IF4F2_YEAST - dbPTM
IF4F2_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID IF4F2_YEAST
UniProt AC P39936
Protein Name Eukaryotic initiation factor 4F subunit p130
Gene Name TIF4632
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 914
Subcellular Localization Cytoplasm .
Protein Description Component of the eIF4F complex, which interacts with the mRNA cap structure and serves as an initial point of assembly for the translation apparatus. Stimulates translation by interaction with polyadenylate-binding protein PAB1, bringing the 5'- and 3'-ends of the mRNA in proximity. The formation of this circular mRNP structure appears to be critical for the synergistic effects of the cap and the poly(A) tail in facilitating translation initiation, recycling of ribosomes, and mRNA stability. TIF4632 is probably essential when TIF4631 is missing..
Protein Sequence MTDQRGPPPPHPQQANGYKKFPPHDNQYSGANNSQPNNHYNENLYSAREPHNNKQYQSKNGKYGTNKYNNRNNSQGNAQYYNNRFNNGYRLNNNDYNPAMLPGMQWPANYYAPQMYYIPQQMVPVASPPYTHQPLNTNPEPPSTPKTTKIEITTKTGERLNLKKFHEEKKASKGEEKNDGVEQKSKSGTPFEKEATPVLPANEAVKDTLTETSNEKSTSEAENTKRLFLEQVRLRKAAMERKKNGLISETEKKQETSNHDNTDTTKPNSVIESEPIKEAPKPTGEANEVVIDGKSGASVKTPQHVTGSVTKSVTFNEPENESSSQDVDELVKDDDTTEISDTTGGKTVNKSDDETINSVITTEENTVKETEPSTSDIEMPTVSQLLETLGKAQPISDIYEFAYPENVERPDIKYKKPSVKYTYGPTFLLQFKDKLKFRPDPAWVEAVSSKIVIPPHIARNKPKDSGRFGGDFRSPSMRGMDHTSSSRVSSKRRSKRMGDDRRSNRGYTSRKDREKAAEKAEEQAPKEEIAPLVPSANRWIPKSRVKKTEKKLAPDGKTELFDKEEVERKMKSLLNKLTLEMFDSISSEILDIANQSKWEDDGETLKIVIEQIFHKACDEPHWSSMYAQLCGKVVKDLDPNIKDKENEGKNGPKLVLHYLVARCHEEFEKGWADKLPAGEDGNPLEPEMMSDEYYIAAAAKRRGLGLVRFIGYLYCLNLLTGKMMFECFRRLMKDLNNDPSEETLESVIELLNTVGEQFEHDKFVTPQATLEGSVLLDNLFMLLQHIIDGGTISNRIKFKLIDVKELREIKHWNSAKKDAGPKTIQQIHQEEEQLRQKKNSQRSNSRFNNHNQSNSNRYSSNRRNMQNTQRDSFASTKTGSFRNNQRNARKVEEVSQAPRANMFDALMNNDGDSD
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
67AcetylationNGKYGTNKYNNRNNS
CCCCCCCCCCCCCCC		49.5525381059
74PhosphorylationKYNNRNNSQGNAQYY
CCCCCCCCCCCHHHC		42.9122369663
155AcetylationTKIEITTKTGERLNL
CEEEEEECCCCCCCH		45.9725381059
185PhosphorylationNDGVEQKSKSGTPFE
CCCCCCCCCCCCCCC		31.5724961812
187PhosphorylationGVEQKSKSGTPFEKE
CCCCCCCCCCCCCCC		55.8028889911
189PhosphorylationEQKSKSGTPFEKEAT
CCCCCCCCCCCCCCC		31.7125752575
193AcetylationKSGTPFEKEATPVLP
CCCCCCCCCCCCCCC		53.6924489116
196PhosphorylationTPFEKEATPVLPANE
CCCCCCCCCCCCCCH		18.2822369663
208PhosphorylationANEAVKDTLTETSNE
CCHHHHHHHHHCCCC		29.8422369663
210PhosphorylationEAVKDTLTETSNEKS
HHHHHHHHHCCCCCC		39.0322369663
212PhosphorylationVKDTLTETSNEKSTS
HHHHHHHCCCCCCCC		31.4522369663
218PhosphorylationETSNEKSTSEAENTK
HCCCCCCCCHHHHHH		41.4728889911
248PhosphorylationRKKNGLISETEKKQE
HHHCCCCCCCHHCCC		43.4330377154
256PhosphorylationETEKKQETSNHDNTD
CCHHCCCCCCCCCCC		32.1329136822
257PhosphorylationTEKKQETSNHDNTDT
CHHCCCCCCCCCCCC		31.2629136822
262PhosphorylationETSNHDNTDTTKPNS
CCCCCCCCCCCCCCC		40.5629136822
264PhosphorylationSNHDNTDTTKPNSVI
CCCCCCCCCCCCCCC		34.3821440633
265PhosphorylationNHDNTDTTKPNSVIE
CCCCCCCCCCCCCCC		47.5229136822
269PhosphorylationTDTTKPNSVIESEPI
CCCCCCCCCCCCCCC		32.7621440633
301PhosphorylationKSGASVKTPQHVTGS
CCCCCCCCCCCCCEE		26.4817330950
306PhosphorylationVKTPQHVTGSVTKSV
CCCCCCCCEEEEEEE		22.9328132839
308PhosphorylationTPQHVTGSVTKSVTF
CCCCCCEEEEEEEEC		19.7621440633
310PhosphorylationQHVTGSVTKSVTFNE
CCCCEEEEEEEECCC		21.2121440633
312PhosphorylationVTGSVTKSVTFNEPE
CCEEEEEEEECCCCC		19.6122369663
314PhosphorylationGSVTKSVTFNEPENE
EEEEEEEECCCCCCC		28.0320377248
322PhosphorylationFNEPENESSSQDVDE
CCCCCCCCCCCCHHH		47.0422369663
323PhosphorylationNEPENESSSQDVDEL
CCCCCCCCCCCHHHH		26.3222369663
324PhosphorylationEPENESSSQDVDELV
CCCCCCCCCCHHHHH		39.4120377248
336PhosphorylationELVKDDDTTEISDTT
HHHCCCCCCEEECCC		33.0724961812
337PhosphorylationLVKDDDTTEISDTTG
HHCCCCCCEEECCCC		38.0121551504
340PhosphorylationDDDTTEISDTTGGKT
CCCCCEEECCCCCCE		23.7528889911
342PhosphorylationDTTEISDTTGGKTVN
CCCEEECCCCCCEEC		22.1321551504
343PhosphorylationTTEISDTTGGKTVNK
CCEEECCCCCCEECC		49.2624961812
347PhosphorylationSDTTGGKTVNKSDDE
ECCCCCCEECCCCCC		32.3625521595
351PhosphorylationGGKTVNKSDDETINS
CCCEECCCCCCCCCC		45.1222369663
355PhosphorylationVNKSDDETINSVITT
ECCCCCCCCCCEEEC		32.2425521595
358PhosphorylationSDDETINSVITTEEN
CCCCCCCCEEECCCC		15.8522890988
361PhosphorylationETINSVITTEENTVK
CCCCCEEECCCCCCC		26.4622890988
362PhosphorylationTINSVITTEENTVKE
CCCCEEECCCCCCCC		30.1222890988
366PhosphorylationVITTEENTVKETEPS
EEECCCCCCCCCCCC		35.9122890988
375PhosphorylationKETEPSTSDIEMPTV
CCCCCCCCCCCCCHH		40.7121440633
474PhosphorylationRFGGDFRSPSMRGMD
CCCCCCCCHHHCCCC		22.7120377248
476PhosphorylationGGDFRSPSMRGMDHT
CCCCCCHHHCCCCCC		23.5120377248
483PhosphorylationSMRGMDHTSSSRVSS
HHCCCCCCCCCCCCC		26.4920377248
484PhosphorylationMRGMDHTSSSRVSSK
HCCCCCCCCCCCCCH		23.9320377248
485PhosphorylationRGMDHTSSSRVSSKR
CCCCCCCCCCCCCHH		24.2620377248
486PhosphorylationGMDHTSSSRVSSKRR
CCCCCCCCCCCCHHH		36.1520377248
489PhosphorylationHTSSSRVSSKRRSKR
CCCCCCCCCHHHHHH		29.0920377248
490PhosphorylationTSSSRVSSKRRSKRM
CCCCCCCCHHHHHHC		27.5920377248
503PhosphorylationRMGDDRRSNRGYTSR
HCCCCHHHCCCCCCH		31.6017287358
508PhosphorylationRRSNRGYTSRKDREK
HHHCCCCCCHHHHHH		25.5317287358
509PhosphorylationRSNRGYTSRKDREKA
HHCCCCCCHHHHHHH		28.9317287358
653AcetylationNEGKNGPKLVLHYLV
CCCCCCHHHHHHHHH		53.2624489116
799AcetylationISNRIKFKLIDVKEL
CCCCEEEEEECHHHH		39.2624489116
843PhosphorylationQKKNSQRSNSRFNNH
HHHHHHHHHHHHCCC		31.3628889911
845PhosphorylationKNSQRSNSRFNNHNQ
HHHHHHHHHHCCCCC		39.2225005228
853PhosphorylationRFNNHNQSNSNRYSS
HHCCCCCCCCCHHHH		47.7624603354
855PhosphorylationNNHNQSNSNRYSSNR
CCCCCCCCCHHHHHH		28.1224909858
859PhosphorylationQSNSNRYSSNRRNMQ
CCCCCHHHHHHHHCC		20.2125005228
860PhosphorylationSNSNRYSSNRRNMQN
CCCCHHHHHHHHCCH		25.9725005228
868PhosphorylationNRRNMQNTQRDSFAS
HHHHCCHHHHHCCHH		14.2123749301
872PhosphorylationMQNTQRDSFASTKTG
CCHHHHHCCHHHHCC		25.5424909858
878PhosphorylationDSFASTKTGSFRNNQ
HCCHHHHCCCHHCCH		37.8424961812
880PhosphorylationFASTKTGSFRNNQRN
CHHHHCCCHHCCHHH		26.6824961812
895PhosphorylationARKVEEVSQAPRANM
HCHHHHHHHCCCHHH		24.7321551504
913PhosphorylationLMNNDGDSD------
HHCCCCCCC------		51.2322369663
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 IF4F2_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of IF4F2_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 IF4F2_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SUI1_YEASTSUI1physical
12861028
IF5_YEASTTIF5physical
12861028
SUI1_YEASTSUI1physical
15145951
PABP_YEASTPAB1physical
10357826
PABP_YEASTPAB1physical
9418852
PABP_YEASTPAB1physical
9256432
SGN1_YEASTSGN1genetic
10764794
IF4F1_YEASTTIF4631genetic
8336723
IF4A_YEASTTIF2genetic
10409745
CAF20_YEASTCAF20genetic
9372919
IF4E_YEASTCDC33genetic
10409745
FBRL_YEASTNOP1physical
16554755
NAB2_YEASTNAB2physical
16554755
IF4A_YEASTTIF2physical
16554755
IF4E_YEASTCDC33physical
16554755
PABP_YEASTPAB1physical
16429126
IF4E_YEASTCDC33physical
16429126
H4_YEASTHHF1physical
16429126
PABP_YEASTPAB1physical
9003792
DED1_YEASTDED1physical
18467557
PUB1_YEASTPUB1physical
18467557
GFD1_YEASTGFD1physical
18467557
HPR1_YEASTHPR1genetic
19061648
SAC3_YEASTSAC3genetic
19061648
PFD5_YEASTGIM5genetic
19061648
CSI1_YEASTCSI1genetic
19061648
IF4E_YEASTCDC33genetic
20463023
IF4A_YEASTTIF2genetic
20463023
SCD6_YEASTSCD6physical
22284680
NOP3_YEASTNPL3physical
22284680
SSBP1_YEASTSBP1physical
22284680
DED1_YEASTDED1physical
22615397
GIS2_YEASTGIS2physical
23285195
IF4B_YEASTTIF3genetic
23184954
IF4B_YEASTTIF3physical
23184954
IF4E_YEASTCDC33physical
23184954
CDK1_YEASTCDC28genetic
27708008
ACT_YEASTACT1genetic
27708008
EXO70_YEASTEXO70genetic
27708008
SSL1_YEASTSSL1genetic
27708008
RU1C_YEASTYHC1genetic
27708008
SC61A_YEASTSEC61genetic
27708008
LST8_YEASTLST8genetic
27708008
TYSY_YEASTCDC21genetic
27708008
MAK16_YEASTMAK16genetic
27708008
MAK5_YEASTMAK5genetic
27708008
TECR_YEASTTSC13genetic
27708008
LCB2_YEASTLCB2genetic
27708008
SC61G_YEASTSSS1genetic
27708008
DOP1_YEASTDOP1genetic
27708008
SEC7_YEASTSEC7genetic
27708008
KGUA_YEASTGUK1genetic
27708008
TSC11_YEASTTSC11genetic
27708008
CDC14_YEASTCDC14genetic
27708008
STT3_YEASTSTT3genetic
27708008
PRP31_YEASTPRP31genetic
27708008
NUP57_YEASTNUP57genetic
27708008
KTHY_YEASTCDC8genetic
27708008
YJ9I_YEASTYJR141Wgenetic
27708008
SYFB_YEASTFRS1genetic
27708008
SEC22_YEASTSEC22genetic
27708008
SMC6_YEASTSMC6genetic
27708008
ARP9_YEASTARP9genetic
27708008
LCB1_YEASTLCB1genetic
27708008
SEC62_YEASTSEC62genetic
27708008
RL36A_YEASTRPL36Agenetic
29158977
DOM34_YEASTDOM34genetic
29158977
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of IF4F2_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 THR-196; THR-314; THR-347AND SER-351, 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 THR-196; THR-347 ANDSER-351, 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-503; THR-508 ANDSER-509, 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 THR-301 AND SER-913, ANDMASS SPECTROMETRY.

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