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Protein

Ephrin type-B receptor 2

Gene

Ephb2

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. Functions in axon guidance during development. Involved in the guidance of commissural axons, that form a major interhemispheric connection between the 2 temporal lobes of the cerebral cortex. Also involved in guidance of contralateral inner ear efferent growth cones at the midline and of retinal ganglion cell axons to the optic disk. In addition to axon guidance, also regulates dendritic spines development and maturation and stimulates the formation of excitatory synapses. Upon activation by EFNB1, abolishes the ARHGEF15-mediated negative regulation on excitatory synapse formation. Controls other aspects of development including angiogenesis, palate development and in inner ear development through regulation of endolymph production. Forward and reverse signaling through the EFNB2/EPHB2 complex regulate movement and adhesion of cells that tubularize the urethra and septate the cloaca. May function as a tumor suppressor.7 Publications

Catalytic activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei653ATPPROSITE-ProRule annotation1
Active sitei746Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi627 – 635ATPPROSITE-ProRule annotation9

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • axon guidance receptor activity Source: MGI
  • ephrin receptor activity Source: MGI
  • protein tyrosine kinase activity Source: UniProtKB
  • receptor activity Source: MGI
  • receptor binding Source: MGI
  • transmembrane-ephrin receptor activity Source: UniProtKB

GO - Biological processi

  • angiogenesis Source: UniProtKB
  • animal organ morphogenesis Source: MGI
  • axonal fasciculation Source: UniProtKB
  • axon guidance Source: UniProtKB
  • camera-type eye morphogenesis Source: MGI
  • cell morphogenesis Source: MGI
  • central nervous system projection neuron axonogenesis Source: MGI
  • commissural neuron axon guidance Source: UniProtKB
  • corpus callosum development Source: UniProtKB
  • dendritic spine development Source: UniProtKB
  • dendritic spine morphogenesis Source: UniProtKB
  • ephrin receptor signaling pathway Source: UniProtKB
  • inner ear morphogenesis Source: UniProtKB
  • learning Source: MGI
  • negative regulation of axonogenesis Source: MGI
  • optic nerve morphogenesis Source: MGI
  • palate development Source: UniProtKB
  • peptidyl-tyrosine phosphorylation Source: UniProtKB
  • phosphorylation Source: UniProtKB
  • positive regulation of long-term neuronal synaptic plasticity Source: MGI
  • positive regulation of synapse assembly Source: UniProtKB
  • protein phosphorylation Source: MGI
  • regulation of axonogenesis Source: MGI
  • regulation of body fluid levels Source: UniProtKB
  • regulation of neuronal synaptic plasticity Source: MGI
  • retinal ganglion cell axon guidance Source: MGI
  • transmembrane receptor protein tyrosine kinase signaling pathway Source: MGI
  • urogenital system development Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

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

Keywords - Biological processi

Neurogenesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-MMU-2682334. EPH-Ephrin signaling.
R-MMU-3928662. EPHB-mediated forward signaling.
R-MMU-3928664. Ephrin signaling.
R-MMU-3928665. EPH-ephrin mediated repulsion of cells.

Names & Taxonomyi

Protein namesi
Recommended name:
Ephrin type-B receptor 2Curated (EC:2.7.10.1)
Alternative name(s):
Neural kinase
Nuk receptor tyrosine kinase
Tyrosine-protein kinase receptor EPH-3
Tyrosine-protein kinase receptor SEK-3
Gene namesi
Name:Ephb2Imported
Synonyms:Epth3, Nuk1 Publication, Sek3Imported
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:99611. Ephb2.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini19 – 543ExtracellularSequence analysisAdd BLAST525
Transmembranei544 – 564HelicalSequence analysisAdd BLAST21
Topological domaini565 – 986CytoplasmicSequence analysisAdd BLAST422

GO - Cellular componenti

  • axon Source: UniProtKB
  • dendrite Source: UniProtKB
  • integral component of plasma membrane Source: UniProtKB
  • neuronal cell body Source: MGI
  • plasma membrane Source: Reactome
  • synapse Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Membrane

Pathology & Biotechi

Disruption phenotypei

Mice are long-lived and fertile. They display strain-specific circling behavior, are hyperactive and exhibit rapid head bobbing and twirled excessively when picked-up by the tail. This is probably due to abnormal vestibular function.2 Publications

Chemistry databases

ChEMBLiCHEMBL5961.
GuidetoPHARMACOLOGYi1831.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 18Sequence analysisAdd BLAST18
ChainiPRO_000001682819 – 986Ephrin type-B receptor 2Sequence analysisAdd BLAST968

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi62 ↔ 1841 Publication
Disulfide bondi97 ↔ 1071 Publication
Glycosylationi265N-linked (GlcNAc...)1 Publication1
Glycosylationi336N-linked (GlcNAc...)Sequence analysis1
Glycosylationi428N-linked (GlcNAc...)Sequence analysis1
Glycosylationi482N-linked (GlcNAc...)1 Publication1
Modified residuei602PhosphotyrosineBy similarity1

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiP54763.
PaxDbiP54763.
PRIDEiP54763.

PTM databases

iPTMnetiP54763.
PhosphoSitePlusiP54763.
SwissPalmiP54763.

Expressioni

Tissue specificityi

Expressed in the epithelial dark cells of the inner ear. Expressed in the region of the proximal tubules of the kidney nephron.1 Publication

Developmental stagei

Highly expressed in ventral cells of the neural tube and within axons of the peripheral nervous system during development. Expressed in the vestibulo-acoustic system and hindbrain as early as E11.5. Detected in the spinal cord at E12. Expressed in cells of the developing outer retina. Also expressed in mesenchyme adjacent to vessels.4 Publications

Gene expression databases

BgeeiENSMUSG00000028664.
CleanExiMM_EPHB2.
ExpressionAtlasiP54763. baseline and differential.

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). Interacts (via PDZ-binding motif) with GRIP1 and PICK1 (via PDZ domain) (By similarity). Interacts with ARHGEF15; mediates ARHGEF15 phosphorylation, ubiquitination and degradation by the proteasome. Interacts with AQP1; involved in endolymph production in the inner ear.By similarity5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-537711,EBI-537711
Arhgef15Q5FWH6-23EBI-537711,EBI-2943608
Epha4Q031373EBI-537711,EBI-1539152
Grip1Q925T62EBI-537711,EBI-537752
Ptk2P341523EBI-537711,EBI-77070
SrcP054803EBI-537711,EBI-298680

GO - Molecular functioni

  • receptor binding Source: MGI

Protein-protein interaction databases

DIPiDIP-34917N.
IntActiP54763. 11 interactors.
MINTiMINT-3381667.
STRINGi10090.ENSMUSP00000101471.

Chemistry databases

BindingDBiP54763.

Structurei

Secondary structure

1986
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi20 – 25Combined sources6
Helixi26 – 28Combined sources3
Beta strandi36 – 39Combined sources4
Beta strandi44 – 49Combined sources6
Beta strandi55 – 61Combined sources7
Beta strandi66 – 68Combined sources3
Beta strandi71 – 74Combined sources4
Beta strandi84 – 94Combined sources11
Helixi97 – 99Combined sources3
Beta strandi100 – 102Combined sources3
Beta strandi110 – 121Combined sources12
Beta strandi125 – 128Combined sources4
Beta strandi130 – 132Combined sources3
Beta strandi135 – 142Combined sources8
Beta strandi147 – 152Combined sources6
Beta strandi155 – 166Combined sources12
Beta strandi171 – 182Combined sources12
Beta strandi185 – 195Combined sources11
Helixi599 – 601Combined sources3
Beta strandi602 – 604Combined sources3
Helixi605 – 612Combined sources8
Helixi618 – 620Combined sources3
Beta strandi621 – 629Combined sources9
Beta strandi631 – 640Combined sources10
Beta strandi643 – 645Combined sources3
Beta strandi648 – 654Combined sources7
Helixi661 – 674Combined sources14
Beta strandi685 – 689Combined sources5
Beta strandi691 – 694Combined sources4
Beta strandi696 – 700Combined sources5
Helixi707 – 712Combined sources6
Turni713 – 716Combined sources4
Helixi720 – 739Combined sources20
Helixi749 – 751Combined sources3
Beta strandi752 – 754Combined sources3
Beta strandi760 – 762Combined sources3
Helixi790 – 792Combined sources3
Helixi795 – 799Combined sources5
Helixi805 – 820Combined sources16
Turni821 – 823Combined sources3
Turni826 – 829Combined sources4
Helixi832 – 840Combined sources9
Helixi853 – 862Combined sources10
Turni867 – 869Combined sources3
Helixi873 – 885Combined sources13
Helixi887 – 890Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1JPAX-ray1.91A/B587-898[»]
1KGYX-ray2.70A/B/C/D20-199[»]
1NUKX-ray2.90A20-202[»]
1SHWX-ray2.20B19-199[»]
2HENX-ray2.60A/B/C/D614-898[»]
3ETPX-ray2.00A20-199[»]
ProteinModelPortaliP54763.
SMRiP54763.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP54763.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini20 – 202Eph LBDPROSITE-ProRule annotationAdd BLAST183
Domaini324 – 434Fibronectin type-III 1PROSITE-ProRule annotationAdd BLAST111
Domaini435 – 530Fibronectin type-III 2PROSITE-ProRule annotationAdd BLAST96
Domaini621 – 884Protein kinasePROSITE-ProRule annotationAdd BLAST264
Domaini913 – 977SAMPROSITE-ProRule annotationAdd BLAST65

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi984 – 986PDZ-binding3

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi184 – 321Cys-richAdd BLAST138

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.
InParanoidiP54763.
KOiK05111.
OMAiVNNLDKM.
OrthoDBiEOG091G00W0.
TreeFamiTF315608.

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.
IPR009030. Growth_fac_rcpt_.
IPR013783. Ig-like_fold.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001660. SAM.
IPR013761. SAM/pointed.
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.
PF07699. Ephrin_rec_like. 1 hit.
PF00041. fn3. 2 hits.
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.
SM01411. Ephrin_rec_like. 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.
SSF57184. SSF57184. 2 hits.
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]

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

Isoform 3Curated (identifier: P54763-3) [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
MAVRRLGAAL LLLPLLAAVE ETLMDSTTAT AELGWMVHPP SGWEEVSGYD
60 70 80 90 100
ENMNTIRTYQ VCNVFESSQN NWLRTKFIRR RGAHRIHVEM KFSVRDCSSI
110 120 130 140 150
PSVPGSCKET FNLYYYEADF DLATKTFPNW MENPWVKVDT IAADESFSQV
160 170 180 190 200
DLGGRVMKIN TEVRSFGPVS RNGFYLAFQD YGGCMSLIAV RVFYRKCPRI
210 220 230 240 250
IQNGAIFQET LSGAESTSLV AARGSCIANA EEVDVPIKLY CNGDGEWLVP
260 270 280 290 300
IGRCMCKAGF EAVENGTVCR GCPSGTFKAN QGDEACTHCP INSRTTSEGA
310 320 330 340 350
TNCVCRNGYY RADLDPLDMP CTTIPSAPQA VISSVNETSL MLEWTPPRDS
360 370 380 390 400
GGREDLVYNI ICKSCGSGRG ACTRCGDNVQ YAPRQLGLTE PRIYISDLLA
410 420 430 440 450
HTQYTFEIQA VNGVTDQSPF SPQFASVNIT TNQAAPSAVS IMHQVSRTVD
460 470 480 490 500
SITLSWSQPD QPNGVILDYE LQYYEKELSE YNATAIKSPT NTVTVQGLKA
510 520 530 540 550
GAIYVFQVRA RTVAGYGRYS GKMYFQTMTE AEYQTSIKEK LPLIVGSSAA
560 570 580 590 600
GLVFLIAVVV IAIVCNRRGF ERADSEYTDK LQHYTSGHMT PGMKIYIDPF
610 620 630 640 650
TYEDPNEAVR EFAKEIDISC VKIEQVIGAG EFGEVCSGHL KLPGKREIFV
660 670 680 690 700
AIKTLKSGYT EKQRRDFLSE ASIMGQFDHP NVIHLEGVVT KSTPVMIITE
710 720 730 740 750
FMENGSLDSF LRQNDGQFTV IQLVGMLRGI AAGMKYLADM NYVHRDLAAR
760 770 780 790 800
NILVNSNLVC KVSDFGLSRF LEDDTSDPTY TSALGGKIPI RWTAPEAIQY
810 820 830 840 850
RKFTSASDVW SYGIVMWEVM SYGERPYWDM TNQDVINAIE QDYRLPPPMD
860 870 880 890 900
CPSALHQLML DCWQKDRNHR PKFGQIVNTL DKMIRNPNSL KAMAPLSSGI
910 920 930 940 950
NLPLLDRTIP DYTSFNTVDE WLEAIKMGQY KESFANAGFT SFDVVSQMMM
960 970 980
EDILRVGVTL AGHQKKILNS IQVMRAQMNQ IQSVEV
Length:986
Mass (Da):109,899
Last modified:October 14, 2015 - v3
Checksum:i92DB5234F18758A7
GO
Isoform 2Curated (identifier: P54763-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     566-566: N → NR

Note: No experimental confirmation available.
Show »
Length:987
Mass (Da):110,055
Checksum:iEE04E7A723307E4B
GO
Isoform 4Curated (identifier: P54763-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     476-476: K → KQ

Note: No experimental confirmation available.
Show »
Length:987
Mass (Da):110,027
Checksum:i586D4C475F42641F
GO

Sequence cautioni

The sequence AAA72411 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAH62924 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_057932476K → KQ in isoform 4. Curated1
Alternative sequenceiVSP_057933566N → NR in isoform 2. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL627214 Genomic DNA. No translation available.
AL627345 Genomic DNA. No translation available.
AL671173 Genomic DNA. No translation available.
BC043088 mRNA. Translation: AAH43088.2.
BC062924 mRNA. Translation: AAH62924.1. Different initiation.
L25890 mRNA. Translation: AAA72411.1. Different initiation.
X76011 mRNA. Translation: CAA53598.1.
RefSeqiNP_001277682.1. NM_001290753.2. [P54763-4]
NP_034272.1. NM_010142.4. [P54763-3]
XP_006538594.1. XM_006538531.3. [P54763-2]
UniGeneiMm.250981.

Genome annotation databases

EnsembliENSMUST00000059287; ENSMUSP00000058135; ENSMUSG00000028664. [P54763-4]
ENSMUST00000105845; ENSMUSP00000101471; ENSMUSG00000028664. [P54763-3]
ENSMUST00000105846; ENSMUSP00000101472; ENSMUSG00000028664. [P54763-2]
GeneIDi13844.
KEGGimmu:13844.
UCSCiuc008vim.2. mouse.
uc008vin.2. mouse.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL627214 Genomic DNA. No translation available.
AL627345 Genomic DNA. No translation available.
AL671173 Genomic DNA. No translation available.
BC043088 mRNA. Translation: AAH43088.2.
BC062924 mRNA. Translation: AAH62924.1. Different initiation.
L25890 mRNA. Translation: AAA72411.1. Different initiation.
X76011 mRNA. Translation: CAA53598.1.
RefSeqiNP_001277682.1. NM_001290753.2. [P54763-4]
NP_034272.1. NM_010142.4. [P54763-3]
XP_006538594.1. XM_006538531.3. [P54763-2]
UniGeneiMm.250981.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1JPAX-ray1.91A/B587-898[»]
1KGYX-ray2.70A/B/C/D20-199[»]
1NUKX-ray2.90A20-202[»]
1SHWX-ray2.20B19-199[»]
2HENX-ray2.60A/B/C/D614-898[»]
3ETPX-ray2.00A20-199[»]
ProteinModelPortaliP54763.
SMRiP54763.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-34917N.
IntActiP54763. 11 interactors.
MINTiMINT-3381667.
STRINGi10090.ENSMUSP00000101471.

Chemistry databases

BindingDBiP54763.
ChEMBLiCHEMBL5961.
GuidetoPHARMACOLOGYi1831.

PTM databases

iPTMnetiP54763.
PhosphoSitePlusiP54763.
SwissPalmiP54763.

Proteomic databases

MaxQBiP54763.
PaxDbiP54763.
PRIDEiP54763.

Protocols and materials databases

DNASUi13844.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000059287; ENSMUSP00000058135; ENSMUSG00000028664. [P54763-4]
ENSMUST00000105845; ENSMUSP00000101471; ENSMUSG00000028664. [P54763-3]
ENSMUST00000105846; ENSMUSP00000101472; ENSMUSG00000028664. [P54763-2]
GeneIDi13844.
KEGGimmu:13844.
UCSCiuc008vim.2. mouse.
uc008vin.2. mouse.

Organism-specific databases

CTDi2048.
MGIiMGI:99611. Ephb2.

Phylogenomic databases

eggNOGiKOG0196. Eukaryota.
COG0515. LUCA.
GeneTreeiENSGT00760000118975.
HOGENOMiHOG000233856.
HOVERGENiHBG062180.
InParanoidiP54763.
KOiK05111.
OMAiVNNLDKM.
OrthoDBiEOG091G00W0.
TreeFamiTF315608.

Enzyme and pathway databases

ReactomeiR-MMU-2682334. EPH-Ephrin signaling.
R-MMU-3928662. EPHB-mediated forward signaling.
R-MMU-3928664. Ephrin signaling.
R-MMU-3928665. EPH-ephrin mediated repulsion of cells.

Miscellaneous databases

ChiTaRSiEphb2. mouse.
EvolutionaryTraceiP54763.
PROiP54763.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000028664.
CleanExiMM_EPHB2.
ExpressionAtlasiP54763. baseline and differential.

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.
IPR009030. Growth_fac_rcpt_.
IPR013783. Ig-like_fold.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001660. SAM.
IPR013761. SAM/pointed.
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.
PF07699. Ephrin_rec_like. 1 hit.
PF00041. fn3. 2 hits.
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.
SM01411. Ephrin_rec_like. 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.
SSF57184. SSF57184. 2 hits.
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]
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Entry informationi

Entry nameiEPHB2_MOUSE
AccessioniPrimary (citable) accession number: P54763
Secondary accession number(s): A3KG00
, A3KG01, A3KG02, A3KG89, A3KG90, Q62213, Q6GTQ7, Q6P5F1, Q9QVY4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 14, 2015
Last modified: November 30, 2016
This is version 177 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  4. 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.