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Protein

Ephrin type-B receptor 3

Gene

Ephb3

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

Functioni

Receptor tyrosine kinase which binds promiscuously transmembrane ephrin-B family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Generally has an overlapping and redundant function with EPHB2. Like EPHB2, functions in axon guidance during development regulating for instance the neurons forming the corpus callosum and the anterior commissure, 2 major interhemispheric connections between the temporal lobes of the cerebral cortex. In addition to its role in axon guidance plays also an important redundant role with other ephrin-B receptors in development and maturation of dendritic spines and the formation of excitatory synapses. Controls other aspects of development through regulation of cell migration and positioning. This includes angiogenesis, palate development and thymic epithelium development for instance. Forward and reverse signaling through the EFNB2/EPHB3 complex also regulate migration and adhesion of cells that tubularize the urethra and septate the cloaca. Finally, plays an important role in intestinal epithelium differentiation segregating progenitor from differentiated cells in the crypt.6 Publications

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei660 – 6601ATPPROSITE-ProRule annotation
Active sitei753 – 7531Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi634 – 6429ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. axon guidance receptor activity Source: MGI
  3. ephrin receptor activity Source: UniProtKB
  4. transmembrane-ephrin receptor activity Source: MGI

GO - Biological processi

  1. angiogenesis Source: UniProtKB
  2. axonal fasciculation Source: UniProtKB
  3. axon guidance Source: UniProtKB
  4. cell migration Source: UniProtKB
  5. central nervous system projection neuron axonogenesis Source: MGI
  6. corpus callosum development Source: UniProtKB
  7. dendritic spine development Source: UniProtKB
  8. dendritic spine morphogenesis Source: UniProtKB
  9. digestive tract morphogenesis Source: UniProtKB
  10. ephrin receptor signaling pathway Source: UniProtKB
  11. palate development Source: UniProtKB
  12. positive regulation of synapse assembly Source: UniProtKB
  13. protein autophosphorylation Source: UniProtKB
  14. regulation of axonogenesis Source: UniProtKB
  15. regulation of cell-cell adhesion Source: UniProtKB
  16. regulation of GTPase activity Source: UniProtKB
  17. retinal ganglion cell axon guidance Source: MGI
  18. substrate adhesion-dependent cell spreading Source: UniProtKB
  19. thymus development Source: UniProtKB
  20. urogenital system development Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Kinase, Receptor, Transferase, Tyrosine-protein kinase

Keywords - Biological processi

Angiogenesis, Neurogenesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.10.1. 3474.
ReactomeiREACT_278281. Ephrin signaling.
REACT_292566. EPH-Ephrin signaling.
REACT_313804. EPHB-mediated forward signaling.
REACT_314615. EPH-ephrin mediated repulsion of cells.

Names & Taxonomyi

Protein namesi
Recommended name:
Ephrin type-B receptor 3 (EC:2.7.10.1)
Alternative name(s):
Developmental kinase 5
Short name:
mDK-5
Tyrosine-protein kinase receptor SEK-4
Gene namesi
Name:Ephb3
Synonyms:Etk2, Mdk5, Sek4
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 16

Organism-specific databases

MGIiMGI:104770. Ephb3.

Subcellular locationi

  1. Cell membrane 1 Publication; Single-pass type I membrane protein 1 Publication
  2. Cell projectiondendrite 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini30 – 554525ExtracellularSequence AnalysisAdd
BLAST
Transmembranei555 – 57521HelicalSequence AnalysisAdd
BLAST
Topological domaini576 – 993418CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. dendrite Source: UniProtKB-SubCell
  2. integral component of plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Membrane

Pathology & Biotechi

Disruption phenotypei

Mice are viable and fertile and show no obvious abnormal behavior. The corpus callosum, the main axon tract connecting the left and right cerebral hemispheres, is not formed in a significant fraction of newborns. This is associated with defects in guidance of callosal axons across the midline.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2929Sequence AnalysisAdd
BLAST
Chaini30 – 993964Ephrin type-B receptor 3PRO_0000016832Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi73 ↔ 191By similarity
Glycosylationi343 – 3431N-linked (GlcNAc...)Sequence Analysis
Glycosylationi440 – 4401N-linked (GlcNAc...)Sequence Analysis
Modified residuei609 – 6091Phosphotyrosine; by autocatalysisBy similarity

Post-translational modificationi

Phosphorylated. Autophosphorylates upon ligand-binding. Autophosphorylation on Tyr-609 is required for interaction with SH2 domain-containing proteins (By similarity).By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiP54754.
PaxDbiP54754.
PRIDEiP54754.

PTM databases

PhosphoSiteiP54754.

Expressioni

Tissue specificityi

Expressed in cells of the retinal ganglion cell layer during retinal axon guidance to the optic disk. Expressed by Paneth and progenitor cells in the crypts of the intestinal epithelium (at protein level).2 Publications

Developmental stagei

Expressed during development in yolk sacs and by embryonic endothelial cells. Expressed in the developing intestinal epithelium at the bottom of the intervillus pockets where undifferentiated cells are allocated (at protein level).2 Publications

Gene expression databases

BgeeiP54754.
CleanExiMM_EPHB3.
ExpressionAtlasiP54754. baseline and differential.
GenevestigatoriP54754.

Interactioni

Subunit structurei

Heterotetramer upon binding of the ligand. The heterotetramer is composed of an ephrin dimer and a receptor dimer. Oligomerization is probably required to induce biological responses (By similarity).By similarity

Protein-protein interaction databases

BioGridi199477. 3 interactions.

Structurei

3D structure databases

SMRiP54754. Positions 29-537, 543-899, 917-987.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini31 – 209179Eph LBDPROSITE-ProRule annotationAdd
BLAST
Domaini331 – 446116Fibronectin type-III 1PROSITE-ProRule annotationAdd
BLAST
Domaini447 – 54094Fibronectin type-III 2PROSITE-ProRule annotationAdd
BLAST
Domaini628 – 891264Protein kinasePROSITE-ProRule annotationAdd
BLAST
Domaini920 – 98465SAMPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi991 – 9933PDZ-bindingSequence Analysis

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi191 – 328138Cys-richAdd
BLAST

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.
InParanoidiP54754.
KOiK05112.
OMAiNLRPKFA.
OrthoDBiEOG7VTDM6.
TreeFamiTF315608.

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.
IPR017441. Protein_kinase_ATP_BS.
IPR001660. SAM.
IPR013761. SAM/pointed.
IPR021129. SAM_type1.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR011641. Tyr-kin_ephrin_A/B_rcpt-like.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
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.
PF00536. SAM_1. 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.
SM00219. TyrKc. 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.
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]

Sequencei

Sequence statusi: Complete.

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

P54754-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGARPPPGL LPLLAPLLLP LLLPAGCWAL EETLMDTKWV TSELAWTSHP
60 70 80 90 100
ESGWEEVSGY DEAMNPIRTY QVCNVRESSQ NNWLRTGFIW RREVQRVYVE
110 120 130 140 150
LKFTVRDCNS IPNIPGSCKE TFNLFYYEAD SDVASASSPF WMENPYVKVD
160 170 180 190 200
TIAPDESFSR LDAGRVNTKV RSFGPLSKAG FYLAFQDQGA CMSLISVRAF
210 220 230 240 250
YKKCASTTAG FALFPETLTG AEPTSLVIAP GTCIANAVEV SVPLKLYCNG
260 270 280 290 300
DGEWMVPVGA CTCATGHEPA AKESQCRACP PGSYKAKQGE GPCLPCPPNS
310 320 330 340 350
RTTSPAASIC TCHNNFYRAD SDSADSACTT VPSPPRGVIS NVNETSLILE
360 370 380 390 400
WSEPRDLGGR DDLLYNVICK KCRGSSGAGG PATCSRCDDN VEFVPRQLGL
410 420 430 440 450
TERRVHISHL LAHTRYTFEV QAVNGVSGKS PLPPRYAAVN ITTNQAAPSE
460 470 480 490 500
VPTLHLHSSS GSSLTLSWAP PERPNGVILD YEMKYFEKSK GIASTVTSQK
510 520 530 540 550
NSVQLDGLQP DARYVVQVRA RTVAGYGQYS HPAEFETTSE RGSGAQQLQE
560 570 580 590 600
QLPLIVGSTV AGFVFMVVVV VIALVCLRKQ RHGPDAEYTE KLQQYIAPGM
610 620 630 640 650
KVYIDPFTYE DPNEAVREFA KEIDVSCVKI EEVIGAGEFG EVCRGRLKLP
660 670 680 690 700
GRREVFVAIK TLKVGYTERQ RRDFLSEASI MGQFDHPNII RLEGVVTKSR
710 720 730 740 750
PVMILTEFME NCALDSFLRL NDGQFTVIQL VGMLRGIAAG MKYLSEMNYV
760 770 780 790 800
HRDLAARNIL VNSNLVCKVS DFGLSRFLED DPSDPTYTSS LGGKIPIRWT
810 820 830 840 850
APEAIAYRKF TSASDVWSYG IVMWEVMSYG ERPYWDMSNQ DVINAVEQDY
860 870 880 890 900
RLPPPMDCPT ALHQLMLDCW VRDRNLRPKF SQIVNTLDKL IRNAASLKVT
910 920 930 940 950
ASAPSGMSQP LLDRTVPDYT TFTTVGDWLD AIKMGRYKES FVGAGFASFD
960 970 980 990
LVAQMTAEDL LRIGVTLAGH QKKILCSIQD MRLQMNQTLP VQV
Length:993
Mass (Da):109,662
Last modified:July 27, 2011 - v2
Checksum:i07C6EF2AC98AE1B4
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti200 – 2012FY → GD in CAA88910 (PubMed:7478528).Curated
Sequence conflicti331 – 3311V → E in CAA88910 (PubMed:7478528).Curated
Sequence conflicti567 – 5671V → M in CAA88910 (PubMed:7478528).Curated
Sequence conflicti719 – 7191R → Q in CAA53599 (PubMed:7947319).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z49086 mRNA. Translation: CAA88910.1.
BC014822 mRNA. Translation: AAH14822.1.
BC053085 mRNA. Translation: AAH53085.1.
X76012 mRNA. Translation: CAA53599.1.
CCDSiCCDS28060.1.
PIRiI48653.
I48761.
RefSeqiNP_034273.1. NM_010143.1.
UniGeneiMm.6972.

Genome annotation databases

EnsembliENSMUST00000006112; ENSMUSP00000006112; ENSMUSG00000005958.
GeneIDi13845.
KEGGimmu:13845.
UCSCiuc007yrg.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z49086 mRNA. Translation: CAA88910.1.
BC014822 mRNA. Translation: AAH14822.1.
BC053085 mRNA. Translation: AAH53085.1.
X76012 mRNA. Translation: CAA53599.1.
CCDSiCCDS28060.1.
PIRiI48653.
I48761.
RefSeqiNP_034273.1. NM_010143.1.
UniGeneiMm.6972.

3D structure databases

SMRiP54754. Positions 29-537, 543-899, 917-987.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi199477. 3 interactions.

Chemistry

GuidetoPHARMACOLOGYi1832.

PTM databases

PhosphoSiteiP54754.

Proteomic databases

MaxQBiP54754.
PaxDbiP54754.
PRIDEiP54754.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000006112; ENSMUSP00000006112; ENSMUSG00000005958.
GeneIDi13845.
KEGGimmu:13845.
UCSCiuc007yrg.1. mouse.

Organism-specific databases

CTDi2049.
MGIiMGI:104770. Ephb3.

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118975.
HOGENOMiHOG000233856.
HOVERGENiHBG062180.
InParanoidiP54754.
KOiK05112.
OMAiNLRPKFA.
OrthoDBiEOG7VTDM6.
TreeFamiTF315608.

Enzyme and pathway databases

BRENDAi2.7.10.1. 3474.
ReactomeiREACT_278281. Ephrin signaling.
REACT_292566. EPH-Ephrin signaling.
REACT_313804. EPHB-mediated forward signaling.
REACT_314615. EPH-ephrin mediated repulsion of cells.

Miscellaneous databases

ChiTaRSiEphb3. mouse.
NextBioi284688.
PROiP54754.
SOURCEiSearch...

Gene expression databases

BgeeiP54754.
CleanExiMM_EPHB3.
ExpressionAtlasiP54754. baseline and differential.
GenevestigatoriP54754.

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.
IPR017441. Protein_kinase_ATP_BS.
IPR001660. SAM.
IPR013761. SAM/pointed.
IPR021129. SAM_type1.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR011641. Tyr-kin_ephrin_A/B_rcpt-like.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
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.
PF00536. SAM_1. 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.
SM00219. TyrKc. 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.
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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning, characterization, and differential expression of MDK2 and MDK5, two novel receptor tyrosine kinases of the eck/eph family."
    Ciossek T., Lerch M.M., Ullrich A.
    Oncogene 11:2085-2095(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BALB/c.
    Tissue: Embryo.
  2. "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].
    Strain: C57BL/6 and FVB/N.
    Tissue: Brain and Mammary tumor.
  3. "Several receptor tyrosine kinase genes of the Eph family are segmentally expressed in the developing hindbrain."
    Becker N., Seitanidou T., Murphy P., Mattei M.-G., Topilko P., Nieto A., Wilkinson D.G., Charnay P., Gilardi P.
    Mech. Dev. 47:3-17(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 719-993.
    Strain: BALB/c.
    Tissue: Brain.
  4. "Sek4 and Nuk receptors cooperate in guidance of commissural axons and in palate formation."
    Orioli D., Henkemeyer M., Lemke G., Klein R., Pawson T.
    EMBO J. 15:6035-6049(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION IN AXON GUIDANCE, FUNCTION IN PALATE DEVELOPMENT.
  5. "Roles of ephrinB ligands and EphB receptors in cardiovascular development: demarcation of arterial/venous domains, vascular morphogenesis, and sprouting angiogenesis."
    Adams R.H., Wilkinson G.A., Weiss C., Diella F., Gale N.W., Deutsch U., Risau W., Klein R.
    Genes Dev. 13:295-306(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN ANGIOGENESIS, DEVELOPMENTAL STAGE.
  6. "Complementary expression of transmembrane ephrins and their receptors in the mouse spinal cord: a possible role in constraining the orientation of longitudinally projecting axons."
    Imondi R., Wideman C., Kaprielian Z.
    Development 127:1397-1410(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  7. "Beta-catenin and TCF mediate cell positioning in the intestinal epithelium by controlling the expression of EphB/ephrinB."
    Batlle E., Henderson J.T., Beghtel H., van den Born M.M., Sancho E., Huls G., Meeldijk J., Robertson J., van de Wetering M., Pawson T., Clevers H.
    Cell 111:251-263(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN INTESTINAL EPITHELIUM DIFFERENTIATION, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY.
  8. "Multiple EphB receptor tyrosine kinases shape dendritic spines in the hippocampus."
    Henkemeyer M., Itkis O.S., Ngo M., Hickmott P.W., Ethell I.M.
    J. Cell Biol. 163:1313-1326(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN DENDRITIC SPINE DEVELOPMENT, FUNCTION IN EXCITATORY SYNAPSE FORMATION, SUBCELLULAR LOCATION.
  9. "Bidirectional signaling mediated by ephrin-B2 and EphB2 controls urorectal development."
    Dravis C., Yokoyama N., Chumley M.J., Cowan C.A., Silvany R.E., Shay J., Baker L.A., Henkemeyer M.
    Dev. Biol. 271:272-290(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN URORECTAL DEVELOPMENT.
  10. "On the role of Eph signalling in thymus histogenesis; EphB2/B3 and the organizing of the thymic epithelial network."
    Garcia-Ceca J., Jimenez E., Alfaro D., Cejalvo T., Chumley M.J., Henkemeyer M., Munoz J.J., Zapata A.G.
    Int. J. Dev. Biol. 53:971-982(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN THYMUS DEVELOPMENT.

Entry informationi

Entry nameiEPHB3_MOUSE
AccessioniPrimary (citable) accession number: P54754
Secondary accession number(s): Q62214, Q91YS9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: July 27, 2011
Last modified: April 29, 2015
This is version 151 of the entry and version 2 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

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 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.