EPHB3_HUMAN - dbPTM
EPHB3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EPHB3_HUMAN
UniProt AC P54753
Protein Name Ephrin type-B receptor 3
Gene Name EPHB3
Organism Homo sapiens (Human).
Sequence Length 998
Subcellular Localization Cell membrane
Single-pass type I membrane protein . Cell projection, dendrite.
Protein Description 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..
Protein Sequence MARARPPPPPSPPPGLLPLLPPLLLLPLLLLPAGCRALEETLMDTKWVTSELAWTSHPESGWEEVSGYDEAMNPIRTYQVCNVRESSQNNWLRTGFIWRRDVQRVYVELKFTVRDCNSIPNIPGSCKETFNLFYYEADSDVASASSPFWMENPYVKVDTIAPDESFSRLDAGRVNTKVRSFGPLSKAGFYLAFQDQGACMSLISVRAFYKKCASTTAGFALFPETLTGAEPTSLVIAPGTCIPNAVEVSVPLKLYCNGDGEWMVPVGACTCATGHEPAAKESQCRPCPPGSYKAKQGEGPCLPCPPNSRTTSPAASICTCHNNFYRADSDSADSACTTVPSPPRGVISNVNETSLILEWSEPRDLGGRDDLLYNVICKKCHGAGGASACSRCDDNVEFVPRQLGLTERRVHISHLLAHTRYTFEVQAVNGVSGKSPLPPRYAAVNITTNQAAPSEVPTLRLHSSSGSSLTLSWAPPERPNGVILDYEMKYFEKSEGIASTVTSQMNSVQLDGLRPDARYVVQVRARTVAGYGQYSRPAEFETTSERGSGAQQLQEQLPLIVGSATAGLVFVVAVVVIAIVCLRKQRHGSDSEYTEKLQQYIAPGMKVYIDPFTYEDPNEAVREFAKEIDVSCVKIEEVIGAGEFGEVCRGRLKQPGRREVFVAIKTLKVGYTERQRRDFLSEASIMGQFDHPNIIRLEGVVTKSRPVMILTEFMENCALDSFLRLNDGQFTVIQLVGMLRGIAAGMKYLSEMNYVHRDLAARNILVNSNLVCKVSDFGLSRFLEDDPSDPTYTSSLGGKIPIRWTAPEAIAYRKFTSASDVWSYGIVMWEVMSYGERPYWDMSNQDVINAVEQDYRLPPPMDCPTALHQLMLDCWVRDRNLRPKFSQIVNTLDKLIRNAASLKVIASAQSGMSQPLLDRTVPDYTTFTTVGDWLDAIKMGRYKESFVSAGFASFDLVAQMTAEDLLRIGVTLAGHQKKILSSIQDMRLQMNQTLPVQV
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
167PhosphorylationIAPDESFSRLDAGRV
ECCCCCCCCCCCCCC		41.01-
190PhosphorylationPLSKAGFYLAFQDQG
CHHHHCEEEEEECCC		9.0126074081
201PhosphorylationQDQGACMSLISVRAF
ECCCCHHHHHHHHHH		23.5726074081
204PhosphorylationGACMSLISVRAFYKK
CCHHHHHHHHHHHHH		15.7326074081
209PhosphorylationLISVRAFYKKCASTT
HHHHHHHHHHHHCCC		14.4626074081
249PhosphorylationIPNAVEVSVPLKLYC
CCCCEEEEEEEEEEE		12.43-
341PhosphorylationSACTTVPSPPRGVIS
CCCCCCCCCCCCCCC		43.1117081983
351N-linked_GlycosylationRGVISNVNETSLILE
CCCCCCCCCCEEEEE		51.59UniProtKB CARBOHYD
390O-linked_GlycosylationAGGASACSRCDDNVE
CCCCHHCCCCCCCCE		35.3429351928
413PhosphorylationTERRVHISHLLAHTR
CCCEEEHHHHHHHCC		8.00-
441PhosphorylationKSPLPPRYAAVNITT
CCCCCCCEEEEEEEC		12.5125278378
445N-linked_GlycosylationPPRYAAVNITTNQAA
CCCEEEEEEECCCCC		22.59UniProtKB CARBOHYD
447PhosphorylationRYAAVNITTNQAAPS
CEEEEEEECCCCCCC		17.9425278378
448PhosphorylationYAAVNITTNQAAPSE
EEEEEEECCCCCCCC		22.8724043423
454PhosphorylationTTNQAAPSEVPTLRL
ECCCCCCCCCCEEEE		46.6425278378
458PhosphorylationAAPSEVPTLRLHSSS
CCCCCCCEEEEECCC		29.6825278378
589PhosphorylationLRKQRHGSDSEYTEK
HHHHHCCCCHHHHHH		31.6626356563
591PhosphorylationKQRHGSDSEYTEKLQ
HHHCCCCHHHHHHHH		33.9126356563
593PhosphorylationRHGSDSEYTEKLQQY
HCCCCHHHHHHHHHH		24.9325884760
594PhosphorylationHGSDSEYTEKLQQYI
CCCCHHHHHHHHHHH		23.6926356563
600PhosphorylationYTEKLQQYIAPGMKV
HHHHHHHHHCCCCEE		6.0121945579
608PhosphorylationIAPGMKVYIDPFTYE
HCCCCEEEECCCCCC		8.2921945579
613PhosphorylationKVYIDPFTYEDPNEA
EEEECCCCCCCHHHH		31.2421945579
614PhosphorylationVYIDPFTYEDPNEAV
EEECCCCCCCHHHHH		20.7921945579
666PhosphorylationEVFVAIKTLKVGYTE
HEEEEEEEECCCCCH		26.2123312004
731PhosphorylationRLNDGQFTVIQLVGM
ECCCCCEEHHHHHHH		14.60-
748PhosphorylationGIAAGMKYLSEMNYV
HHHHHHHHHHHCCCC		13.4323312004
750PhosphorylationAAGMKYLSEMNYVHR
HHHHHHHHHCCCCCH		31.5423312004
754PhosphorylationKYLSEMNYVHRDLAA
HHHHHCCCCCHHHHH		9.0522817900
768PhosphorylationARNILVNSNLVCKVS
HHCCEECCCEEEEEC		24.86-
773UbiquitinationVNSNLVCKVSDFGLS
ECCCEEEEECHHCHH		36.9821987572
775PhosphorylationSNLVCKVSDFGLSRF
CCEEEEECHHCHHHH		16.83-
780PhosphorylationKVSDFGLSRFLEDDP
EECHHCHHHHCCCCC		22.7419369195
788PhosphorylationRFLEDDPSDPTYTSS
HHCCCCCCCCCEECC		64.3221945579
791PhosphorylationEDDPSDPTYTSSLGG
CCCCCCCCEECCCCC		44.4121945579
792PhosphorylationDDPSDPTYTSSLGGK
CCCCCCCEECCCCCC		15.2621945579
793PhosphorylationDPSDPTYTSSLGGKI
CCCCCCEECCCCCCC		17.8321945579
794PhosphorylationPSDPTYTSSLGGKIP
CCCCCEECCCCCCCC		17.1021945579
795PhosphorylationSDPTYTSSLGGKIPI
CCCCEECCCCCCCCE		24.1921945579
799UbiquitinationYTSSLGGKIPIRWTA
EECCCCCCCCEEEEC		43.4429901268
812PhosphorylationTAPEAIAYRKFTSAS
ECCHHHHCCCCCCHH		14.28-
891PhosphorylationKFSQIVNTLDKLIRN
HHHHHHHHHHHHHHH		25.9923312004
901PhosphorylationKLIRNAASLKVIASA
HHHHHHHHHHHHHHC		26.72-
920PhosphorylationSQPLLDRTVPDYTTF
CCCCCCCCCCCCCCE		35.7425106551
924PhosphorylationLDRTVPDYTTFTTVG
CCCCCCCCCCEEEHH		11.1226356563
925PhosphorylationDRTVPDYTTFTTVGD
CCCCCCCCCEEEHHH		23.8626356563
926PhosphorylationRTVPDYTTFTTVGDW
CCCCCCCCEEEHHHH		16.8621082442
953PhosphorylationFVSAGFASFDLVAQM
HHHCCCCCHHHHHCC		19.6119369195
971PhosphorylationDLLRIGVTLAGHQKK
HHHHHCCEEHHHHHH		12.9917192257
993PhosphorylationMRLQMNQTLPVQV--
HHHHHCCCCCCCC--		28.2027470641
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
614YPhosphorylationKinaseEPHB3P54753
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EPHB3_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of EPHB3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
EFNB3_HUMANEFNB3physical
9484836
RASA1_HUMANRASA1physical
9674711
GLGB_HUMANGBE1physical
21988832
NFRKB_HUMANNFRKBphysical
21988832
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of EPHB3_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-608; TYR-614; TYR-792AND THR-971, AND MASS SPECTROMETRY.
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells.";
Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.;
J. Proteome Res. 8:3852-3861(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-792, AND MASSSPECTROMETRY.
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-600, AND MASSSPECTROMETRY.

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