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Reviewed, UniProtKB/Swiss-Prot Q62413 (EPHA6_MOUSE)

Last modified February 9, 2010. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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 lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

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 for members of the ephrin-A family. Binds to ephrin-A1, -A2, -A3, -A4 and -A5.

Catalytic activity

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

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 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 – 57021 Potential
Topological domain571 – 1035465Cytoplasmic Potential
Domain330 – 434105Fibronectin type-III 1
Domain438 – 53396Fibronectin type-III 2
Domain630 – 943314Protein kinase
Domain960 – 102465SAM
Nucleotide binding636 – 6449ATP By similarity
Region33 – 206174Ephrin-binding
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 conflict4771T → I in BAC27868. Ref.2
Sequence conflict9051Q → H in BAC27868. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q62413-1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 560B264194A5EF74

FASTA1,035116,137
        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 RSLAMFPDTI 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 AILDYETKYY 

       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 
PPSLQQLMLH 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]"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.
AK032436 mRNA. Translation: BAC27868.1.
IPIIPI00125887.
UniGeneMm.439753
Mm.455790

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ62413.

PTM databases

PhosphoSiteQ62413.

Proteomic databases

PRIDEQ62413.

Genome annotation databases

EnsemblENSMUST00000068860; ENSMUSP00000066734; ENSMUSG00000055540; Mus musculus. [Genome view]
UCSCuc007zpo.1. mouse.

Organism-specific databases

MGIMGI:108034. Epha6.

Phylogenomic databases

HOGENOMHBG755340.
HOVERGENQ62413.
InParanoidQ62413.

Enzyme and pathway databases

BRENDA2.7.10.1. 244.

Gene expression databases

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

Family and domain databases

InterProIPR001090. Ephrin_rcpt_lig-bd.
IPR008957. Fibronectin_typ-III-like_fold.
IPR003961. FN_III.
IPR008979. Galactose-bd-like.
IPR009030. Growth_fac_rcpt.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001660. SAM.
IPR010993. SAM_homology.
IPR021129. SAM_type1.
IPR020635. Tyr_Pkinase_cat_dom.
IPR020685. Tyr_prot_kinase.
IPR008266. Tyr_prot_kinase_AS.
IPR016257. Tyr_prot_kinase_ephrin_rcpt.
IPR001426. Tyr_prot_kinase_rcpt_V_CS.
[Graphical view]
Gene3DG3DSA:2.60.40.30. FN_III-like. 2 hits.
PANTHERPTHR23256. Tyr_prot_kinase. 1 hit.
PfamPF01404. Ephrin_lbd. 1 hit.
PF00041. fn3. 2 hits.
PF00536. SAM_1. 1 hit.
[Graphical view]
PIRSFPIRSF000666. TyrPK_ephrin_receptor. 1 hit.
SMARTSM00615. EPH_lbd. 1 hit.
SM00060. FN3. 2 hits.
SM00454. SAM. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
PROSITEPS50853. 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 Resources

SOURCESearch...

Entry information

Entry nameEPHA6_MOUSE
AccessionPrimary (citable) accession number: Q62413
Secondary accession number(s): Q8CCN2
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: February 9, 2010
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

MGD cross-references

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

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents