EF1B_YEAST - dbPTM
EF1B_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EF1B_YEAST
UniProt AC P32471
Protein Name Elongation factor 1-beta
Gene Name EFB1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 206
Subcellular Localization
Protein Description Catalytic subunit of the guanine nucleotide exchange factor (GEF) (eEF1B subcomplex) of the eukaryotic elongation factor 1 complex (eEF1). Stimulates the exchange of GDP for GTP on elongation factor 1A (eEF1A), probably by displacing GDP from the nucleotide binding pocket in eEF1A. The 30-fold higher concentration of GTP compared to GDP in cells favors the formation of eEF1A-GTP, which rapidly forms a ternary complex with aminoacyl-tRNA that in turn displaces eEF1B from the complex..
Protein Sequence MASTDFSKIETLKQLNASLADKSYIEGTAVSQADVTVFKAFQSAYPEFSRWFNHIASKADEFDSFPAASAAAAEEEEDDDVDLFGSDDEEADAEAEKLKAERIAAYNAKKAAKPAKPAAKSIVTLDVKPWDDETNLEEMVANVKAIEMEGLTWGAHQFIPIGFGIKKLQINCVVEDDKVSLDDLQQSIEEDEDHVQSTDIAAMQKL
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
2Acetylation------MASTDFSKI
------CCCCCHHHH		22.579298649
3Phosphorylation-----MASTDFSKIE
-----CCCCCHHHHH		27.4928152593
4Phosphorylation----MASTDFSKIET
----CCCCCHHHHHH		31.3715665377
7Phosphorylation-MASTDFSKIETLKQ
-CCCCCHHHHHHHHH		35.2228152593
82-HydroxyisobutyrylationMASTDFSKIETLKQL
CCCCCHHHHHHHHHH		44.55-
8SuccinylationMASTDFSKIETLKQL
CCCCCHHHHHHHHHH		44.5523954790
8UbiquitinationMASTDFSKIETLKQL
CCCCCHHHHHHHHHH		44.5522817900
8AcetylationMASTDFSKIETLKQL
CCCCCHHHHHHHHHH		44.5524489116
11PhosphorylationTDFSKIETLKQLNAS
CCHHHHHHHHHHCHH		42.6128152593
13UbiquitinationFSKIETLKQLNASLA
HHHHHHHHHHCHHHC		61.2223749301
13SuccinylationFSKIETLKQLNASLA
HHHHHHHHHHCHHHC		61.2223954790
13AcetylationFSKIETLKQLNASLA
HHHHHHHHHHCHHHC		61.2224489116
18PhosphorylationTLKQLNASLADKSYI
HHHHHCHHHCCCCCC		24.0222369663
22UbiquitinationLNASLADKSYIEGTA
HCHHHCCCCCCCCCC		39.2823749301
22AcetylationLNASLADKSYIEGTA
HCHHHCCCCCCCCCC		39.2824489116
31PhosphorylationYIEGTAVSQADVTVF
CCCCCCCCHHHHHHH		19.7225752575
36PhosphorylationAVSQADVTVFKAFQS
CCCHHHHHHHHHHHH		22.2924961812
39UbiquitinationQADVTVFKAFQSAYP
HHHHHHHHHHHHHCH		43.9119722269
43PhosphorylationTVFKAFQSAYPEFSR
HHHHHHHHHCHHHHH		24.2625752575
45PhosphorylationFKAFQSAYPEFSRWF
HHHHHHHCHHHHHHH		14.4521082442
49PhosphorylationQSAYPEFSRWFNHIA
HHHCHHHHHHHHHHH		27.2628889911
57PhosphorylationRWFNHIASKADEFDS
HHHHHHHHHCHHHCC		27.9828889911
64PhosphorylationSKADEFDSFPAASAA
HHCHHHCCCHHHHHH		38.1522369663
69PhosphorylationFDSFPAASAAAAEEE
HCCCHHHHHHHHHHC		22.1322369663
86PhosphorylationDDVDLFGSDDEEADA
CCCCCCCCCHHHHHH		34.2622369663
106PhosphorylationKAERIAAYNAKKAAK
HHHHHHHHHHHHCCC		13.4627717283
109UbiquitinationRIAAYNAKKAAKPAK
HHHHHHHHHCCCCCC		39.0323749301
109SuccinylationRIAAYNAKKAAKPAK
HHHHHHHHHCCCCCC		39.0323954790
1092-HydroxyisobutyrylationRIAAYNAKKAAKPAK
HHHHHHHHHCCCCCC		39.03-
109AcetylationRIAAYNAKKAAKPAK
HHHHHHHHHCCCCCC		39.0325381059
116SuccinylationKKAAKPAKPAAKSIV
HHCCCCCCCCCCCEE		43.6523954790
121PhosphorylationPAKPAAKSIVTLDVK
CCCCCCCCEEEEECC		19.9821440633
128SuccinylationSIVTLDVKPWDDETN
CEEEEECCCCCCCCC		39.8023954790
128UbiquitinationSIVTLDVKPWDDETN
CEEEEECCCCCCCCC		39.8023749301
128AcetylationSIVTLDVKPWDDETN
CEEEEECCCCCCCCC		39.8024489116
166UbiquitinationIPIGFGIKKLQINCV
EEECCCCEEEEEEEE		48.0523749301
166AcetylationIPIGFGIKKLQINCV
EEECCCCEEEEEEEE		48.0524489116
167UbiquitinationPIGFGIKKLQINCVV
EECCCCEEEEEEEEE		43.6422817900
178AcetylationNCVVEDDKVSLDDLQ
EEEEECCCCCHHHHH		46.1525381059
180PhosphorylationVVEDDKVSLDDLQQS
EEECCCCCHHHHHHH		31.6428132839
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_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EF1B_YEAST !!
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_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
EF1A_YEASTTEF2physical
11134944
EF1A_YEASTTEF2genetic
8647386
EF3A_YEASTYEF3physical
17179749
EF1G2_YEASTTEF4physical
17179749
PAT1_YEASTPAT1genetic
19061648
LSM1_YEASTLSM1genetic
19061648
TRM10_YEASTTRM10genetic
19061648
TOP1_YEASTTOP1genetic
19061648
RRP6_YEASTRRP6genetic
19061648
HIR2_YEASTHIR2genetic
19061648
DBP5_YEASTDBP5genetic
19061648
LSM7_YEASTLSM7genetic
19061648
SN309_YEASTSNT309genetic
19061648
PFD5_YEASTGIM5genetic
19061648
EF1A_YEASTTEF2physical
19095653
PPZ1_YEASTPPZ1physical
11278758
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of EF1B_YEAST

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Proteome studies of Saccharomyces cerevisiae: identification andcharacterization of abundant proteins.";
Garrels J.I., McLaughlin C.S., Warner J.R., Futcher B., Latter G.I.,Kobayashi R., Schwender B., Volpe T., Anderson D.S.,Mesquita-Fuentes R., Payne W.E.;
Electrophoresis 18:1347-1360(1997).
Cited for: ACETYLATION AT ALA-2.
Phosphorylation
ReferencePubMed
"A multidimensional chromatography technology for in-depthphosphoproteome analysis.";
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
Mol. Cell. Proteomics 7:1389-1396(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31; SER-43 AND SER-86,AND MASS SPECTROMETRY.
"Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry.";
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86, AND MASSSPECTROMETRY.
"Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae.";
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.;
J. Proteome Res. 6:1190-1197(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86, AND MASSSPECTROMETRY.
"Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway.";
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.;
Mol. Cell. Proteomics 4:310-327(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-4 AND SER-86, AND MASSSPECTROMETRY.

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