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Protein

Ephrin type-A receptor 7

Gene

EPHA7

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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.PROSITE-ProRule annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei665ATPPROSITE-ProRule annotation1
Active sitei758Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi639 – 647ATPPROSITE-ProRule annotation9

GO - Molecular functioni

GO - Biological processi

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

BioCyciZFISH:HS05982-MONOMER.
BRENDAi2.7.10.1. 2681.
ReactomeiR-HSA-2682334. EPH-Ephrin signaling.
R-HSA-3928663. EPHA-mediated growth cone collapse.
R-HSA-3928665. EPH-ephrin mediated repulsion of cells.
SignaLinkiQ15375.
SIGNORiQ15375.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:3390. EPHA7.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini28 – 555ExtracellularSequence analysisAdd BLAST528
Transmembranei556 – 576HelicalSequence analysisAdd BLAST21
Topological domaini577 – 998CytoplasmicSequence analysisAdd BLAST422

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Organism-specific databases

DisGeNETi2045.
OpenTargetsiENSG00000135333.
PharmGKBiPA27822.

Chemistry databases

ChEMBLiCHEMBL4602.
GuidetoPHARMACOLOGYi1827.

Polymorphism and mutation databases

BioMutaiEPHA7.
DMDMi146345416.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 27Sequence analysisAdd BLAST27
ChainiPRO_000001681828 – 998Ephrin type-A receptor 7Add BLAST971

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi343N-linked (GlcNAc...)Sequence analysis1
Glycosylationi410N-linked (GlcNAc...)Sequence analysis1
Modified residuei608Phosphotyrosine; by autocatalysisSequence analysis1
Modified residuei614Phosphotyrosine; by autocatalysisSequence analysis1
Modified residuei791Phosphotyrosine; by autocatalysisSequence analysis1
Modified residuei940Phosphotyrosine; by autocatalysisSequence analysis1

Post-translational modificationi

Phosphorylated.By similarity

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

EPDiQ15375.
MaxQBiQ15375.
PaxDbiQ15375.
PeptideAtlasiQ15375.
PRIDEiQ15375.

PTM databases

iPTMnetiQ15375.
PhosphoSitePlusiQ15375.
SwissPalmiQ15375.

Expressioni

Tissue specificityi

Widely expressed.

Gene expression databases

BgeeiENSG00000135333.
CleanExiHS_EPHA7.
GenevisibleiQ15375. HS.

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).By similarity

Binary interactionsi

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

Protein-protein interaction databases

BioGridi108359. 43 interactors.
IntActiQ15375. 10 interactors.
MINTiMINT-1538326.
STRINGi9606.ENSP00000358309.

Chemistry databases

BindingDBiQ15375.

Structurei

Secondary structure

1998
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi33 – 37Combined sources5
Beta strandi48 – 51Combined sources4
Beta strandi54 – 61Combined sources8
Beta strandi67 – 74Combined sources8
Beta strandi78 – 80Combined sources3
Beta strandi83 – 86Combined sources4
Beta strandi96 – 106Combined sources11
Turni109 – 111Combined sources3
Beta strandi121 – 132Combined sources12
Helixi140 – 142Combined sources3
Beta strandi144 – 150Combined sources7
Beta strandi168 – 174Combined sources7
Beta strandi178 – 190Combined sources13
Beta strandi192 – 202Combined sources11
Helixi611 – 613Combined sources3
Beta strandi614 – 616Combined sources3
Helixi617 – 624Combined sources8
Helixi630 – 632Combined sources3
Beta strandi633 – 641Combined sources9
Beta strandi643 – 652Combined sources10
Beta strandi655 – 657Combined sources3
Beta strandi660 – 666Combined sources7
Helixi673 – 686Combined sources14
Beta strandi697 – 701Combined sources5
Beta strandi703 – 705Combined sources3
Beta strandi708 – 712Combined sources5
Helixi719 – 725Combined sources7
Turni726 – 728Combined sources3
Helixi732 – 751Combined sources20
Helixi761 – 763Combined sources3
Beta strandi764 – 766Combined sources3
Beta strandi772 – 774Combined sources3
Helixi800 – 802Combined sources3
Helixi805 – 810Combined sources6
Helixi815 – 830Combined sources16
Turni836 – 839Combined sources4
Helixi842 – 850Combined sources9
Helixi863 – 872Combined sources10
Helixi877 – 879Combined sources3
Helixi883 – 895Combined sources13
Helixi897 – 899Combined sources3
Helixi928 – 934Combined sources7
Helixi938 – 940Combined sources3
Helixi941 – 946Combined sources6
Helixi952 – 956Combined sources5
Helixi960 – 965Combined sources6
Helixi971 – 988Combined sources18

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ15375.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini32 – 210Eph LBDPROSITE-ProRule annotationAdd BLAST179
Domaini331 – 441Fibronectin type-III 1PROSITE-ProRule annotationAdd BLAST111
Domaini442 – 537Fibronectin type-III 2PROSITE-ProRule annotationAdd BLAST96
Domaini633 – 894Protein kinasePROSITE-ProRule annotationAdd BLAST262
Domaini923 – 987SAMPROSITE-ProRule annotationAdd BLAST65

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi996 – 998PDZ-bindingSequence analysis3

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi192 – 328Cys-richAdd BLAST137

Sequence similaritiesi

Belongs to the protein kinase superfamily. Tyr protein kinase family. Ephrin receptor subfamily.PROSITE-ProRule annotation
Contains 1 Eph LBD (Eph ligand-binding) domain.PROSITE-ProRule annotation
Contains 2 fibronectin type-III domains.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation
Contains 1 SAM (sterile alpha motif) domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0196. Eukaryota.
COG0515. LUCA.
GeneTreeiENSGT00760000118975.
HOVERGENiHBG062180.
InParanoidiQ15375.
KOiK05108.
OMAiTRHPSWI.
OrthoDBiEOG091G00W0.
PhylomeDBiQ15375.
TreeFamiTF315608.

Family and domain databases

CDDicd00063. FN3. 2 hits.
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. FN3_dom.
IPR008979. Galactose-bd-like.
IPR009030. Growth_fac_rcpt_.
IPR013783. Ig-like_fold.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001660. SAM.
IPR013761. SAM/pointed.
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.
PF07699. Ephrin_rec_like. 1 hit.
PF00041. fn3. 2 hits.
PF07714. Pkinase_Tyr. 1 hit.
PF00536. SAM_1. 1 hit.
[Graphical view]
PIRSFiPIRSF000666. TyrPK_ephrin_receptor. 1 hit.
PRINTSiPR00109. TYRKINASE.
SMARTiSM00615. EPH_lbd. 1 hit.
SM01411. Ephrin_rec_like. 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. AlignAdd to basket

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

        10         20         30         40         50
MVFQTRYPSW IILCYIWLLR FAHTGEAQAA KEVLLLDSKA QQTELEWISS
60 70 80 90 100
PPNGWEEISG LDENYTPIRT YQVCQVMEPN QNNWLRTNWI SKGNAQRIFV
110 120 130 140 150
ELKFTLRDCN SLPGVLGTCK ETFNLYYYET DYDTGRNIRE NLYVKIDTIA
160 170 180 190 200
ADESFTQGDL GERKMKLNTE VREIGPLSKK GFYLAFQDVG ACIALVSVKV
210 220 230 240 250
YYKKCWSIIE NLAIFPDTVT GSEFSSLVEV RGTCVSSAEE EAENAPRMHC
260 270 280 290 300
SAEGEWLVPI GKCICKAGYQ QKGDTCEPCG RGFYKSSSQD LQCSRCPTHS
310 320 330 340 350
FSDKEGSSRC ECEDGYYRAP SDPPYVACTR PPSAPQNLIF NINQTTVSLE
360 370 380 390 400
WSPPADNGGR NDVTYRILCK RCSWEQGECV PCGSNIGYMP QQTGLEDNYV
410 420 430 440 450
TVMDLLAHAN YTFEVEAVNG VSDLSRSQRL FAAVSITTGQ AAPSQVSGVM
460 470 480 490 500
KERVLQRSVE LSWQEPEHPN GVITEYEIKY YEKDQRERTY STVKTKSTSA
510 520 530 540 550
SINNLKPGTV YVFQIRAFTA AGYGNYSPRL DVATLEEATG KMFEATAVSS
560 570 580 590 600
EQNPVIIIAV VAVAGTIILV FMVFGFIIGR RHCGYSKADQ EGDEELYFHF
610 620 630 640 650
KFPGTKTYID PETYEDPNRA VHQFAKELDA SCIKIERVIG AGEFGEVCSG
660 670 680 690 700
RLKLPGKRDV AVAIKTLKVG YTEKQRRDFL CEASIMGQFD HPNVVHLEGV
710 720 730 740 750
VTRGKPVMIV IEFMENGALD AFLRKHDGQF TVIQLVGMLR GIAAGMRYLA
760 770 780 790 800
DMGYVHRDLA ARNILVNSNL VCKVSDFGLS RVIEDDPEAV YTTTGGKIPV
810 820 830 840 850
RWTAPEAIQY RKFTSASDVW SYGIVMWEVM SYGERPYWDM SNQDVIKAIE
860 870 880 890 900
EGYRLPAPMD CPAGLHQLML DCWQKERAER PKFEQIVGIL DKMIRNPNSL
910 920 930 940 950
KTPLGTCSRP ISPLLDQNTP DFTTFCSVGE WLQAIKMERY KDNFTAAGYN
960 970 980 990
SLESVARMTI EDVMSLGITL VGHQKKIMSS IQTMRAQMLH LHGTGIQV
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.Curated
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 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Isoform 3 (identifier: Q15375-3)
Sequence conflicti278R → C in AAH27940 (PubMed:15489334).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_022105138I → V.2 PublicationsCorresponds to variant rs2278107dbSNPEnsembl.1
Natural variantiVAR_042150170E → K in a colorectal adenocarcinoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_042151232G → R in a metastatic melanoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_022106278P → S.1 PublicationCorresponds to variant rs2278106dbSNPEnsembl.1
Natural variantiVAR_036090371R → W in a colorectal cancer sample; somatic mutation. 1 PublicationCorresponds to variant rs371089003dbSNPEnsembl.1
Natural variantiVAR_042152903P → S in a metastatic melanoma sample; somatic mutation. 1 Publication1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_014380278 – 279PC → RK in isoform 3. 1 Publication2
Alternative sequenceiVSP_014381280 – 998Missing in isoform 3. 1 PublicationAdd BLAST719
Alternative sequenceiVSP_041943442 – 450APSQVSGVM → GMFCVYLH in isoform 5. Curated9
Alternative sequenceiVSP_041944451 – 998Missing in isoform 5. CuratedAdd BLAST548
Alternative sequenceiVSP_014382540 – 544Missing in isoform 2. 3 Publications5
Alternative sequenceiVSP_041945600 – 604FKFPG → C in isoform 4. 1 Publication5

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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]
CCDS75494.1. [Q15375-3]
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_005248669.2. [Q15375-4]
UniGeneiHs.73962.

Genome annotation databases

EnsembliENST00000369297; ENSP00000358303; ENSG00000135333. [Q15375-3]
ENST00000369303; ENSP00000358309; ENSG00000135333. [Q15375-1]
GeneIDi2045.
KEGGihsa:2045.
UCSCiuc003poe.5. human. [Q15375-1]

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:
EMBLi
GenBanki
DDBJi
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]
CCDS75494.1. [Q15375-3]
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_005248669.2. [Q15375-4]
UniGeneiHs.73962.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108359. 43 interactors.
IntActiQ15375. 10 interactors.
MINTiMINT-1538326.
STRINGi9606.ENSP00000358309.

Chemistry databases

BindingDBiQ15375.
ChEMBLiCHEMBL4602.
GuidetoPHARMACOLOGYi1827.

PTM databases

iPTMnetiQ15375.
PhosphoSitePlusiQ15375.
SwissPalmiQ15375.

Polymorphism and mutation databases

BioMutaiEPHA7.
DMDMi146345416.

Proteomic databases

EPDiQ15375.
MaxQBiQ15375.
PaxDbiQ15375.
PeptideAtlasiQ15375.
PRIDEiQ15375.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000369297; ENSP00000358303; ENSG00000135333. [Q15375-3]
ENST00000369303; ENSP00000358309; ENSG00000135333. [Q15375-1]
GeneIDi2045.
KEGGihsa:2045.
UCSCiuc003poe.5. human. [Q15375-1]

Organism-specific databases

CTDi2045.
DisGeNETi2045.
GeneCardsiEPHA7.
HGNCiHGNC:3390. EPHA7.
HPAiCAB010496.
MIMi602190. gene.
neXtProtiNX_Q15375.
OpenTargetsiENSG00000135333.
PharmGKBiPA27822.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0196. Eukaryota.
COG0515. LUCA.
GeneTreeiENSGT00760000118975.
HOVERGENiHBG062180.
InParanoidiQ15375.
KOiK05108.
OMAiTRHPSWI.
OrthoDBiEOG091G00W0.
PhylomeDBiQ15375.
TreeFamiTF315608.

Enzyme and pathway databases

BioCyciZFISH:HS05982-MONOMER.
BRENDAi2.7.10.1. 2681.
ReactomeiR-HSA-2682334. EPH-Ephrin signaling.
R-HSA-3928663. EPHA-mediated growth cone collapse.
R-HSA-3928665. EPH-ephrin mediated repulsion of cells.
SignaLinkiQ15375.
SIGNORiQ15375.

Miscellaneous databases

ChiTaRSiEPHA7. human.
EvolutionaryTraceiQ15375.
GeneWikiiEPHA7.
GenomeRNAii2045.
PROiQ15375.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000135333.
CleanExiHS_EPHA7.
GenevisibleiQ15375. HS.

Family and domain databases

CDDicd00063. FN3. 2 hits.
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. FN3_dom.
IPR008979. Galactose-bd-like.
IPR009030. Growth_fac_rcpt_.
IPR013783. Ig-like_fold.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001660. SAM.
IPR013761. SAM/pointed.
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.
PF07699. Ephrin_rec_like. 1 hit.
PF00041. fn3. 2 hits.
PF07714. Pkinase_Tyr. 1 hit.
PF00536. SAM_1. 1 hit.
[Graphical view]
PIRSFiPIRSF000666. TyrPK_ephrin_receptor. 1 hit.
PRINTSiPR00109. TYRKINASE.
SMARTiSM00615. EPH_lbd. 1 hit.
SM01411. Ephrin_rec_like. 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]
ProtoNetiSearch...

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: November 30, 2016
This is version 181 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.