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O08644

- EPHB6_MOUSE

UniProt

O08644 - EPHB6_MOUSE

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Protein

Ephrin type-B receptor 6

Gene

Ephb6

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli

Functioni

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).By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi669 – 6779ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. ephrin receptor activity Source: InterPro

GO - Biological processi

  1. calcium ion homeostasis Source: MGI
  2. parathyroid hormone secretion Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_241951. Ephrin signaling.
REACT_243590. EPH-ephrin mediated repulsion of cells.
REACT_257656. EPHB-mediated forward signaling.
REACT_258158. EPH-Ephrin signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
Ephrin type-B receptor 6
Alternative name(s):
MEP
Tyrosine-protein kinase-defective receptor EPH-6
Gene namesi
Name:Ephb6
Synonyms:Cekl
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 6

Organism-specific databases

MGIiMGI:1096338. Ephb6.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini33 – 591559ExtracellularSequence AnalysisAdd
BLAST
Transmembranei592 – 61221HelicalSequence AnalysisAdd
BLAST
Topological domaini613 – 1014402CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-KW
  2. integral component of plasma membrane Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3232By similarityAdd
BLAST
Chaini33 – 1014982Ephrin type-B receptor 6PRO_0000016838Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi473 – 4731N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

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).By similarity

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiO08644.
PaxDbiO08644.
PRIDEiO08644.

PTM databases

PhosphoSiteiO08644.

Expressioni

Tissue specificityi

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.1 Publication

Gene expression databases

BgeeiO08644.
CleanExiMM_EPHB6.
GenevestigatoriO08644.

Interactioni

Subunit structurei

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

Structurei

3D structure databases

ProteinModelPortaliO08644.
SMRiO08644. Positions 32-580, 640-919, 949-1000.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini34 – 232199Eph LBDPROSITE-ProRule annotationAdd
BLAST
Domaini364 – 479116Fibronectin type-III 1PROSITE-ProRule annotationAdd
BLAST
Domaini480 – 57596Fibronectin type-III 2PROSITE-ProRule annotationAdd
BLAST
Domaini663 – 912250Protein kinasePROSITE-ProRule annotationAdd
BLAST
Domaini941 – 100565SAMPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi1012 – 10143PDZ-bindingSequence Analysis

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi168 – 1736Poly-Ser
Compositional biasi214 – 361148Cys-richAdd
BLAST
Compositional biasi874 – 8774Poly-Pro

Domaini

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).PROSITE-ProRule annotation

Sequence similaritiesi

Belongs to the protein kinase superfamily. Tyr protein kinase family. Ephrin receptor subfamily.PROSITE-ProRule annotation
Contains 1 Eph LBD (Eph ligand-binding) domain.PROSITE-ProRule annotation
Contains 2 fibronectin type-III domains.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation
Contains 1 SAM (sterile alpha motif) domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118975.
HOGENOMiHOG000233856.
HOVERGENiHBG062180.
InParanoidiO08644.
KOiK05114.
OMAiEQAVAIQ.
OrthoDBiEOG7VTDM6.
PhylomeDBiO08644.
TreeFamiTF314013.

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.
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]
PfamiPF14575. 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]
PIRSFiPIRSF000666. TyrPK_ephrin_receptor. 1 hit.
PRINTSiPR00109. TYRKINASE.
SMARTiSM00615. EPH_lbd. 1 hit.
SM00060. FN3. 2 hits.
SM00454. SAM. 1 hit.
[Graphical view]
SUPFAMiSSF47769. SSF47769. 1 hit.
SSF49265. SSF49265. 1 hit.
SSF49785. SSF49785. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS51550. 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]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. Align

Note: Additional isoforms seem to exist.

Isoform 1 (identifier: O08644-1) [UniParc]FASTAAdd to Basket

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

        10         20         30         40         50
MATEGTTGSG SRVVAGMVCS LWLLVLGSSV LALEEVLLDT TGETSEIGWL
60 70 80 90 100
TYPPGGWDEV SVLDDQRRLT RTFEACHVAG LPPGSGQDNW LQTHFVERRG
110 120 130 140 150
AQRAHIRLHF SVRACSSLGV SGGTCRETFT LYYRQADEPD GPDSIAAWHL
160 170 180 190 200
KRWTKVDTIA ADESFPASSS SSSWAVGPHR TGQRVGLQLN VKERSFGPLT
210 220 230 240 250
QRGFYVAFQD TGACLALVAV KLFSYTCPSV LRAFASFPET QASGAGGASL
260 270 280 290 300
VAAVGTCVAH AEPEEDGVGG QAGGSPPRLH CNGEGRWMVA VGGCRCQPGH
310 320 330 340 350
QPARGDKLCQ ACPEGSYKAL AGNVPCSPCP ARSHSPDPAA PVCPCLQGFY
360 370 380 390 400
RASSDPPEAP CTGPPSAPRE LWFEVQGSAL MLHWRLPQEL GGRGDLLFNV
410 420 430 440 450
VCKECGGHGE PSSGGMCRRC RDEVHFDPRQ RGLTESRVLV GGLRAHVPYI
460 470 480 490 500
LEVQAVNGVS ELSPDPPQAA AINVSTSHEV PSAVPVMHQV SRAANSITVS
510 520 530 540 550
WPQPEQTNGN ILDYQLRYYD QAEDESHSFT MTSETNTATV TRLSPGHIYG
560 570 580 590 600
FQVRARTAAG HGPYGGKVYF QTLPQGELSS QLPEKLSLVI GSILGALAFL
610 620 630 640 650
LLAAITVLAV IFQRKRRGTG YTEQLQQYSS PGLGVKYYID PSTYDDPCQA
660 670 680 690 700
IRELAREVDP TYIKIEEVIG AGSFGEVRRG RLQPRGRREQ AVAIQALWAG
710 720 730 740 750
GAESLKMTFL GRAALLGQFQ HPNILRLEGV VTKSRPVMVL TELMELGPLD
760 770 780 790 800
SFLRQREGQF SSLQLVAMQR GVAAAMQYLS SFAFVHRALS ARSVLVNSHL
810 820 830 840 850
VCKVARLGHS PQGSSSLLRW AAPEVITHGK YTTSSDVWSF GILMWEVMSY
860 870 880 890 900
GERPYWDMNE QEVLNAIEQE FRLPPPPGCP PGLHLLMLDT WQKDRARRPH
910 920 930 940 950
FDQLVAAFDK MIRKPDTLQA EGGSGDRPSQ ALLNPVALDF PCLDSPQAWL
960 970 980 990 1000
SAIGLECYQD NFSKFGLSTF SDVAQLSLED LPGLGITLAG HQKKLLHNIQ
1010
LLQQHLRQPG SVEV
Length:1,014
Mass (Da):110,107
Last modified:April 20, 2010 - v4
Checksum:i1091796E1F68A842
GO
Isoform 2 (identifier: O08644-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     328-328: P → PCPALPLFTEHSRPEVC
     329-1014: Missing.

Show »
Length:344
Mass (Da):36,465
Checksum:i58A33AC4FD2DC032
GO
Isoform 3 (identifier: O08644-3) [UniParc]FASTAAdd to Basket

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

Show »
Length:583
Mass (Da):62,298
Checksum:i08E5C159BE0F376A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti527 – 5271H → Y in BAC39868. (PubMed:16141072)Curated
Sequence conflicti544 – 5441S → T in AAH31924. (PubMed:15489334)Curated
Sequence conflicti732 – 7321T → A in AAB51430. (PubMed:8761299)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei328 – 3281P → PCPALPLFTEHSRPEVC in isoform 2. 1 PublicationVSP_003020
Alternative sequencei329 – 1014686Missing in isoform 2. 1 PublicationVSP_003021Add
BLAST
Alternative sequencei583 – 5831P → S in isoform 3. 1 PublicationVSP_003022
Alternative sequencei584 – 1014431Missing in isoform 3. 1 PublicationVSP_003023Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L77867 mRNA. Translation: AAB51430.1.
AK087423 mRNA. Translation: BAC39868.1.
AK163823 mRNA. Translation: BAE37507.1.
BC031924 mRNA. Translation: AAH31924.1.
CCDSiCCDS20051.1. [O08644-1]
RefSeqiNP_001139823.1. NM_001146351.1. [O08644-1]
NP_031706.3. NM_007680.4. [O08644-1]
UniGeneiMm.271976.

Genome annotation databases

EnsembliENSMUST00000114732; ENSMUSP00000110380; ENSMUSG00000029869. [O08644-1]
GeneIDi13848.
KEGGimmu:13848.
UCSCiuc009bqa.2. mouse. [O08644-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L77867 mRNA. Translation: AAB51430.1 .
AK087423 mRNA. Translation: BAC39868.1 .
AK163823 mRNA. Translation: BAE37507.1 .
BC031924 mRNA. Translation: AAH31924.1 .
CCDSi CCDS20051.1. [O08644-1 ]
RefSeqi NP_001139823.1. NM_001146351.1. [O08644-1 ]
NP_031706.3. NM_007680.4. [O08644-1 ]
UniGenei Mm.271976.

3D structure databases

ProteinModelPortali O08644.
SMRi O08644. Positions 32-580, 640-919, 949-1000.
ModBasei Search...
MobiDBi Search...

PTM databases

PhosphoSitei O08644.

Proteomic databases

MaxQBi O08644.
PaxDbi O08644.
PRIDEi O08644.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000114732 ; ENSMUSP00000110380 ; ENSMUSG00000029869 . [O08644-1 ]
GeneIDi 13848.
KEGGi mmu:13848.
UCSCi uc009bqa.2. mouse. [O08644-1 ]

Organism-specific databases

CTDi 2051.
MGIi MGI:1096338. Ephb6.

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00760000118975.
HOGENOMi HOG000233856.
HOVERGENi HBG062180.
InParanoidi O08644.
KOi K05114.
OMAi EQAVAIQ.
OrthoDBi EOG7VTDM6.
PhylomeDBi O08644.
TreeFami TF314013.

Enzyme and pathway databases

Reactomei REACT_241951. Ephrin signaling.
REACT_243590. EPH-ephrin mediated repulsion of cells.
REACT_257656. EPHB-mediated forward signaling.
REACT_258158. EPH-Ephrin signaling.

Miscellaneous databases

ChiTaRSi Ephb6. mouse.
NextBioi 284696.
PROi O08644.
SOURCEi Search...

Gene expression databases

Bgeei O08644.
CleanExi MM_EPHB6.
Genevestigatori O08644.

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.
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 ]
Pfami PF14575. 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 ]
PIRSFi PIRSF000666. TyrPK_ephrin_receptor. 1 hit.
PRINTSi PR00109. TYRKINASE.
SMARTi SM00615. EPH_lbd. 1 hit.
SM00060. FN3. 2 hits.
SM00454. SAM. 1 hit.
[Graphical view ]
SUPFAMi SSF47769. SSF47769. 1 hit.
SSF49265. SSF49265. 1 hit.
SSF49785. SSF49785. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEi PS51550. 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiEPHB6_MOUSE
AccessioniPrimary (citable) accession number: O08644
Secondary accession number(s): Q3TQ77, Q8BN76, Q8K0A9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: April 20, 2010
Last modified: November 26, 2014
This is version 149 of the entry and version 4 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