EF1B_MOUSE - dbPTM
EF1B_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EF1B_MOUSE
UniProt AC O70251
Protein Name Elongation factor 1-beta
Gene Name Eef1b
Organism Mus musculus (Mouse).
Sequence Length 225
Subcellular Localization
Protein Description EF-1-beta and EF-1-delta stimulate the exchange of GDP bound to EF-1-alpha to GTP..
Protein Sequence MGFGDLKTPAGLQVLNDYLADKSYIEGYVPSQADVAVFEAVSGPPPADLCHALRWYNHIKSYEKEKASLPGVKKSLGKYGPSSVEDTTGSGAADAKDDDDIDLFGSDDEEESEEAKKLREERLAQYESKKAKKPAVVAKSSILLDVKPWDDETDMTKLEECVRSIQADGLVWGSSKLVPVGYGIKKLQIQCVVEDDKVGTDMLEEQITAFEDYVQSMDVAAFNKI
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
7Ubiquitination-MGFGDLKTPAGLQV
-CCCCCCCCHHHHHH		58.14-
7Succinylation-MGFGDLKTPAGLQV
-CCCCCCCCHHHHHH		58.1423954790
7Acetylation-MGFGDLKTPAGLQV
-CCCCCCCCHHHHHH		58.1422826441
42PhosphorylationVAVFEAVSGPPPADL
EEEEECCCCCCCHHH		53.26-
50S-nitrosocysteineGPPPADLCHALRWYN
CCCCHHHHHHHHHHH		1.49-
50GlutathionylationGPPPADLCHALRWYN
CCCCHHHHHHHHHHH		1.4924333276
50S-nitrosylationGPPPADLCHALRWYN
CCCCHHHHHHHHHHH		1.4922178444
60UbiquitinationLRWYNHIKSYEKEKA
HHHHHHHHHHHHHHC		39.1622790023
60AcetylationLRWYNHIKSYEKEKA
HHHHHHHHHHHHHHC		39.1622826441
73UbiquitinationKASLPGVKKSLGKYG
HCCCCCHHHHHHCCC		42.4327667366
75PhosphorylationSLPGVKKSLGKYGPS
CCCCHHHHHHCCCCC		36.3129514104
78AcetylationGVKKSLGKYGPSSVE
CHHHHHHCCCCCCCC		52.9422826441
78UbiquitinationGVKKSLGKYGPSSVE
CHHHHHHCCCCCCCC		52.9427667366
78MalonylationGVKKSLGKYGPSSVE
CHHHHHHCCCCCCCC		52.9426320211
79PhosphorylationVKKSLGKYGPSSVED
HHHHHHCCCCCCCCC		32.2527087446
82PhosphorylationSLGKYGPSSVEDTTG
HHHCCCCCCCCCCCC		42.5324925903
83PhosphorylationLGKYGPSSVEDTTGS
HHCCCCCCCCCCCCC		32.4325521595
87PhosphorylationGPSSVEDTTGSGAAD
CCCCCCCCCCCCCCC		21.3924925903
88PhosphorylationPSSVEDTTGSGAADA
CCCCCCCCCCCCCCC		41.4924925903
90PhosphorylationSVEDTTGSGAADAKD
CCCCCCCCCCCCCCC		24.1425521595
106PhosphorylationDDIDLFGSDDEEESE
CCCCCCCCCCHHHHH		34.2624925903
112PhosphorylationGSDDEEESEEAKKLR
CCCCHHHHHHHHHHH		43.9725521595
126PhosphorylationREERLAQYESKKAKK
HHHHHHHHHHHCCCC		19.3025367039
128PhosphorylationERLAQYESKKAKKPA
HHHHHHHHHCCCCCC		34.2327149854
129MalonylationRLAQYESKKAKKPAV
HHHHHHHHCCCCCCE		44.8226320211
129AcetylationRLAQYESKKAKKPAV
HHHHHHHHCCCCCCE		44.8230585453
129SuccinylationRLAQYESKKAKKPAV
HHHHHHHHCCCCCCE		44.8223954790
129UbiquitinationRLAQYESKKAKKPAV
HHHHHHHHCCCCCCE		44.8227667366
133MalonylationYESKKAKKPAVVAKS
HHHHCCCCCCEEEEC		42.9726320211
133UbiquitinationYESKKAKKPAVVAKS
HHHHCCCCCCEEEEC		42.9727667366
140PhosphorylationKPAVVAKSSILLDVK
CCCEEEECCEECCCC		16.9319060867
141PhosphorylationPAVVAKSSILLDVKP
CCEEEECCEECCCCC		19.2927600695
147UbiquitinationSSILLDVKPWDDETD
CCEECCCCCCCCCCC		39.8022790023
147AcetylationSSILLDVKPWDDETD
CCEECCCCCCCCCCC		39.8023954790
161GlutathionylationDMTKLEECVRSIQAD
CHHHHHHHHHHHHHC		1.9424333276
161S-nitrosylationDMTKLEECVRSIQAD
CHHHHHHHHHHHHHC		1.9421278135
161S-nitrosocysteineDMTKLEECVRSIQAD
CHHHHHHHHHHHHHC		1.94-
174PhosphorylationADGLVWGSSKLVPVG
HCCCEECCCCEEEEC		14.4825619855
175PhosphorylationDGLVWGSSKLVPVGY
CCCEECCCCEEEECC		26.5225619855
176AcetylationGLVWGSSKLVPVGYG
CCEECCCCEEEECCC		56.0223236377
176UbiquitinationGLVWGSSKLVPVGYG
CCEECCCCEEEECCC		56.0222790023
182PhosphorylationSKLVPVGYGIKKLQI
CCEEEECCCEEEEEE		18.8625367039
185MalonylationVPVGYGIKKLQIQCV
EEECCCEEEEEEEEE		42.9726320211
185UbiquitinationVPVGYGIKKLQIQCV
EEECCCEEEEEEEEE		42.9727667366
185AcetylationVPVGYGIKKLQIQCV
EEECCCEEEEEEEEE		42.9722826441
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 EF1B_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EF1B_MOUSE !!
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 EF1B_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of EF1B_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of EF1B_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry.";
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
Mol. Cell. Proteomics 8:904-912(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, AND MASSSPECTROMETRY.
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.;
Immunity 30:143-154(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, AND MASSSPECTROMETRY.
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, AND MASSSPECTROMETRY.
"Specific phosphopeptide enrichment with immobilized titanium ionaffinity chromatography adsorbent for phosphoproteome analysis.";
Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
J. Proteome Res. 7:3957-3967(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, AND MASSSPECTROMETRY.
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83 AND SER-106, AND MASSSPECTROMETRY.
"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry.";
Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
J. Proteome Res. 6:250-262(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, AND MASSSPECTROMETRY.
"Phosphoproteomic analysis of the developing mouse brain.";
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
Mol. Cell. Proteomics 3:1093-1101(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, AND MASSSPECTROMETRY.
"Identification of phosphoproteins and their phosphorylation sites inthe WEHI-231 B lymphoma cell line.";
Shu H., Chen S., Bi Q., Mumby M., Brekken D.L.;
Mol. Cell. Proteomics 3:279-286(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, AND MASSSPECTROMETRY.

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