MBP1_YEAST - dbPTM
MBP1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MBP1_YEAST
UniProt AC P39678
Protein Name Transcription factor MBP1
Gene Name MBP1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 833
Subcellular Localization Nucleus.
Protein Description Binds to MCB elements (Mlu I cell cycle box) found in the promoter of most DNA synthesis genes. Transcriptional activation by MBF has an important role in the transition from G1 to S phase. It may have a dual role in that it behaves as an activator of transcription at the G1-S boundary and as a repressor during other stages of the cell cycle..
Protein Sequence MSNQIYSARYSGVDVYEFIHSTGSIMKRKKDDWVNATHILKAANFAKAKRTRILEKEVLKETHEKVQGGFGKYQGTWVPLNIAKQLAEKFSVYDQLKPLFDFTQTDGSASPPPAPKHHHASKVDRKKAIRSASTSAIMETKRNNKKAEENQFQSSKILGNPTAAPRKRGRPVGSTRGSRRKLGVNLQRSQSDMGFPRPAIPNSSISTTQLPSIRSTMGPQSPTLGILEEERHDSRQQQPQQNNSAQFKEIDLEDGLSSDVEPSQQLQQVFNQNTGFVPQQQSSLIQTQQTESMATSVSSSPSLPTSPGDFADSNPFEERFPGGGTSPIISMIPRYPVTSRPQTSDINDKVNKYLSKLVDYFISNEMKSNKSLPQVLLHPPPHSAPYIDAPIDPELHTAFHWACSMGNLPIAEALYEAGTSIRSTNSQGQTPLMRSSLFHNSYTRRTFPRIFQLLHETVFDIDSQSQTVIHHIVKRKSTTPSAVYYLDVVLSKIKDFSPQYRIELLLNTQDKNGDTALHIASKNGDVVFFNTLVKMGALTTISNKEGLTANEIMNQQYEQMMIQNGTNQHVNSSNTDLNIHVNTNNIETKNDVNSMVIMSPVSPSDYITYPSQIATNISRNIPNVVNSMKQMASIYNDLHEQHDNEIKSLQKTLKSISKTKIQVSLKTLEVLKESSKDENGEAQTNDDFEILSRLQEQNTKKLRKRLIRYKRLIKQKLEYRQTVLLNKLIEDETQATTNNTVEKDNNTLERLELAQELTMLQLQRKNKLSSLVKKFEDNAKIHKYRRIIREGTEMNIEEVDSSLDVILQTLIANNNKNKGAEQIITISNANSHA
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
10PhosphorylationNQIYSARYSGVDVYE
CCCEEECCCCCCHHH		14.9730377154
11PhosphorylationQIYSARYSGVDVYEF
CCEEECCCCCCHHHH		27.1330377154
37PhosphorylationKDDWVNATHILKAAN
CCCCCCHHHHHHHHH		12.3025521595
41UbiquitinationVNATHILKAANFAKA
CCHHHHHHHHHHHHH		44.8715699485
56UbiquitinationKRTRILEKEVLKETH
HHHHHHHHHHHHHHH		50.0717644757
60UbiquitinationILEKEVLKETHEKVQ
HHHHHHHHHHHHHHC		66.7817644757
65UbiquitinationVLKETHEKVQGGFGK
HHHHHHHHHCCCCCC		32.0517644757
72UbiquitinationKVQGGFGKYQGTWVP
HHCCCCCCCCCEEEE		31.9417644757
89UbiquitinationIAKQLAEKFSVYDQL
HHHHHHHHCCHHHHC		37.0115699485
91PhosphorylationKQLAEKFSVYDQLKP
HHHHHHCCHHHHCHH		30.7322369663
93PhosphorylationLAEKFSVYDQLKPLF
HHHHCCHHHHCHHHC		9.2122369663
97UbiquitinationFSVYDQLKPLFDFTQ
CCHHHHCHHHCCCCC		33.7615699485
103PhosphorylationLKPLFDFTQTDGSAS
CHHHCCCCCCCCCCC		32.1922369663
105PhosphorylationPLFDFTQTDGSASPP
HHCCCCCCCCCCCCC		38.9922369663
108PhosphorylationDFTQTDGSASPPPAP
CCCCCCCCCCCCCCC		28.5120377248
110PhosphorylationTQTDGSASPPPAPKH
CCCCCCCCCCCCCCC		39.3722369663
131PhosphorylationDRKKAIRSASTSAIM
CHHHHHHHHHHHHHH		22.0622369663
133PhosphorylationKKAIRSASTSAIMET
HHHHHHHHHHHHHHH		24.9222369663
134PhosphorylationKAIRSASTSAIMETK
HHHHHHHHHHHHHHH		23.1522369663
135PhosphorylationAIRSASTSAIMETKR
HHHHHHHHHHHHHHH		17.1922369663
140PhosphorylationSTSAIMETKRNNKKA
HHHHHHHHHHHCHHH		20.2327717283
141AcetylationTSAIMETKRNNKKAE
HHHHHHHHHHCHHHH		39.5625381059
146AcetylationETKRNNKKAEENQFQ
HHHHHCHHHHHHHHC		64.2524489116
155PhosphorylationEENQFQSSKILGNPT
HHHHHCHHHHCCCCC		16.9730377154
156AcetylationENQFQSSKILGNPTA
HHHHCHHHHCCCCCC		47.3924489116
156UbiquitinationENQFQSSKILGNPTA
HHHHCHHHHCCCCCC		47.3915699485
167UbiquitinationNPTAAPRKRGRPVGS
CCCCCCCCCCCCCCC		59.1315699485
189PhosphorylationLGVNLQRSQSDMGFP
HCCCCCCCCCCCCCC		22.5222369663
191PhosphorylationVNLQRSQSDMGFPRP
CCCCCCCCCCCCCCC		30.7022369663
212PhosphorylationISTTQLPSIRSTMGP
CCCCCCCHHHHCCCC		38.9525752575
215PhosphorylationTQLPSIRSTMGPQSP
CCCCHHHHCCCCCCC		22.5228889911
216PhosphorylationQLPSIRSTMGPQSPT
CCCHHHHCCCCCCCC		19.1227017623
221PhosphorylationRSTMGPQSPTLGILE
HHCCCCCCCCCCCCC		24.0017330950
223PhosphorylationTMGPQSPTLGILEEE
CCCCCCCCCCCCCHH		42.7528889911
244PhosphorylationQQPQQNNSAQFKEID
HCCCCCCCHHCEEEC		30.8822369663
257PhosphorylationIDLEDGLSSDVEPSQ
ECCCCCCCCCCCHHH		29.9823810556
258PhosphorylationDLEDGLSSDVEPSQQ
CCCCCCCCCCCHHHH		51.2023810556
325PhosphorylationERFPGGGTSPIISMI
CCCCCCCCCCCHHCC		34.3123810556
326PhosphorylationRFPGGGTSPIISMIP
CCCCCCCCCCHHCCC		19.8525752575
330PhosphorylationGGTSPIISMIPRYPV
CCCCCCHHCCCCCCC		16.0428889911
339PhosphorylationIPRYPVTSRPQTSDI
CCCCCCCCCCCCCCC		42.0430377154
343PhosphorylationPVTSRPQTSDINDKV
CCCCCCCCCCCHHHH		30.9230377154
344PhosphorylationVTSRPQTSDINDKVN
CCCCCCCCCCHHHHH		31.1130377154
349AcetylationQTSDINDKVNKYLSK
CCCCCHHHHHHHHHH		43.1324489116
599PhosphorylationVNSMVIMSPVSPSDY
CCCEEEECCCCHHHH		15.8323749301
602PhosphorylationMVIMSPVSPSDYITY
EEEECCCCHHHHCCC		23.2823749301
604PhosphorylationIMSPVSPSDYITYPS
EECCCCHHHHCCCHH		35.2223810556
606PhosphorylationSPVSPSDYITYPSQI
CCCCHHHHCCCHHHH		10.2530377154
627PhosphorylationNIPNVVNSMKQMASI
CCHHHHHHHHHHHHH		18.7530377154
666AcetylationTKIQVSLKTLEVLKE
CCEEEEHHHHHHHHH		43.4922865919
727UbiquitinationRQTVLLNKLIEDETQ
HHHHHHHHHHCCCCC		51.3017644757
743UbiquitinationTTNNTVEKDNNTLER
CCCCCCCCCCCHHHH		62.5117644757
743AcetylationTTNNTVEKDNNTLER
CCCCCCCCCCCHHHH		62.5124489116
825PhosphorylationKGAEQIITISNANSH
CCCCEEEEEECCCCC		21.7130377154
827PhosphorylationAEQIITISNANSHA-
CCEEEEEECCCCCC-		22.6523810556
831PhosphorylationITISNANSHA-----
EEEECCCCCC-----		20.5523810556
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 MBP1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MBP1_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 MBP1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SWI6_YEASTSWI6physical
11805826
SWI6_YEASTSWI6physical
8649372
SWI4_YEASTSWI4genetic
8372350
SKN7_YEASTSKN7genetic
10512874
SWI6_YEASTSWI6physical
16554755
NRM1_YEASTNRM1physical
16916637
RPN4_YEASTRPN4genetic
17314980
NHP10_YEASTNHP10genetic
17314980
MSA1_YEASTMSA1physical
18160399
CKS1_YEASTCKS1genetic
19269370
YPD1_YEASTYPD1genetic
19269370
SWI4_YEASTSWI4genetic
19269370
2ABA_YEASTCDC55genetic
19269370
RPN10_YEASTRPN10genetic
19269370
HSL1_YEASTHSL1genetic
19269370
PFD4_YEASTGIM3genetic
19269370
STB1_YEASTSTB1genetic
18794370
BUB3_YEASTBUB3genetic
19547744
TBCA_YEASTRBL2genetic
19547744
SWI6_YEASTSWI6physical
19820714
AIM3_YEASTAIM3genetic
21035341
BUB1_YEASTBUB1genetic
20959818
RRP6_YEASTRRP6genetic
20959818
SWI4_YEASTSWI4genetic
20959818
UBP8_YEASTUBP8genetic
20959818
SODC_YEASTSOD1genetic
20959818
SGF73_YEASTSGF73genetic
20959818
UBP3_YEASTUBP3genetic
20959818
CG11_YEASTCLN1genetic
10545447
CG12_YEASTCLN2genetic
10545447
SWI4_YEASTSWI4genetic
10545447
SWI6_YEASTSWI6genetic
10512874
KPC1_YEASTPKC1genetic
10512874
SPO14_YEASTSPO14physical
22875988
SWI6_YEASTSWI6physical
23382076
NRM1_YEASTNRM1physical
23382076
NRM1_YEASTNRM1physical
23593391
SWI6_YEASTSWI6physical
23593391
SWI4_YEASTSWI4physical
23593391
SWI4_YEASTSWI4physical
23690630
BEM2_YEASTBEM2genetic
27708008
HSP26_YEASTHSP26genetic
27708008
MNN10_YEASTMNN10genetic
27708008
RV167_YEASTRVS167genetic
27708008
RL27B_YEASTRPL27Bgenetic
27708008
SWI4_YEASTSWI4genetic
27708008
RPN10_YEASTRPN10genetic
27708008
IMPX_YEASTIMP2genetic
27708008
RPA34_YEASTRPA34genetic
27708008
MOG1_YEASTMOG1genetic
27708008
HSL1_YEASTHSL1genetic
27708008
SIC1_YEASTSIC1genetic
27708008
PABC_YEASTABZ2genetic
27708008
SIN3_YEASTSIN3genetic
27708008
WHI5_YEASTWHI5genetic
26310445
BCK2_YEASTBCK2genetic
26310445
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MBP1_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-110; SER-133; SER-135;SER-191; SER-212; SER-221; SER-326; SER-602 AND SER-827, AND MASSSPECTROMETRY.
"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-191, AND MASSSPECTROMETRY.

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