IF2B_YEAST - dbPTM
IF2B_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID IF2B_YEAST
UniProt AC P09064
Protein Name Eukaryotic translation initiation factor 2 subunit beta
Gene Name SUI3
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 285
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 MSSDLAAELGFDPALKKKKKTKKVIPDDFDAAVNGKENGSGDDLFAGLKKKKKKSKSVSADAEAEKEPTDDIAEALGELSLKKKKKKTKDSSVDAFEKELAKAGLDNVDAESKEGTPSANSSIQQEVGLPYSELLSRFFNILRTNNPELAGDRSGPKFRIPPPVCLRDGKKTIFSNIQDIAEKLHRSPEHLIQYLFAELGTSGSVDGQKRLVIKGKFQSKQMENVLRRYILEYVTCKTCKSINTELKREQSNRLFFMVCKSCGSTRSVSSIKTGFQATVGKRRRM
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------MSSDLAAEL
------CCHHHHHHH		32.3422369663
3Phosphorylation-----MSSDLAAELG
-----CCHHHHHHHC		35.0322369663
36UbiquitinationFDAAVNGKENGSGDD
CHHHHCCCCCCCCCC		42.6824961812
40PhosphorylationVNGKENGSGDDLFAG
HCCCCCCCCCCCHHH		51.1022369663
49UbiquitinationDDLFAGLKKKKKKSK
CCCHHHHHHHCCCCC		62.7224961812
49AcetylationDDLFAGLKKKKKKSK
CCCHHHHHHHCCCCC		62.7224489116
49SuccinylationDDLFAGLKKKKKKSK
CCCHHHHHHHCCCCC		62.7223954790
50UbiquitinationDLFAGLKKKKKKSKS
CCHHHHHHHCCCCCC		74.9124961812
50AcetylationDLFAGLKKKKKKSKS
CCHHHHHHHCCCCCC		74.9124489116
55PhosphorylationLKKKKKKSKSVSADA
HHHHCCCCCCCCCCH		38.7621440633
56UbiquitinationKKKKKKSKSVSADAE
HHHCCCCCCCCCCHH		64.8524961812
57PhosphorylationKKKKKSKSVSADAEA
HHCCCCCCCCCCHHH		28.5322369663
59PhosphorylationKKKSKSVSADAEAEK
CCCCCCCCCCHHHHC		27.7622369663
66AcetylationSADAEAEKEPTDDIA
CCCHHHHCCCCHHHH		75.8524489116
66UbiquitinationSADAEAEKEPTDDIA
CCCHHHHCCCCHHHH		75.8524961812
69PhosphorylationAEAEKEPTDDIAEAL
HHHHCCCCHHHHHHH		47.6022369663
80PhosphorylationAEALGELSLKKKKKK
HHHHHHHCCCCCCCC		33.5622369663
82AcetylationALGELSLKKKKKKTK
HHHHHCCCCCCCCCC		60.2024489116
82UbiquitinationALGELSLKKKKKKTK
HHHHHCCCCCCCCCC		60.2024961812
88PhosphorylationLKKKKKKTKDSSVDA
CCCCCCCCCCCHHHH		49.3028889911
89AcetylationKKKKKKTKDSSVDAF
CCCCCCCCCCHHHHH		65.5724489116
91PhosphorylationKKKKTKDSSVDAFEK
CCCCCCCCHHHHHHH		33.5421082442
92PhosphorylationKKKTKDSSVDAFEKE
CCCCCCCHHHHHHHH		33.8625521595
98UbiquitinationSSVDAFEKELAKAGL
CHHHHHHHHHHHCCC		52.1224961812
98AcetylationSSVDAFEKELAKAGL
CHHHHHHHHHHHCCC		52.1224489116
102UbiquitinationAFEKELAKAGLDNVD
HHHHHHHHCCCCCCC		56.4623749301
102AcetylationAFEKELAKAGLDNVD
HHHHHHHHCCCCCCC		56.4624489116
112PhosphorylationLDNVDAESKEGTPSA
CCCCCCCCCCCCCCC		37.4122369663
113UbiquitinationDNVDAESKEGTPSAN
CCCCCCCCCCCCCCC		52.2324961812
116PhosphorylationDAESKEGTPSANSSI
CCCCCCCCCCCCHHH		18.3722369663
118PhosphorylationESKEGTPSANSSIQQ
CCCCCCCCCCHHHHH		39.6622369663
121PhosphorylationEGTPSANSSIQQEVG
CCCCCCCHHHHHHHC		28.6522369663
122PhosphorylationGTPSANSSIQQEVGL
CCCCCCHHHHHHHCC		24.9922890988
131PhosphorylationQQEVGLPYSELLSRF
HHHHCCCHHHHHHHH		21.5922890988
132PhosphorylationQEVGLPYSELLSRFF
HHHCCCHHHHHHHHH		21.5922890988
136PhosphorylationLPYSELLSRFFNILR
CCHHHHHHHHHHHHH		39.4022890988
154PhosphorylationPELAGDRSGPKFRIP
HHHCCCCCCCCCCCC		65.2723749301
157UbiquitinationAGDRSGPKFRIPPPV
CCCCCCCCCCCCCCE		51.2924961812
183AcetylationNIQDIAEKLHRSPEH
HHHHHHHHHCCCHHH		40.3424489116
220AcetylationIKGKFQSKQMENVLR
EEEECCHHHHHHHHH		42.7724489116
241PhosphorylationVTCKTCKSINTELKR
HHHHHCCHHCHHHHH		24.1827017623
251PhosphorylationTELKREQSNRLFFMV
HHHHHHHCCCEEEEE		21.1117287358
260UbiquitinationRLFFMVCKSCGSTRS
CEEEEEECCCCCCCC		37.0524961812
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 IF2B_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of IF2B_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 IF2B_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
EIF3B_YEASTPRT1physical
11018020
IF5_YEASTTIF5physical
11018020
IF5_YEASTTIF5physical
10075937
EI2BE_YEASTGCD6physical
10075937
IF5_YEASTTIF5physical
15964804
IF2G_YEASTGCD11physical
15964804
SUI1_YEASTSUI1physical
15377664
IF2G_YEASTGCD11physical
10769173
IF2B_YEASTSUI3physical
16522633
IF2G_YEASTGCD11physical
16522633
IF5_YEASTTIF5physical
16522633
EI2BE_YEASTGCD6physical
16522633
IF2A_YEASTSUI2physical
16522633
IF5A1_YEASTHYP2physical
17974565
SUI1_YEASTSUI1physical
17974565
IF4F2_YEASTTIF4632genetic
20463023
EI2BE_YEASTGCD6physical
20805354
EI2BB_YEASTGCD7physical
20805354
EI2BG_YEASTGCD1physical
20805354
EI2BA_YEASTGCN3physical
20805354
IF2G_YEASTGCD11physical
20805354
IF2A_YEASTSUI2physical
20805354
EI2BD_YEASTGCD2physical
20805354
IF1A_YEASTTIF11genetic
17332751
SUI1_YEASTSUI1genetic
21930786
IF1A_YEASTTIF11genetic
21930786
PKH1_YEASTPKH1physical
22326914
IF5_YEASTTIF5physical
22683627
EI2BE_YEASTGCD6physical
22683627
IF5_YEASTTIF5physical
21745818
IF2A_YEASTSUI2physical
21745818
EIF3B_YEASTPRT1physical
21745818
BZW2_HUMANBZW2physical
21745818
IF2G_YEASTGCD11physical
23775072
RS8A_YEASTRPS8Agenetic
27708008
RS8B_YEASTRPS8Agenetic
27708008
MUM2_YEASTMUM2genetic
27708008
SAC3_YEASTSAC3genetic
27708008
SEM1_YEASTSEM1genetic
27708008
UBP6_YEASTUBP6genetic
27708008
NPR3_YEASTNPR3genetic
27708008
RPA34_YEASTRPA34genetic
27708008
DAS1_YEASTDAS1genetic
27708008
TCTP_YEASTTMA19genetic
27708008
CTK1_YEASTCTK1genetic
27708008
DOA1_YEASTDOA1genetic
27708008
SRP40_YEASTSRP40genetic
27708008
RL8B_YEASTRPL8Bgenetic
27708008
EOS1_YEASTEOS1genetic
27708008
EIF3A_YEASTRPG1genetic
27708008
CDC1_YEASTCDC1genetic
27708008
TCPZ_YEASTCCT6genetic
27708008
RPB7_YEASTRPB7genetic
27708008
RCC1_YEASTSRM1genetic
27708008
XPO1_YEASTCRM1genetic
27708008
MED6_YEASTMED6genetic
27708008
CDC12_YEASTCDC12genetic
27708008
SMC3_YEASTSMC3genetic
27708008
GWT1_YEASTGWT1genetic
27708008
KRE9_YEASTKRE9genetic
27708008
IF2A_YEASTSUI2genetic
27708008
KTHY_YEASTCDC8genetic
27708008
UGPA1_YEASTUGP1genetic
27708008
SEC13_YEASTSEC13genetic
27708008
CD123_YEASTCDC123genetic
27708008
EI2BB_YEASTGCD7genetic
27708008
TAD3_YEASTTAD3genetic
27708008
CDC91_YEASTGAB1genetic
27708008
TEM1_YEASTTEM1genetic
27708008
PDS5_YEASTPDS5genetic
27708008
CBF3B_YEASTCEP3genetic
27708008
TRM6_YEASTGCD10genetic
27708008
RPC6_YEASTRPC34genetic
27708008
DED1_YEASTDED1genetic
27708008
EI2BG_YEASTGCD1genetic
27708008
ARP7_YEASTARP7genetic
27708008
NU170_YEASTNUP170genetic
27708008
CSG2_YEASTCSG2genetic
27708008
PHO87_YEASTPHO87genetic
27708008
PER1_YEASTPER1genetic
27708008
PAT1_YEASTPAT1genetic
27708008
TPS2_YEASTTPS2genetic
27708008
ARO1_YEASTARO1genetic
27708008
UME6_YEASTUME6genetic
27708008
LSM6_YEASTLSM6genetic
27708008
SNF1_YEASTSNF1genetic
27708008
STL1_YEASTSTL1genetic
27708008
UBP3_YEASTUBP3genetic
27708008
AAKG_YEASTSNF4genetic
27708008
AROC_YEASTARO2genetic
27708008
XRN1_YEASTXRN1genetic
27708008
CTU1_YEASTNCS6genetic
27708008
UBA4_YEASTUBA4genetic
27708008
STB5_YEASTSTB5genetic
27708008
URM1_YEASTURM1genetic
27708008
LSM1_YEASTLSM1genetic
27708008
IF4A_YEASTTIF2genetic
27708008
MDHM_YEASTMDH1genetic
27708008
XPOT_YEASTLOS1genetic
27708008
MEH1_YEASTMEH1genetic
27708008
EI2BA_YEASTGCN3genetic
27708008
BAS1_YEASTBAS1genetic
27708008
SDHB_YEASTSDH2genetic
27708008
METK1_YEASTSAM1genetic
27708008
SEC72_YEASTSEC72genetic
27708008
PPZ1_YEASTPPZ1genetic
27708008
NU188_YEASTNUP188genetic
27708008
GTR1_YEASTGTR1genetic
27708008
MUB1_YEASTMUB1genetic
27708008
UBP8_YEASTUBP8genetic
27708008
CTU2_YEASTNCS2genetic
27708008
BRE5_YEASTBRE5genetic
27708008
GSHB_YEASTGSH2genetic
27708008
RTG1_YEASTRTG1genetic
27708008
SDHF2_YEASTSDH5genetic
27708008
SYC1_YEASTSYC1genetic
27708008
GSP2_YEASTGSP2genetic
27708008
YME1_YEASTYME1genetic
27708008
IF2G_YEASTGCD11physical
12137565
RS5_YEASTRPS5genetic
26134896
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of IF2B_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-2; SER-40; SER-59;THR-69; SER-80; SER-91; SER-92; SER-112; THR-116 AND SER-118, AND MASSSPECTROMETRY.
"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-40; SER-92; SER-112 ANDTHR-116, 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-251, 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-40 AND SER-112, AND MASSSPECTROMETRY.

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