IF4B_YEAST - dbPTM
IF4B_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID IF4B_YEAST
UniProt AC P34167
Protein Name Eukaryotic translation initiation factor 4B
Gene Name TIF3
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 436
Subcellular Localization
Protein Description Involved in translation initiation. May be the homolog of mammalian eIF4B and be part of an RNA helicase. STM1/TIF3 is a non-essential gene..
Protein Sequence MAPPKKTVKKMDLTSFLNDDTFGSSWAEEDVDLNKITIPIETANANTIPLSELAHAKNNSNNTRSGGFGGSFGGRSRLDPALGGGSSDRREEYPVPDAPPYRAVINNIPWDITPEGVQAWVEDGLVKPEAVEEVVLPKNLRDPTRLKGNAFVTLKERADLVAVLKFNGTKLNERTVYVSVAAPRRGGGADVDWSSARGSNFQGDGREDAPDLDWGAARGSNFRGPRREREEVDIDWTAARGSNFQGSSRPPRREREEVDIDWSAARGSNFQGSSRPPRREREEPDIDWSAARGSNFQSSSRPPRREREEPDIDWSAARGSNFQSSSRPPRREREKEEPALDWGAARGAQFGKPQQTKNTYKDRSLTNKKTTDEQPKIQKSVYDVLRTEDDDEDEEAEKQNGDAKENKVDAAVEKLQDKTAQLTVEDGDNWEVVGKK
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
14PhosphorylationTVKKMDLTSFLNDDT
CCCCCCHHHHHCCCC		17.1130377154
15PhosphorylationVKKMDLTSFLNDDTF
CCCCCHHHHHCCCCC		34.7330377154
24PhosphorylationLNDDTFGSSWAEEDV
HCCCCCCCCCCCCCC		20.6530377154
25PhosphorylationNDDTFGSSWAEEDVD
CCCCCCCCCCCCCCC		30.5921440633
47PhosphorylationIETANANTIPLSELA
EEECCCCCCCHHHHH		22.8921551504
51PhosphorylationNANTIPLSELAHAKN
CCCCCCHHHHHHHHC		25.8021440633
57UbiquitinationLSELAHAKNNSNNTR
HHHHHHHHCCCCCCC		46.9624961812
65PhosphorylationNNSNNTRSGGFGGSF
CCCCCCCCCCCCCCC		41.0322369663
71PhosphorylationRSGGFGGSFGGRSRL
CCCCCCCCCCCCCCC		22.5422369663
76PhosphorylationGGSFGGRSRLDPALG
CCCCCCCCCCCCCCC		40.2330377154
86PhosphorylationDPALGGGSSDRREEY
CCCCCCCCCCCCCCC		32.1328889911
87PhosphorylationPALGGGSSDRREEYP
CCCCCCCCCCCCCCC		38.1128889911
153PhosphorylationLKGNAFVTLKERADL
CCCCEEEEEHHHCCE		26.1724909858
155AcetylationGNAFVTLKERADLVA
CCEEEEEHHHCCEEE		35.4722865919
155SuccinylationGNAFVTLKERADLVA
CCEEEEEHHHCCEEE		35.4723954790
165AcetylationADLVAVLKFNGTKLN
CCEEEEEEECCEECC		30.1324489116
175PhosphorylationGTKLNERTVYVSVAA
CEECCCCEEEEEEEC		15.2621440633
194PhosphorylationGGADVDWSSARGSNF
CCCCCCHHHCCCCCC		15.0630377154
195PhosphorylationGADVDWSSARGSNFQ
CCCCCHHHCCCCCCC		20.1028889911
199PhosphorylationDWSSARGSNFQGDGR
CHHHCCCCCCCCCCC		28.9923749301
242PhosphorylationDWTAARGSNFQGSSR
CCHHHCCCCCCCCCC		28.9928889911
247PhosphorylationRGSNFQGSSRPPRRE
CCCCCCCCCCCCCCC		16.6428132839
248PhosphorylationGSNFQGSSRPPRRER
CCCCCCCCCCCCCCC		56.4828132839
263PhosphorylationEEVDIDWSAARGSNF
CEECCCHHHHCCCCC		14.3330377154
289PhosphorylationEEPDIDWSAARGSNF
CCCCCCHHHHCCCCC		14.3328889911
294PhosphorylationDWSAARGSNFQSSSR
CHHHHCCCCCCCCCC		28.9928889911
298PhosphorylationARGSNFQSSSRPPRR
HCCCCCCCCCCCCCC		26.5828889911
299PhosphorylationRGSNFQSSSRPPRRE
CCCCCCCCCCCCCCC		21.4228132839
300PhosphorylationGSNFQSSSRPPRRER
CCCCCCCCCCCCCCC		54.7923749301
315PhosphorylationEEPDIDWSAARGSNF
CCCCCCHHHHCCCCC		14.3328889911
320PhosphorylationDWSAARGSNFQSSSR
CHHHHCCCCCCCCCC		28.9928889911
324PhosphorylationARGSNFQSSSRPPRR
HCCCCCCCCCCCCCC		26.5828889911
326PhosphorylationGSNFQSSSRPPRRER
CCCCCCCCCCCCCHH		54.7923749301
335AcetylationPPRREREKEEPALDW
CCCCHHHCCCCCHHH		73.8624489116
352AcetylationARGAQFGKPQQTKNT
HHCCCCCCCCCCCCC		40.7325381059
357AcetylationFGKPQQTKNTYKDRS
CCCCCCCCCCCCCCC		42.8425381059
364PhosphorylationKNTYKDRSLTNKKTT
CCCCCCCCCCCCCCC		50.0719823750
366PhosphorylationTYKDRSLTNKKTTDE
CCCCCCCCCCCCCCC		46.3619823750
370PhosphorylationRSLTNKKTTDEQPKI
CCCCCCCCCCCCCHH		40.8821440633
371PhosphorylationSLTNKKTTDEQPKIQ
CCCCCCCCCCCCHHH		46.5519823750
376AcetylationKTTDEQPKIQKSVYD
CCCCCCCHHHHHHHH		58.4225381059
376UbiquitinationKTTDEQPKIQKSVYD
CCCCCCCHHHHHHHH		58.4223749301
379AcetylationDEQPKIQKSVYDVLR
CCCCHHHHHHHHHHC		45.4124489116
380PhosphorylationEQPKIQKSVYDVLRT
CCCHHHHHHHHHHCC		14.9928889911
387PhosphorylationSVYDVLRTEDDDEDE
HHHHHHCCCCCCHHH		39.3422369663
398AcetylationDEDEEAEKQNGDAKE
CHHHHHHHHHCCHHH		56.9924489116
398UbiquitinationDEDEEAEKQNGDAKE
CHHHHHHHHHCCHHH		56.9923749301
414AcetylationKVDAAVEKLQDKTAQ
HHHHHHHHHCCCCCE		44.8624489116
423PhosphorylationQDKTAQLTVEDGDNW
CCCCCEEEEECCCCC		15.1230377154
435AcetylationDNWEVVGKK------
CCCEEECCC------		43.6424489116
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 IF4B_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of IF4B_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 IF4B_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
IF4E_YEASTCDC33genetic
9144215
CAF20_YEASTCAF20genetic
9144215
APQ12_YEASTAPQ12genetic
19061648
AEP3_YEASTAEP3genetic
19061648
EAF3_YEASTEAF3genetic
19061648
PUF2_YEASTPUF2genetic
19061648
EF1A_YEASTTEF2genetic
19061648
SAP30_YEASTSAP30genetic
19061648
CHD1_YEASTCHD1genetic
19061648
SSB2_YEASTSSB2physical
19536198
HSP71_YEASTSSA1physical
19536198
SSB1_YEASTSSB1physical
19536198
SRS2_YEASTSRS2genetic
21459050
DED1_YEASTDED1genetic
9144215
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of IF4B_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-65; SER-71 AND THR-370,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-71, AND MASSSPECTROMETRY.

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