EPHB2_HUMAN - dbPTM
EPHB2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EPHB2_HUMAN
UniProt AC P29323
Protein Name Ephrin type-B receptor 2
Gene Name EPHB2
Organism Homo sapiens (Human).
Sequence Length 1055
Subcellular Localization Cell membrane
Single-pass type I membrane protein. Cell projection, axon. 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. 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..
Protein Sequence MALRRLGAALLLLPLLAAVEETLMDSTTATAELGWMVHPPSGWEEVSGYDENMNTIRTYQVCNVFESSQNNWLRTKFIRRRGAHRIHVEMKFSVRDCSSIPSVPGSCKETFNLYYYEADFDSATKTFPNWMENPWVKVDTIAADESFSQVDLGGRVMKINTEVRSFGPVSRSGFYLAFQDYGGCMSLIAVRVFYRKCPRIIQNGAIFQETLSGAESTSLVAARGSCIANAEEVDVPIKLYCNGDGEWLVPIGRCMCKAGFEAVENGTVCRGCPSGTFKANQGDEACTHCPINSRTTSEGATNCVCRNGYYRADLDPLDMPCTTIPSAPQAVISSVNETSLMLEWTPPRDSGGREDLVYNIICKSCGSGRGACTRCGDNVQYAPRQLGLTEPRIYISDLLAHTQYTFEIQAVNGVTDQSPFSPQFASVNITTNQAAPSAVSIMHQVSRTVDSITLSWSQPDQPNGVILDYELQYYEKELSEYNATAIKSPTNTVTVQGLKAGAIYVFQVRARTVAGYGRYSGKMYFQTMTEAEYQTSIQEKLPLIIGSSAAGLVFLIAVVVIAIVCNRRGFERADSEYTDKLQHYTSGHMTPGMKIYIDPFTYEDPNEAVREFAKEIDISCVKIEQVIGAGEFGEVCSGHLKLPGKREIFVAIKTLKSGYTEKQRRDFLSEASIMGQFDHPNVIHLEGVVTKSTPVMIITEFMENGSLDSFLRQNDGQFTVIQLVGMLRGIAAGMKYLADMNYVHRDLAARNILVNSNLVCKVSDFGLSRFLEDDTSDPTYTSALGGKIPIRWTAPEAIQYRKFTSASDVWSYGIVMWEVMSYGERPYWDMTNQDVINAIEQDYRLPPPMDCPSALHQLMLDCWQKDRNHRPKFGQIVNTLDKMIRNPNSLKAMAPLSSGINLPLLDRTIPDYTSFNTVDEWLEAIKMGQYKESFANAGFTSFDVVSQMMMEDILRVGVTLAGHQKKILNSIQVMRAQMNQIQSVEGQPLARRPRATGRTKRCQPRDVTKKTCNSNDGKKKGMGKKKTDPGRGREIQGIFFKEDSHKESNDCSCGG
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
99PhosphorylationFSVRDCSSIPSVPGS
EEECCCCCCCCCCCC		44.8723879269
102PhosphorylationRDCSSIPSVPGSCKE
CCCCCCCCCCCCCCC		38.9923879269
106PhosphorylationSIPSVPGSCKETFNL
CCCCCCCCCCCEEEE		18.8823879269
148PhosphorylationIAADESFSQVDLGGR
EECCCCCCCEECCCC		38.2819060867
175PhosphorylationPVSRSGFYLAFQDYG
CCCCCCEEEEEEECC		10.7218083107
181PhosphorylationFYLAFQDYGGCMSLI
EEEEEEECCCCHHHH		12.4818083107
194PhosphorylationLIAVRVFYRKCPRII
HHHHHHHHHHCCHHH		13.3018083107
212PhosphorylationAIFQETLSGAESTSL
CEEEHHCCCCCCCCC		43.2925332170
265N-linked_GlycosylationAGFEAVENGTVCRGC
CCCEEECCCCEECCC		44.85UniProtKB CARBOHYD
276PhosphorylationCRGCPSGTFKANQGD
ECCCCCCCEECCCCC		26.7124719451
336N-linked_GlycosylationQAVISSVNETSLMLE
HHHHCCCCCCCEEEE		49.10UniProtKB CARBOHYD
389PhosphorylationAPRQLGLTEPRIYIS
CCHHCCCCCCEEEHH		41.9923532336
428N-linked_GlycosylationSPQFASVNITTNQAA
CCCEEEEEEECCCCC		24.32UniProtKB CARBOHYD
481PhosphorylationYEKELSEYNATAIKS
HHHHHHHHCCCCCCC		13.51-
482N-linked_GlycosylationEKELSEYNATAIKSP
HHHHHHHCCCCCCCC		27.11UniProtKB CARBOHYD
494O-linked_GlycosylationKSPTNTVTVQGLKAG
CCCCCEEEEECCCCC		12.6930379171
504PhosphorylationGLKAGAIYVFQVRAR
CCCCCEEEEEEEEEE		8.48-
524PhosphorylationGRYSGKMYFQTMTEA
CCCCCEEEEEECCHH		8.95-
575PhosphorylationRGFERADSEYTDKLQ
CCCCCCCHHHHHHCH		31.3622322096
577PhosphorylationFERADSEYTDKLQHY
CCCCCHHHHHHCHHH		24.9625884760
578PhosphorylationERADSEYTDKLQHYT
CCCCHHHHHHCHHHC		23.7028796482
580UbiquitinationADSEYTDKLQHYTSG
CCHHHHHHCHHHCCC		42.10-
584PhosphorylationYTDKLQHYTSGHMTP
HHHHCHHHCCCCCCC		6.9420007894
585PhosphorylationTDKLQHYTSGHMTPG
HHHCHHHCCCCCCCC		26.5522322096
586PhosphorylationDKLQHYTSGHMTPGM
HHCHHHCCCCCCCCC		21.3822322096
590PhosphorylationHYTSGHMTPGMKIYI
HHCCCCCCCCCEEEE		15.8322322096
595PhosphorylationHMTPGMKIYIDPFTY
CCCCCCEEEECCCCC		2.4317016520
596PhosphorylationMTPGMKIYIDPFTYE
CCCCCEEEECCCCCC		8.1821945579
601PhosphorylationKIYIDPFTYEDPNEA
EEEECCCCCCCHHHH		31.2421945579
602PhosphorylationIYIDPFTYEDPNEAV
EEECCCCCCCHHHHH		20.7921945579
645UbiquitinationGHLKLPGKREIFVAI
CCCCCCCCCEEEEEE		44.94-
659PhosphorylationIKTLKSGYTEKQRRD
EEEHHCCCCHHHHHH		20.8610572014
699PhosphorylationSTPVMIITEFMENGS
CCCEEEEEEEHHCCC		16.5522210691
706PhosphorylationTEFMENGSLDSFLRQ
EEEHHCCCHHHHHHC		40.3522210691
709PhosphorylationMENGSLDSFLRQNDG
HHCCCHHHHHHCCCC		31.3222210691
736PhosphorylationGIAAGMKYLADMNYV
HHHHHCHHHHHCCCH		9.7610572014
742PhosphorylationKYLADMNYVHRDLAA
HHHHHCCCHHHHHHH		7.3220071362
756PhosphorylationARNILVNSNLVCKVS
HHCEEECCCEEEEEC		24.86-
763PhosphorylationSNLVCKVSDFGLSRF
CCEEEEECHHCHHHH		16.83-
768PhosphorylationKVSDFGLSRFLEDDT
EECHHCHHHHCCCCC		22.7422817900
775PhosphorylationSRFLEDDTSDPTYTS
HHHCCCCCCCCCCCC		47.5621945579
776PhosphorylationRFLEDDTSDPTYTSA
HHCCCCCCCCCCCCC		48.8922322096
779PhosphorylationEDDTSDPTYTSALGG
CCCCCCCCCCCCCCC		44.4121945579
780PhosphorylationDDTSDPTYTSALGGK
CCCCCCCCCCCCCCC		12.2321945579
781PhosphorylationDTSDPTYTSALGGKI
CCCCCCCCCCCCCCC		15.2521945579
782PhosphorylationTSDPTYTSALGGKIP
CCCCCCCCCCCCCCC		15.8721945579
800PhosphorylationTAPEAIQYRKFTSAS
ECCHHHHCCCCCCHH		15.0610572014
879PhosphorylationKFGQIVNTLDKMIRN
CHHHHHHHHHHHHCC		25.9919369195
897PhosphorylationLKAMAPLSSGINLPL
HHHHEECCCCCCCCC		26.0119060867
898PhosphorylationKAMAPLSSGINLPLL
HHHEECCCCCCCCCC		51.9124173317
908PhosphorylationNLPLLDRTIPDYTSF
CCCCCCCCCCCCCCC		36.2125106551
912PhosphorylationLDRTIPDYTSFNTVD
CCCCCCCCCCCCCHH		10.0325106551
930PhosphorylationEAIKMGQYKESFANA
HHHHHCCCHHHHHCC		15.828798570
959PhosphorylationDILRVGVTLAGHQKK
HHHHHCCCHHHHHHH		12.6420071362
970PhosphorylationHQKKILNSIQVMRAQ
HHHHHHHHHHHHHHH		15.7928509920
983 (in isoform 2)Phosphorylation-24.6219369195
983PhosphorylationAQMNQIQSVEGQPLA
HHHHHHHCCCCCCCC		24.6219369195
984 (in isoform 3)Phosphorylation-5.7019369195
1020AcetylationNSNDGKKKGMGKKKT
CCCCCCCCCCCCCCC		58.5819822051
1024AcetylationGKKKGMGKKKTDPGR
CCCCCCCCCCCCCCC		42.0519822057
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

Oops, there are no upstream regulatory protein records of EPHB2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EPHB2_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 EPHB2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
STK26_HUMANSTK26genetic
11641781
PPAC_HUMANACP1physical
9499402
RASA1_HUMANRASA1physical
9233798
SRC_HUMANSRCphysical
10644995
EPHB2_HUMANEPHB2physical
9933164
EFNB2_HUMANEFNB2physical
11780069
SRC_HUMANSRCphysical
9632142
YES_HUMANYES1physical
9632142
PLCG1_HUMANPLCG1physical
9632142
ABL1_HUMANABL1physical
11494128
ABL2_HUMANABL2physical
11494128
EPHB2_HUMANEPHB2physical
18797457
KDM4A_HUMANKDM4Aphysical
26344197
MTMRE_HUMANMTMR14physical
28065597
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
176807Prostate cancer (PC)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of EPHB2_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 SER-148; TYR-596; TYR-602;THR-775; SER-776; THR-779; TYR-780; SER-897 AND SER-983, AND MASSSPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-776 AND TYR-780, ANDMASS SPECTROMETRY.
"Proteomics analysis of protein kinases by target class-selectiveprefractionation and tandem mass spectrometry.";
Wissing J., Jaensch L., Nimtz M., Dieterich G., Hornberger R.,Keri G., Wehland J., Daub H.;
Mol. Cell. Proteomics 6:537-547(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-775, AND MASSSPECTROMETRY.
"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-602 AND TYR-780, ANDMASS SPECTROMETRY.
"Multiple reaction monitoring for robust quantitative proteomicanalysis of cellular signaling networks.";
Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M.;
Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-596, AND MASSSPECTROMETRY.
"Time-resolved mass spectrometry of tyrosine phosphorylation sites inthe epidermal growth factor receptor signaling network reveals dynamicmodules.";
Zhang Y., Wolf-Yadlin A., Ross P.L., Pappin D.J., Rush J.,Lauffenburger D.A., White F.M.;
Mol. Cell. Proteomics 4:1240-1250(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-596 AND TYR-602, ANDMASS SPECTROMETRY.

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