EPHB4_HUMAN - dbPTM
EPHB4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EPHB4_HUMAN
UniProt AC P54760
Protein Name Ephrin type-B receptor 4
Gene Name EPHB4
Organism Homo sapiens (Human).
Sequence Length 987
Subcellular Localization Cell membrane
Single-pass type I membrane protein .
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. Together with its cognate ligand/functional ligand EFNB2 plays a central role in heart morphogenesis and angiogenesis through regulation of cell adhesion and cell migration. EPHB4-mediated forward signaling controls cellular repulsion and segregation form EFNB2-expressing cells. Plays also a role in postnatal blood vessel remodeling, morphogenesis and permeability and is thus important in the context of tumor angiogenesis..
Protein Sequence MELRVLLCWASLAAALEETLLNTKLETADLKWVTFPQVDGQWEELSGLDEEQHSVRTYEVCDVQRAPGQAHWLRTGWVPRRGAVHVYATLRFTMLECLSLPRAGRSCKETFTVFYYESDADTATALTPAWMENPYIKVDTVAAEHLTRKRPGAEATGKVNVKTLRLGPLSKAGFYLAFQDQGACMALLSLHLFYKKCAQLTVNLTRFPETVPRELVVPVAGSCVVDAVPAPGPSPSLYCREDGQWAEQPVTGCSCAPGFEAAEGNTKCRACAQGTFKPLSGEGSCQPCPANSHSNTIGSAVCQCRVGYFRARTDPRGAPCTTPPSAPRSVVSRLNGSSLHLEWSAPLESGGREDLTYALRCRECRPGGSCAPCGGDLTFDPGPRDLVEPWVVVRGLRPDFTYTFEVTALNGVSSLATGPVPFEPVNVTTDREVPPAVSDIRVTRSSPSSLSLAWAVPRAPSGAVLDYEVKYHEKGAEGPSSVRFLKTSENRAELRGLKRGASYLVQVRARSEAGYGPFGQEHHSQTQLDESEGWREQLALIAGTAVVGVVLVLVVIVVAVLCLRKQSNGREAEYSDKHGQYLIGHGTKVYIDPFTYEDPNEAVREFAKEIDVSYVKIEEVIGAGEFGEVCRGRLKAPGKKESCVAIKTLKGGYTERQRREFLSEASIMGQFEHPNIIRLEGVVTNSMPVMILTEFMENGALDSFLRLNDGQFTVIQLVGMLRGIASGMRYLAEMSYVHRDLAARNILVNSNLVCKVSDFGLSRFLEENSSDPTYTSSLGGKIPIRWTAPEAIAFRKFTSASDAWSYGIVMWEVMSFGERPYWDMSNQDVINAIEQDYRLPPPPDCPTSLHQLMLDCWQKDRNARPRFPQVVSALDKMIRNPASLKIVARENGGASHPLLDQRQPHYSAFGSVGEWLRAIKMGRYEESFAAAGFGSFELVSQISAEDLLRIGVTLAGHQKKILASVQHMKSQAKPGTPGGTGGPAPQY
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
34PhosphorylationTADLKWVTFPQVDGQ
CCCCEEEECCCCCCC		28.6024719451
99PhosphorylationFTMLECLSLPRAGRS
EHHHHHHCCCCCCCC		48.2424719451
196AcetylationSLHLFYKKCAQLTVN
HHHHHHHHHHHCCCC		24.357662381
203N-linked_GlycosylationKCAQLTVNLTRFPET
HHHHCCCCCCCCCCC		30.38UniProtKB CARBOHYD
210PhosphorylationNLTRFPETVPRELVV
CCCCCCCCCCHHHEE		35.7328634120
321PhosphorylationDPRGAPCTTPPSAPR
CCCCCCCCCCCCCCH		41.08-
322PhosphorylationPRGAPCTTPPSAPRS
CCCCCCCCCCCCCHH		39.66-
332PhosphorylationSAPRSVVSRLNGSSL
CCCHHHHHHCCCCCE		28.97-
335N-linked_GlycosylationRSVVSRLNGSSLHLE
HHHHHHCCCCCEEEE		47.38UniProtKB CARBOHYD
337PhosphorylationVVSRLNGSSLHLEWS
HHHHCCCCCEEEEEE		28.75-
357PhosphorylationGGREDLTYALRCREC
CCCCCCEEEEECCCC		15.78-
426N-linked_GlycosylationPVPFEPVNVTTDREV
CCCCCCCCCCCCCCC		35.81UniProtKB CARBOHYD
474UbiquitinationYEVKYHEKGAEGPSS
EEEEECCCCCCCCCC		50.54-
502PhosphorylationRGLKRGASYLVQVRA
HHHHCCCEEEEEEEE		23.0924702127
503PhosphorylationGLKRGASYLVQVRAR
HHHCCCEEEEEEEEC		15.4524702127
544PhosphorylationQLALIAGTAVVGVVL
HHHHHHHHHHHHHHH		13.78-
574PhosphorylationSNGREAEYSDKHGQY
CCCCEEEEECCCCCE		29.2627273156
575PhosphorylationNGREAEYSDKHGQYL
CCCEEEEECCCCCEE		31.5222322096
577UbiquitinationREAEYSDKHGQYLIG
CEEEEECCCCCEEEC		43.63-
581PhosphorylationYSDKHGQYLIGHGTK
EECCCCCEEECCCCE		12.6021945579
587PhosphorylationQYLIGHGTKVYIDPF
CEEECCCCEEEECCC		16.2121945579
590PhosphorylationIGHGTKVYIDPFTYE
ECCCCEEEECCCCCC		10.9321945579
595PhosphorylationKVYIDPFTYEDPNEA
EEEECCCCCCCCCHH		31.2421945579
596PhosphorylationVYIDPFTYEDPNEAV
EEECCCCCCCCCHHH		20.7921945579
608UbiquitinationEAVREFAKEIDVSYV
HHHHHHHHHCCCEEE		61.60-
613PhosphorylationFAKEIDVSYVKIEEV
HHHHCCCEEEEEEEE		22.0621815630
614PhosphorylationAKEIDVSYVKIEEVI
HHHCCCEEEEEEEEE		12.9528102081
640UbiquitinationRLKAPGKKESCVAIK
CCCCCCCCCCEEEEE		61.85-
647UbiquitinationKESCVAIKTLKGGYT
CCCEEEEEEECCCCC		37.76-
650UbiquitinationCVAIKTLKGGYTERQ
EEEEEEECCCCCHHH		56.36-
713PhosphorylationRLNDGQFTVIQLVGM
ECCCCCEEEHHHHHH		14.60-
750PhosphorylationARNILVNSNLVCKVS
HHCEEECCCEEEEEC		24.86-
757PhosphorylationSNLVCKVSDFGLSRF
CCEEEEECHHCHHHH		16.83-
762PhosphorylationKVSDFGLSRFLEENS
EECHHCHHHHHHHCC		22.7422817900
769PhosphorylationSRFLEENSSDPTYTS
HHHHHHCCCCCCEEC		39.1221945579
770PhosphorylationRFLEENSSDPTYTSS
HHHHHCCCCCCEECC		60.2221945579
773PhosphorylationEENSSDPTYTSSLGG
HHCCCCCCEECCCCC		44.4121945579
774PhosphorylationENSSDPTYTSSLGGK
HCCCCCCEECCCCCC		15.2621945579
775PhosphorylationNSSDPTYTSSLGGKI
CCCCCCEECCCCCCC		17.8321945579
776PhosphorylationSSDPTYTSSLGGKIP
CCCCCEECCCCCCCC		17.1021945579
777PhosphorylationSDPTYTSSLGGKIPI
CCCCEECCCCCCCCE		24.1921945579
781UbiquitinationYTSSLGGKIPIRWTA
EECCCCCCCCEEEEC		43.44-
872PhosphorylationPRFPQVVSALDKMIR
CCHHHHHHHHHHHHC		25.0226074081
885UbiquitinationIRNPASLKIVARENG
HCCCCCCEEEEECCC		32.41-
906PhosphorylationLDQRQPHYSAFGSVG
CCCCCCCCCCCCCHH		14.3722322096
907PhosphorylationDQRQPHYSAFGSVGE
CCCCCCCCCCCCHHH		17.6828152594
911PhosphorylationPHYSAFGSVGEWLRA
CCCCCCCCHHHHHHH		22.0921082442
924PhosphorylationRAIKMGRYEESFAAA
HHHHCCCCCHHHHCC		20.51-
935PhosphorylationFAAAGFGSFELVSQI
HHCCCCCCEEEEEEC		17.1821609022
943PhosphorylationFELVSQISAEDLLRI
EEEEEECCHHHHHHH		20.2624275569
953PhosphorylationDLLRIGVTLAGHQKK
HHHHHCEEEHHHHHH		12.9917192257
960UbiquitinationTLAGHQKKILASVQH
EEHHHHHHHHHHHHH		36.06-
964PhosphorylationHQKKILASVQHMKSQ
HHHHHHHHHHHHHHC		20.9020071362
970PhosphorylationASVQHMKSQAKPGTP
HHHHHHHHCCCCCCC		28.0021945579
973UbiquitinationQHMKSQAKPGTPGGT
HHHHHCCCCCCCCCC		36.022190698
976PhosphorylationKSQAKPGTPGGTGGP
HHCCCCCCCCCCCCC		27.5621945579
980PhosphorylationKPGTPGGTGGPAPQY
CCCCCCCCCCCCCCC		44.9021945579
987PhosphorylationTGGPAPQY-------
CCCCCCCC-------		100.0021945579
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 EPHB4_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EPHB4_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 EPHB4_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
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 EPHB4_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-574; TYR-614; SER-769;SER-770; TYR-774; THR-775; SER-776; TYR-906; SER-907; SER-911; THR-976AND TYR-987, AND MASS SPECTROMETRY.
"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-769; TYR-774; SER-911;THR-953 AND THR-976, AND MASS SPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-976, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-976, 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-574; TYR-774 ANDTYR-987, AND MASS 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-590 AND TYR-774, ANDMASS SPECTROMETRY.

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