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Protein

Ephrin type-A receptor 7

Gene

Epha7

Organism
Mus musculus (Mouse)
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. Isoform 4 which lacks the kinase domain may regulate isoform 1 adhesive properties.3 Publications

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei665 – 6651ATPPROSITE-ProRule annotation
Active sitei758 – 7581Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi639 – 6479ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. axon guidance receptor activity Source: UniProtKB
  3. chemorepellent activity Source: MGI
  4. GPI-linked ephrin receptor activity Source: UniProtKB

GO - Biological processi

  1. brain development Source: UniProtKB
  2. branching morphogenesis of a nerve Source: MGI
  3. ephrin receptor signaling pathway Source: UniProtKB
  4. negative chemotaxis Source: GOC
  5. nephric duct morphogenesis Source: MGI
  6. phosphorylation Source: UniProtKB
  7. positive regulation of neuron apoptotic process Source: MGI
  8. regulation of cell-cell adhesion Source: UniProtKB
  9. regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
  10. regulation of ERK1 and ERK2 cascade Source: UniProtKB
  11. regulation of peptidyl-tyrosine phosphorylation Source: UniProtKB
  12. regulation of protein autophosphorylation Source: UniProtKB
  13. retinal ganglion cell axon guidance Source: MGI
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. 3474.
ReactomeiREACT_280640. EPHA-mediated growth cone collapse.
REACT_292566. EPH-Ephrin signaling.
REACT_314615. EPH-ephrin mediated repulsion of cells.

Names & Taxonomyi

Protein namesi
Recommended name:
Ephrin type-A receptor 7 (EC:2.7.10.1)
Alternative name(s):
Developmental kinase 1
Short name:
mDK-1
EPH homology kinase 3
Short name:
EHK-3
Embryonic brain kinase
Short name:
EBK
Gene namesi
Name:Epha7
Synonyms:Ebk, Ehk3, Mdk1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:95276. Epha7.

Subcellular locationi

Cell membrane 1 Publication; Single-pass type I membrane protein 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini28 – 555528ExtracellularSequence AnalysisAdd
BLAST
Transmembranei556 – 57621HelicalSequence AnalysisAdd
BLAST
Topological domaini577 – 998422CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. dendrite Source: Ensembl
  2. integral component of plasma membrane Source: UniProtKB
  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

Disruption phenotypei

Mice are viable, fertile and show no gross morphological or behavioral defects. However, topographic targeting errors of nasal and temporal retinal axons appear during development of the retinocollicular projections in the visual system. 10 percent of the embryos also display exencephalic overgrowth of forebrain tissues which might be the result of reduced apoptosis.2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2727Sequence AnalysisAdd
BLAST
Chaini28 – 998971Ephrin type-A receptor 7PRO_0000016819Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi64 – 641N-linked (GlcNAc...)Sequence Analysis
Glycosylationi343 – 3431N-linked (GlcNAc...)Sequence Analysis
Glycosylationi410 – 4101N-linked (GlcNAc...)Sequence Analysis
Modified residuei608 – 6081Phosphotyrosine; by autocatalysisSequence Analysis
Modified residuei614 – 6141Phosphotyrosine; by autocatalysisSequence Analysis
Modified residuei791 – 7911Phosphotyrosine; by autocatalysisBy similarity
Modified residuei940 – 9401Phosphotyrosine; by autocatalysisSequence Analysis

Post-translational modificationi

Phosphorylated. Isoform 4 inhibits isoform 1 phosphorylation and may regulate its function in adhesion.1 Publication

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ61772.
PaxDbiQ61772.
PRIDEiQ61772.

PTM databases

PhosphoSiteiQ61772.

Expressioni

Tissue specificityi

Widely expressed in embryo. In adult, expression restricted to hippocampus, testis and spleen.

Developmental stagei

During visual system development, expressed in an anterior to posterior decreasing gradient stretching through the entire midbrain. This gradient has the reverse orientation to the one defined by the expression of ephrins. Isoform 4 and isoform 5 are expressed at the edges of the embryonic cranial neural fold.2 Publications

Gene expression databases

BgeeiQ61772.
CleanExiMM_EPHA7.
ExpressionAtlasiQ61772. baseline and differential.
GenevestigatoriQ61772.

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 similarity1 Publication

Protein-protein interaction databases

BioGridi199474. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliQ61772.
SMRiQ61772. Positions 30-989.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini32 – 210179Eph LBDPROSITE-ProRule annotationAdd
BLAST
Domaini331 – 441111Fibronectin type-III 1PROSITE-ProRule annotationAdd
BLAST
Domaini442 – 53796Fibronectin type-III 2PROSITE-ProRule annotationAdd
BLAST
Domaini633 – 894262Protein kinasePROSITE-ProRule annotationAdd
BLAST
Domaini923 – 98765SAMPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi996 – 9983PDZ-bindingSequence Analysis

Compositional bias

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

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

eggNOGiCOG0515.
GeneTreeiENSGT00760000118975.
HOGENOMiHOG000233856.
HOVERGENiHBG062180.
InParanoidiQ61772.
KOiK05108.
OMAiENSPKMH.
OrthoDBiEOG7VTDM6.
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. FN3_dom.
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.
IPR021129. SAM_type1.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
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.
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.
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: Q61772-1) [UniParc]FASTAAdd to basket

Also known as: MDK1, 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
MVVQTRFPSW IILCYIWLLG FAHTGEAQAA KEVLLLDSKA QQTELEWISS
60 70 80 90 100
PPSGWEEISG 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
YYKKCWSIVE NLAVFPDTVT GSEFSSLVEV RGTCVSSAEE EAENSPRMHC
260 270 280 290 300
SAEGEWLVPI GKCICKAGYQ QKGDTCEPCG RRFYKSSSQD LQCSRCPTHS
310 320 330 340 350
FSDREGSSRC 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
KERVLQRSVQ LSWQEPEHPN GVITEYEIKY YEKDQRERTY STLKTKSTSA
510 520 530 540 550
SINNLKPGTV YVFQIRAVTA AGYGNYSPRL DVATLEEASG 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 DCWQKDRAER PKFEQIVGIL DKMIRNPSSL
910 920 930 940 950
KTPLGTCSRP LSPLLDQSTP DFTAFCSVGE WLQAIKMERY KDNFTAAGYN
960 970 980 990
SLESVARMTI DDVMSLGITL VGHQKKIMSS IQTMRAQMLH LHGTGIQV
Length:998
Mass (Da):111,860
Last modified:July 26, 2011 - v2
Checksum:iFCA1E83490E746E1
GO
Isoform 2 (identifier: Q61772-2) [UniParc]FASTAAdd to basket

Also known as: MDK1-1, Ebk-td1

The sequence of this isoform differs from the canonical sequence as follows:
     540-544: Missing.

Show »
Length:993
Mass (Da):111,268
Checksum:i2D1C811BCD1FA937
GO
Isoform 3 (identifier: Q61772-3) [UniParc]FASTAAdd to basket

Also known as: MDK1-2

The sequence of this isoform differs from the canonical sequence as follows:
     601-604: Missing.

Show »
Length:994
Mass (Da):111,431
Checksum:i25ADED280A8D9FBF
GO
Isoform 4 (identifier: Q61772-4) [UniParc]FASTAAdd to basket

Also known as: MDK1-T1, EPHA7-T1

The sequence of this isoform differs from the canonical sequence as follows:
     600-610: FKFPGTKTYID → SLVTNEHLSVL
     611-998: Missing.

Note: Truncated receptor lacking the kinase domain.

Show »
Length:610
Mass (Da):68,286
Checksum:iE61310A72FE1E739
GO
Isoform 5 (identifier: Q61772-5) [UniParc]FASTAAdd to basket

Also known as: MDK1-T2, EPHA7-T2

The sequence of this isoform differs from the canonical sequence as follows:
     600-626: FKFPGTKTYIDPETYEDPNRAVHQFAK → SLYRERGDGMEKTQHNKKWMIASCSRL
     627-998: Missing.

Note: Truncated receptor lacking the kinase domain.

Show »
Length:626
Mass (Da):70,300
Checksum:iF929755DC75B5664
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti207 – 2071S → T in CAA55687 (PubMed:7824284).Curated
Sequence conflicti207 – 2071S → T in CAA55688 (PubMed:7824284).Curated
Sequence conflicti207 – 2071S → T in CAA55689 (PubMed:7824284).Curated
Sequence conflicti480 – 4801Y → H in CAA57224 (PubMed:8541219).Curated
Sequence conflicti657 – 6571K → Q in CAA55687 (PubMed:7824284).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei540 – 5445Missing in isoform 2. 1 PublicationVSP_003006
Alternative sequencei600 – 62627FKFPG…HQFAK → SLYRERGDGMEKTQHNKKWM IASCSRL in isoform 5. CuratedVSP_003010Add
BLAST
Alternative sequencei600 – 61011FKFPGTKTYID → SLVTNEHLSVL in isoform 4. CuratedVSP_003008Add
BLAST
Alternative sequencei601 – 6044Missing in isoform 3. CuratedVSP_003007
Alternative sequencei611 – 998388Missing in isoform 4. CuratedVSP_003009Add
BLAST
Alternative sequencei627 – 998372Missing in isoform 5. CuratedVSP_003011Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X79082 mRNA. Translation: CAA55687.1.
X79083 mRNA. Translation: CAA55688.1.
X79084 mRNA. Translation: CAA55689.1.
AK030480 mRNA. Translation: BAC26982.1.
BX000989 Genomic DNA. Translation: CAM21483.1.
CH466538 Genomic DNA. Translation: EDL05518.1.
X81466 mRNA. Translation: CAA57224.1.
CCDSiCCDS18013.1. [Q61772-1]
CCDS51132.1. [Q61772-4]
CCDS71353.1. [Q61772-3]
PIRiI48612.
I48614.
JC5672.
RefSeqiNP_001277363.1. NM_001290434.1.
NP_034271.3. NM_010141.4. [Q61772-1]
XP_006537669.1. XM_006537606.2. [Q61772-2]
XP_006537670.1. XM_006537607.2. [Q61772-5]
UniGeneiMm.257266.

Genome annotation databases

EnsembliENSMUST00000029964; ENSMUSP00000029964; ENSMUSG00000028289. [Q61772-1]
ENSMUST00000080934; ENSMUSP00000079735; ENSMUSG00000028289. [Q61772-4]
ENSMUST00000108194; ENSMUSP00000103829; ENSMUSG00000028289. [Q61772-5]
GeneIDi13841.
KEGGimmu:13841.
UCSCiuc008sen.2. mouse. [Q61772-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X79082 mRNA. Translation: CAA55687.1.
X79083 mRNA. Translation: CAA55688.1.
X79084 mRNA. Translation: CAA55689.1.
AK030480 mRNA. Translation: BAC26982.1.
BX000989 Genomic DNA. Translation: CAM21483.1.
CH466538 Genomic DNA. Translation: EDL05518.1.
X81466 mRNA. Translation: CAA57224.1.
CCDSiCCDS18013.1. [Q61772-1]
CCDS51132.1. [Q61772-4]
CCDS71353.1. [Q61772-3]
PIRiI48612.
I48614.
JC5672.
RefSeqiNP_001277363.1. NM_001290434.1.
NP_034271.3. NM_010141.4. [Q61772-1]
XP_006537669.1. XM_006537606.2. [Q61772-2]
XP_006537670.1. XM_006537607.2. [Q61772-5]
UniGeneiMm.257266.

3D structure databases

ProteinModelPortaliQ61772.
SMRiQ61772. Positions 30-989.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi199474. 1 interaction.

PTM databases

PhosphoSiteiQ61772.

Proteomic databases

MaxQBiQ61772.
PaxDbiQ61772.
PRIDEiQ61772.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000029964; ENSMUSP00000029964; ENSMUSG00000028289. [Q61772-1]
ENSMUST00000080934; ENSMUSP00000079735; ENSMUSG00000028289. [Q61772-4]
ENSMUST00000108194; ENSMUSP00000103829; ENSMUSG00000028289. [Q61772-5]
GeneIDi13841.
KEGGimmu:13841.
UCSCiuc008sen.2. mouse. [Q61772-1]

Organism-specific databases

CTDi2045.
MGIiMGI:95276. Epha7.

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118975.
HOGENOMiHOG000233856.
HOVERGENiHBG062180.
InParanoidiQ61772.
KOiK05108.
OMAiENSPKMH.
OrthoDBiEOG7VTDM6.
TreeFamiTF315608.

Enzyme and pathway databases

BRENDAi2.7.10.1. 3474.
ReactomeiREACT_280640. EPHA-mediated growth cone collapse.
REACT_292566. EPH-Ephrin signaling.
REACT_314615. EPH-ephrin mediated repulsion of cells.

Miscellaneous databases

ChiTaRSiEpha7. mouse.
NextBioi284676.
PROiQ61772.
SOURCEiSearch...

Gene expression databases

BgeeiQ61772.
CleanExiMM_EPHA7.
ExpressionAtlasiQ61772. baseline and differential.
GenevestigatoriQ61772.

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. FN3_dom.
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.
IPR021129. SAM_type1.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
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.
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.
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...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of alternatively spliced mRNAs encoding variants of MDK1, a novel receptor tyrosine kinase expressed in the murine nervous system."
    Ciossek T., Millauer B., Ullrich A.
    Oncogene 10:97-108(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING.
    Strain: BALB/c.
    Tissue: Brain.
  2. "A novel truncated variant form of Ebk/MDK1 receptor tyrosine kinase is expressed in embryonic mouse brain."
    Talukder A.H., Muramatsu T., Kaneda N.
    Cell Struct. Funct. 22:477-485(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Pituitary.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  5. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 431-998 (ISOFORM 1).
    Tissue: Brain.
  7. "PDZ proteins bind, cluster, and synaptically colocalize with Eph receptors and their ephrin ligands."
    Torres R., Firestein B.L., Dong H., Staudinger J., Olson E.N., Huganir R.L., Bredt D.S., Gale N.W., Yancopoulos G.D.
    Neuron 21:1453-1463(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GRIP1 AND PICK1, IDENTIFICATION OF PDZ-BINDING MOTIF.
  8. "Regulation of repulsion versus adhesion by different splice forms of an Eph receptor."
    Holmberg J., Clarke D.L., Frisen J.
    Nature 408:203-206(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CELL ADHESION AND REPULSION (ISOFORMS 1 AND 4), EFNA5 LIGAND-BINDING, PHOSPHORYLATION, DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION.
  9. "Ephrin signalling controls brain size by regulating apoptosis of neural progenitors."
    Depaepe V., Suarez-Gonzalez N., Dufour A., Passante L., Gorski J.A., Jones K.R., Ledent C., Vanderhaeghen P.
    Nature 435:1244-1250(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION IN APOPTOSIS.
  10. "Opposing gradients of ephrin-As and EphA7 in the superior colliculus are essential for topographic mapping in the mammalian visual system."
    Rashid T., Upton A.L., Blentic A., Ciossek T., Knoell B., Thompson I.D., Drescher U.
    Neuron 47:57-69(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION IN TOPOGRAPHIC MAPPING, DEVELOPMENTAL STAGE.
  11. "Dissociation of corticothalamic and thalamocortical axon targeting by an EphA7-mediated mechanism."
    Torii M., Levitt P.
    Neuron 48:563-575(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CORTICOTHALAMIC AXON GUIDANCE.

Entry informationi

Entry nameiEPHA7_MOUSE
AccessioniPrimary (citable) accession number: Q61772
Secondary accession number(s): Q61505
, Q61773, Q61774, Q8BSU8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 1997
Last sequence update: July 26, 2011
Last modified: March 31, 2015
This is version 158 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.