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Q61772 (EPHA7_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 149. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Epha7
Synonyms:Ebk, Ehk3, Mdk1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length998 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.8 Ref.9 Ref.10 Ref.11

Catalytic activity

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

Subunit structure

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). Ref.7

Subcellular location

Cell membrane Probable; Single-pass type I membrane protein Probable Ref.8.

Tissue specificity

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

Developmental stage

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. Ref.8 Ref.10

Post-translational modification

Phosphorylated. Isoform 4 inhibits isoform 1 phosphorylation and may regulate its function in adhesion. Ref.8

Disruption phenotype

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. Ref.9 Ref.10

Sequence similarities

Belongs to the protein kinase superfamily. Tyr protein kinase family. Ephrin receptor subfamily.

Contains 1 Eph LBD (Eph ligand-binding) domain.

Contains 2 fibronectin type-III domains.

Contains 1 protein kinase domain.

Contains 1 SAM (sterile alpha motif) domain.

Ontologies

Keywords
   Biological processApoptosis
Neurogenesis
   Cellular componentCell membrane
Membrane
   Coding sequence diversityAlternative splicing
   DomainRepeat
Signal
Transmembrane
Transmembrane helix
   LigandATP-binding
Nucleotide-binding
   Molecular functionDevelopmental protein
Kinase
Receptor
Transferase
Tyrosine-protein kinase
   PTMGlycoprotein
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processbrain development

Inferred from mutant phenotype Ref.9. Source: UniProtKB

branching morphogenesis of a nerve

Inferred from mutant phenotype Ref.10. Source: MGI

ephrin receptor signaling pathway

Inferred from direct assay Ref.8. Source: UniProtKB

negative chemotaxis

Inferred from direct assay Ref.10. Source: GOC

phosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of neuron apoptotic process

Inferred from mutant phenotype Ref.9. Source: MGI

regulation of ERK1 and ERK2 cascade

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of cell-cell adhesion

Inferred from direct assay Ref.8. Source: UniProtKB

regulation of cysteine-type endopeptidase activity involved in apoptotic process

Inferred from direct assay Ref.9. Source: UniProtKB

regulation of peptidyl-tyrosine phosphorylation

Inferred from direct assay Ref.8. Source: UniProtKB

regulation of protein autophosphorylation

Inferred from direct assay Ref.8. Source: UniProtKB

retinal ganglion cell axon guidance

Inferred from mutant phenotype Ref.10. Source: MGI

   Cellular_componentdendrite

Inferred from electronic annotation. Source: Ensembl

integral component of plasma membrane

Inferred by curator Ref.8. Source: UniProtKB

neuromuscular junction

Inferred from electronic annotation. Source: Ensembl

neuronal cell body

Inferred from electronic annotation. Source: Ensembl

postsynaptic membrane

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

GPI-linked ephrin receptor activity

Inferred from direct assay Ref.8. Source: UniProtKB

axon guidance receptor activity

Inferred from mutant phenotype Ref.11. Source: UniProtKB

chemorepellent activity

Inferred from direct assay Ref.10. Source: MGI

Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q61772-1)

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.
Isoform 2 (identifier: Q61772-2)

Also known as: MDK1-1; Ebk-td1;

The sequence of this isoform differs from the canonical sequence as follows:
     540-544: Missing.
Isoform 3 (identifier: Q61772-3)

Also known as: MDK1-2;

The sequence of this isoform differs from the canonical sequence as follows:
     601-604: Missing.
Isoform 4 (identifier: Q61772-4)

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.
Isoform 5 (identifier: Q61772-5)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727 Potential
Chain28 – 998971Ephrin type-A receptor 7
PRO_0000016819

Regions

Topological domain28 – 555528Extracellular Potential
Transmembrane556 – 57621Helical; Potential
Topological domain577 – 998422Cytoplasmic Potential
Domain32 – 210179Eph LBD
Domain331 – 441111Fibronectin type-III 1
Domain442 – 53796Fibronectin type-III 2
Domain633 – 894262Protein kinase
Domain923 – 98765SAM
Nucleotide binding639 – 6479ATP By similarity
Motif996 – 9983PDZ-binding Potential
Compositional bias192 – 328137Cys-rich

Sites

Active site7581Proton acceptor By similarity
Binding site6651ATP By similarity

Amino acid modifications

Modified residue6081Phosphotyrosine; by autocatalysis Potential
Modified residue6141Phosphotyrosine; by autocatalysis Potential
Modified residue7911Phosphotyrosine; by autocatalysis By similarity
Modified residue9401Phosphotyrosine; by autocatalysis Potential
Glycosylation641N-linked (GlcNAc...) Potential
Glycosylation3431N-linked (GlcNAc...) Potential
Glycosylation4101N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence540 – 5445Missing in isoform 2.
VSP_003006
Alternative sequence600 – 62627FKFPG…HQFAK → SLYRERGDGMEKTQHNKKWM IASCSRL in isoform 5.
VSP_003010
Alternative sequence600 – 61011FKFPGTKTYID → SLVTNEHLSVL in isoform 4.
VSP_003008
Alternative sequence601 – 6044Missing in isoform 3.
VSP_003007
Alternative sequence611 – 998388Missing in isoform 4.
VSP_003009
Alternative sequence627 – 998372Missing in isoform 5.
VSP_003011

Experimental info

Sequence conflict2071S → T in CAA55687. Ref.1
Sequence conflict2071S → T in CAA55688. Ref.1
Sequence conflict2071S → T in CAA55689. Ref.1
Sequence conflict4801Y → H in CAA57224. Ref.6
Sequence conflict6571K → Q in CAA55687. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (MDK1) (EPHA7-FL) [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: FCA1E83490E746E1

FASTA998111,860
        10         20         30         40         50         60 
MVVQTRFPSW IILCYIWLLG FAHTGEAQAA KEVLLLDSKA QQTELEWISS PPSGWEEISG 

        70         80         90        100        110        120 
LDENYTPIRT YQVCQVMEPN QNNWLRTNWI SKGNAQRIFV ELKFTLRDCN SLPGVLGTCK 

       130        140        150        160        170        180 
ETFNLYYYET DYDTGRNIRE NLYVKIDTIA ADESFTQGDL GERKMKLNTE VREIGPLSKK 

       190        200        210        220        230        240 
GFYLAFQDVG ACIALVSVKV YYKKCWSIVE NLAVFPDTVT GSEFSSLVEV RGTCVSSAEE 

       250        260        270        280        290        300 
EAENSPRMHC SAEGEWLVPI GKCICKAGYQ QKGDTCEPCG RRFYKSSSQD LQCSRCPTHS 

       310        320        330        340        350        360 
FSDREGSSRC ECEDGYYRAP SDPPYVACTR PPSAPQNLIF NINQTTVSLE WSPPADNGGR 

       370        380        390        400        410        420 
NDVTYRILCK RCSWEQGECV PCGSNIGYMP QQTGLEDNYV TVMDLLAHAN YTFEVEAVNG 

       430        440        450        460        470        480 
VSDLSRSQRL FAAVSITTGQ AAPSQVSGVM KERVLQRSVQ LSWQEPEHPN GVITEYEIKY 

       490        500        510        520        530        540 
YEKDQRERTY STLKTKSTSA SINNLKPGTV YVFQIRAVTA AGYGNYSPRL DVATLEEASG 

       550        560        570        580        590        600 
KMFEATAVSS EQNPVIIIAV VAVAGTIILV FMVFGFIIGR RHCGYSKADQ EGDEELYFHF 

       610        620        630        640        650        660 
KFPGTKTYID PETYEDPNRA VHQFAKELDA SCIKIERVIG AGEFGEVCSG RLKLPGKRDV 

       670        680        690        700        710        720 
AVAIKTLKVG YTEKQRRDFL CEASIMGQFD HPNVVHLEGV VTRGKPVMIV IEFMENGALD 

       730        740        750        760        770        780 
AFLRKHDGQF TVIQLVGMLR GIAAGMRYLA DMGYVHRDLA ARNILVNSNL VCKVSDFGLS 

       790        800        810        820        830        840 
RVIEDDPEAV YTTTGGKIPV RWTAPEAIQY RKFTSASDVW SYGIVMWEVM SYGERPYWDM 

       850        860        870        880        890        900 
SNQDVIKAIE EGYRLPAPMD CPAGLHQLML DCWQKDRAER PKFEQIVGIL DKMIRNPSSL 

       910        920        930        940        950        960 
KTPLGTCSRP LSPLLDQSTP DFTAFCSVGE WLQAIKMERY KDNFTAAGYN SLESVARMTI 

       970        980        990 
DDVMSLGITL VGHQKKIMSS IQTMRAQMLH LHGTGIQV 

« Hide

Isoform 2 (MDK1-1) (Ebk-td1) [UniParc].

Checksum: 2D1C811BCD1FA937
Show »

FASTA993111,268
Isoform 3 (MDK1-2) [UniParc].

Checksum: 25ADED280A8D9FBF
Show »

FASTA994111,431
Isoform 4 (MDK1-T1) (EPHA7-T1) [UniParc].

Checksum: E61310A72FE1E739
Show »

FASTA61068,286
Isoform 5 (MDK1-T2) (EPHA7-T2) [UniParc].

Checksum: F929755DC75B5664
Show »

FASTA62670,300

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
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]"Embryo brain kinase: a novel gene of the eph/elk receptor tyrosine kinase family."
Ellis J., Liu Q., Breitman M., Jenkins N.A., Gilbert D.J., Copeland N.G., Tempest H.V., Warren S., Muir E., Schilling H., Fletcher F.A., Ziegler S.F., Rogers J.H.
Mech. Dev. 52:319-341(1995) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRI48612.
I48614.
JC5672.
RefSeqNP_034271.3. NM_010141.3.
XP_006537669.1. XM_006537606.1.
XP_006537670.1. XM_006537607.1.
UniGeneMm.257266.

3D structure databases

ProteinModelPortalQ61772.
SMRQ61772. Positions 30-899, 919-989.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid199474. 1 interaction.

PTM databases

PhosphoSiteQ61772.

Proteomic databases

PaxDbQ61772.
PRIDEQ61772.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000029964; ENSMUSP00000029964; ENSMUSG00000028289. [Q61772-1]
ENSMUST00000080934; ENSMUSP00000079735; ENSMUSG00000028289. [Q61772-4]
ENSMUST00000108194; ENSMUSP00000103829; ENSMUSG00000028289. [Q61772-5]
GeneID13841.
KEGGmmu:13841.
UCSCuc008sen.2. mouse. [Q61772-1]

Organism-specific databases

CTD2045.
MGIMGI:95276. Epha7.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00750000117255.
HOGENOMHOG000233856.
HOVERGENHBG062180.
InParanoidQ8BSU8.
KOK05108.
OMAPSGWEEI.
OrthoDBEOG7VTDM6.
TreeFamTF315608.

Enzyme and pathway databases

BRENDA2.7.10.1. 3474.

Gene expression databases

ArrayExpressQ61772.
BgeeQ61772.
CleanExMM_EPHA7.
GenevestigatorQ61772.

Family and domain databases

Gene3D1.10.150.50. 1 hit.
2.60.120.260. 1 hit.
2.60.40.10. 2 hits.
InterProIPR027936. 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]
PfamPF14575. 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]
PIRSFPIRSF000666. TyrPK_ephrin_receptor. 1 hit.
PRINTSPR00109. TYRKINASE.
SMARTSM00615. EPH_lbd. 1 hit.
SM00060. FN3. 2 hits.
SM00454. SAM. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMSSF47769. SSF47769. 1 hit.
SSF49265. SSF49265. 1 hit.
SSF49785. SSF49785. 1 hit.
SSF56112. SSF56112. 1 hit.
SSF57184. SSF57184. 1 hit.
PROSITEPS01186. 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]
ProtoNetSearch...

Other

ChiTaRSEPHA7. mouse.
NextBio284676.
PROQ61772.
SOURCESearch...

Entry information

Entry nameEPHA7_MOUSE
AccessionPrimary (citable) accession number: Q61772
Secondary accession number(s): Q61505 expand/collapse secondary AC list , Q61773, Q61774, Q8BSU8
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 27, 2011
Last modified: April 16, 2014
This is version 149 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot