EIF2A_YEAST - dbPTM
EIF2A_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EIF2A_YEAST
UniProt AC P53235
Protein Name Eukaryotic translation initiation factor 2A
Gene Name YGR054W
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 642
Subcellular Localization
Protein Description Functions in the early steps of protein synthesis of a small number of specific mRNAs. Acts by directing the binding of methionyl-tRNAi to 40S ribosomal subunits. In contrast to the eIF-2 complex, it binds methionyl-tRNAi to 40S subunits in a codon-dependent manner, whereas the eIF-2 complex binds methionyl-tRNAi to 40S subunits in a GTP-dependent manner. Specifically associates with both 40S subunits and 80S ribosomes..
Protein Sequence MSSQFFLKTSQDIELFQSYPTFEQSNTNSKDFPVISSVLSPCGRFLALSTKENVKVFTGPCLDNVLLTMKLSDVYDLHFSPAGNYLSTWERASIQDPNHKNVKVWYLNKPFKKDCVSEDIVPAYEYQAKSQSGWFLQFSKLDNYGLRLFKHDLKIVKLSSANADNFDFQSPFAVLSDDETSQHFTTYLISPAEHPTICTFTPEKGGKPAQLIIWALSEGKITKKIASKTFFKADSCQLKWNPLGNAILCLAITDFDSSNKSYYGENTLYLLSFQGVNGTLGGNSVRVSLTTGPVHDFTWSPTSRQFGVIAGYMPATISFFDLRGNVVHSLPQQAKNTMLFSPSGHYILIAGFGNLQGSVEILDRLDKFKCVSKFDATNTSVCKWSPGGEFIMTATTSPRLRVDNGVKIWHVSGSLVFVKEFKELLKVDWRSPCNYKTLENKDEAFFENHIINNWEPLPDSTTSSLDPKISNKSELQIHSSVQEYISQHPSREASSNGNGSKAKAGGAYKPPHARRTGGGRIVPGVPPGAAKKTIPGLVPGMSANKDANTKNRRRRANKKSSETSPDSTPAPSAPASTNAPTNNKETSPEEKKIRSLLKKLRAIETLKERQAVGDKLEDTQVLKIQTEEKVLKDLEKLGWKDE
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
50PhosphorylationGRFLALSTKENVKVF
CCEEEEECCCCEEEE		43.1327017623
51AcetylationRFLALSTKENVKVFT
CEEEEECCCCEEEEE		43.8724489116
55UbiquitinationLSTKENVKVFTGPCL
EECCCCEEEEECCCH		43.1223749301
109AcetylationVKVWYLNKPFKKDCV
EEEEEECCCCCCCCC		49.5922865919
112AcetylationWYLNKPFKKDCVSED
EEECCCCCCCCCCCC		57.1224489116
154AcetylationRLFKHDLKIVKLSSA
EEEECCEEEEECCCC		52.0625381059
227PhosphorylationKITKKIASKTFFKAD
CCCHHHHCCEEEECC		35.3819823750
229PhosphorylationTKKIASKTFFKADSC
CHHHHCCEEEECCCC		31.6319823750
235PhosphorylationKTFFKADSCQLKWNP
CEEEECCCCCCEECC		14.5019823750
300PhosphorylationPVHDFTWSPTSRQFG
CCCCCEECCCCCCCC		18.4223749301
302PhosphorylationHDFTWSPTSRQFGVI
CCCEECCCCCCCCEE		30.9023749301
341PhosphorylationAKNTMLFSPSGHYIL
HCCEEEECCCCCEEE		17.7527017623
346PhosphorylationLFSPSGHYILIAGFG
EECCCCCEEEEEECC		10.8427017623
358PhosphorylationGFGNLQGSVEILDRL
ECCCCCCHHHHHHHH		12.0127017623
373AcetylationDKFKCVSKFDATNTS
HCCEEEECCCCCCCC		27.1925381059
383UbiquitinationATNTSVCKWSPGGEF
CCCCCEEEECCCCCE		48.8523749301
422AcetylationLVFVKEFKELLKVDW
EEEHHHHHHHHCCCC		48.8524489116
426AcetylationKEFKELLKVDWRSPC
HHHHHHHCCCCCCCC		51.2624489116
532AcetylationVPPGAAKKTIPGLVP
CCCCCCHHCCCCCCC		47.1325381059
542PhosphorylationPGLVPGMSANKDANT
CCCCCCCCCCCCCCH		34.3121440633
545AcetylationVPGMSANKDANTKNR
CCCCCCCCCCCHHHH		58.9124489116
560PhosphorylationRRRANKKSSETSPDS
HHHCHHCCCCCCCCC		34.7122369663
561PhosphorylationRRANKKSSETSPDST
HHCHHCCCCCCCCCC		54.4922369663
563PhosphorylationANKKSSETSPDSTPA
CHHCCCCCCCCCCCC		47.7322369663
564PhosphorylationNKKSSETSPDSTPAP
HHCCCCCCCCCCCCC		23.7425521595
567PhosphorylationSSETSPDSTPAPSAP
CCCCCCCCCCCCCCC		39.4122369663
568PhosphorylationSETSPDSTPAPSAPA
CCCCCCCCCCCCCCC		30.7422369663
572PhosphorylationPDSTPAPSAPASTNA
CCCCCCCCCCCCCCC		49.3322369663
576PhosphorylationPAPSAPASTNAPTNN
CCCCCCCCCCCCCCC		22.5722890988
577PhosphorylationAPSAPASTNAPTNNK
CCCCCCCCCCCCCCC		37.1922890988
581PhosphorylationPASTNAPTNNKETSP
CCCCCCCCCCCCCCH		49.3522890988
586PhosphorylationAPTNNKETSPEEKKI
CCCCCCCCCHHHHHH		51.7121440633
587PhosphorylationPTNNKETSPEEKKIR
CCCCCCCCHHHHHHH		31.2622369663
615AcetylationERQAVGDKLEDTQVL
HHHHHCCCCCCCCEE		48.0924489116
615UbiquitinationERQAVGDKLEDTQVL
HHHHHCCCCCCCCEE		48.0923749301
629AcetylationLKIQTEEKVLKDLEK
EEEECHHHHHHHHHH		46.7824489116
636AcetylationKVLKDLEKLGWKDE-
HHHHHHHHCCCCCC-		60.6424489116
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 EIF2A_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EIF2A_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 EIF2A_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NOP3_YEASTNPL3physical
11805837
H2B2_YEASTHTB2physical
11805837
NAT10_YEASTKRE33physical
11805837
IF4E_YEASTCDC33genetic
15718232
EIF2A_YEASTYGR054Wphysical
18467557
BRE5_YEASTBRE5physical
18467557
GIS2_YEASTGIS2physical
18467557
NAP1_YEASTNAP1physical
18467557
CAF20_YEASTCAF20physical
18467557
DED1_YEASTDED1physical
18467557
LSP1_YEASTLSP1physical
18467557
IF4A_YEASTTIF2genetic
19061648
PFD6_YEASTYKE2genetic
19547744
PABP_YEASTPAB1physical
21915340
XRN1_YEASTXRN1physical
21915340
SSB2_YEASTSSB2physical
21915340
DED1_YEASTDED1physical
21915340
RL15B_YEASTRPL15Bphysical
21915340
RS4A_YEASTRPS4Aphysical
21915340
RS4B_YEASTRPS4Aphysical
21915340
RL3_YEASTRPL3physical
21915340
RS8A_YEASTRPS8Aphysical
21915340
RS8B_YEASTRPS8Aphysical
21915340
RL4B_YEASTRPL4Bphysical
21915340
RL7A_YEASTRPL7Aphysical
21915340
RL1A_YEASTRPL1Bphysical
21915340
RL1B_YEASTRPL1Bphysical
21915340
EIF2A_YEASTYGR054Wphysical
22615397
STU1_YEASTSTU1genetic
27708008
EIF3A_YEASTRPG1genetic
27708008
CDC37_YEASTCDC37genetic
27708008
ERF3_YEASTSUP35genetic
27708008
GPI8_YEASTGPI8genetic
27708008
GPI17_YEASTGPI17genetic
27708008
PSB3_YEASTPUP3genetic
27708008
MOB2_YEASTMOB2genetic
27708008
ACT_YEASTACT1genetic
27708008
CDC91_YEASTGAB1genetic
27708008
PROF_YEASTPFY1genetic
27708008
DED1_YEASTDED1genetic
27708008
SYA_YEASTALA1genetic
27708008
EIF3B_YEASTPRT1genetic
27708008
PSA7_YEASTPRE10genetic
27708008
RLA4_YEASTRPP2Bgenetic
27708008
AIM11_YEASTAIM11genetic
27708008
IES1_YEASTIES1genetic
27708008
XRN1_YEASTXRN1genetic
27708008
IF4A_YEASTTIF2genetic
27708008
ALAM_YEASTALT1genetic
27708008
RL37A_YEASTRPL37Agenetic
27708008
VPS38_YEASTVPS38genetic
27708008
NST1_YEASTNST1genetic
27708008
PFD4_YEASTGIM3genetic
27708008
TOP1_YEASTTOP1genetic
27708008
NOP12_YEASTNOP12genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of EIF2A_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-560; SER-561; THR-563;SER-564 AND THR-568, 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-560; SER-561; THR-563;SER-564 AND SER-567, 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-564, AND MASSSPECTROMETRY.

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