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O08644 (EPHB6_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 143. 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-B receptor 6
Alternative name(s):
MEP
Tyrosine-protein kinase-defective receptor EPH-6
Gene names
Name:Ephb6
Synonyms:Cekl
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1014 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Kinase-defective receptor for members of the ephrin-B family. Binds to ephrin-B1 and ephrin-B2. Modulates cell adhesion and migration by exerting both positive and negative effects upon stimulation with ephrin-B2. Inhibits JNK activation, T-cell receptor-induced IL-2 secretion and CD25 expression upon stimulation with ephrin-B2 By similarity.

Subunit structure

Interacts with CBL and EPHB1. Interacts with FYN; this interaction takes place in a ligand-independent manner By similarity.

Subcellular location

Isoform 1: Cell membrane; Single-pass type I membrane protein.

Isoform 2: Secreted.

Isoform 3: Secreted.

Tissue specificity

High level in thymus, and brain. Very low levels of expression in kidney, lung, liver, bone marrow, skeletal muscle, spleen from 2 week old and adult mice, heart, testes and embryonic stem cells. Ref.1

Domain

The protein kinase domain is predicted to be catalytically inactive. Its extracellular domain is capable of promoting cell adhesion and migration in response to low concentrations of ephrin-B2, but its cytoplasmic domain is essential for cell repulsion and inhibition of migration induced by high concentrations of ephrin-B2 By similarity.

Post-translational modification

Ligand-binding increases phosphorylation on tyrosine residues. Phosphorylation on tyrosine residues is mediated by transphosphorylation by the catalytically active EPHB1 in a ligand-independent manner. Tyrosine phosphorylation of the receptor may act as a switch on the functional transition from cell adhesion/attraction to de-adhesion/repulsion By similarity.

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.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform 1 (identifier: O08644-1)

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: O08644-2)

The sequence of this isoform differs from the canonical sequence as follows:
     328-328: P → PCPALPLFTEHSRPEVC
     329-1014: Missing.
Isoform 3 (identifier: O08644-3)

The sequence of this isoform differs from the canonical sequence as follows:
     583-583: P → S
     584-1014: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3232 By similarity
Chain33 – 1014982Ephrin type-B receptor 6
PRO_0000016838

Regions

Topological domain33 – 591559Extracellular Potential
Transmembrane592 – 61221Helical; Potential
Topological domain613 – 1014402Cytoplasmic Potential
Domain34 – 232199Eph LBD
Domain364 – 479116Fibronectin type-III 1
Domain480 – 57596Fibronectin type-III 2
Domain663 – 912250Protein kinase
Domain941 – 100565SAM
Nucleotide binding669 – 6779ATP By similarity
Motif1012 – 10143PDZ-binding Potential
Compositional bias168 – 1736Poly-Ser
Compositional bias214 – 361148Cys-rich
Compositional bias874 – 8774Poly-Pro

Amino acid modifications

Glycosylation4731N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence3281P → PCPALPLFTEHSRPEVC in isoform 2.
VSP_003020
Alternative sequence329 – 1014686Missing in isoform 2.
VSP_003021
Alternative sequence5831P → S in isoform 3.
VSP_003022
Alternative sequence584 – 1014431Missing in isoform 3.
VSP_003023

Experimental info

Sequence conflict5271H → Y in BAC39868. Ref.2
Sequence conflict5441S → T in AAH31924. Ref.3
Sequence conflict7321T → A in AAB51430. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified April 20, 2010. Version 4.
Checksum: 1091796E1F68A842

FASTA1,014110,107
        10         20         30         40         50         60 
MATEGTTGSG SRVVAGMVCS LWLLVLGSSV LALEEVLLDT TGETSEIGWL TYPPGGWDEV 

        70         80         90        100        110        120 
SVLDDQRRLT RTFEACHVAG LPPGSGQDNW LQTHFVERRG AQRAHIRLHF SVRACSSLGV 

       130        140        150        160        170        180 
SGGTCRETFT LYYRQADEPD GPDSIAAWHL KRWTKVDTIA ADESFPASSS SSSWAVGPHR 

       190        200        210        220        230        240 
TGQRVGLQLN VKERSFGPLT QRGFYVAFQD TGACLALVAV KLFSYTCPSV LRAFASFPET 

       250        260        270        280        290        300 
QASGAGGASL VAAVGTCVAH AEPEEDGVGG QAGGSPPRLH CNGEGRWMVA VGGCRCQPGH 

       310        320        330        340        350        360 
QPARGDKLCQ ACPEGSYKAL AGNVPCSPCP ARSHSPDPAA PVCPCLQGFY RASSDPPEAP 

       370        380        390        400        410        420 
CTGPPSAPRE LWFEVQGSAL MLHWRLPQEL GGRGDLLFNV VCKECGGHGE PSSGGMCRRC 

       430        440        450        460        470        480 
RDEVHFDPRQ RGLTESRVLV GGLRAHVPYI LEVQAVNGVS ELSPDPPQAA AINVSTSHEV 

       490        500        510        520        530        540 
PSAVPVMHQV SRAANSITVS WPQPEQTNGN ILDYQLRYYD QAEDESHSFT MTSETNTATV 

       550        560        570        580        590        600 
TRLSPGHIYG FQVRARTAAG HGPYGGKVYF QTLPQGELSS QLPEKLSLVI GSILGALAFL 

       610        620        630        640        650        660 
LLAAITVLAV IFQRKRRGTG YTEQLQQYSS PGLGVKYYID PSTYDDPCQA IRELAREVDP 

       670        680        690        700        710        720 
TYIKIEEVIG AGSFGEVRRG RLQPRGRREQ AVAIQALWAG GAESLKMTFL GRAALLGQFQ 

       730        740        750        760        770        780 
HPNILRLEGV VTKSRPVMVL TELMELGPLD SFLRQREGQF SSLQLVAMQR GVAAAMQYLS 

       790        800        810        820        830        840 
SFAFVHRALS ARSVLVNSHL VCKVARLGHS PQGSSSLLRW AAPEVITHGK YTTSSDVWSF 

       850        860        870        880        890        900 
GILMWEVMSY GERPYWDMNE QEVLNAIEQE FRLPPPPGCP PGLHLLMLDT WQKDRARRPH 

       910        920        930        940        950        960 
FDQLVAAFDK MIRKPDTLQA EGGSGDRPSQ ALLNPVALDF PCLDSPQAWL SAIGLECYQD 

       970        980        990       1000       1010 
NFSKFGLSTF SDVAQLSLED LPGLGITLAG HQKKLLHNIQ LLQQHLRQPG SVEV 

« Hide

Isoform 2 [UniParc].

Checksum: 58A33AC4FD2DC032
Show »

FASTA34436,465
Isoform 3 [UniParc].

Checksum: 08E5C159BE0F376A
Show »

FASTA58362,298

References

« Hide 'large scale' references
[1]"A new member of the Eph family of receptors that lacks protein tyrosine kinase activity."
Gurniak C.B., Berg L.J.
Oncogene 13:777-786(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), TISSUE SPECIFICITY.
Strain: BALB/C X 129.
Tissue: Thymus.
[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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Strain: C57BL/6J.
Tissue: Eye and Head.
[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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Strain: FVB/N.
Tissue: Salivary gland.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L77867 mRNA. Translation: AAB51430.1.
AK087423 mRNA. Translation: BAC39868.1.
AK163823 mRNA. Translation: BAE37507.1.
BC031924 mRNA. Translation: AAH31924.1.
RefSeqNP_001139823.1. NM_001146351.1.
NP_031706.3. NM_007680.4.
UniGeneMm.271976.

3D structure databases

ProteinModelPortalO08644.
SMRO08644. Positions 32-580, 614-934, 949-1000.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteO08644.

Proteomic databases

PaxDbO08644.
PRIDEO08644.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000114732; ENSMUSP00000110380; ENSMUSG00000029869. [O08644-1]
GeneID13848.
KEGGmmu:13848.
UCSCuc009bqa.2. mouse. [O08644-1]

Organism-specific databases

CTD2051.
MGIMGI:1096338. Ephb6.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00740000115081.
HOGENOMHOG000233856.
HOVERGENHBG062180.
KOK05114.
OMAFAFVHRA.
OrthoDBEOG7VTDM6.
PhylomeDBO08644.
TreeFamTF314013.

Gene expression databases

BgeeO08644.
CleanExMM_EPHB6.
GenevestigatorO08644.

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.
IPR013783. Ig-like_fold.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR001660. SAM.
IPR013761. SAM/pointed.
IPR011510. SAM_2.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR011641. Tyr-kin_ephrin_A/B_rcpt-like.
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.
PF07699. GCC2_GCC3. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
PF07647. SAM_2. 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.
[Graphical view]
SUPFAMSSF47769. SSF47769. 1 hit.
SSF49265. SSF49265. 1 hit.
SSF49785. SSF49785. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEPS51550. EPH_LBD. 1 hit.
PS50853. FN3. 2 hits.
PS50011. PROTEIN_KINASE_DOM. 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

ChiTaRSEPHB6. mouse.
NextBio284696.
PROO08644.
SOURCESearch...

Entry information

Entry nameEPHB6_MOUSE
AccessionPrimary (citable) accession number: O08644
Secondary accession number(s): Q3TQ77, Q8BN76, Q8K0A9
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: April 20, 2010
Last modified: April 16, 2014
This is version 143 of the entry and version 4 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