EFNB1_HUMAN - dbPTM
EFNB1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EFNB1_HUMAN
UniProt AC P98172
Protein Name Ephrin-B1
Gene Name EFNB1
Organism Homo sapiens (Human).
Sequence Length 346
Subcellular Localization Membrane
Single-pass type I membrane protein.
Protein Description Binds to the receptor tyrosine kinases EPHB1 and EPHA1. Binds to, and induce the collapse of, commissural axons/growth cones in vitro. May play a role in constraining the orientation of longitudinally projecting axons (By similarity).; 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 the receptor tyrosine kinases EPHB3 (preferred), EPHB1 and EPHA1. Binds to, and induce the collapse of, commissural axons/growth cones in vitro. May play a role in constraining the orientation of longitudinally projecting axons (By similarity)..
Protein Sequence MARPGQRWLGKWLVAMVVWALCRLATPLAKNLEPVSWSSLNPKFLSGKGLVIYPKIGDKLDIICPRAEAGRPYEYYKLYLVRPEQAAACSTVLDPNVLVTCNRPEQEIRFTIKFQEFSPNYMGLEFKKHHDYYITSTSNGSLEGLENREGGVCRTRTMKIIMKVGQDPNAVTPEQLTTSRPSKEADNTVKMATQAPGSRGSLGDSDGKHETVNQEEKSGPGASGGSSGDPDGFFNSKVALFAAVGAGCVIFLLIIIFLTVLLLKLRKRHRKHTQQRAAALSLSTLASPKGGSGTAGTEPSDIIIPLRTTENNYCPHYEKVSGDYGHPVYIVQEMPPQSPANIYYKV
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
26PhosphorylationWALCRLATPLAKNLE
HHHHHHHCHHHHCCC		24.3528258704
36PhosphorylationAKNLEPVSWSSLNPK
HHCCCCCCHHHCCHH		31.7728258704
38PhosphorylationNLEPVSWSSLNPKFL
CCCCCCHHHCCHHHH		19.9029978859
39PhosphorylationLEPVSWSSLNPKFLS
CCCCCHHHCCHHHHC		26.3823403867
46PhosphorylationSLNPKFLSGKGLVIY
HCCHHHHCCCCEEEE		41.4128258704
79PhosphorylationPYEYYKLYLVRPEQA
CCEEEEEEEECHHHH		10.0522817900
139N-linked_GlycosylationYYITSTSNGSLEGLE
EEEEECCCCCEECCC		44.13UniProtKB CARBOHYD
163UbiquitinationRTMKIIMKVGQDPNA
CEEEEEEEECCCCCC		32.57-
172O-linked_GlycosylationGQDPNAVTPEQLTTS
CCCCCCCCHHHCCCC		20.7855835709
177O-linked_GlycosylationAVTPEQLTTSRPSKE
CCCHHHCCCCCCCHH		23.5555835715
178O-linked_GlycosylationVTPEQLTTSRPSKEA
CCHHHCCCCCCCHHH		31.1955835721
179O-linked_GlycosylationTPEQLTTSRPSKEAD
CHHHCCCCCCCHHHC		36.6455835727
188O-linked_GlycosylationPSKEADNTVKMATQA
CCHHHCCCCCCCCCC		23.2755835771
198O-linked_GlycosylationMATQAPGSRGSLGDS
CCCCCCCCCCCCCCC		32.20OGP
201O-linked_GlycosylationQAPGSRGSLGDSDGK
CCCCCCCCCCCCCCC		28.2455827673
211O-linked_GlycosylationDSDGKHETVNQEEKS
CCCCCCCCCCCHHHC		25.2055825315
211PhosphorylationDSDGKHETVNQEEKS
CCCCCCCCCCCHHHC		25.20-
218PhosphorylationTVNQEEKSGPGASGG
CCCCHHHCCCCCCCC		54.20-
223PhosphorylationEKSGPGASGGSSGDP
HHCCCCCCCCCCCCC		49.99-
226PhosphorylationGPGASGGSSGDPDGF
CCCCCCCCCCCCCCC		34.37-
227PhosphorylationPGASGGSSGDPDGFF
CCCCCCCCCCCCCCC		50.95-
281PhosphorylationQQRAAALSLSTLASP
HHHHHHHHHHHHCCC		18.6230266825
283PhosphorylationRAAALSLSTLASPKG
HHHHHHHHHHCCCCC		20.2830266825
284PhosphorylationAAALSLSTLASPKGG
HHHHHHHHHCCCCCC		31.4730266825
287PhosphorylationLSLSTLASPKGGSGT
HHHHHHCCCCCCCCC		30.2030266825
289UbiquitinationLSTLASPKGGSGTAG
HHHHCCCCCCCCCCC		73.7021963094
292PhosphorylationLASPKGGSGTAGTEP
HCCCCCCCCCCCCCC		41.4630266825
294PhosphorylationSPKGGSGTAGTEPSD
CCCCCCCCCCCCCCC		24.5030266825
297PhosphorylationGGSGTAGTEPSDIII
CCCCCCCCCCCCEEE		42.1130266825
300PhosphorylationGTAGTEPSDIIIPLR
CCCCCCCCCEEEECE		34.9030266825
308PhosphorylationDIIIPLRTTENNYCP
CEEEECEECCCCCCC		46.2628796482
309PhosphorylationIIIPLRTTENNYCPH
EEEECEECCCCCCCC		30.2228796482
313PhosphorylationLRTTENNYCPHYEKV
CEECCCCCCCCCEEC		20.9520007894
317PhosphorylationENNYCPHYEKVSGDY
CCCCCCCCEECCCCC		11.5527273156
319UbiquitinationNYCPHYEKVSGDYGH
CCCCCCEECCCCCCC		34.2429967540
321PhosphorylationCPHYEKVSGDYGHPV
CCCCEECCCCCCCCE		36.6921945579
324PhosphorylationYEKVSGDYGHPVYIV
CEECCCCCCCCEEEE		22.3621945579
329PhosphorylationGDYGHPVYIVQEMPP
CCCCCCEEEEEECCC		10.3821945579
338PhosphorylationVQEMPPQSPANIYYK
EEECCCCCCCCCEEE		31.5821945579
343PhosphorylationPQSPANIYYKV----
CCCCCCCEEEC----		9.3121945579
344PhosphorylationQSPANIYYKV-----
CCCCCCEEEC-----		11.0721945579
345UbiquitinationSPANIYYKV------
CCCCCEEEC------		25.2121906983
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 EFNB1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EFNB1_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 EFNB1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PTN13_HUMANPTPN13physical
9920925
SDCB1_HUMANSDCBPphysical
9920925
NCK2_HUMANNCK2physical
11557983
SMUF2_HUMANSMURF2physical
23475958
SMUF1_HUMANSMURF1physical
23475958
MYC_HUMANMYCphysical
21988832
1433T_HUMANYWHAQphysical
21988832
SRBS1_HUMANSORBS1physical
11557983
Drug and Disease Associations
Kegg Disease
H00458 Craniosynostosis, including: Pfeiffer syndrome; Apert syndrome; Crouzon syndrome; Jackson-Weiss synd
OMIM Disease
304110Craniofrontonasal syndrome (CFNS)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of EFNB1_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-287, 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-313 AND TYR-317, 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-317, AND MASSSPECTROMETRY.

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