IF5_YEAST - dbPTM
IF5_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID IF5_YEAST
UniProt AC P38431
Protein Name Eukaryotic translation initiation factor 5
Gene Name TIF5
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 405
Subcellular Localization
Protein Description Catalyzes the hydrolysis of GTP bound to the 40S ribosomal initiation complex (40S.mRNA.Met-tRNA[F].eIF-2.GTP) with the subsequent joining of a 60S ribosomal subunit resulting in the release of eIF-2 and the guanine nucleotide. The subsequent joining of a 60S ribosomal subunit results in the formation of a functional 80S initiation complex (80S.mRNA.Met-tRNA[F]). eIF-5 is essential for cell viability..
Protein Sequence MSINICRDNHDPFYRYKMPPIQAKVEGRGNGIKTAVLNVADISHALNRPAPYIVKYFGFELGAQTSISVDKDRYLVNGVHEPAKLQDVLDGFINKFVLCGSCKNPETEIIITKDNDLVRDCKACGKRTPMDLRHKLSSFILKNPPDSVSGSKKKKKAATASANVRGGGLSISDIAQGKSQNAPSDGTGSSTPQHHDEDEDELSRQIKAAASTLEDIEVKDDEWAVDMSEEAIRARAKELEVNSELTQLDEYGEWILEQAGEDKENLPSDVELYKKAAELDVLNDPKIGCVLAQCLFDEDIVNEIAEHNAFFTKILVTPEYEKNFMGGIERFLGLEHKDLIPLLPKILVQLYNNDIISEEEIMRFGTKSSKKFVPKEVSKKVRRAAKPFITWLETAESDDDEEDDE
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
24AcetylationKMPPIQAKVEGRGNG
CCCCEEEEEECCCCC		25.1724489116
113AcetylationETEIIITKDNDLVRD
CCEEEEECCCHHHHH		44.0924489116
135AcetylationTPMDLRHKLSSFILK
CCCHHHHHHHHHHHH		43.5624489116
138PhosphorylationDLRHKLSSFILKNPP
HHHHHHHHHHHHCCC		27.0921440633
142UbiquitinationKLSSFILKNPPDSVS
HHHHHHHHCCCCCCC		63.6924961812
142AcetylationKLSSFILKNPPDSVS
HHHHHHHHCCCCCCC		63.6924489116
147PhosphorylationILKNPPDSVSGSKKK
HHHCCCCCCCCCHHH		24.7730377154
149PhosphorylationKNPPDSVSGSKKKKK
HCCCCCCCCCHHHHC		41.1028889911
151PhosphorylationPPDSVSGSKKKKKAA
CCCCCCCCHHHHCCC		33.5228889911
159PhosphorylationKKKKKAATASANVRG
HHHHCCCCCCCCCCC		26.4628889911
161PhosphorylationKKKAATASANVRGGG
HHCCCCCCCCCCCCC		18.9324961812
170PhosphorylationNVRGGGLSISDIAQG
CCCCCCCCHHHHHCC		24.2622369663
172PhosphorylationRGGGLSISDIAQGKS
CCCCCCHHHHHCCCC		21.4222369663
178UbiquitinationISDIAQGKSQNAPSD
HHHHHCCCCCCCCCC		36.4723749301
179PhosphorylationSDIAQGKSQNAPSDG
HHHHCCCCCCCCCCC		35.1822890988
184PhosphorylationGKSQNAPSDGTGSST
CCCCCCCCCCCCCCC		46.3822369663
187PhosphorylationQNAPSDGTGSSTPQH
CCCCCCCCCCCCCCC		38.5922369663
189PhosphorylationAPSDGTGSSTPQHHD
CCCCCCCCCCCCCCC		30.7722369663
190PhosphorylationPSDGTGSSTPQHHDE
CCCCCCCCCCCCCCC		45.5122369663
191PhosphorylationSDGTGSSTPQHHDED
CCCCCCCCCCCCCCC		28.7622369663
203PhosphorylationDEDEDELSRQIKAAA
CCCHHHHHHHHHHHH		21.7922369663
207UbiquitinationDELSRQIKAAASTLE
HHHHHHHHHHHHCHH		24.5124961812
211PhosphorylationRQIKAAASTLEDIEV
HHHHHHHHCHHHCEE		28.8821440633
212PhosphorylationQIKAAASTLEDIEVK
HHHHHHHCHHHCEEC		29.4628889911
228PhosphorylationDEWAVDMSEEAIRAR
CCEEECCCHHHHHHH		28.0228889911
237UbiquitinationEAIRARAKELEVNSE
HHHHHHHHHHHCCHH		58.2224961812
243PhosphorylationAKELEVNSELTQLDE
HHHHHCCHHCCHHHH		38.8819795423
246PhosphorylationLEVNSELTQLDEYGE
HHCCHHCCHHHHHHH		24.0421440633
251PhosphorylationELTQLDEYGEWILEQ
HCCHHHHHHHHHHHH		21.7319795423
263UbiquitinationLEQAGEDKENLPSDV
HHHHCCCCCCCCCHH		44.1724961812
268PhosphorylationEDKENLPSDVELYKK
CCCCCCCCHHHHHHH		58.4122369663
273PhosphorylationLPSDVELYKKAAELD
CCCHHHHHHHHHHCC		9.2722369663
274UbiquitinationPSDVELYKKAAELDV
CCHHHHHHHHHHCCC		48.8622817900
274SuccinylationPSDVELYKKAAELDV
CCHHHHHHHHHHCCC		48.8623954790
274AcetylationPSDVELYKKAAELDV
CCHHHHHHHHHHCCC		48.8624489116
275UbiquitinationSDVELYKKAAELDVL
CHHHHHHHHHHCCCC		38.9923749301
317PhosphorylationFFTKILVTPEYEKNF
CEEEEECCHHHHHHC		13.6328889911
320PhosphorylationKILVTPEYEKNFMGG
EEECCHHHHHHCHHH		33.1521440633
322AcetylationLVTPEYEKNFMGGIE
ECCHHHHHHCHHHHH		55.3624489116
322UbiquitinationLVTPEYEKNFMGGIE
ECCHHHHHHCHHHHH		55.3623749301
337AcetylationRFLGLEHKDLIPLLP
HHHCCCHHHHHHHHH		44.8724489116
366PhosphorylationEEIMRFGTKSSKKFV
HHHHHHCCCCCCCCC		25.6628889911
390PhosphorylationRAAKPFITWLETAES
HHHCCCCHHHHHCCC		25.1122369663
394PhosphorylationPFITWLETAESDDDE
CCCHHHHHCCCCCCC		33.2922369663
397PhosphorylationTWLETAESDDDEEDD
HHHHHCCCCCCCCCC		43.8222369663
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 IF5_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of IF5_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 IF5_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
EIF3B_YEASTPRT1physical
11805826
ATG9_YEASTATG9physical
11805826
EIF3J_YEASTHCR1physical
11805826
LSG1_YEASTLSG1physical
11805826
KTR5_YEASTKTR5physical
11805826
YG036_YEASTYGL036Wphysical
11805826
EIF3C_YEASTNIP1physical
11805826
NOG1_YEASTNOG1physical
11805826
RLI1_YEASTRLI1physical
11805826
SPT5_YEASTSPT5physical
11805826
EIF3I_YEASTTIF34physical
11805826
EIF3G_YEASTTIF35physical
11805826
UTP6_YEASTUTP6physical
11805826
PESC_YEASTNOP7physical
11805826
IF2P_YEASTFUN12physical
11805826
IF2B_YEASTSUI3physical
11018020
IF2B_YEASTSUI3physical
10075937
IF4F2_YEASTTIF4632physical
12861028
IF2G_YEASTGCD11physical
11018020
IF2G_YEASTGCD11physical
10075937
EIF3C_YEASTNIP1physical
11018020
EIF3C_YEASTNIP1physical
10075937
EIF3B_YEASTPRT1physical
11018020
EIF3B_YEASTPRT1physical
10075937
SUI1_YEASTSUI1physical
11018020
IF2A_YEASTSUI2physical
11018020
IF2A_YEASTSUI2physical
10075937
EIF3I_YEASTTIF34physical
11018020
EIF3I_YEASTTIF34physical
10075937
EIF3C_YEASTNIP1physical
9671501
EI2BB_YEASTGCD7physical
9395514
SUI1_YEASTSUI1physical
15145951
SUI1_YEASTSUI1physical
15964804
SUI1_YEASTSUI1physical
15377664
EIF3C_YEASTNIP1physical
15485912
IF2B_YEASTSUI3physical
9395514
EIF3A_YEASTRPG1physical
15838098
EIF3C_YEASTNIP1physical
15838098
EIF3B_YEASTPRT1physical
15838098
EIF3I_YEASTTIF34physical
15838098
EIF3G_YEASTTIF35physical
15838098
SUI1_YEASTSUI1physical
15838098
IF2A_YEASTSUI2physical
15838098
IF2G_YEASTGCD11physical
15838098
IF2B_YEASTSUI3physical
15964804
IF2B_YEASTSUI3physical
15377664
EIF3C_YEASTNIP1physical
15377664
EIF3B_YEASTPRT1physical
11331597
SUI1_YEASTSUI1physical
11331597
SUI1_YEASTSUI1genetic
15485912
SUI1_YEASTSUI1genetic
15377664
IF2B_YEASTSUI3genetic
15377664
IF2A_YEASTSUI2physical
16554755
EIF3I_YEASTTIF34physical
16554755
ATG9_YEASTATG9physical
16429126
IF2P_YEASTFUN12physical
16429126
EIF3J_YEASTHCR1physical
16429126
EIF3C_YEASTNIP1physical
16429126
RLI1_YEASTRLI1physical
16429126
EIF3A_YEASTRPG1physical
16429126
RS11A_YEASTRPS11Aphysical
16429126
RS11B_YEASTRPS11Aphysical
16429126
RS4A_YEASTRPS4Aphysical
16429126
RS4B_YEASTRPS4Aphysical
16429126
RS7A_YEASTRPS7Aphysical
16429126
EIF3I_YEASTTIF34physical
16429126
EIF3G_YEASTTIF35physical
16429126
DED1_YEASTDED1physical
16429126
EIF3B_YEASTPRT1physical
16429126
RS3_YEASTRPS3physical
16429126
RS5_YEASTRPS5physical
16429126
RS7B_YEASTRPS7Bphysical
16429126
RS9B_YEASTRPS9Bphysical
16429126
RL16A_YEASTRPL16Aphysical
16429126
RL18A_YEASTRPL18Aphysical
16429126
RL18B_YEASTRPL18Aphysical
16429126
RL13A_YEASTRPL13Aphysical
16429126
RL16B_YEASTRPL16Bphysical
16429126
RL6A_YEASTRPL6Aphysical
16429126
RL7A_YEASTRPL7Aphysical
16429126
IF2B_YEASTSUI3genetic
15964804
SSB1_YEASTSSB1physical
19536198
IF2B_YEASTSUI3physical
10769173
EI2BE_YEASTGCD6physical
16522633
IF2A_YEASTSUI2physical
16522633
IF2G_YEASTGCD11physical
16522633
BDH1_YEASTBDH1genetic
20093466
OAF1_YEASTOAF1genetic
20093466
SWD1_YEASTSWD1genetic
20093466
KIN3_YEASTKIN3genetic
20093466
MIX23_YEASTMIX23genetic
20093466
RTG3_YEASTRTG3genetic
20093466
SCS22_YEASTSCS22genetic
20093466
TREB_YEASTNTH2genetic
20093466
TYDP1_YEASTTDP1genetic
20093466
ADY3_YEASTADY3genetic
20093466
AIR2_YEASTAIR2genetic
20093466
GDIR_YEASTRDI1genetic
20093466
RXT3_YEASTRXT3genetic
20093466
VPS41_YEASTVPS41genetic
20093466
SPO71_YEASTSPO71genetic
20093466
RPA14_YEASTRPA14genetic
20093466
SHE9_YEASTSHE9genetic
20093466
CLG1_YEASTCLG1genetic
20093466
RCK1_YEASTRCK1genetic
20093466
ECT1_YEASTECT1genetic
20093466
NAM8_YEASTNAM8genetic
20093466
IF4A_YEASTTIF2genetic
20093466
GYP6_YEASTGYP6genetic
20093466
RAD26_YEASTRAD26genetic
20093466
YJ66_YEASTYJR096Wgenetic
20093466
YJ9S_YEASTYJR154Wgenetic
20093466
DCOR_YEASTSPE1genetic
20093466
MEH1_YEASTMEH1genetic
20093466
IF1A_YEASTTIF11genetic
17332751
IF2A_YEASTSUI2physical
16990799
SUI1_YEASTSUI1physical
16990799
EIF3B_YEASTPRT1physical
16990799
EI2BE_YEASTGCD6physical
16990799
IF2G_YEASTGCD11physical
16990799
RS22A_YEASTRPS22Aphysical
16990799
SUI1_YEASTSUI1genetic
21930786
EIF3C_YEASTNIP1physical
22718758
RCK1_YEASTRCK1genetic
22282571
IF2G_YEASTGCD11physical
21745818
IF2A_YEASTSUI2physical
21745818
EIF3B_YEASTPRT1physical
21745818
SUI1_YEASTSUI1physical
21745818
EI2BE_YEASTGCD6genetic
21745818
SUI1_YEASTSUI1physical
24335188
IF2A_YEASTSUI2physical
24352424
RS5_YEASTRPS5genetic
26134896
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of IF5_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-170; THR-187; SER-190;THR-191; SER-211; THR-212; SER-228; SER-243; THR-317 AND SER-397, ANDMASS 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-184; THR-187; SER-189;SER-190 AND THR-191, AND MASS SPECTROMETRY.
"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 THR-191 AND SER-397, ANDMASS SPECTROMETRY.
"Phosphoproteome analysis by mass spectrometry and its application toSaccharomyces cerevisiae.";
Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M.,Shabanowitz J., Hunt D.F., White F.M.;
Nat. Biotechnol. 20:301-305(2002).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-397, AND MASSSPECTROMETRY.

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