EPHA7 (EPH receptor A7)

Identity

Other names	EHK3
	HEK11
Hugo	EPHA7
Location	6q16.1

DNA/RNA

Description	The EPHA7 gene maps on chromosome 6q16.1 spanning 178,134 bp. it contains 17 exons, the orientation of the gene is complement.
Transcription	rTanscript of 5,229 bp.

Protein

Description	EPHA7 encodes 998 amino acids, theoretical pI is 5.58, theoretical molecular weight is 112 KDa, tyrosine kinase, catalytic domain, sterile alpha motif, 2 fibronectin type 3 domains, ephrin receptor ligand binding domain and tumor necrosis factor receptor domain.
Expression	in brain, skeletal muscle, lung, kidney, liver, colorectum and nerve system.
Localisation	Located in the membrane.
Function	ATP Binding, ephrin receptor activity, nucleotide binding, protein binding, receptor activity, transferase activity.
Homology	Homo sapiens: EPHA5 isoform b [NP_872272] (64%), EPHA5 isoform a [NP_004430] (63%), EPHA4 [NP_004429] (63%), EPHA3 [AAG43576] (63%).

Implicated in

Entity	Colorectal cancer
Note	A significant reduction of EphA7 expression in human colorectal cancers was shown using semiquantitative reverse transcription-polymerase chain reaction analysis in 59 colorectal cancer tissues, compared to corresponding normal mucosas (P=0.008), and five colon cancer cell lines. To investigate the mechanism of EphA7 downregulation in colorectal cancer, we examined the methylation status of the 5'CpG island around the translation start site in five colon cancer cell lines using restriction enzymes, methylation-specific PCR, and bisulfite sequencing and found evidence of aberrant methylation. The expression of EphA7 in colon cancer cell lines was restored after treatment with 5-aza-2'-deoxycytidine. Analysis of methylation status in totally 75 tumors compared to clinicopathological parameters revealed that hypermethylation of colorectal cancers was more frequent in male than in female, and in moderately differentiated than in well-differentiated adenocarcinomas. There was a tendency that hypermethylation in rectal cancers was more frequent than in colon cancers. Hypermethylation was also observed in colorectal adenomas. This is the first report describing the downregulation of an Eph family gene in a solid tumor via aberrant 5'CpG island methylation. It provides the evidence that EphA7 gene is involved in human colorectal carcinogenesis.

External links

	Nomenclature
Hugo	EPHA7
GDB	EPHA7
Entrez_Gene	EPHA7  2045  EPH receptor A7
	Cards
Atlas	EPHA7ID40466ch6q16
GeneCards	EPHA7
Ensembl	EPHA7 [Search_View]   ENSG00000135333 [Gene_View]
Genatlas	EPHA7
GeneLynx	EPHA7
eGenome	EPHA7
euGene	2045
	Genomic and cartography
GoldenPath	EPHA7  -  6q16.1   chr6:94007862-94185993 -  6q16.1   [Description]    (hg18-Mar_2006)
Ensembl	EPHA7 - 6q16.1 [CytoView]
NCBI	Mapview
OMIM	Disease map [OMIM]
HomoloGene	EPHA7
	Gene and transcription
Genbank	AB209269 [ ENTREZ ]
Genbank	AL699163 [ ENTREZ ]
Genbank	BC027940 [ ENTREZ ]
Genbank	BC126125 [ ENTREZ ]
Genbank	BC126151 [ ENTREZ ]
RefSeq	NM_004440 [ SRS ]    NM_004440 [ ENTREZ ]
RefSeq	AC_000049 [ SRS ]    AC_000049 [ ENTREZ ]
RefSeq	NC_000006 [ SRS ]    NC_000006 [ ENTREZ ]
RefSeq	NT_007299 [ SRS ]    NT_007299 [ ENTREZ ]
RefSeq	NW_923184 [ SRS ]    NW_923184 [ ENTREZ ]
AceView	EPHA7 AceView - NCBI
Unigene	Hs.73962 [ SRS ]    Hs.73962 [ NCBI ]     HS73962 [ spliceNest ]
Fast-db	15625 (alternative variants)
	Protein : pattern, domain, 3D structure
SwissProt	Q15375 [ SRS]    Q15375 [ EXPASY ]     Q15375 [ INTERPRO ]
Prosite	PS01186 EGF_2 [ SRS ]    PS01186 EGF_2 [ Expasy ]
Prosite	PS50853 FN3 [ SRS ]    PS50853 FN3 [ Expasy ]
Prosite	PS00107 PROTEIN_KINASE_ATP [ SRS ]    PS00107 PROTEIN_KINASE_ATP [ Expasy ]
Prosite	PS50011 PROTEIN_KINASE_DOM [ SRS ]    PS50011 PROTEIN_KINASE_DOM [ Expasy ]
Prosite	PS00109 PROTEIN_KINASE_TYR [ SRS ]    PS00109 PROTEIN_KINASE_TYR [ Expasy ]
Prosite	PS00790 RECEPTOR_TYR_KIN_V_1 [ SRS ]    PS00790 RECEPTOR_TYR_KIN_V_1 [ Expasy ]
Prosite	PS00791 RECEPTOR_TYR_KIN_V_2 [ SRS ]    PS00791 RECEPTOR_TYR_KIN_V_2 [ Expasy ]
Prosite	PS50105 SAM_DOMAIN [ SRS ]    PS50105 SAM_DOMAIN [ Expasy ]
Interpro	IPR013032 EGF_like_reg_CS [ SRS ]    IPR013032 EGF_like_reg_CS [ EBI ]
Interpro	IPR001090 Eph_rcpt_lig_bd [ SRS ]    IPR001090 Eph_rcpt_lig_bd [ EBI ]
Interpro	IPR008957 Fibronectin_typ-III-like_fold [ SRS ]    IPR008957 Fibronectin_typ-III-like_fold [ EBI ]
Interpro	IPR003961 FN_III [ SRS ]    IPR003961 FN_III [ EBI ]
Interpro	IPR003962 FnIII_subd [ SRS ]    IPR003962 FnIII_subd [ EBI ]
Interpro	IPR000719 Prot_kinase_core [ SRS ]    IPR000719 Prot_kinase_core [ EBI ]
Interpro	IPR001660 SAM [ SRS ]    IPR001660 SAM [ EBI ]
Interpro	IPR013761 SAM_type [ SRS ]    IPR013761 SAM_type [ EBI ]
Interpro	IPR001245 Tyr_pkinase [ SRS ]    IPR001245 Tyr_pkinase [ EBI ]
Interpro	IPR008266 Tyr_pkinase_AS [ SRS ]    IPR008266 Tyr_pkinase_AS [ EBI ]
Interpro	IPR001426 YKase_receptorV_CS [ SRS ]    IPR001426 YKase_receptorV_CS [ EBI ]
CluSTr	Q15375
Pfam	PF01404 Ephrin_lbd [ SRS ]    PF01404 Ephrin_lbd [ Sanger ]    pfam01404 [ NCBI-CDD ]
Pfam	PF00041 fn3 [ SRS ]    PF00041 fn3 [ Sanger ]    pfam00041 [ NCBI-CDD ]
Pfam	PF07714 Pkinase_Tyr [ SRS ]    PF07714 Pkinase_Tyr [ Sanger ]    pfam07714 [ NCBI-CDD ]
Pfam	PF00536 SAM_1 [ SRS ]    PF00536 SAM_1 [ Sanger ]    pfam00536 [ NCBI-CDD ]
Smart	SM00615 EPH_lbd [EMBL]
Smart	SM00060 FN3 [EMBL]
Smart	SM00454 SAM [EMBL]
Smart	SM00219 TyrKc [EMBL]
Prodom	PD001495 Ephrin_receptor[INRA-Toulouse]
Prodom	Q15375 EPHA7_HUMAN [ Domain structure ]   Q15375 EPHA7_HUMAN  [ sequences sharing at least 1 domain ]
Prodom	PD001495[INRA-Toulouse]
Prodom	Q15375 EPHA7_HUMAN [ Domain structure ]   Q15375 EPHA7_HUMAN  [ sequences sharing at least 1 domain ]
Blocks	Q15375
HPRD	03721
	Protein Interaction databases
DIP	Q15375
IntAct	Q15375
	Polymorphism : SNP, mutations, diseases
OMIM	602190    [ map ]
GENECLINICS	602190
SNP	EPHA7 [dbSNP-NCBI]
SNP	NM_004440 [SNP-NCI]
SNP	EPHA7 [GeneSNPs - Utah]  EPHA7] [HGBASE - SRS]
HAPMAP	EPHA7 [HAPMAP]
COSMIC	EPHA7 [Somatic mutation (COSMIC-CGP-Sanger)]
HGMD	EPHA7
	General knowledge
Family Browser	EPHA7 [UCSC Family Browser]
SOURCE	NM_004440
SMD	Hs.73962
SAGE	Hs.73962
Enzyme	2.7.10.1 [ Enzyme-SRS ]   2.7.10.1 [ Brenda-SRS ]   2.7.10.1 [ KEGG ]   2.7.10.1 [ WIT ]
GO	nucleotide binding [Amigo]  nucleotide binding
GO	receptor activity [Amigo]  receptor activity
GO	ephrin receptor activity [Amigo]  ephrin receptor activity
GO	protein binding [Amigo]  protein binding
GO	ATP binding [Amigo]  ATP binding
GO	protein amino acid phosphorylation [Amigo]  protein amino acid phosphorylation
GO	transmembrane receptor protein tyrosine kinase signaling pathway [Amigo]  transmembrane receptor protein tyrosine kinase signaling pathway
GO	membrane [Amigo]  membrane
GO	integral to membrane [Amigo]  integral to membrane
GO	transferase activity [Amigo]  transferase activity
KEGG	Axon guidance
PubGene	EPHA7
TreeFam	EPHA7
CTD	2045 [Comparative ToxicoGenomics Database]
	Other databases
	Probes
Probe	EPHA7 Related clones (RZPD - Berlin)
	PubMed
PubMed	25 Pubmed reference(s) in LocusLink

Bibliography

Regulation of repulsion versus adhesion by different splice forms of an Eph receptor.

Holmberg J, Clarke DL, Frisˆ©n J

Nature. 2000 ; 408 (6809) : 203-206.

PMID 11089974

Differential gene expression of Eph receptors and ephrins in benign human tissues and cancers.

Hafner C, Schmitz G, Meyer S, Bataille F, Hau P, Langmann T, Dietmaier W, Landthaler M, Vogt T

Clinical chemistry. 2004 ; 50 (3) : 490-499.

PMID 14726470

Downregulation of EphA7 by hypermethylation in colorectal cancer.

Wang J, Kataoka H, Suzuki M, Sato N, Nakamura R, Tao H, Maruyama K, Isogaki J, Kanaoka S, Ihara M, Tanaka M, Kanamori M, Nakamura T, Shinmura K, Sugimura H

Oncogene. 2005 ; 24 (36) : 5637-5647.

PMID 16007213

Inhibition of EphA7 up-regulation after spinal cord injury reduces apoptosis and promotes locomotor recovery.

Figueroa JD, Benton RL, Velazquez I, Torrado AI, Ortiz CM, Hernandez CM, Diaz JJ, Magnuson DS, Whittemore SR, Miranda JD

Journal of neuroscience research. 2006 ; 84 (7) : 1438-1451.

PMID 16983667

Expression profile of Eph receptors and ephrin ligands in human skin and downregulation of EphA1 in nonmelanoma skin cancer.

Hafner C, Becker B, Landthaler M, Vogt T

Modern pathology : an official journal of the United States and Canadian Academy of Pathology, Inc. 2006 ; 19 (10) : 1369-1377.

PMID 16862074

Absence of tyrosine kinase mutations in Japanese colorectal cancer patients.

Shao RX, Kato N, Lin LJ, Muroyama R, Moriyama M, Ikenoue T, Watabe H, Otsuka M, Guleng B, Ohta M, Tanaka Y, Kondo S, Dharel N, Chang JH, Yoshida H, Kawabe T, Omata M

Oncogene. 2007 ; 26 (14) : 2133-2135.

PMID 17016444

Mutations in HOXD13 underlie syndactyly type V and a novel brachydactyly-syndactyly syndrome.

Zhao X, Sun M, Zhao J, Leyva JA, Zhu H, Yang W, Zeng X, Ao Y, Liu Q, Liu G, Lo WH, Jabs EW, Amzel LM, Shan X, Zhang X

American journal of human genetics. 2007 ; 80 (2) : 361-371.

PMID 17236141

REVIEW articles	automatic search in PubMed
Last year publications	automatic search in PubMed

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Contributor(s)

Written	02-2007	Haruhiko Sugimura, Hiroki Mori, Tomoyasu Bunai, Masaya Suzuki

Citation

This paper should be referenced as such :

Sugimura H, Mori H, Bunai T, Suzuki M . EPHA7 (EPH receptor A7). Atlas Genet Cytogenet Oncol Haematol. February 2007 . URL : http://AtlasGeneticsOncology.org/Genes/EPHA7ID40466ch6q16.html

© Atlas of Genetics and Cytogenetics in Oncology and Haematology

indexed on : Wed Jul 2 08:23:21 2008