MBF1_YEAST - dbPTM
MBF1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MBF1_YEAST
UniProt AC O14467
Protein Name Multiprotein-bridging factor 1
Gene Name MBF1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 151
Subcellular Localization Cytoplasm . Nucleus .
Protein Description Transcriptional coactivator that stimulates GCN4-dependent transcriptional activity by bridging the DNA-binding region of GCN4 and TBP (SPT15), thereby recruiting TBP to GCN4-bound promoters..
Protein Sequence MSDWDTNTIIGSRARAGGSGPRANVARSQGQINAARRQGLVVSVDKKYGSTNTRGDNEGQRLTKVDRETDIVKPKKLDPNVGRAISRARTDKKMSQKDLATKINEKPTVVNDYEAARAIPNQQVLSKLERALGVKLRGNNIGSPLGAPKKK
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------MSDWDTNTI
------CCCCCCCCC		47.6224909858
6Phosphorylation--MSDWDTNTIIGSR
--CCCCCCCCCCCCC		29.9728889911
8PhosphorylationMSDWDTNTIIGSRAR
CCCCCCCCCCCCCCC		18.9624909858
12PhosphorylationDTNTIIGSRARAGGS
CCCCCCCCCCCCCCC		16.6224909858
19PhosphorylationSRARAGGSGPRANVA
CCCCCCCCCCCHHHH		44.7121440633
28PhosphorylationPRANVARSQGQINAA
CCHHHHHHHHCHHHH		29.0022369663
43PhosphorylationRRQGLVVSVDKKYGS
HHCCCEEEEEECCCC		19.6728889911
46AcetylationGLVVSVDKKYGSTNT
CCEEEEEECCCCCCC		45.8224489116
46UbiquitinationGLVVSVDKKYGSTNT
CCEEEEEECCCCCCC		45.8222817900
47AcetylationLVVSVDKKYGSTNTR
CEEEEEECCCCCCCC		50.8324489116
47UbiquitinationLVVSVDKKYGSTNTR
CEEEEEECCCCCCCC		50.8322817900
50PhosphorylationSVDKKYGSTNTRGDN
EEEECCCCCCCCCCC		18.5221440633
51PhosphorylationVDKKYGSTNTRGDNE
EEECCCCCCCCCCCH		35.9223749301
642-HydroxyisobutyrylationNEGQRLTKVDRETDI
CHHCCCCEECCCCCC		46.89-
64UbiquitinationNEGQRLTKVDRETDI
CHHCCCCEECCCCCC		46.8922817900
73AcetylationDRETDIVKPKKLDPN
CCCCCCCCCCCCCCC		51.9925381059
76AcetylationTDIVKPKKLDPNVGR
CCCCCCCCCCCCHHH		67.6525381059
92UbiquitinationISRARTDKKMSQKDL
HHHHHHCCCCCHHHH		50.1622817900
93UbiquitinationSRARTDKKMSQKDLA
HHHHHCCCCCHHHHH		46.7422817900
97UbiquitinationTDKKMSQKDLATKIN
HCCCCCHHHHHHHHH		47.6122817900
97AcetylationTDKKMSQKDLATKIN
HCCCCCHHHHHHHHH		47.6124489116
102AcetylationSQKDLATKINEKPTV
CHHHHHHHHHCCCCE		37.6224489116
106AcetylationLATKINEKPTVVNDY
HHHHHHCCCCEECHH		41.3124489116
106UbiquitinationLATKINEKPTVVNDY
HHHHHHCCCCEECHH		41.3123749301
108PhosphorylationTKINEKPTVVNDYEA
HHHHCCCCEECHHHH		48.4227214570
126PhosphorylationIPNQQVLSKLERALG
CCCHHHHHHHHHHHC		36.0222369663
127AcetylationPNQQVLSKLERALGV
CCHHHHHHHHHHHCC		50.6424489116
135AcetylationLERALGVKLRGNNIG
HHHHHCCCCCCCCCC		30.5725381059
143PhosphorylationLRGNNIGSPLGAPKK
CCCCCCCCCCCCCCC		17.1022369663
149AcetylationGSPLGAPKKK-----
CCCCCCCCCC-----		73.0725381059
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 MBF1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MBF1_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 MBF1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GCN4_YEASTGCN4physical
9710580
TBP_YEASTSPT15physical
9710580
SAC3_YEASTSAC3genetic
19547744
UBP3_YEASTUBP3genetic
19547744
TBP_YEASTSPT15physical
17440176
RRP6_YEASTRRP6genetic
20959818
THP2_YEASTTHP2genetic
20959818
RDR1_YEASTRDR1genetic
20959818
SEC22_YEASTSEC22genetic
20959818
ENV11_YEASTENV11genetic
20959818
DOT6_YEASTDOT6genetic
20959818
HMO1_YEASTHMO1genetic
20959818
VMS1_YEASTVMS1genetic
20959818
GLN3_YEASTGLN3genetic
20959818
SAC3_YEASTSAC3genetic
20959818
SEM1_YEASTSEM1genetic
20959818
SIF2_YEASTSIF2genetic
20959818
IES1_YEASTIES1genetic
20959818
UBP3_YEASTUBP3genetic
20959818
IES3_YEASTIES3genetic
21127252
RTG1_YEASTRTG1genetic
21127252
CHA4_YEASTCHA4genetic
21127252
KAPA_YEASTTPK1genetic
21127252
MKK1_YEASTMKK1genetic
21127252
HRK1_YEASTHRK1genetic
21127252
BUB1_YEASTBUB1genetic
21127252
ATG8_YEASTATG8genetic
27708008
SGF29_YEASTSGF29genetic
27708008
MBP1_YEASTMBP1genetic
27708008
GNTK_YEASTYDR248Cgenetic
27708008
HRQ1_YEASTHRQ1genetic
27708008
YG37_YEASTYGR127Wgenetic
27708008
QCR9_YEASTQCR9genetic
27708008
YG51_YEASTYGR237Cgenetic
27708008
YIF5_YEASTYIL055Cgenetic
27708008
MDL1_YEASTMDL1genetic
27708008
PEX13_YEASTPEX13genetic
27708008
YL194_YEASTYLR194Cgenetic
27708008
PIG1_YEASTPIG1genetic
27708008
YM14_YEASTYMR130Wgenetic
27708008
DYN3_YEASTDYN3genetic
27708008
YNE6_YEASTYNL046Wgenetic
27708008
DMA2_YEASTDMA2genetic
27708008
ADE_YEASTAAH1genetic
27708008
HIR1_YEASTHIR1genetic
27708008
FMT_YEASTFMT1genetic
27708008
YBF9_YEASTYBL059Wgenetic
27708008
OLA1_YEASTOLA1genetic
27708008
AIM4_YEASTAIM4genetic
27708008
MTU1_YEASTSLM3genetic
27708008
MCH1_YEASTMCH1genetic
27708008
RLA1_YEASTRPP1Agenetic
27708008
VMS1_YEASTVMS1genetic
27708008
YD179_YEASTYDR179W-Agenetic
27708008
HPRT_YEASTHPT1genetic
27708008
CP56_YEASTDIT2genetic
27708008
DIT1_YEASTDIT1genetic
27708008
RGD2_YEASTRGD2genetic
27708008
YFF4_YEASTYFL054Cgenetic
27708008
YG036_YEASTYGL036Wgenetic
27708008
PYC1_YEASTPYC1genetic
27708008
RTG2_YEASTRTG2genetic
27708008
VPS62_YEASTVPS62genetic
27708008
HTD2_YEASTHTD2genetic
27708008
GGA2_YEASTGGA2genetic
27708008
LAM1_YEASTYSP1genetic
27708008
ATG7_YEASTATG7genetic
27708008
YIF4_YEASTYIL054Wgenetic
27708008
VHR1_YEASTVHR1genetic
27708008
SGN1_YEASTSGN1genetic
27708008
SDHX_YEASTYJL045Wgenetic
27708008
IME2_YEASTIME2genetic
27708008
DPOD3_YEASTPOL32genetic
27708008
MRT4_YEASTMRT4genetic
27708008
FABG_YEASTOAR1genetic
27708008
BCH2_YEASTBCH2genetic
27708008
MLP1_YEASTMLP1genetic
27708008
BAS1_YEASTBAS1genetic
27708008
MMM1_YEASTMMM1genetic
27708008
ATG10_YEASTATG10genetic
27708008
RSSA2_YEASTRPS0Bgenetic
27708008
SRN2_YEASTSRN2genetic
27708008
YL287_YEASTYLR287Cgenetic
27708008
GLRX8_YEASTGRX8genetic
27708008
ART10_YEASTART10genetic
27708008
RCF1_YEASTRCF1genetic
27708008
ATR1_YEASTATR1genetic
27708008
MSC1_YEASTMSC1genetic
27708008
CTF18_YEASTCTF18genetic
27708008
DDR48_YEASTDDR48genetic
27708008
ECM5_YEASTECM5genetic
27708008
CUE1_YEASTCUE1genetic
27708008
MAS5_YEASTYDJ1genetic
27708008
RNH2A_YEASTRNH201genetic
27708008
YO13A_YEASTYOL013W-Agenetic
27708008
MDM38_YEASTMDM38genetic
27708008
SIL1_YEASTSIL1genetic
27708008
PEX15_YEASTPEX15genetic
27708008
HMI1_YEASTHMI1genetic
27708008
HSP7F_YEASTSSE1genetic
27708008
ODC1_YEASTODC1genetic
27708008
KIP2_YEASTKIP2genetic
27708008
CG12_YEASTCLN2genetic
27708008
MLC2_YEASTMLC2genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MBF1_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-108 AND SER-143, ANDMASS 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-143, AND MASSSPECTROMETRY.
"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-143, 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-143, AND MASSSPECTROMETRY.
"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-143, AND MASSSPECTROMETRY.

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