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Protein

Ephrin type-B receptor 6

Gene

Ephb6

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Nucleotide bindingi669 – 677ATPPROSITE-ProRule annotation9

GO - Molecular functioni

GO - Biological processi

  • activated T cell proliferation Source: MGI
  • cytokine secretion Source: MGI
  • positive regulation of protein binding Source: MGI
  • positive regulation of T cell costimulation Source: MGI
  • T cell mediated immunity Source: MGI
  • type IV hypersensitivity Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Ligandi

ATP-binding, Nucleotide-binding

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
Proteomesi
  • UP000000589 Componenti: Chromosome 6

Organism-specific databases

MGIiMGI:1096338. Ephb6.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini33 – 591ExtracellularSequence analysisAdd BLAST559
Transmembranei592 – 612HelicalSequence analysisAdd BLAST21
Topological domaini613 – 1014CytoplasmicSequence analysisAdd BLAST402

GO - Cellular componenti

  • cell surface Source: MGI
  • extracellular region Source: UniProtKB-SubCell
  • integral component of plasma membrane Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Secreted

Pathology & Biotechi

Chemistry databases

GuidetoPHARMACOLOGYi1834.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 32By similarityAdd BLAST32
ChainiPRO_000001683833 – 1014Ephrin type-B receptor 6Add BLAST982

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi473N-linked (GlcNAc...)Sequence analysis1

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.
PeptideAtlasiO08644.
PRIDEiO08644.

PTM databases

iPTMnetiO08644.
PhosphoSitePlusiO08644.

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

BgeeiENSMUSG00000029869.
CleanExiMM_EPHB6.
ExpressionAtlasiO08644. baseline and differential.
GenevisibleiO08644. MM.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000110380.

Structurei

3D structure databases

ProteinModelPortaliO08644.
SMRiO08644.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini34 – 232Eph LBDPROSITE-ProRule annotationAdd BLAST199
Domaini364 – 479Fibronectin type-III 1PROSITE-ProRule annotationAdd BLAST116
Domaini480 – 575Fibronectin type-III 2PROSITE-ProRule annotationAdd BLAST96
Domaini663 – 912Protein kinasePROSITE-ProRule annotationAdd BLAST250
Domaini941 – 1005SAMPROSITE-ProRule annotationAdd BLAST65

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi1012 – 1014PDZ-bindingSequence analysis3

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi168 – 173Poly-Ser6
Compositional biasi214 – 361Cys-richAdd BLAST148
Compositional biasi874 – 877Poly-Pro4

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

eggNOGiKOG0196. Eukaryota.
COG0515. LUCA.
GeneTreeiENSGT00760000118975.
HOGENOMiHOG000233856.
HOVERGENiHBG062180.
InParanoidiO08644.
KOiK05114.
OMAiEQAVAIQ.
OrthoDBiEOG091G00W0.
PhylomeDBiO08644.
TreeFamiTF314013.

Family and domain databases

CDDicd00063. FN3. 2 hits.
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. FN3_dom.
IPR008979. Galactose-bd-like.
IPR013783. Ig-like_fold.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR001660. SAM.
IPR013761. SAM/pointed.
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.
PF07699. Ephrin_rec_like. 1 hit.
PF00041. fn3. 2 hits.
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.
SM01411. Ephrin_rec_like. 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. AlignAdd to basket

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)DescriptionActionsGraphical viewLength
Sequence conflicti527H → Y in BAC39868 (PubMed:16141072).Curated1
Sequence conflicti544S → T in AAH31924 (PubMed:15489334).Curated1
Sequence conflicti732T → A in AAB51430 (PubMed:8761299).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_003020328P → PCPALPLFTEHSRPEVC in isoform 2. 1 Publication1
Alternative sequenceiVSP_003021329 – 1014Missing in isoform 2. 1 PublicationAdd BLAST686
Alternative sequenceiVSP_003022583P → S in isoform 3. 1 Publication1
Alternative sequenceiVSP_003023584 – 1014Missing in isoform 3. 1 PublicationAdd BLAST431

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.
CCDSiCCDS20051.1. [O08644-1]
RefSeqiNP_001139823.1. NM_001146351.1. [O08644-1]
NP_031706.3. NM_007680.4. [O08644-1]
UniGeneiMm.271976.

3D structure databases

ProteinModelPortaliO08644.
SMRiO08644.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000110380.

Chemistry databases

GuidetoPHARMACOLOGYi1834.

PTM databases

iPTMnetiO08644.
PhosphoSitePlusiO08644.

Proteomic databases

MaxQBiO08644.
PaxDbiO08644.
PeptideAtlasiO08644.
PRIDEiO08644.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi2051.
MGIiMGI:1096338. Ephb6.

Phylogenomic databases

eggNOGiKOG0196. Eukaryota.
COG0515. LUCA.
GeneTreeiENSGT00760000118975.
HOGENOMiHOG000233856.
HOVERGENiHBG062180.
InParanoidiO08644.
KOiK05114.
OMAiEQAVAIQ.
OrthoDBiEOG091G00W0.
PhylomeDBiO08644.
TreeFamiTF314013.

Miscellaneous databases

ChiTaRSiEphb6. mouse.
PROiO08644.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000029869.
CleanExiMM_EPHB6.
ExpressionAtlasiO08644. baseline and differential.
GenevisibleiO08644. MM.

Family and domain databases

CDDicd00063. FN3. 2 hits.
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. FN3_dom.
IPR008979. Galactose-bd-like.
IPR013783. Ig-like_fold.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR001660. SAM.
IPR013761. SAM/pointed.
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.
PF07699. Ephrin_rec_like. 1 hit.
PF00041. fn3. 2 hits.
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.
SM01411. Ephrin_rec_like. 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]
ProtoNetiSearch...

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 30, 2016
This is version 165 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.