EFNB2_HUMAN - dbPTM
EFNB2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EFNB2_HUMAN
UniProt AC P52799
Protein Name Ephrin-B2
Gene Name EFNB2
Organism Homo sapiens (Human).
Sequence Length 333
Subcellular Localization Membrane
Single-pass type I membrane protein.
Protein Description Cell surface transmembrane ligand for Eph receptors, a family of receptor tyrosine kinases which are crucial for migration, repulsion and adhesion during neuronal, vascular and epithelial development. Binds promiscuously Eph receptors 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. Binds to receptor tyrosine kinase including EPHA4, EPHA3 and EPHB4. Together with EPHB4 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 from EFNB2-expressing cells. May play a role in constraining the orientation of longitudinally projecting axons.; (Microbial infection) Acts as a receptor for Hendra virus and Nipah virus..
Protein Sequence MAVRRDSVWKYCWGVLMVLCRTAISKSIVLEPIYWNSSNSKFLPGQGLVLYPQIGDKLDIICPKVDSKTVGQYEYYKVYMVDKDQADRCTIKKENTPLLNCAKPDQDIKFTIKFQEFSPNLWGLEFQKNKDYYIISTSNGSLEGLDNQEGGVCQTRAMKILMKVGQDASSAGSTRNKDPTRRPELEAGTNGRSSTTSPFVKPNPGSSTDGNSAGHSGNNILGSEVALFAGIASGCIIFIVIIITLVVLLLKYRRRHRKHSPQHTTTLSLSTLATPKRSGNNNGSEPSDIIIPLRTADSVFCPHYEKVSGDYGHPVYIVQEMPPQSPANIYYKV
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
11PhosphorylationRRDSVWKYCWGVLMV
CHHHHHHHHHHHHHH		4.26-
36N-linked_GlycosylationVLEPIYWNSSNSKFL
CEEEEEECCCCCCCC		20.7018488039
69PhosphorylationCPKVDSKTVGQYEYY
ECCCCCCCEEEEEEE		33.54-
79PhosphorylationQYEYYKVYMVDKDQA
EEEEEEEEEECHHHC		6.3023532336
90PhosphorylationKDQADRCTIKKENTP
HHHCCCCEECCCCCC		36.4023532336
139N-linked_GlycosylationYYIISTSNGSLEGLD
EEEEECCCCCEECCC		44.13UniProtKB CARBOHYD
180O-linked_GlycosylationSTRNKDPTRRPELEA
CCCCCCCCCCCCCCC		49.8255823849
189O-linked_GlycosylationRPELEAGTNGRSSTT
CCCCCCCCCCCCCCC		41.3655823855
260PhosphorylationRRRHRKHSPQHTTTL
HHHHHCCCCCCCEEE		29.3229255136
264PhosphorylationRKHSPQHTTTLSLST
HCCCCCCCEEEEEEE		19.0729255136
265PhosphorylationKHSPQHTTTLSLSTL
CCCCCCCEEEEEEEC		24.5029255136
266PhosphorylationHSPQHTTTLSLSTLA
CCCCCCEEEEEEECC		18.5929255136
268PhosphorylationPQHTTTLSLSTLATP
CCCCEEEEEEECCCC		20.4123927012
270PhosphorylationHTTTLSLSTLATPKR
CCEEEEEEECCCCCC		20.2825219547
271PhosphorylationTTTLSLSTLATPKRS
CEEEEEEECCCCCCC		26.2125219547
274PhosphorylationLSLSTLATPKRSGNN
EEEEECCCCCCCCCC		32.2423927012
277MethylationSTLATPKRSGNNNGS
EECCCCCCCCCCCCC		51.50-
278PhosphorylationTLATPKRSGNNNGSE
ECCCCCCCCCCCCCC		52.5823898821
284PhosphorylationRSGNNNGSEPSDIII
CCCCCCCCCCCCEEE		48.7527470641
287PhosphorylationNNNGSEPSDIIIPLR
CCCCCCCCCEEEEEC		37.0727470641
294PhosphorylationSDIIIPLRTADSVFC
CCEEEEECCCCCEEC		23.6332142685
294UbiquitinationSDIIIPLRTADSVFC
CCEEEEECCCCCEEC		23.6333845483
298PhosphorylationIPLRTADSVFCPHYE
EEECCCCCEECCCCE		18.0328152594
301UbiquitinationRTADSVFCPHYEKVS
CCCCCEECCCCEECC		1.5833845483
304PhosphorylationDSVFCPHYEKVSGDY
CCEECCCCEECCCCC		11.5527273156
308PhosphorylationCPHYEKVSGDYGHPV
CCCCEECCCCCCCCE		36.6921945579
311PhosphorylationYEKVSGDYGHPVYIV
CEECCCCCCCCEEEE		22.3621945579
316PhosphorylationGDYGHPVYIVQEMPP
CCCCCCEEEEEECCC		10.3821945579
325PhosphorylationVQEMPPQSPANIYYK
EEECCCCCCCCCEEE		31.5821945579
330PhosphorylationPQSPANIYYKV----
CCCCCCCEEEC----		9.3121945579
331PhosphorylationQSPANIYYKV-----
CCCCCCEEEC-----		11.0721945579
332UbiquitinationSPANIYYKV------
CCCCCEEEC------		25.2121963094
334UbiquitinationANIYYKV--------
CCCEEEC--------		21963094
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
304YPhosphorylationKinaseEPHB2P29323
PhosphoELM
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EFNB2_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 EFNB2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
EFNB1_HUMANEFNB1physical
26186194
PHLP1_HUMANPHLPP1physical
26186194
CAND2_HUMANCAND2physical
26186194
PK3CB_HUMANPIK3CBphysical
26186194
EI2BD_HUMANEIF2B4physical
26186194
MA7D2_HUMANMAP7D2physical
26186194
EPHB2_HUMANEPHB2physical
26186194
EPHB3_HUMANEPHB3physical
26186194
EPHA5_HUMANEPHA5physical
26186194
EPHB4_HUMANEPHB4physical
26186194
SAAL1_HUMANSAAL1physical
26186194
DIP2B_HUMANDIP2Bphysical
26186194
DIP2A_HUMANDIP2Aphysical
26186194
PKHH3_HUMANPLEKHH3physical
26186194
P121A_HUMANPOM121physical
26186194
MTMR5_HUMANSBF1physical
26186194
KIF14_HUMANKIF14physical
26186194
RETST_HUMANRETSATphysical
26186194
MET13_HUMANMETTL13physical
26186194
TYK2_HUMANTYK2physical
26186194
SDC2_HUMANSDC2physical
26186194
P85B_HUMANPIK3R2physical
26186194
P85A_HUMANPIK3R1physical
26186194
P55G_HUMANPIK3R3physical
26186194
UBE3C_HUMANUBE3Cphysical
26186194
MAOX_HUMANME1physical
26186194
DYN3_HUMANDNM3physical
26186194
USO1_HUMANUSO1physical
26186194
MA7D3_HUMANMAP7D3physical
26186194
AT2B2_HUMANATP2B2physical
26186194
MED16_HUMANMED16physical
26186194
PKP2_HUMANPKP2physical
26186194
HPS3_HUMANHPS3physical
26186194
AAAS_HUMANAAASphysical
26186194
PKHG4_HUMANPLEKHG4physical
26186194
EI2BB_HUMANEIF2B2physical
26186194
MTMR1_HUMANMTMR1physical
26186194
F120A_HUMANFAM120Aphysical
26186194
P4K2B_HUMANPI4K2Bphysical
26186194
PKN3_HUMANPKN3physical
26186194
MRRP3_HUMANKIAA0391physical
26186194
F1712_HUMANFAM171A2physical
26186194
NF1_HUMANNF1physical
26186194
DPH1_HUMANDPH1physical
26186194
LMBR1_HUMANLMBR1physical
26186194
DEN6A_HUMANDENND6Aphysical
26186194
EI2BE_HUMANEIF2B5physical
26186194
PK3CA_HUMANPIK3CAphysical
26186194
DAD1_HUMANDAD1physical
26186194
TIGD5_HUMANTIGD5physical
26186194
RADIL_HUMANRADILphysical
26186194
EPHB2_HUMANEPHB2physical
28514442
EFNB1_HUMANEFNB1physical
28514442
EPHB4_HUMANEPHB4physical
28514442
EPHB3_HUMANEPHB3physical
28514442
DIP2B_HUMANDIP2Bphysical
28514442
F1712_HUMANFAM171A2physical
28514442
USO1_HUMANUSO1physical
28514442
DIP2A_HUMANDIP2Aphysical
28514442
EPHA5_HUMANEPHA5physical
28514442
DEN6A_HUMANDENND6Aphysical
28514442
PHLP1_HUMANPHLPP1physical
28514442
MTMR5_HUMANSBF1physical
28514442
CAND2_HUMANCAND2physical
28514442
PKN3_HUMANPKN3physical
28514442
TEX2_HUMANTEX2physical
28514442
MA7D2_HUMANMAP7D2physical
28514442
P4K2B_HUMANPI4K2Bphysical
28514442
MAOX_HUMANME1physical
28514442
KIF14_HUMANKIF14physical
28514442
TIGD5_HUMANTIGD5physical
28514442
MTMR1_HUMANMTMR1physical
28514442
DYN3_HUMANDNM3physical
28514442
PKP2_HUMANPKP2physical
28514442
PK3CB_HUMANPIK3CBphysical
28514442
AT2B2_HUMANATP2B2physical
28514442
SDC2_HUMANSDC2physical
28514442
LMBR1_HUMANLMBR1physical
28514442
TYK2_HUMANTYK2physical
28514442
NGBR_HUMANNUS1physical
28514442
TSN3_HUMANTSPAN3physical
28514442
PK3CA_HUMANPIK3CAphysical
28514442
SDC3_HUMANSDC3physical
28514442
EI2BB_HUMANEIF2B2physical
28514442
P85B_HUMANPIK3R2physical
28514442
DPH1_HUMANDPH1physical
28514442
PKHG4_HUMANPLEKHG4physical
28514442
PKHH3_HUMANPLEKHH3physical
28514442
RADIL_HUMANRADILphysical
28514442
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 EFNB2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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 SER-325, 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-304; TYR-311; TYR-316AND TYR-330, 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-304, 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-304 AND TYR-330, ANDMASS SPECTROMETRY.

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