EIF3G_YEAST - dbPTM
EIF3G_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EIF3G_YEAST
UniProt AC Q04067
Protein Name Eukaryotic translation initiation factor 3 subunit G {ECO:0000255|HAMAP-Rule:MF_03006}
Gene Name TIF35 {ECO:0000255|HAMAP-Rule:MF_03006}
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 274
Subcellular Localization Cytoplasm .
Protein Description RNA-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation (Potential). Binds to the 18S rRNA but non-specifically. [PubMed: 10085088]
Protein Sequence MSEVAPEEIIENADGSRSIITYKIEDGVKYKITQKVKEVKVLEKVHKSVAERKNWHKYGSEKGSPAGPSAVTARLGEEVELRLSRNWKQAEEERIQKEKASLTKTGLQCRLCGNDHMTMNCPFKTILSELSALEDPATNEGGVEAASEEKAGQVGGAGSIPGQYVPPSRRAGARDPSSDAYRDSRERDDMCTLKIMQVNENADENSLREELLFPFAPIPRVSVVRNKETGKSRGLAFVTFSSEEVAEQALRFLDGRGYMNLILRVEWSKPKVKE
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------MSEVAPEEI
------CCCCCHHHH		40.5522814378
2Phosphorylation------MSEVAPEEI
------CCCCCHHHH		40.5522369663
23AcetylationSRSIITYKIEDGVKY
CCEEEEEEECCCCEE		30.8524489116
29AcetylationYKIEDGVKYKITQKV
EEECCCCEEEEEECC		46.4824489116
44AcetylationKEVKVLEKVHKSVAE
CHHHHHHHHHHHHHH		45.5425381059
57UbiquitinationAERKNWHKYGSEKGS
HHHCCHHHHCCCCCC		42.8122817900
58PhosphorylationERKNWHKYGSEKGSP
HHCCHHHHCCCCCCC		17.0127214570
60PhosphorylationKNWHKYGSEKGSPAG
CCHHHHCCCCCCCCC		32.8025752575
62AcetylationWHKYGSEKGSPAGPS
HHHHCCCCCCCCCCC		67.4025381059
62UbiquitinationWHKYGSEKGSPAGPS
HHHHCCCCCCCCCCC		67.4023749301
64PhosphorylationKYGSEKGSPAGPSAV
HHCCCCCCCCCCCHH		23.7322369663
69PhosphorylationKGSPAGPSAVTARLG
CCCCCCCCHHHHHCC		34.1629688323
72PhosphorylationPAGPSAVTARLGEEV
CCCCCHHHHHCCCEE		13.0429688323
104UbiquitinationKEKASLTKTGLQCRL
HHHHHHHHHCCEEEE		45.9823749301
125PhosphorylationTMNCPFKTILSELSA
CCCCCHHHHHHHHHH		27.7730377154
128PhosphorylationCPFKTILSELSALED
CCHHHHHHHHHHCCC		32.4230377154
131PhosphorylationKTILSELSALEDPAT
HHHHHHHHHCCCCCC		27.1028889911
147PhosphorylationEGGVEAASEEKAGQV
CCCCCCCCHHHCCCC		54.0228152593
159PhosphorylationGQVGGAGSIPGQYVP
CCCCCCCCCCCCCCC		25.6928152593
168PhosphorylationPGQYVPPSRRAGARD
CCCCCCHHHCCCCCC		28.4723749301
177PhosphorylationRAGARDPSSDAYRDS
CCCCCCCCCHHHCCH		45.1829136822
178PhosphorylationAGARDPSSDAYRDSR
CCCCCCCCHHHCCHH		31.4829136822
184PhosphorylationSSDAYRDSRERDDMC
CCHHHCCHHHHHCCC		27.3528889911
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 EIF3G_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EIF3G_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 EIF3G_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DED1_YEASTDED1physical
14759368
EIF3C_YEASTNIP1physical
14759368
EIF3B_YEASTPRT1physical
14759368
EIF3J_YEASTHCR1physical
14759368
EIF3A_YEASTRPG1physical
14759368
EIF3I_YEASTTIF34physical
14759368
EIF3G_YEASTTIF35physical
14759368
GNA1_YEASTGNA1physical
10688190
EIF3I_YEASTTIF34physical
9660829
EIF3B_YEASTPRT1physical
11179233
EIF3B_YEASTPRT1physical
9660829
CLU_YEASTCLU1physical
10358023
IF4B_YEASTTIF3physical
10358023
EIF3I_YEASTTIF34physical
9362495
EIF3A_YEASTRPG1physical
11179233
EIF3I_YEASTTIF34physical
11179233
EIF3J_YEASTHCR1physical
11179233
IF2G_YEASTGCD11physical
11179233
EIF3I_YEASTTIF34physical
16554755
EIF3C_YEASTNIP1physical
16554755
EIF3B_YEASTPRT1physical
16554755
IF2P_YEASTFUN12physical
16429126
IF2G_YEASTGCD11physical
16429126
EIF3J_YEASTHCR1physical
16429126
EIF3C_YEASTNIP1physical
16429126
RLI1_YEASTRLI1physical
16429126
EIF3A_YEASTRPG1physical
16429126
RS11A_YEASTRPS11Aphysical
16429126
RS11B_YEASTRPS11Aphysical
16429126
RS17A_YEASTRPS17Aphysical
16429126
RS22A_YEASTRPS22Aphysical
16429126
RS7A_YEASTRPS7Aphysical
16429126
RS8A_YEASTRPS8Aphysical
16429126
RS8B_YEASTRPS8Aphysical
16429126
EIF3I_YEASTTIF34physical
16429126
IF5_YEASTTIF5physical
16429126
RS22B_YEASTRPS22Bphysical
16429126
DED1_YEASTDED1physical
16429126
RS3A2_YEASTRPS1Bphysical
16429126
EIF3B_YEASTPRT1physical
16429126
RS10B_YEASTRPS10Bphysical
16429126
RS5_YEASTRPS5physical
16429126
SUI1_YEASTSUI1physical
16429126
RIC1_YEASTRIC1genetic
19061648
RU1C_YEASTYHC1genetic
19061648
NOT2_YEASTCDC36genetic
19061648
RRP8_YEASTRRP8genetic
19061648
POP7_YEASTPOP7genetic
19061648
RS6A_YEASTRPS6Bgenetic
19061648
RS6B_YEASTRPS6Bgenetic
19061648
MUD2_YEASTMUD2genetic
19061648
NU120_YEASTNUP120genetic
19061648
H2AZ_YEASTHTZ1genetic
19061648
SNU66_YEASTSNU66genetic
19061648
NCBP1_YEASTSTO1genetic
19061648
SWM2_YEASTSWM2genetic
19061648
MEX67_YEASTMEX67genetic
19061648
TGS1_YEASTTGS1genetic
19061648
PRP19_YEASTPRP19genetic
19061648
NRP1_YEASTNRP1genetic
19061648
FBRL_YEASTNOP1genetic
19061648
EF1A_YEASTTEF2genetic
19061648
CSE1_YEASTCSE1genetic
19061648
MAK11_YEASTMAK11genetic
19061648
PAP2_YEASTPAP2genetic
19061648
NOP15_YEASTNOP15genetic
19061648
SYNC_YEASTDED81genetic
19061648
EIF3I_YEASTTIF34physical
20679478
EIF3B_YEASTPRT1physical
20679478
EIF3A_YEASTRPG1physical
20679478
IF2G_YEASTGCD11physical
20679478
IF5A1_YEASTHYP2physical
20679478
RS3_YEASTRPS3physical
20679478
RS20_YEASTRPS20physical
20679478
SUI1_YEASTSUI1genetic
20679478
IF1A_YEASTTIF11genetic
20679478
EIF3B_YEASTPRT1physical
22090426
EIF3I_YEASTTIF34physical
22090426
ERF1_YEASTSUP45physical
24278036
NOP14_YEASTNOP14genetic
27708008
KRE9_YEASTKRE9genetic
27708008
CDC91_YEASTGAB1genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of EIF3G_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-60; SER-64; SER-131;SER-159 AND SER-168, 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-64, AND MASSSPECTROMETRY.

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