

109 – 111

3

Beta strand

121 – 132

12

Helix

140 – 142

3

Beta strand

144 – 150

7

Beta strand

168 – 174

7

Beta strand

178 – 190

13

Beta strand

192 – 202

11

Helix

611 – 613

3

Beta strand

614 – 616

3

Helix

617 – 624

8

Helix

630 – 632

3

Beta strand

633 – 641

9

Beta strand

643 – 652

10

Beta strand

655 – 657

3

Beta strand

660 – 666

7

Helix

673 – 686

14

Beta strand

697 – 701

5

Beta strand

703 – 705

3

Beta strand

708 – 712

5

Helix

719 – 725

7

Turn

726 – 728

3

Helix

732 – 751

20

Helix

761 – 763

3

Beta strand

764 – 766

3

Beta strand

772 – 774

3

Helix

800 – 802

3

Helix

805 – 810

6

Helix

815 – 830

16

Turn

836 – 839

4

Helix

842 – 850

9

Helix

863 – 872

10

Helix

877 – 879

3

Helix

883 – 895

13

Helix

897 – 899

3

Helix

928 – 934

7

Helix

938 – 940

3

Helix

941 – 946

6

Helix

952 – 956

5

Helix

960 – 965

6

Helix

971 – 988

18

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (EPHA7-FL) [UniParc]. Last modified May 1, 2007. Version 3. Checksum: 479B9CA0D2BB06EB	FASTA	998	112,097
	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
	Isoform 2 [UniParc]. Checksum: 4DEE43AD86F2CA11	FASTA	993	111,504
	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 DVATLEEATA 550 560 570 580 590 600 TAVSSEQNPV IIIAVVAVAG TIILVFMVFG FIIGRRHCGY SKADQEGDEE LYFHFKFPGT 610 620 630 640 650 660 KTYIDPETYE DPNRAVHQFA KELDASCIKI ERVIGAGEFG EVCSGRLKLP GKRDVAVAIK 670 680 690 700 710 720 TLKVGYTEKQ RRDFLCEASI MGQFDHPNVV HLEGVVTRGK PVMIVIEFME NGALDAFLRK 730 740 750 760 770 780 HDGQFTVIQL VGMLRGIAAG MRYLADMGYV HRDLAARNIL VNSNLVCKVS DFGLSRVIED 790 800 810 820 830 840 DPEAVYTTTG GKIPVRWTAP EAIQYRKFTS ASDVWSYGIV MWEVMSYGER PYWDMSNQDV 850 860 870 880 890 900 IKAIEEGYRL PAPMDCPAGL HQLMLDCWQK ERAERPKFEQ IVGILDKMIR NPNSLKTPLG 910 920 930 940 950 960 TCSRPISPLL DQNTPDFTTF CSVGEWLQAI KMERYKDNFT AAGYNSLESV ARMTIEDVMS 970 980 990 LGITLVGHQK KIMSSIQTMR AQMLHLHGTG IQV
	Isoform 3 [UniParc]. Checksum: 54A2687994762500	FASTA	279	31,833
	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 EAENAPRMHC SAEGEWLVPI GKCICKAGYQ QKGDTCERK
	Isoform 4 [UniParc]. Checksum: E35ED97999DBF944	FASTA	994	111,623
	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 EGDEELYFHC 610 620 630 640 650 660 TKTYIDPETY EDPNRAVHQF AKELDASCIK IERVIGAGEF GEVCSGRLKL PGKRDVAVAI 670 680 690 700 710 720 KTLKVGYTEK QRRDFLCEAS IMGQFDHPNV VHLEGVVTRG KPVMIVIEFM ENGALDAFLR 730 740 750 760 770 780 KHDGQFTVIQ LVGMLRGIAA GMRYLADMGY VHRDLAARNI LVNSNLVCKV SDFGLSRVIE 790 800 810 820 830 840 DDPEAVYTTT GGKIPVRWTA PEAIQYRKFT SASDVWSYGI VMWEVMSYGE RPYWDMSNQD 850 860 870 880 890 900 VIKAIEEGYR LPAPMDCPAG LHQLMLDCWQ KERAERPKFE QIVGILDKMI RNPNSLKTPL 910 920 930 940 950 960 GTCSRPISPL LDQNTPDFTT FCSVGEWLQA IKMERYKDNF TAAGYNSLES VARMTIEDVM 970 980 990 SLGITLVGHQ KKIMSSIQTM RAQMLHLHGT GIQV
	Isoform 5 (EPHA7-S) [UniParc]. Checksum: 4E15BF1881AC175A	FASTA	449	50,521
	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 VSDLSRSQRL FAAVSITTGQ AGMFCVYLH

References

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

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

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.

IPI

IPI00016645.
IPI00607655.
IPI00607878.

PIR

I58351.

RefSeq

NP_004431.1. NM_004440.3.

UniGene

Hs.73962.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2REI	X-ray	1.60	A	590-899	[»]
3DKO	X-ray	2.00	A	590-899	[»]
3H8M	X-ray	2.10	A/B	919-990	[»]
3NRU	X-ray	2.30	A/B/C/D/E/F/G/H/I/J/K/L	32-204	[»]

ProteinModelPortal

Q15375.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q15375. 8 interactions.

STRING

9606.ENSP00000358309.

PTM databases

PhosphoSite

Q15375.

Polymorphism databases

DMDM

146345416.

Proteomic databases

PaxDb

Q15375.

PRIDE

Q15375.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000369297; ENSP00000358303; ENSG00000135333.
ENST00000369303; ENSP00000358309; ENSG00000135333.

GeneID

2045.

KEGG

hsa:2045.

UCSC

uc003poe.3. human.
uc003pof.3. human.
uc003pog.4. human.

Organism-specific databases

CTD

2045.

GeneCards

GC06M094007.

HGNC

HGNC:3390. EPHA7.

HPA

CAB010496.

MIM

602190. gene.

neXtProt

NX_Q15375.

PharmGKB

PA27822.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0515.

HOVERGEN

HBG062180.

InParanoid

Q15375.

KO

K05108.

OMA

LEDNYVT.

OrthoDB

EOG4H19TZ.

PhylomeDB

Q15375.

Enzyme and pathway databases

BRENDA

2.7.10.1. 2681.

Pathway_Interaction_DB

epha_fwdpathway. EPHA forward signaling.
ephrina_ephapathway. EphrinA-EPHA pathway.

Gene expression databases

Bgee

Q15375.

CleanEx

HS_EPHA7.

Genevestigator

Q15375.

GermOnline

ENSG00000135333. Homo sapiens.

Family and domain databases

Gene3D

1.10.150.50. 1 hit.
2.60.40.10. 2 hits.

InterPro

IPR001090. Ephrin_rcpt_lig-bd_dom.
IPR003961. Fibronectin_type3.
IPR008979. Galactose-bd-like.
IPR009030. Growth_fac_rcpt.
IPR013783. Ig-like_fold.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_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]

Pfam

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]

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.
SSF57184. Grow_fac_recept. 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

Q15375.

ChEMBL

CHEMBL4602.

EvolutionaryTrace

Q15375.

GenomeRNAi

2045.

NextBio

8311.

SOURCE

Search...

Entry information

Entry name

EPHA7_HUMAN

Accession

Primary (citable) accession number: Q15375
Secondary accession number(s): A0AUX7 , 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:	May 1, 2013
This is version 142 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.