SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q15375

- EPHA7_HUMAN

UniProt

Q15375 - EPHA7_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Ephrin type-A receptor 7
Gene
EPHA7, EHK3, HEK11
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 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 EPHA7.1 Publication

Catalytic activityi

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei665 – 6651ATP By similarity
Active sitei758 – 7581Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi639 – 6479ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. GPI-linked ephrin receptor activity Source: UniProtKB
  3. axon guidance receptor activity Source: UniProtKB
  4. chemorepellent activity Source: UniProtKB
  5. protein binding Source: IntAct
  6. protein tyrosine kinase activity Source: UniProtKB

GO - Biological processi

  1. brain development Source: UniProtKB
  2. branching morphogenesis of a nerve Source: UniProtKB
  3. ephrin receptor signaling pathway Source: UniProtKB
  4. negative chemotaxis Source: UniProtKB
  5. peptidyl-tyrosine phosphorylation Source: GOC
  6. phosphorylation Source: UniProtKB
  7. positive regulation of neuron apoptotic process Source: UniProtKB
  8. regulation of ERK1 and ERK2 cascade Source: UniProtKB
  9. regulation of cell-cell adhesion Source: UniProtKB
  10. regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
  11. regulation of peptidyl-tyrosine phosphorylation Source: UniProtKB
  12. regulation of protein autophosphorylation Source: UniProtKB
  13. retinal ganglion cell axon guidance Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Kinase, Receptor, Transferase, Tyrosine-protein kinase

Keywords - Biological processi

Apoptosis, Neurogenesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.10.1. 2681.
SignaLinkiQ15375.

Names & Taxonomyi

Protein namesi
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 namesi
Name:EPHA7
Synonyms:EHK3, HEK11
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:3390. EPHA7.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini28 – 555528Extracellular Reviewed prediction
Add
BLAST
Transmembranei556 – 57621Helical; Reviewed prediction
Add
BLAST
Topological domaini577 – 998422Cytoplasmic Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. dendrite Source: Ensembl
  2. integral component of plasma membrane Source: InterPro
  3. neuromuscular junction Source: Ensembl
  4. neuronal cell body Source: Ensembl
  5. postsynaptic membrane Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27822.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2727 Reviewed prediction
Add
BLAST
Chaini28 – 998971Ephrin type-A receptor 7
PRO_0000016818Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi343 – 3431N-linked (GlcNAc...) Reviewed prediction
Glycosylationi410 – 4101N-linked (GlcNAc...) Reviewed prediction
Modified residuei608 – 6081Phosphotyrosine; by autocatalysis Reviewed prediction
Modified residuei614 – 6141Phosphotyrosine; by autocatalysis Reviewed prediction
Modified residuei791 – 7911Phosphotyrosine; by autocatalysis Reviewed prediction
Modified residuei940 – 9401Phosphotyrosine; by autocatalysis Reviewed prediction

Post-translational modificationi

Phosphorylated By similarity.

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ15375.
PaxDbiQ15375.
PRIDEiQ15375.

PTM databases

PhosphoSiteiQ15375.

Expressioni

Tissue specificityi

Widely expressed.

Gene expression databases

BgeeiQ15375.
CleanExiHS_EPHA7.
GenevestigatoriQ15375.

Organism-specific databases

HPAiCAB010496.

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

Binary interactionsi

WithEntry#Exp.IntActNotes
Efna1P527932EBI-1383428,EBI-5241529From a different organism.
EPHA2P293173EBI-1383428,EBI-702104

Protein-protein interaction databases

BioGridi108359. 8 interactions.
IntActiQ15375. 9 interactions.
MINTiMINT-1538326.
STRINGi9606.ENSP00000358309.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi33 – 375
Beta strandi48 – 514
Beta strandi54 – 618
Beta strandi67 – 748
Beta strandi78 – 803
Beta strandi83 – 864
Beta strandi96 – 10611
Turni109 – 1113
Beta strandi121 – 13212
Helixi140 – 1423
Beta strandi144 – 1507
Beta strandi168 – 1747
Beta strandi178 – 19013
Beta strandi192 – 20211
Helixi611 – 6133
Beta strandi614 – 6163
Helixi617 – 6248
Helixi630 – 6323
Beta strandi633 – 6419
Beta strandi643 – 65210
Beta strandi655 – 6573
Beta strandi660 – 6667
Helixi673 – 68614
Beta strandi697 – 7015
Beta strandi703 – 7053
Beta strandi708 – 7125
Helixi719 – 7257
Turni726 – 7283
Helixi732 – 75120
Helixi761 – 7633
Beta strandi764 – 7663
Beta strandi772 – 7743
Helixi800 – 8023
Helixi805 – 8106
Helixi815 – 83016
Turni836 – 8394
Helixi842 – 8509
Helixi863 – 87210
Helixi877 – 8793
Helixi883 – 89513
Helixi897 – 8993
Helixi928 – 9347
Helixi938 – 9403
Helixi941 – 9466
Helixi952 – 9565
Helixi960 – 9656
Helixi971 – 98818

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliQ15375.
SMRiQ15375. Positions 30-899, 919-989.

Miscellaneous databases

EvolutionaryTraceiQ15375.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini32 – 210179Eph LBD
Add
BLAST
Domaini331 – 441111Fibronectin type-III 1
Add
BLAST
Domaini442 – 53796Fibronectin type-III 2
Add
BLAST
Domaini633 – 894262Protein kinase
Add
BLAST
Domaini923 – 98765SAM
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi996 – 9983PDZ-binding Reviewed prediction

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi192 – 328137Cys-rich
Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0515.
HOVERGENiHBG062180.
InParanoidiQ15375.
KOiK05108.
OMAiENSPKMH.
OrthoDBiEOG7VTDM6.
PhylomeDBiQ15375.
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.
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]
PfamiPF14575. 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]
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.
SSF57184. SSF57184. 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 (5)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 5 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q15375-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MVFQTRYPSW IILCYIWLLR FAHTGEAQAA KEVLLLDSKA QQTELEWISS    50
PPNGWEEISG LDENYTPIRT YQVCQVMEPN QNNWLRTNWI SKGNAQRIFV 100
ELKFTLRDCN SLPGVLGTCK ETFNLYYYET DYDTGRNIRE NLYVKIDTIA 150
ADESFTQGDL GERKMKLNTE VREIGPLSKK GFYLAFQDVG ACIALVSVKV 200
YYKKCWSIIE NLAIFPDTVT GSEFSSLVEV RGTCVSSAEE EAENAPRMHC 250
SAEGEWLVPI GKCICKAGYQ QKGDTCEPCG RGFYKSSSQD LQCSRCPTHS 300
FSDKEGSSRC ECEDGYYRAP SDPPYVACTR PPSAPQNLIF NINQTTVSLE 350
WSPPADNGGR NDVTYRILCK RCSWEQGECV PCGSNIGYMP QQTGLEDNYV 400
TVMDLLAHAN YTFEVEAVNG VSDLSRSQRL FAAVSITTGQ AAPSQVSGVM 450
KERVLQRSVE LSWQEPEHPN GVITEYEIKY YEKDQRERTY STVKTKSTSA 500
SINNLKPGTV YVFQIRAFTA AGYGNYSPRL DVATLEEATG KMFEATAVSS 550
EQNPVIIIAV VAVAGTIILV FMVFGFIIGR RHCGYSKADQ EGDEELYFHF 600
KFPGTKTYID PETYEDPNRA VHQFAKELDA SCIKIERVIG AGEFGEVCSG 650
RLKLPGKRDV AVAIKTLKVG YTEKQRRDFL CEASIMGQFD HPNVVHLEGV 700
VTRGKPVMIV IEFMENGALD AFLRKHDGQF TVIQLVGMLR GIAAGMRYLA 750
DMGYVHRDLA ARNILVNSNL VCKVSDFGLS RVIEDDPEAV YTTTGGKIPV 800
RWTAPEAIQY RKFTSASDVW SYGIVMWEVM SYGERPYWDM SNQDVIKAIE 850
EGYRLPAPMD CPAGLHQLML DCWQKERAER PKFEQIVGIL DKMIRNPNSL 900
KTPLGTCSRP ISPLLDQNTP DFTTFCSVGE WLQAIKMERY KDNFTAAGYN 950
SLESVARMTI EDVMSLGITL VGHQKKIMSS IQTMRAQMLH LHGTGIQV 998
Length:998
Mass (Da):112,097
Last modified:May 1, 2007 - v3
Checksum:i479B9CA0D2BB06EB
GO
Isoform 2 (identifier: Q15375-2) [UniParc]FASTAAdd to Basket

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.

Show »
Length:993
Mass (Da):111,504
Checksum:i4DEE43AD86F2CA11
GO
Isoform 3 (identifier: Q15375-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     278-279: PC → RK
     280-998: Missing.

Note: No experimental confirmation available.

Show »
Length:279
Mass (Da):31,833
Checksum:i54A2687994762500
GO
Isoform 4 (identifier: Q15375-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     600-604: FKFPG → C

Note: No experimental confirmation available.

Show »
Length:994
Mass (Da):111,623
Checksum:iE35ED97999DBF944
GO
Isoform 5 (identifier: Q15375-5) [UniParc]FASTAAdd to Basket

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.

Show »
Length:449
Mass (Da):50,521
Checksum:i4E15BF1881AC175A
GO

Sequence cautioni

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

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti138 – 1381I → V.2 Publications
Corresponds to variant rs2278107 [ dbSNP | Ensembl ].
VAR_022105
Natural varianti170 – 1701E → K in a colorectal adenocarcinoma sample; somatic mutation. 1 Publication
VAR_042150
Natural varianti232 – 2321G → R in a metastatic melanoma sample; somatic mutation. 1 Publication
VAR_042151
Natural varianti278 – 2781P → S.1 Publication
Corresponds to variant rs2278106 [ dbSNP | Ensembl ].
VAR_022106
Natural varianti371 – 3711R → W in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_036090
Natural varianti903 – 9031P → S in a metastatic melanoma sample; somatic mutation. 1 Publication
VAR_042152

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei278 – 2792PC → RK in isoform 3.
VSP_014380
Alternative sequencei280 – 998719Missing in isoform 3.
VSP_014381Add
BLAST
Alternative sequencei442 – 4509APSQVSGVM → GMFCVYLH in isoform 5.
VSP_041943
Alternative sequencei451 – 998548Missing in isoform 5.
VSP_041944Add
BLAST
Alternative sequencei540 – 5445Missing in isoform 2.
VSP_014382
Alternative sequencei600 – 6045FKFPG → C in isoform 4.
VSP_041945

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Isoform 3 (identifier: Q15375-3)
Sequence conflicti278 – 2781R → C in AAH27940. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS5031.1. [Q15375-1]
PIRiI58351.
RefSeqiNP_001275558.1. NM_001288629.1. [Q15375-2]
NP_001275559.1. NM_001288630.1. [Q15375-3]
NP_004431.1. NM_004440.3. [Q15375-1]
XP_005248726.1. XM_005248669.1. [Q15375-4]
UniGeneiHs.73962.

Genome annotation databases

EnsembliENST00000369297; ENSP00000358303; ENSG00000135333. [Q15375-3]
ENST00000369303; ENSP00000358309; ENSG00000135333. [Q15375-1]
GeneIDi2045.
KEGGihsa:2045.
UCSCiuc003poe.3. human. [Q15375-1]
uc003pof.3. human. [Q15375-2]
uc003pog.4. human. [Q15375-3]
uc011eac.2. human. [Q15375-4]

Polymorphism databases

DMDMi146345416.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS5031.1. [Q15375-1 ]
PIRi I58351.
RefSeqi NP_001275558.1. NM_001288629.1. [Q15375-2 ]
NP_001275559.1. NM_001288630.1. [Q15375-3 ]
NP_004431.1. NM_004440.3. [Q15375-1 ]
XP_005248726.1. XM_005248669.1. [Q15375-4 ]
UniGenei Hs.73962.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali Q15375.
SMRi Q15375. Positions 30-899, 919-989.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108359. 8 interactions.
IntActi Q15375. 9 interactions.
MINTi MINT-1538326.
STRINGi 9606.ENSP00000358309.

Chemistry

BindingDBi Q15375.
ChEMBLi CHEMBL4602.
GuidetoPHARMACOLOGYi 1827.

PTM databases

PhosphoSitei Q15375.

Polymorphism databases

DMDMi 146345416.

Proteomic databases

MaxQBi Q15375.
PaxDbi Q15375.
PRIDEi Q15375.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000369297 ; ENSP00000358303 ; ENSG00000135333 . [Q15375-3 ]
ENST00000369303 ; ENSP00000358309 ; ENSG00000135333 . [Q15375-1 ]
GeneIDi 2045.
KEGGi hsa:2045.
UCSCi uc003poe.3. human. [Q15375-1 ]
uc003pof.3. human. [Q15375-2 ]
uc003pog.4. human. [Q15375-3 ]
uc011eac.2. human. [Q15375-4 ]

Organism-specific databases

CTDi 2045.
GeneCardsi GC06M094007.
HGNCi HGNC:3390. EPHA7.
HPAi CAB010496.
MIMi 602190. gene.
neXtProti NX_Q15375.
PharmGKBi PA27822.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
HOVERGENi HBG062180.
InParanoidi Q15375.
KOi K05108.
OMAi ENSPKMH.
OrthoDBi EOG7VTDM6.
PhylomeDBi Q15375.
TreeFami TF315608.

Enzyme and pathway databases

BRENDAi 2.7.10.1. 2681.
SignaLinki Q15375.

Miscellaneous databases

EvolutionaryTracei Q15375.
GeneWikii EPHA7.
GenomeRNAii 2045.
NextBioi 8311.
PROi Q15375.
SOURCEi Search...

Gene expression databases

Bgeei Q15375.
CleanExi HS_EPHA7.
Genevestigatori Q15375.

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.
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 ]
Pfami PF14575. 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 ]
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.
SSF57184. SSF57184. 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. "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. 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. 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.

Entry informationi

Entry nameiEPHA7_HUMAN
AccessioniPrimary (citable) accession number: Q15375
Secondary accession number(s): A0AUX7
, B2R8W1, B7ZLJ9, B7ZLK0, Q59G40, Q5VTU0, Q8N368, Q9H124
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 1, 2007
Last modified: July 9, 2014
This is version 155 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 6
    Human chromosome 6: 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

Similar proteinsi