IF4E_YEAST - dbPTM
IF4E_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID IF4E_YEAST
UniProt AC P07260
Protein Name Eukaryotic translation initiation factor 4E
Gene Name CDC33
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 213
Subcellular Localization
Protein Description Recognizes and binds the 7-methylguanosine-containing mRNA cap during an early step in the initiation of protein synthesis and facilitates ribosome binding by inducing the unwinding of the mRNAs secondary structures..
Protein Sequence MSVEEVSKKFEENVSVDDTTATPKTVLSDSAHFDVKHPLNTKWTLWYTKPAVDKSESWSDLLRPVTSFQTVEEFWAIIQNIPEPHELPLKSDYHVFRNDVRPEWEDEANAKGGKWSFQLRGKGADIDELWLRTLLAVIGETIDEDDSQINGVVLSIRKGGNKFALWTKSEDKEPLLRIGGKFKQVLKLTDDGHLEFFPHSSANGRHPQPSITL
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
2Phosphorylation------MSVEEVSKK
------CCHHHHHHH		37.9329136822
7Phosphorylation-MSVEEVSKKFEENV
-CCHHHHHHHHHHCC		33.1529136822
8AcetylationMSVEEVSKKFEENVS
CCHHHHHHHHHHCCC		67.6624489116
9AcetylationSVEEVSKKFEENVSV
CHHHHHHHHHHCCCC		50.9624489116
9UbiquitinationSVEEVSKKFEENVSV
CHHHHHHHHHHCCCC		50.9623749301
15PhosphorylationKKFEENVSVDDTTAT
HHHHHCCCCCCCCCC		31.2622369663
19PhosphorylationENVSVDDTTATPKTV
HCCCCCCCCCCCCEE		17.5425521595
20PhosphorylationNVSVDDTTATPKTVL
CCCCCCCCCCCCEEC		35.2122369663
22PhosphorylationSVDDTTATPKTVLSD
CCCCCCCCCCEECCC		24.1922369663
25PhosphorylationDTTATPKTVLSDSAH
CCCCCCCEECCCCCC		28.0822369663
28PhosphorylationATPKTVLSDSAHFDV
CCCCEECCCCCCCEE		25.7822369663
30PhosphorylationPKTVLSDSAHFDVKH
CCEECCCCCCCEECC		21.9222369663
36UbiquitinationDSAHFDVKHPLNTKW
CCCCCEECCCCCCCE		41.1524961812
36AcetylationDSAHFDVKHPLNTKW
CCCCCEECCCCCCCE		41.1524489116
36SuccinylationDSAHFDVKHPLNTKW
CCCCCEECCCCCCCE		41.1523954790
42AcetylationVKHPLNTKWTLWYTK
ECCCCCCCEEEEEEC		36.7924489116
49AcetylationKWTLWYTKPAVDKSE
CEEEEEECCCCCCCC		18.4524489116
111SuccinylationWEDEANAKGGKWSFQ
CCHHHHHCCCEEEEE		68.9223954790
111AcetylationWEDEANAKGGKWSFQ
CCHHHHHCCCEEEEE		68.9224489116
111UbiquitinationWEDEANAKGGKWSFQ
CCHHHHHCCCEEEEE		68.9223749301
114UbiquitinationEANAKGGKWSFQLRG
HHHHCCCEEEEEECC		48.6223749301
114AcetylationEANAKGGKWSFQLRG
HHHHCCCEEEEEECC		48.6224489116
1142-HydroxyisobutyrylationEANAKGGKWSFQLRG
HHHHCCCEEEEEECC		48.62-
122UbiquitinationWSFQLRGKGADIDEL
EEEEECCCCCCHHHH		44.4824961812
122AcetylationWSFQLRGKGADIDEL
EEEEECCCCCCHHHH		44.4824489116
133PhosphorylationIDELWLRTLLAVIGE
HHHHHHHHHHHHHCC		24.7727017623
147PhosphorylationETIDEDDSQINGVVL
CCCCCCCCCCCEEEE		45.3327017623
155PhosphorylationQINGVVLSIRKGGNK
CCCEEEEEEEECCCE		14.5627017623
158AcetylationGVVLSIRKGGNKFAL
EEEEEEEECCCEEEE		70.2924489116
162AcetylationSIRKGGNKFALWTKS
EEEECCCEEEEEECC		34.9824489116
162UbiquitinationSIRKGGNKFALWTKS
EEEECCCEEEEEECC		34.9823749301
168UbiquitinationNKFALWTKSEDKEPL
CEEEEEECCCCCCCC		40.0222817900
172AcetylationLWTKSEDKEPLLRIG
EEECCCCCCCCEEEC		58.1224489116
172UbiquitinationLWTKSEDKEPLLRIG
EEECCCCCCCCEEEC		58.1222817900
181AcetylationPLLRIGGKFKQVLKL
CCEEECCEEEEEEEE		44.1425381059
187AcetylationGKFKQVLKLTDDGHL
CEEEEEEEECCCCCE		50.9524489116
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
2SPhosphorylationKinaseCK2-FAMILY-GPS
2SPhosphorylationKinaseCK2-Uniprot
2SPhosphorylationKinaseCK2_GROUP-PhosphoELM
15SPhosphorylationKinaseCK2-FAMILY-GPS
15SPhosphorylationKinaseCK2-Uniprot
15SPhosphorylationKinaseCK2_GROUP-PhosphoELM
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of IF4E_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 IF4E_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
LHP1_YEASTLHP1physical
11805826
DPOE_YEASTPOL2physical
11805826
ROM2_YEASTROM2physical
11805826
SSBP1_YEASTSBP1physical
11805826
NCBP1_YEASTSTO1physical
11805826
IF4F1_YEASTTIF4631physical
11805826
IF4F2_YEASTTIF4632physical
11805826
UTP20_YEASTUTP20physical
11805826
EAP1_YEASTEAP1physical
11805837
LCF4_YEASTFAA4physical
11805837
TRPE_YEASTTRP2physical
11805837
AAKG_YEASTSNF4physical
11805837
AHA1_YEASTAHA1physical
11805837
CAF20_YEASTCAF20physical
10688190
IF4F1_YEASTTIF4631physical
8336723
XRN1_YEASTXRN1genetic
10790382
RIR2_YEASTRNR2genetic
10585489
CG12_YEASTCLN2genetic
11479284
CG13_YEASTCLN3genetic
11479284
DED1_YEASTDED1genetic
10409745
DED1_YEASTDED1genetic
9144215
DBP1_YEASTDBP1genetic
9144215
DED1_YEASTDED1genetic
9045610
FBRL_YEASTNOP1physical
16554755
PABP_YEASTPAB1physical
16429126
IF4F2_YEASTTIF4632physical
16429126
IMDH4_YEASTIMD4physical
16429126
RS8A_YEASTRPS8Aphysical
16429126
RS8B_YEASTRPS8Aphysical
16429126
GBP2_YEASTGBP2physical
16429126
XRN1_YEASTXRN1physical
16429126
LHP1_YEASTLHP1physical
16429126
DPOE_YEASTPOL2physical
16429126
SSBP1_YEASTSBP1physical
16429126
NCBP1_YEASTSTO1physical
16429126
IF4F1_YEASTTIF4631physical
16429126
RS4A_YEASTRPS4Aphysical
16429126
RS4B_YEASTRPS4Aphysical
16429126
RS9B_YEASTRPS9Bphysical
16429126
RRP5_YEASTRRP5physical
16429126
RS22B_YEASTRPS22Bphysical
16429126
POP2_YEASTPOP2genetic
17439972
KAPR_YEASTBCY1genetic
3062383
DED1_YEASTDED1physical
21925384
SCD6_YEASTSCD6physical
22284680
CAF20_YEASTCAF20genetic
9144215
IF4F1_YEASTTIF4631physical
23226381
IF4E_YEASTCDC33physical
24183571
HSP77_YEASTSSC1physical
25826658
IF4F1_YEASTTIF4631physical
25826658
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of IF4E_YEAST

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Related Literatures of Post-Translational Modification
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-15; THR-22; SER-28 ANDSER-30, AND MASS SPECTROMETRY.
"Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases.";
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.;
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15; THR-22; SER-28 ANDSER-30, 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-15, 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-15; THR-22 AND SER-30,AND MASS SPECTROMETRY.
"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 SER-15, AND MASSSPECTROMETRY.
"Characterization of the in vivo phosphorylation sites of themRNA.cap-binding complex proteins eukaryotic initiation factor-4E andp20 in Saccharomyces cerevisiae.";
Zanchin N.I.T., McCarthy J.E.G.;
J. Biol. Chem. 270:26505-26510(1995).
Cited for: PHOSPHORYLATION AT SER-2 AND SER-15.

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