EI2BE_YEAST - dbPTM
EI2BE_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EI2BE_YEAST
UniProt AC P32501
Protein Name Translation initiation factor eIF-2B subunit epsilon
Gene Name GCD6
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 712
Subcellular Localization
Protein Description Acts as a catalytic component of the translation initiation factor 2B (eIF2-B or GCD complex), which catalyzes the exchange of eukaryotic initiation factor 2 (eIF-2)-bound GDP for GTP and is regulated by phosphorylated eIF-2. It activates the synthesis of GCN4 in yeast under amino acid starvation conditions by suppressing the inhibitory effects of multiple AUG codons present in the leader of GCN4 mRNA. It may promote either repression or activation of GCN4 expression depending on amino acid availability. GCD6 and GCD7 repress GCN4 expression at the translational level by ensuring that ribosomes which have translated UORF1 will reinitiate at UORF2, -3, or -4 and thus fail to reach the GCN4 start site..
Protein Sequence MAGKKGQKKSGLGNHGKNSDMDVEDRLQAVVLTDSYETRFMPLTAVKPRCLLPLANVPLIEYTLEFLAKAGVHEVFLICSSHANQINDYIENSKWNLPWSPFKITTIMSPEARCTGDVMRDLDNRGIITGDFILVSGDVLTNIDFSKMLEFHKKMHLQDKDHISTMCLSKASTYPKTRTIEPAAFVLDKSTSRCIYYQDLPLPSSREKTSIQIDPELLDNVDEFVIRNDLIDCRIDICTSHVPLIFQENFDYQSLRTDFVKGVISSDILGKHIYAYLTDEYAVRVESWQTYDTISQDFLGRWCYPLVLDSNIQDDQTYSYESRHIYKEKDVVLAQSCKIGKCTAIGSGTKIGEGTKIENSVIGRNCQIGENIRIKNSFIWDDCIIGNNSIIDHSLIASNATLGSNVRLNDGCIIGFNVKIDDNMDLDRNTKISASPLKNAGSRMYDNESNEQFDQDLDDQTLAVSIVGDKGVGYIYESEVSDDEDSSTEACKEINTLSNQLDELYLSDDSISSATKKTKKRRTMSVNSIYTDREEIDSEFEDEDFEKEGIATVERAMENNHDLDTALLELNTLRMSMNVTYHEVRIATITALLRRVYHFIATQTLGPKDAVVKVFNQWGLLFKRQAFDEEEYIDLMNIIMEKIVEQSFDKPDLILFSALVSLYDNDIIEEDVIYKWWDNVSTDPRYDEVKKLTVKWVEWLQNADEESSSEEE
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
10PhosphorylationGKKGQKKSGLGNHGK
CCCCCCCCCCCCCCC		46.4130377154
19PhosphorylationLGNHGKNSDMDVEDR
CCCCCCCCCCCHHHH		37.4928889911
189AcetylationPAAFVLDKSTSRCIY
CCEEEEECCCCEEEE		52.0124489116
189UbiquitinationPAAFVLDKSTSRCIY
CCEEEEECCCCEEEE		52.0124961812
265PhosphorylationDFVKGVISSDILGKH
HHHHCCCCHHHHCHH		21.3930377154
266PhosphorylationFVKGVISSDILGKHI
HHHCCCCHHHHCHHH		19.9730377154
274PhosphorylationDILGKHIYAYLTDEY
HHHCHHHHEEECCCC		6.7430377154
278PhosphorylationKHIYAYLTDEYAVRV
HHHHEEECCCCEEEE		17.7030377154
281PhosphorylationYAYLTDEYAVRVESW
HEEECCCCEEEECCC		17.1330377154
338UbiquitinationVVLAQSCKIGKCTAI
EEEEECCEECCCEEE		60.7923749301
350UbiquitinationTAIGSGTKIGEGTKI
EEECCCCEECCCCEE		52.8423749301
356AcetylationTKIGEGTKIENSVIG
CEECCCCEEECCEEC		59.9024489116
356UbiquitinationTKIGEGTKIENSVIG
CEECCCCEEECCEEC		59.9023749301
404PhosphorylationASNATLGSNVRLNDG
CCCCCCCCCCEECCC		34.9528889911
435PhosphorylationRNTKISASPLKNAGS
CCCCCCCCCCCCCCC		24.7925521595
438UbiquitinationKISASPLKNAGSRMY
CCCCCCCCCCCCCCC		48.4023749301
445PhosphorylationKNAGSRMYDNESNEQ
CCCCCCCCCCCCCHH		17.9520377248
449PhosphorylationSRMYDNESNEQFDQD
CCCCCCCCCHHCCCC		52.5020377248
461PhosphorylationDQDLDDQTLAVSIVG
CCCCCCCEEEEEEEC		24.5527017623
465PhosphorylationDDQTLAVSIVGDKGV
CCCEEEEEEECCCCC		13.1220377248
474PhosphorylationVGDKGVGYIYESEVS
ECCCCCEEEEEEECC		9.6430377154
476PhosphorylationDKGVGYIYESEVSDD
CCCCEEEEEEECCCC		12.6220377248
478PhosphorylationGVGYIYESEVSDDED
CCEEEEEEECCCCCC		26.7322369663
481PhosphorylationYIYESEVSDDEDSST
EEEEEECCCCCCCCH		34.9822369663
486PhosphorylationEVSDDEDSSTEACKE
ECCCCCCCCHHHHHH		36.7920377248
487PhosphorylationVSDDEDSSTEACKEI
CCCCCCCCHHHHHHH		42.4620377248
488PhosphorylationSDDEDSSTEACKEIN
CCCCCCCHHHHHHHH		31.3929688323
496PhosphorylationEACKEINTLSNQLDE
HHHHHHHHHHHHHHH		36.9122890988
498PhosphorylationCKEINTLSNQLDELY
HHHHHHHHHHHHHHH		22.0822890988
505PhosphorylationSNQLDELYLSDDSIS
HHHHHHHHCCCCCCC		11.3422890988
507PhosphorylationQLDELYLSDDSISSA
HHHHHHCCCCCCCCC		26.3017330950
510PhosphorylationELYLSDDSISSATKK
HHHCCCCCCCCCCHH		29.3917330950
512PhosphorylationYLSDDSISSATKKTK
HCCCCCCCCCCHHHC		20.1917330950
513PhosphorylationLSDDSISSATKKTKK
CCCCCCCCCCHHHCC		37.9817330950
515PhosphorylationDDSISSATKKTKKRR
CCCCCCCCHHHCCCC		34.7122890988
523PhosphorylationKKTKKRRTMSVNSIY
HHHCCCCCCCCHHEE		20.1722369663
525PhosphorylationTKKRRTMSVNSIYTD
HCCCCCCCCHHEECC		19.9622369663
528PhosphorylationRRTMSVNSIYTDREE
CCCCCCHHEECCHHH		18.1522369663
530PhosphorylationTMSVNSIYTDREEID
CCCCHHEECCHHHHC		11.4722369663
531PhosphorylationMSVNSIYTDREEIDS
CCCHHEECCHHHHCH		27.2322369663
538PhosphorylationTDREEIDSEFEDEDF
CCHHHHCHHCCCHHH		50.2622369663
608AcetylationATQTLGPKDAVVKVF
HCCCCCCHHHHHHHH		57.4224489116
707PhosphorylationLQNADEESSSEEE--
HHCCCCCCCCCCC--		36.8010805739
708PhosphorylationQNADEESSSEEE---
HCCCCCCCCCCC---		45.0819795423
709PhosphorylationNADEESSSEEE----
CCCCCCCCCCC----		59.3019795423
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 EI2BE_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EI2BE_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 EI2BE_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
EI2BG_YEASTGCD1physical
14759368
IF2G_YEASTGCD11physical
14759368
ACT_YEASTACT1physical
14759368
EI2BD_YEASTGCD2physical
14759368
EI2BE_YEASTGCD6physical
14759368
EI2BB_YEASTGCD7physical
14759368
IF2B_YEASTSUI3physical
14759368
EI2BG_YEASTGCD1physical
11805826
IF2G_YEASTGCD11physical
11805826
EI2BD_YEASTGCD2physical
11805826
EI2BB_YEASTGCD7physical
11805826
EI2BA_YEASTGCN3physical
11805826
IF2A_YEASTSUI2physical
11805826
IF2B_YEASTSUI3physical
11805826
EI2BG_YEASTGCD1physical
10805739
EI2BD_YEASTGCD2physical
10805739
EI2BB_YEASTGCD7physical
10805739
EI2BA_YEASTGCN3physical
10805739
IF2A_YEASTSUI2physical
10805739
EI2BG_YEASTGCD1physical
7565788
EI2BB_YEASTGCD7physical
7565788
EI2BA_YEASTGCN3physical
7565788
IF2A_YEASTSUI2physical
8336705
IF2B_YEASTSUI3physical
8336705
EI2BD_YEASTGCD2physical
10852917
EI2BG_YEASTGCD1physical
10852917
EI2BB_YEASTGCD7physical
10852917
EI2BA_YEASTGCN3physical
10852917
EI2BA_YEASTGCN3physical
8336705
EI2BG_YEASTGCD1physical
8336705
EI2BD_YEASTGCD2physical
8336705
EI2BB_YEASTGCD7physical
8336705
SYKC_YEASTKRS1genetic
3329041
IF2G_YEASTGCD11physical
16554755
EI2BD_YEASTGCD2physical
16554755
IF2A_YEASTSUI2physical
16554755
EI2BA_YEASTGCN3physical
16554755
EI2BB_YEASTGCD7physical
16554755
EI2BG_YEASTGCD1physical
16554755
EI2BG_YEASTGCD1physical
16429126
IF2G_YEASTGCD11physical
16429126
EI2BD_YEASTGCD2physical
16429126
EI2BB_YEASTGCD7physical
16429126
EI2BA_YEASTGCN3physical
16429126
IF2A_YEASTSUI2physical
16429126
IF2B_YEASTSUI3physical
16429126
IF2A_YEASTSUI2physical
17526738
IF2B_YEASTSUI3physical
17526738
IF2G_YEASTGCD11physical
17526738
EI2BD_YEASTGCD2physical
20805354
EI2BB_YEASTGCD7physical
20805354
EI2BG_YEASTGCD1physical
20805354
EI2BA_YEASTGCN3physical
20805354
IF2G_YEASTGCD11physical
20805354
IF2A_YEASTSUI2physical
20805354
IF2B_YEASTSUI3physical
20805354
IF5_YEASTTIF5genetic
16990799
EI2BG_YEASTGCD1physical
22238343
MKAR_YEASTIFA38physical
23263984
EI2BB_YEASTGCD7physical
23263984
PP2C3_YEASTPTC3genetic
27708008
CTK1_YEASTCTK1genetic
27708008
PMS1_YEASTPMS1genetic
27708008
SYIC_YEASTILS1genetic
27708008
CKS1_YEASTCKS1genetic
27708008
APC11_YEASTAPC11genetic
27708008
RRP4_YEASTRRP4genetic
27708008
ARP4_YEASTARP4genetic
27708008
SEC22_YEASTSEC22genetic
27708008
NOP2_YEASTNOP2genetic
27708008
APC5_YEASTAPC5genetic
27708008
HIR1_YEASTHIR1genetic
27708008
MGR1_YEASTMGR1genetic
27708008
GPR1_YEASTGPR1genetic
27708008
MCH1_YEASTMCH1genetic
27708008
RL13A_YEASTRPL13Agenetic
27708008
YG1X_YEASTYGR050Cgenetic
27708008
RL8A_YEASTRPL8Agenetic
27708008
PIH1_YEASTPIH1genetic
27708008
BFA1_YEASTBFA1genetic
27708008
YJ90_YEASTYJR120Wgenetic
27708008
MMR1_YEASTMMR1genetic
27708008
ENT2_YEASTENT2genetic
27708008
MMS22_YEASTMMS22genetic
27708008
COX8_YEASTCOX8genetic
27708008
RL6B_YEASTRPL6Bgenetic
27708008
HRB1_YEASTHRB1genetic
27708008
MKS1_YEASTMKS1genetic
27708008
BRE5_YEASTBRE5genetic
27708008
HIR2_YEASTHIR2genetic
27708008
DIA2_YEASTDIA2genetic
27708008
WHI5_YEASTWHI5genetic
27708008
DGK1_YEASTDGK1genetic
27708008
HAP5_YEASTHAP5genetic
27708008
NCBP2_YEASTCBC2genetic
27708008
YME1_YEASTYME1genetic
27708008
CTF4_YEASTCTF4genetic
27708008
SUI1_YEASTSUI1physical
24335188
IF5_YEASTTIF5genetic
24352424
IF2A_YEASTSUI2physical
24352424
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of EI2BE_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-19; SER-404; SER-478;SER-481; SER-525 AND SER-538, 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 SER-478; SER-481 ANDSER-507, 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-435, AND MASSSPECTROMETRY.
"A proteomics approach to understanding protein ubiquitination.";
Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D.,Marsischky G., Roelofs J., Finley D., Gygi S.P.;
Nat. Biotechnol. 21:921-926(2003).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-538, AND MASSSPECTROMETRY.

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