Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Ephrin type-B receptor 6

Gene

Ephb6

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

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 bindingi668 – 6769ATPPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

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):
Tyrosine-protein kinase-defective receptor EPH-6
Gene namesi
Name:Ephb6
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 4

Organism-specific databases

RGDi1306163. Ephb6.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini32 – 590559ExtracellularSequence analysisAdd
BLAST
Transmembranei591 – 61121HelicalSequence analysisAdd
BLAST
Topological domaini612 – 1013402CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3131By similarityAdd
BLAST
Chaini32 – 1013982Ephrin type-B receptor 6PRO_0000042113Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi472 – 4721N-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

PaxDbiP0C0K7.
PRIDEiP0C0K7.

PTM databases

iPTMnetiP0C0K7.
PhosphoSiteiP0C0K7.

Expressioni

Gene expression databases

BgeeiENSRNOG00000014367.
GenevisibleiP0C0K7. RN.

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

STRINGi10116.ENSRNOP00000019720.

Structurei

3D structure databases

ProteinModelPortaliP0C0K7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini33 – 231199Eph LBDPROSITE-ProRule annotationAdd
BLAST
Domaini363 – 478116Fibronectin type-III 1PROSITE-ProRule annotationAdd
BLAST
Domaini479 – 57496Fibronectin type-III 2PROSITE-ProRule annotationAdd
BLAST
Domaini662 – 911250Protein kinasePROSITE-ProRule annotationAdd
BLAST
Domaini940 – 100465SAMPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi1011 – 10133PDZ-bindingSequence analysis

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi167 – 1726Poly-Ser
Compositional biasi213 – 360148Cys-richAdd
BLAST
Compositional biasi873 – 8764Poly-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

eggNOGiKOG0196. Eukaryota.
COG0515. LUCA.
GeneTreeiENSGT00760000118975.
HOGENOMiHOG000233856.
HOVERGENiHBG062180.
InParanoidiP0C0K7.
KOiK05114.
OMAiEQAVAIQ.
OrthoDBiEOG091G00W0.
PhylomeDBiP0C0K7.
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. 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.
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]

Sequencei

Sequence statusi: Complete.

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

P0C0K7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASENTAGSG SRVAGMVYSL WLLVLGPSVL ALEEVLLDTT GETSEIGWLT
60 70 80 90 100
YPPGGWDEVS VLDDQRRLTR TFEACHVAGL PPGSGQDNWL QTHFVERRGA
110 120 130 140 150
QRAHIRLHFS VRACSSLGVS GGTCRETFTL YYRQADEPDS PDSISAWHLK
160 170 180 190 200
RWTKVDTIAA DESFPASSSS SSWAVGPHRT DQRVGLQLNV KERSFGPLTQ
210 220 230 240 250
RGFYVAFQDT GACLALVAVK LFSYTCPSVL RAFASFPETQ ASGAGGASLV
260 270 280 290 300
AAVGTCVAHA EPEEDGVGGQ AGGSPPRLHC NGEGRWMVAV GGCRCQPGHQ
310 320 330 340 350
PARGDKLCQA CPEGSYKALP GNVPCSPCPA RSHSPDPAAP VCPCLQGFYR
360 370 380 390 400
ASSDPPEAPC TGPPSAPREL WFEVQGSALM LHWRLPQELG GRGDLLFNVV
410 420 430 440 450
CKECGGHKEP SSGGMCRRCR DEVHFDPRQR GLTESRVLVG GLRAHVPYIL
460 470 480 490 500
EVQAVNGVSE LSPDPPQAAA INVSTSHEVP SAVPVMHQVS RAANSITVSW
510 520 530 540 550
PQPEQTNGNI LDYQLRYYDQ AEDESHSFTM TSETNTATVT RLSPGHIYGF
560 570 580 590 600
QVRARTAAGH GPYGGKVYFQ TLPQGELSSQ LPEKLSLVIG SILGALAFLL
610 620 630 640 650
LAAITVLAVI FQRKRRGTGY TEQLQQYSSP GLGVKYYIDP STYDDPCQAI
660 670 680 690 700
RELAREVDPT YIKIEEVIGA GSFGEVRRGR LQPRGRREQA VAIQALWAGG
710 720 730 740 750
AESLKMTFLG RAALLGQFQH PNILRLEGVV TRSRPVMVLT ELMELGPLDS
760 770 780 790 800
FLRQREGQFS SLQLVAMQRG VAAAMQYLSS FAFVHRALSA RSVLVNSHLV
810 820 830 840 850
CKVARLGHSP QGSSSLLRWA APEVITHGKY TTSSDVWSFG ILMWEVMSYG
860 870 880 890 900
ERPYWDMSDQ EVLNAIEQEF RLPPPPGCPT GLHLLMLDTW QKDRARRPHF
910 920 930 940 950
DQLVAAFDKM IRKPDTLQAE GSSGDRPSQA LLNPVALDFP CLDSPQAWLS
960 970 980 990 1000
AIGLECYQDN FSKFGLSTFS DVAQLSLEDL PGLGITLAGH QKKLLHNIQL
1010
LQQHLRQPGS VEV
Length:1,013
Mass (Da):110,313
Last modified:April 20, 2010 - v3
Checksum:i7D62A6C0DBCE2BCB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR03031938 Genomic DNA. No translation available.
RefSeqiNP_001101327.1. NM_001107857.1.
UniGeneiRn.125930.

Genome annotation databases

EnsembliENSRNOT00000019720; ENSRNOP00000019720; ENSRNOG00000014367.
GeneIDi312275.
KEGGirno:312275.
UCSCiRGD:1306163. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR03031938 Genomic DNA. No translation available.
RefSeqiNP_001101327.1. NM_001107857.1.
UniGeneiRn.125930.

3D structure databases

ProteinModelPortaliP0C0K7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000019720.

PTM databases

iPTMnetiP0C0K7.
PhosphoSiteiP0C0K7.

Proteomic databases

PaxDbiP0C0K7.
PRIDEiP0C0K7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000019720; ENSRNOP00000019720; ENSRNOG00000014367.
GeneIDi312275.
KEGGirno:312275.
UCSCiRGD:1306163. rat.

Organism-specific databases

CTDi2051.
RGDi1306163. Ephb6.

Phylogenomic databases

eggNOGiKOG0196. Eukaryota.
COG0515. LUCA.
GeneTreeiENSGT00760000118975.
HOGENOMiHOG000233856.
HOVERGENiHBG062180.
InParanoidiP0C0K7.
KOiK05114.
OMAiEQAVAIQ.
OrthoDBiEOG091G00W0.
PhylomeDBiP0C0K7.
TreeFamiTF314013.

Miscellaneous databases

PROiP0C0K7.

Gene expression databases

BgeeiENSRNOG00000014367.
GenevisibleiP0C0K7. RN.

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. 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.
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_RAT
AccessioniPrimary (citable) accession number: P0C0K7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 27, 2005
Last sequence update: April 20, 2010
Last modified: September 7, 2016
This is version 99 of the entry and version 3 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. 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.