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P54753

- EPHB3_HUMAN

UniProt

P54753 - EPHB3_HUMAN

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Protein

Ephrin type-B receptor 3

Gene

EPHB3

Organism
Homo sapiens (Human)
Status
Reviewed - 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.1 Publication

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei665 – 6651ATPPROSITE-ProRule annotation
Active sitei758 – 7581Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi639 – 6479ATPPROSITE-ProRule annotation

GO - Molecular functioni

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

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: Ensembl
  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 Cdc42 GTPase activity Source: UniProtKB
  16. regulation of cell-cell adhesion Source: UniProtKB
  17. regulation of Rac GTPase activity Source: UniProtKB
  18. retinal ganglion cell axon guidance Source: Ensembl
  19. substrate adhesion-dependent cell spreading Source: UniProtKB
  20. thymus development Source: UniProtKB
  21. 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. 2681.
SignaLinkiP54753.

Names & Taxonomyi

Protein namesi
Recommended name:
Ephrin type-B receptor 3 (EC:2.7.10.1)
Alternative name(s):
EPH-like tyrosine kinase 2
Short name:
EPH-like kinase 2
Embryonic kinase 2
Short name:
EK2
Short name:
hEK2
Tyrosine-protein kinase TYRO6
Gene namesi
Name:EPHB3
Synonyms:ETK2, HEK2, TYRO6
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:3394. EPHB3.

Subcellular locationi

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

GO - Cellular componenti

  1. cell projection Source: UniProtKB-KW
  2. integral component of plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi614 – 6141Y → F: Partial loss of phosphorylation and loss of interaction with SH2-containing proteins. 1 Publication
Mutagenesisi665 – 6651K → R: Kinase-dead. Loss of autophosphorylation. 1 Publication

Organism-specific databases

PharmGKBiPA27826.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3333Sequence AnalysisAdd
BLAST
Chaini34 – 998965Ephrin type-B receptor 3PRO_0000016831Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi81 ↔ 1991 Publication
Glycosylationi351 – 3511N-linked (GlcNAc...)Sequence Analysis
Glycosylationi445 – 4451N-linked (GlcNAc...)Sequence Analysis
Modified residuei614 – 6141Phosphotyrosine; by autocatalysis1 Publication

Post-translational modificationi

Phosphorylated. Autophosphorylates upon ligand-binding. Autophosphorylation on Tyr-614 is required for interaction with SH2 domain-containing proteins.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiP54753.
PaxDbiP54753.
PRIDEiP54753.

PTM databases

PhosphoSiteiP54753.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

BgeeiP54753.
CleanExiHS_EPHB3.
ExpressionAtlasiP54753. baseline and differential.
GenevestigatoriP54753.

Organism-specific databases

HPAiHPA007698.
HPA008184.

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

BioGridi108363. 11 interactions.
IntActiP54753. 4 interactions.
MINTiMINT-1538099.
STRINGi9606.ENSP00000332118.

Structurei

Secondary structure

1
998
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi39 – 446Combined sources
Helixi45 – 473Combined sources
Beta strandi55 – 584Combined sources
Beta strandi63 – 686Combined sources
Beta strandi74 – 807Combined sources
Beta strandi85 – 873Combined sources
Beta strandi90 – 934Combined sources
Beta strandi103 – 11412Combined sources
Helixi116 – 1183Combined sources
Beta strandi130 – 13910Combined sources
Beta strandi155 – 1606Combined sources
Beta strandi175 – 1817Combined sources
Beta strandi186 – 19813Combined sources
Beta strandi200 – 21011Combined sources
Beta strandi633 – 6353Combined sources
Beta strandi648 – 6525Combined sources
Beta strandi660 – 6656Combined sources
Helixi673 – 68614Combined sources
Beta strandi697 – 7015Combined sources
Beta strandi703 – 7064Combined sources
Beta strandi708 – 7125Combined sources
Helixi719 – 7257Combined sources
Turni726 – 7283Combined sources
Helixi732 – 75120Combined sources
Helixi761 – 7633Combined sources
Beta strandi764 – 7663Combined sources
Beta strandi772 – 7743Combined sources
Helixi802 – 8043Combined sources
Helixi807 – 8126Combined sources
Helixi817 – 83216Combined sources
Turni838 – 8414Combined sources
Helixi844 – 8529Combined sources
Helixi865 – 87410Combined sources
Helixi879 – 8813Combined sources
Helixi885 – 89713Combined sources
Helixi899 – 9035Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3P1IX-ray2.10A/B/C39-211[»]
3ZFYX-ray2.20A/B616-910[»]
ProteinModelPortaliP54753.
SMRiP54753. Positions 37-905, 922-992.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP54753.

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini34 – 559526ExtracellularSequence AnalysisAdd
BLAST
Topological domaini581 – 998418CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei560 – 58021HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini39 – 217179Eph LBDPROSITE-ProRule annotationAdd
BLAST
Domaini339 – 451113Fibronectin type-III 1PROSITE-ProRule annotationAdd
BLAST
Domaini452 – 54594Fibronectin type-III 2PROSITE-ProRule annotationAdd
BLAST
Domaini633 – 896264Protein kinasePROSITE-ProRule annotationAdd
BLAST
Domaini925 – 98965SAMPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi996 – 9983PDZ-bindingSequence Analysis

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi199 – 336138Cys-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.
InParanoidiP54753.
KOiK05112.
OMAiNLRPKFA.
OrthoDBiEOG7VTDM6.
PhylomeDBiP54753.
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. Fibronectin_type3.
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.

P54753-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MARARPPPPP SPPPGLLPLL PPLLLLPLLL LPAGCRALEE TLMDTKWVTS
60 70 80 90 100
ELAWTSHPES GWEEVSGYDE AMNPIRTYQV CNVRESSQNN WLRTGFIWRR
110 120 130 140 150
DVQRVYVELK FTVRDCNSIP NIPGSCKETF NLFYYEADSD VASASSPFWM
160 170 180 190 200
ENPYVKVDTI APDESFSRLD AGRVNTKVRS FGPLSKAGFY LAFQDQGACM
210 220 230 240 250
SLISVRAFYK KCASTTAGFA LFPETLTGAE PTSLVIAPGT CIPNAVEVSV
260 270 280 290 300
PLKLYCNGDG EWMVPVGACT CATGHEPAAK ESQCRPCPPG SYKAKQGEGP
310 320 330 340 350
CLPCPPNSRT TSPAASICTC HNNFYRADSD SADSACTTVP SPPRGVISNV
360 370 380 390 400
NETSLILEWS EPRDLGGRDD LLYNVICKKC HGAGGASACS RCDDNVEFVP
410 420 430 440 450
RQLGLTERRV HISHLLAHTR YTFEVQAVNG VSGKSPLPPR YAAVNITTNQ
460 470 480 490 500
AAPSEVPTLR LHSSSGSSLT LSWAPPERPN GVILDYEMKY FEKSEGIAST
510 520 530 540 550
VTSQMNSVQL DGLRPDARYV VQVRARTVAG YGQYSRPAEF ETTSERGSGA
560 570 580 590 600
QQLQEQLPLI VGSATAGLVF VVAVVVIAIV CLRKQRHGSD SEYTEKLQQY
610 620 630 640 650
IAPGMKVYID PFTYEDPNEA VREFAKEIDV SCVKIEEVIG AGEFGEVCRG
660 670 680 690 700
RLKQPGRREV FVAIKTLKVG YTERQRRDFL SEASIMGQFD HPNIIRLEGV
710 720 730 740 750
VTKSRPVMIL TEFMENCALD SFLRLNDGQF TVIQLVGMLR GIAAGMKYLS
760 770 780 790 800
EMNYVHRDLA ARNILVNSNL VCKVSDFGLS RFLEDDPSDP TYTSSLGGKI
810 820 830 840 850
PIRWTAPEAI AYRKFTSASD VWSYGIVMWE VMSYGERPYW DMSNQDVINA
860 870 880 890 900
VEQDYRLPPP MDCPTALHQL MLDCWVRDRN LRPKFSQIVN TLDKLIRNAA
910 920 930 940 950
SLKVIASAQS GMSQPLLDRT VPDYTTFTTV GDWLDAIKMG RYKESFVSAG
960 970 980 990
FASFDLVAQM TAEDLLRIGV TLAGHQKKIL SSIQDMRLQM NQTLPVQV
Length:998
Mass (Da):110,330
Last modified:September 27, 2005 - v2
Checksum:i9B65A4EF58B27407
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti367 – 3671G → V in CAA53021. (PubMed:8397371)Curated
Sequence conflicti406 – 4083TER → SEP in CAA53021. (PubMed:8397371)Curated
Sequence conflicti412 – 4121I → T in CAA53021. (PubMed:8397371)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti168 – 1681R → L in a lung small cell carcinoma sample; somatic mutation. 1 Publication
VAR_042176
Natural varianti440 – 4401R → C.1 Publication
Corresponds to variant rs56029711 [ dbSNP | Ensembl ].
VAR_042177
Natural varianti579 – 5791I → V.1 Publication
Corresponds to variant rs56103851 [ dbSNP | Ensembl ].
VAR_042178
Natural varianti601 – 6011I → L.1 Publication
Corresponds to variant rs56129875 [ dbSNP | Ensembl ].
VAR_042179
Natural varianti724 – 7241R → W in a lung neuroendocrine carcinoma sample; somatic mutation. 1 Publication
VAR_042180

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X75208 mRNA. Translation: CAA53021.1.
BC052968 mRNA. Translation: AAH52968.1.
CCDSiCCDS3268.1.
PIRiS37627.
RefSeqiNP_004434.2. NM_004443.3.
UniGeneiHs.2913.

Genome annotation databases

EnsembliENST00000330394; ENSP00000332118; ENSG00000182580.
GeneIDi2049.
KEGGihsa:2049.
UCSCiuc003foz.3. human.

Polymorphism databases

DMDMi76803655.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X75208 mRNA. Translation: CAA53021.1 .
BC052968 mRNA. Translation: AAH52968.1 .
CCDSi CCDS3268.1.
PIRi S37627.
RefSeqi NP_004434.2. NM_004443.3.
UniGenei Hs.2913.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3P1I X-ray 2.10 A/B/C 39-211 [» ]
3ZFY X-ray 2.20 A/B 616-910 [» ]
ProteinModelPortali P54753.
SMRi P54753. Positions 37-905, 922-992.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108363. 11 interactions.
IntActi P54753. 4 interactions.
MINTi MINT-1538099.
STRINGi 9606.ENSP00000332118.

Chemistry

BindingDBi P54753.
ChEMBLi CHEMBL2363043.
GuidetoPHARMACOLOGYi 1832.

PTM databases

PhosphoSitei P54753.

Polymorphism databases

DMDMi 76803655.

Proteomic databases

MaxQBi P54753.
PaxDbi P54753.
PRIDEi P54753.

Protocols and materials databases

DNASUi 2049.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000330394 ; ENSP00000332118 ; ENSG00000182580 .
GeneIDi 2049.
KEGGi hsa:2049.
UCSCi uc003foz.3. human.

Organism-specific databases

CTDi 2049.
GeneCardsi GC03P184279.
HGNCi HGNC:3394. EPHB3.
HPAi HPA007698.
HPA008184.
MIMi 601839. gene.
neXtProti NX_P54753.
PharmGKBi PA27826.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00760000118975.
HOGENOMi HOG000233856.
HOVERGENi HBG062180.
InParanoidi P54753.
KOi K05112.
OMAi NLRPKFA.
OrthoDBi EOG7VTDM6.
PhylomeDBi P54753.
TreeFami TF315608.

Enzyme and pathway databases

BRENDAi 2.7.10.1. 2681.
SignaLinki P54753.

Miscellaneous databases

EvolutionaryTracei P54753.
GeneWikii EPHB3.
GenomeRNAii 2049.
NextBioi 8331.
PROi P54753.
SOURCEi Search...

Gene expression databases

Bgeei P54753.
CleanExi HS_EPHB3.
ExpressionAtlasi P54753. baseline and differential.
Genevestigatori P54753.

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.
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 ]
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.
PF00536. SAM_1. 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.
SM00219. TyrKc. 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.
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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "PCR mediated detection of a new human receptor-tyrosine-kinase, HEK 2."
    Boehme B., Holtrich U., Wolf G., Luzius H., Grzeschik K.-H., Strebhardt K., Ruebsamen-Waigmann H.
    Oncogene 8:2857-2862(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION OF EFNB1 AND EFNB2 AS LIGANDS, AUTOPHOSPHORYLATION.
    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].
    Tissue: Uterus.
  3. "Unified nomenclature for Eph family receptors and their ligands, the ephrins."
    Eph nomenclature committee
    Cell 90:403-404(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NOMENCLATURE.
  4. "Tyrosine-614, the major autophosphorylation site of the receptor tyrosine kinase HEK2, functions as multi-docking site for SH2-domain mediated interactions."
    Hock B., Boehme B., Karn T., Feller S., Ruebsamen-Waigmann H., Strebhardt K.
    Oncogene 17:255-260(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT TYR-614, MUTAGENESIS OF TYR-614 AND LYS-665.
  5. "Inhibition of integrin-mediated cell adhesion but not directional cell migration requires catalytic activity of EphB3 receptor tyrosine kinase. Role of Rho family small GTPases."
    Miao H., Strebhardt K., Pasquale E.B., Shen T.L., Guan J.L., Wang B.
    J. Biol. Chem. 280:923-932(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: AUTOPHOSPHORYLATION, FUNCTION IN CELL ADHESION, FUNCTION IN CELL MIGRATION, SUBCELLULAR LOCATION.
  6. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "Ligand binding domain of human EPHB3."
    Structural genomics consortium (SGC)
    Submitted (JAN-2011) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 39-211, DISULFIDE BOND.
  8. "Patterns of somatic mutation in human cancer genomes."
    Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
    , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
    Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS [LARGE SCALE ANALYSIS] LEU-168; CYS-440; VAL-579; LEU-601 AND TRP-724.

Entry informationi

Entry nameiEPHB3_HUMAN
AccessioniPrimary (citable) accession number: P54753
Secondary accession number(s): Q7Z740
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: September 27, 2005
Last modified: October 29, 2014
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
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3