IF2A_YEAST - dbPTM
IF2A_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID IF2A_YEAST
UniProt AC P20459
Protein Name Eukaryotic translation initiation factor 2 subunit alpha
Gene Name SUI2
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 304
Subcellular Localization
Protein Description eIF-2 functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA. This complex binds to a 40S ribosomal subunit, followed by mRNA binding to form a 43S preinitiation complex. Junction of the 60S ribosomal subunit to form the 80S initiation complex is preceded by hydrolysis of the GTP bound to eIF-2 and release of an eIF-2-GDP binary complex. In order for eIF-2 to recycle and catalyze another round of initiation, the GDP bound to eIF-2 must exchange with GTP by way of a reaction catalyzed by eIF-2B..
Protein Sequence MSTSHCRFYENKYPEIDDIVMVNVQQIAEMGAYVKLLEYDNIEGMILLSELSRRRIRSIQKLIRVGKNDVAVVLRVDKEKGYIDLSKRRVSSEDIIKCEEKYQKSKTVHSILRYCAEKFQIPLEELYKTIAWPLSRKFGHAYEAFKLSIIDETVWEGIEPPSKDVLDELKNYISKRLTPQAVKIRADVEVSCFSYEGIDAIKDALKSAEDMSTEQMQVKVKLVAAPLYVLTTQALDKQKGIEQLESAIEKITEVITKYGGVCNITMPPKAVTATEDAELQALLESKELDNRSDSEDDEDESDDE
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
49PhosphorylationIEGMILLSELSRRRI
CCHHHHHHHHHHHHH		32.8028889911
52PhosphorylationMILLSELSRRRIRSI
HHHHHHHHHHHHHHH		21.498798780
52UbiquitinationMILLSELSRRRIRSI
HHHHHHHHHHHHHHH		21.4920972266
58PhosphorylationLSRRRIRSIQKLIRV
HHHHHHHHHHHHHHC		27.3124961812
91PhosphorylationDLSKRRVSSEDIIKC
ECCCCCCCHHHHHHC		26.6327214570
92PhosphorylationLSKRRVSSEDIIKCE
CCCCCCCHHHHHHCH		36.1123749301
101AcetylationDIIKCEEKYQKSKTV
HHHHCHHHHHHCHHH		30.5924489116
118AcetylationILRYCAEKFQIPLEE
HHHHHHHHCCCCHHH		24.8424489116
127PhosphorylationQIPLEELYKTIAWPL
CCCHHHHHHHHHHHH		14.9019795423
137AcetylationIAWPLSRKFGHAYEA
HHHHHHHHHCCHHHH		52.9322865919
170AcetylationKDVLDELKNYISKRL
HHHHHHHHHHHHHCC		45.7324489116
183UbiquitinationRLTPQAVKIRADVEV
CCCCCCEEECCEEEE		29.5023749301
1832-HydroxyisobutyrylationRLTPQAVKIRADVEV
CCCCCCEEECCEEEE		29.50-
221UbiquitinationEQMQVKVKLVAAPLY
HHHHHHHHHHHHHHH		31.3723749301
221AcetylationEQMQVKVKLVAAPLY
HHHHHHHHHHHHHHH		31.3724489116
237UbiquitinationLTTQALDKQKGIEQL
HHHHHHHHHHCHHHH		55.5523749301
237AcetylationLTTQALDKQKGIEQL
HHHHHHHHHHCHHHH		55.5524489116
239AcetylationTQALDKQKGIEQLES
HHHHHHHHCHHHHHH		68.5424489116
246PhosphorylationKGIEQLESAIEKITE
HCHHHHHHHHHHHHH		43.0427017623
292PhosphorylationSKELDNRSDSEDDED
CCCCCCCCCCCCCCC		52.3119823750
294PhosphorylationELDNRSDSEDDEDES
CCCCCCCCCCCCCCC		44.1419823750
301PhosphorylationSEDDEDESDDE----
CCCCCCCCCCC----		63.7819823750
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
52SPhosphorylationKinaseGCN2P15442
Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
52SPhosphorylation

1739968
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 IF2A_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
EI2BG_YEASTGCD1physical
11805837
IF2B_YEASTSUI3physical
11805837
IF2G_YEASTGCD11physical
11805837
EI2BE_YEASTGCD6physical
11805837
THRC_YEASTTHR4physical
11805837
IF4E_YEASTCDC33physical
11805837
EI2BD_YEASTGCD2physical
11805837
FAL1_YEASTFAL1physical
11805837
IF4F1_YEASTTIF4631physical
11805837
IF4F2_YEASTTIF4632physical
11805837
IF4A_YEASTTIF2physical
11805837
EI2BA_YEASTGCN3physical
11805837
EI2BD_YEASTGCD2physical
9472020
EI2BA_YEASTGCN3physical
9472020
EI2BG_YEASTGCD1physical
9472020
EI2BG_YEASTGCD1physical
11438658
EI2BG_YEASTGCD1physical
8506384
IF2B_YEASTSUI3physical
8506384
EI2BD_YEASTGCD2physical
8506384
EI2BA_YEASTGCN3physical
8506384
IF2G_YEASTGCD11genetic
11333223
EI2BB_YEASTGCD7genetic
8035796
GCN2_YEASTGCN2genetic
8035796
EI2BA_YEASTGCN3genetic
8035796
RS31_YEASTRPS31genetic
9830035
EI2BA_YEASTGCN3physical
16554755
EI2BB_YEASTGCD7physical
16554755
IF2G_YEASTGCD11physical
18719252
BUD27_YEASTBUD27genetic
19387492
EI2BB_YEASTGCD7genetic
20805354
PKH1_YEASTPKH1physical
22326914
IF2B_YEASTSUI3physical
23193270
E2AK2_HUMANEIF2AK2genetic
21368187
IF2G_YEASTGCD11physical
23775072
MCM1_YEASTMCM1genetic
27708008
RS6A_YEASTRPS6Bgenetic
27708008
RS6B_YEASTRPS6Bgenetic
27708008
SWC5_YEASTSWC5genetic
27708008
KPC1_YEASTPKC1genetic
27708008
CDK1_YEASTCDC28genetic
27708008
POP7_YEASTPOP7genetic
27708008
RPC10_YEASTRPC11genetic
27708008
ERF3_YEASTSUP35genetic
27708008
PANK_YEASTCAB1genetic
27708008
CDC12_YEASTCDC12genetic
27708008
MOB1_YEASTMOB1genetic
27708008
PRS7_YEASTRPT1genetic
27708008
CD123_YEASTCDC123genetic
27708008
MED11_YEASTMED11genetic
27708008
RPC6_YEASTRPC34genetic
27708008
EI2BG_YEASTGCD1genetic
27708008
NU170_YEASTNUP170genetic
27708008
ETR1_YEASTETR1genetic
27708008
MUM2_YEASTMUM2genetic
27708008
YBY9_YEASTYBR139Wgenetic
27708008
ODPB_YEASTPDB1genetic
27708008
RV161_YEASTRVS161genetic
27708008
VAM6_YEASTVAM6genetic
27708008
PHO2_YEASTPHO2genetic
27708008
ATIF_YEASTINH1genetic
27708008
HOSC_YEASTLYS20genetic
27708008
YD183_YEASTYDL183Cgenetic
27708008
UME6_YEASTUME6genetic
27708008
WWM1_YEASTWWM1genetic
27708008
RTG2_YEASTRTG2genetic
27708008
ELP2_YEASTELP2genetic
27708008
STB5_YEASTSTB5genetic
27708008
ACA2_YEASTCST6genetic
27708008
GPP1_YEASTGPP1genetic
27708008
FABG_YEASTOAR1genetic
27708008
XPOT_YEASTLOS1genetic
27708008
EI2BA_YEASTGCN3genetic
27708008
BAS1_YEASTBAS1genetic
27708008
SWI6_YEASTSWI6genetic
27708008
UPS1_YEASTUPS1genetic
27708008
ELP1_YEASTIKI3genetic
27708008
NU188_YEASTNUP188genetic
27708008
MAC1_YEASTMAC1genetic
27708008
GBLP_YEASTASC1genetic
27708008
INP1_YEASTINP1genetic
27708008
IDH1_YEASTIDH1genetic
27708008
MAS5_YEASTYDJ1genetic
27708008
MKS1_YEASTMKS1genetic
27708008
RAS2_YEASTRAS2genetic
27708008
YNL5_YEASTYNL115Cgenetic
27708008
NRK1_YEASTNRK1genetic
27708008
SIN3_YEASTSIN3genetic
27708008
RTG1_YEASTRTG1genetic
27708008
BUB3_YEASTBUB3genetic
27708008
CSK2C_YEASTCKB2genetic
27708008
ELP3_YEASTELP3genetic
27708008
MGR2_YEASTMGR2genetic
27708008
ELP4_YEASTELP4genetic
27708008
BEM4_YEASTBEM4genetic
27708008
YME1_YEASTYME1genetic
27708008
OPY2_YEASTOPY2genetic
27708008
NAM7_YEASTNAM7genetic
27811238
GMCL1_HUMANGMCL1physical
27107014
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of IF2A_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-292; SER-294 ANDSER-301, AND MASS 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-292; SER-294 ANDSER-301, AND MASS SPECTROMETRY.
"Phosphorylation of initiation factor 2 alpha by protein kinase GCN2mediates gene-specific translational control of GCN4 in yeast.";
Dever T.E., Feng L., Wek R.C., Cigan A.M., Donahue T.F.,Hinnebusch A.G.;
Cell 68:585-596(1992).
Cited for: PHOSPHORYLATION AT SER-52 BY GCN2.

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