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Q61772

- EPHA7_MOUSE

UniProt

Q61772 - EPHA7_MOUSE

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Protein
Ephrin type-A receptor 7
Gene
Epha7, Ebk, Ehk3, Mdk1
Organism
Mus musculus (Mouse)
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. Isoform 4 which lacks the kinase domain may regulate isoform 1 adhesive properties.4 Publications

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: MGI
  5. protein binding 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. phosphorylation Source: UniProtKB
  6. positive regulation of neuron apoptotic process Source: MGI
  7. regulation of ERK1 and ERK2 cascade Source: UniProtKB
  8. regulation of cell-cell adhesion Source: UniProtKB
  9. regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
  10. regulation of peptidyl-tyrosine phosphorylation Source: UniProtKB
  11. regulation of protein autophosphorylation Source: UniProtKB
  12. 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.

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: Chromosome 4

Organism-specific databases

MGIiMGI:95276. Epha7.

Subcellular locationi

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

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: 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 – 2727 Reviewed prediction
Add
BLAST
Chaini28 – 998971Ephrin type-A receptor 7
PRO_0000016819Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi64 – 641N-linked (GlcNAc...) Reviewed prediction
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 By similarity
Modified residuei940 – 9401Phosphotyrosine; by autocatalysis Reviewed prediction

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

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

ArrayExpressiQ61772.
BgeeiQ61772.
CleanExiMM_EPHA7.
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).1 Publication

Protein-protein interaction databases

BioGridi199474. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliQ61772.
SMRiQ61772. Positions 30-899, 919-989.

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.
GeneTreeiENSGT00750000117255.
HOGENOMiHOG000233856.
HOVERGENiHBG062180.
InParanoidiQ8BSU8.
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. 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.
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. Align

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

MVVQTRFPSW IILCYIWLLG FAHTGEAQAA KEVLLLDSKA QQTELEWISS    50
PPSGWEEISG LDENYTPIRT YQVCQVMEPN QNNWLRTNWI SKGNAQRIFV 100
ELKFTLRDCN SLPGVLGTCK ETFNLYYYET DYDTGRNIRE NLYVKIDTIA 150
ADESFTQGDL GERKMKLNTE VREIGPLSKK GFYLAFQDVG ACIALVSVKV 200
YYKKCWSIVE NLAVFPDTVT GSEFSSLVEV RGTCVSSAEE EAENSPRMHC 250
SAEGEWLVPI GKCICKAGYQ QKGDTCEPCG RRFYKSSSQD LQCSRCPTHS 300
FSDREGSSRC ECEDGYYRAP SDPPYVACTR PPSAPQNLIF NINQTTVSLE 350
WSPPADNGGR NDVTYRILCK RCSWEQGECV PCGSNIGYMP QQTGLEDNYV 400
TVMDLLAHAN YTFEVEAVNG VSDLSRSQRL FAAVSITTGQ AAPSQVSGVM 450
KERVLQRSVQ LSWQEPEHPN GVITEYEIKY YEKDQRERTY STLKTKSTSA 500
SINNLKPGTV YVFQIRAVTA AGYGNYSPRL DVATLEEASG 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 DCWQKDRAER PKFEQIVGIL DKMIRNPSSL 900
KTPLGTCSRP LSPLLDQSTP DFTAFCSVGE WLQAIKMERY KDNFTAAGYN 950
SLESVARMTI DDVMSLGITL VGHQKKIMSS IQTMRAQMLH LHGTGIQV 998
Length:998
Mass (Da):111,860
Last modified:July 27, 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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei540 – 5445Missing in isoform 2.
VSP_003006
Alternative sequencei600 – 62627FKFPG…HQFAK → SLYRERGDGMEKTQHNKKWM IASCSRL in isoform 5.
VSP_003010Add
BLAST
Alternative sequencei600 – 61011FKFPGTKTYID → SLVTNEHLSVL in isoform 4.
VSP_003008Add
BLAST
Alternative sequencei601 – 6044Missing in isoform 3.
VSP_003007
Alternative sequencei611 – 998388Missing in isoform 4.
VSP_003009Add
BLAST
Alternative sequencei627 – 998372Missing in isoform 5.
VSP_003011Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti207 – 2071S → T in CAA55687. 1 Publication
Sequence conflicti207 – 2071S → T in CAA55688. 1 Publication
Sequence conflicti207 – 2071S → T in CAA55689. 1 Publication
Sequence conflicti480 – 4801Y → H in CAA57224. 1 Publication
Sequence conflicti657 – 6571K → Q in CAA55687. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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_006537606.1. [Q61772-2]
XP_006537670.1. XM_006537607.1. [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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS18013.1. [Q61772-1 ]
CCDS51132.1. [Q61772-4 ]
CCDS71353.1. [Q61772-3 ]
PIRi I48612.
I48614.
JC5672.
RefSeqi NP_001277363.1. NM_001290434.1.
NP_034271.3. NM_010141.4. [Q61772-1 ]
XP_006537669.1. XM_006537606.1. [Q61772-2 ]
XP_006537670.1. XM_006537607.1. [Q61772-5 ]
UniGenei Mm.257266.

3D structure databases

ProteinModelPortali Q61772.
SMRi Q61772. Positions 30-899, 919-989.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 199474. 1 interaction.

PTM databases

PhosphoSitei Q61772.

Proteomic databases

PaxDbi Q61772.
PRIDEi Q61772.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000029964 ; ENSMUSP00000029964 ; ENSMUSG00000028289 . [Q61772-1 ]
ENSMUST00000080934 ; ENSMUSP00000079735 ; ENSMUSG00000028289 . [Q61772-4 ]
ENSMUST00000108194 ; ENSMUSP00000103829 ; ENSMUSG00000028289 . [Q61772-5 ]
GeneIDi 13841.
KEGGi mmu:13841.
UCSCi uc008sen.2. mouse. [Q61772-1 ]

Organism-specific databases

CTDi 2045.
MGIi MGI:95276. Epha7.

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00750000117255.
HOGENOMi HOG000233856.
HOVERGENi HBG062180.
InParanoidi Q8BSU8.
KOi K05108.
OMAi ENSPKMH.
OrthoDBi EOG7VTDM6.
TreeFami TF315608.

Enzyme and pathway databases

BRENDAi 2.7.10.1. 3474.

Miscellaneous databases

ChiTaRSi EPHA7. mouse.
NextBioi 284676.
PROi Q61772.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q61772.
Bgeei Q61772.
CleanExi MM_EPHA7.
Genevestigatori Q61772.

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.
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 ]
Pfami PF14575. 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 ]
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. "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(1995) [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(1997) [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(2005) [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 (JUL-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(1998) [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(2000) [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(2005) [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(2005) [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(2005) [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: November 1, 1997
Last sequence update: July 27, 2011
Last modified: September 3, 2014
This is version 153 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

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