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Q62413 (EPHA6_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 121. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ephrin type-A receptor 6
EC=2.7.10.1
Alternative name(s):
EPH homology kinase 2
Short name=EHK-2
Gene names
Name:Epha6
Synonyms:Ehk-2, Ehk2
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length1035 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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 By similarity.

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.

Subcellular location

Membrane; Single-pass type I membrane protein.

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Potential
Chain23 – 10351013Ephrin type-A receptor 6
PRO_0000016816

Regions

Topological domain23 – 549527Extracellular Potential
Transmembrane550 – 57021Helical; Potential
Topological domain571 – 1035465Cytoplasmic Potential
Domain33 – 211179Eph LBD
Domain330 – 434105Fibronectin type-III 1
Domain438 – 53396Fibronectin type-III 2
Domain630 – 943314Protein kinase
Domain960 – 102465SAM
Nucleotide binding636 – 6449ATP By similarity
Motif1033 – 10353PDZ-binding Potential
Compositional bias193 – 327135Cys-rich

Sites

Active site7971Proton acceptor By similarity
Binding site6621ATP By similarity

Amino acid modifications

Modified residue6051Phosphotyrosine; by autocatalysis Potential
Modified residue6111Phosphotyrosine; by autocatalysis Potential
Modified residue8301Phosphotyrosine; by autocatalysis Potential
Modified residue9771Phosphotyrosine; by autocatalysis Potential
Glycosylation3421N-linked (GlcNAc...) Potential
Glycosylation3961N-linked (GlcNAc...) Potential
Glycosylation4091N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict2121N → S in AAB53836. Ref.1
Sequence conflict4771I → T in AAB53836. Ref.1
Sequence conflict9051H → Q in AAB53836. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q62413 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 9886E5A92B146E44

FASTA1,035116,185
        10         20         30         40         50         60 
MGGCEVREFL LQFGFFLPLL TAWTGDCSHV SNQVVLLDTT TVMGELGWKT YPLNGWDAIT 

        70         80         90        100        110        120 
EMDEHNRPIH TYQVCNVMEP NQNNWLRTNW ISRDAAQKIY VEMKFTLRDC NSIPWVLGTC 

       130        140        150        160        170        180 
KETFNLYYIE SDESHGTKFK PSQYIKIDTI AADESFTQMD LGDRILKLNT EIREVGPIER 

       190        200        210        220        230        240 
KGFYLAFQDI GACIALVSVR VFYKKCPFTV RNLAMFPDTI PRVDSSSLVE VRGSCVKSAE 

       250        260        270        280        290        300 
ERDTPKLYCG ADGDWLVPLG RCICSTGYEE IEGSCHACRP GFYKAFAGNT KCSKCPPHSS 

       310        320        330        340        350        360 
TYVEATSVCH CEKGYFRAEK DPPSMACTRP PSAPRNVAFN INETALILEW SPPSDTGGRK 

       370        380        390        400        410        420 
DLTYSVICKK CGLDTTQCED CGGGLRFIPR HTGLINNSVV VLDFVSHVNY TFEIEAMNGV 

       430        440        450        460        470        480 
SELSISPKPF TAITVTTDHD APSLIGMMRK DWASQNSLAL SWQAPAFSNG AILDYEIKYY 

       490        500        510        520        530        540 
EKEHEQLTYS STRSKAPSVI VTGLKPATTY IFHIRVRTAT GYSGYSQKFE FETGDETSDM 

       550        560        570        580        590        600 
AAEQGQILVI ATAAVGGFTL LVILTLFFLI TGRCQWYIKA KMKSEEKRRT HLQNGHLRFP 

       610        620        630        640        650        660 
GIKTYIDPDT YEDPSLAVHE FAKEIDPSRI RIERVIGAGE FGEVCSGRLK TPGKREIPVA 

       670        680        690        700        710        720 
IKTLKGGHMD RQRRDFLREA SIMGQFDHPN IIRLEGVVTK RSFPAIGVEA FCPSFLRAGF 

       730        740        750        760        770        780 
LNGIQAPHPV TAGGSLPPRI PAGRPVMIVV EYMENGSLDS FLRKHDGHFT VIQLVGMLRG 

       790        800        810        820        830        840 
IASGMKYLSD MGYVHRDLAA RNILVNSNLV CKVSDFGLSR VLEDDPEAAY TTTGGKIPIR 

       850        860        870        880        890        900 
WTAPEAIAYR KFSSASDAWS YGIVMWEVMS YGERPYWEMS NQDVILSIEE GYRLPAPMGC 

       910        920        930        940        950        960 
PPSLHQLMLH CWQKERNHRP KFTDIVSFLD KLIRNPSALH TLVEDILVMP ESPGDVPEYP 

       970        980        990       1000       1010       1020 
LFVTVGDWLD SIKMGQYKSN FMAAGFTTFD LISRMSIDDI RRIGVILIGH QRRIVSSIQT 

      1030 
LRLHMMHIQE KGFHV

« Hide

References

« Hide 'large scale' references
[1]"Cloning of m-ehk2 from the murine inner ear, an eph family receptor tyrosine kinase expressed in the developing and adult cochlea."
Lee A.M., Navaratnam D., Ichimiya S., Greene M.I., Davis J.G.
DNA Cell Biol. 15:817-825(1996) [PubMed: 8892754] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: BALB/c.
[2]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].
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[4]"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: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 397-1035.
Strain: C57BL/6J.
Tissue: Olfactory bulb.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U58332 mRNA. Translation: AAB53836.1.
CH466521 Genomic DNA. Translation: EDK98232.1.
BC141090 mRNA. Translation: AAI41091.1.
AK032436 mRNA. Translation: BAC27868.1.
IPIIPI00990379.
UniGeneMm.455790.

3D structure databases

ProteinModelPortalQ62413.
SMRQ62413. Positions 32-535, 617-1030.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ62413.

PTM databases

PhosphoSiteQ62413.

Proteomic databases

PRIDEQ62413.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000171048; ENSMUSP00000131260; ENSMUSG00000055540.

Organism-specific databases

MGIMGI:108034. Epha6.

Phylogenomic databases

GeneTreeENSGT00600000084150.
HOGENOMHBG755340.
HOVERGENHBG062180.
InParanoidQ62413.
OrthoDBEOG4FR0QX.

Enzyme and pathway databases

BRENDA2.7.10.1. 3474.

Gene expression databases

ArrayExpressQ62413.
BgeeQ62413.
CleanExMM_EPHA6.
GenevestigatorQ62413.
GermOnlineENSMUSG00000055540. Mus musculus.

Family and domain databases

InterProIPR001090. Ephrin_rcpt_lig-bd.
IPR003961. Fibronectin_type3.
IPR008979. Galactose-bd-like.
IPR009030. Growth_fac_rcpt.
IPR013783. Ig-like_fold.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001660. SAM.
IPR013761. SAM/pointed.
IPR021129. SAM_type1.
IPR001245. Ser-Thr/Tyr_kinase.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
IPR016257. Tyr_kinase_ephrin_rcpt.
IPR001426. Tyr_kinase_rcpt_V_CS.
[Graphical view]
Gene3DG3DSA:2.60.40.10. Ig-like_fold. 2 hits.
G3DSA:1.10.150.50. SAM_type. 1 hit.
PfamPF01404. Ephrin_lbd. 1 hit.
PF00041. fn3. 2 hits.
PF07714. Pkinase_Tyr. 2 hits.
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]
SUPFAMSSF49265. FN_III-like. 2 hits.
SSF49785. Gal_bind_like. 1 hit.
SSF57184. Grow_fac_recept. 1 hit.
SSF56112. Kinase_like. 1 hit.
SSF47769. SAM_homology. 1 hit.
PROSITEPS51550. 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

SOURCESearch...

Entry information

Entry nameEPHA6_MOUSE
AccessionPrimary (citable) accession number: Q62413
Secondary accession number(s): B9EIV2, Q8CCN2
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 27, 2011
Last modified: December 14, 2011
This is version 121 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

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

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents