PSB1_YEAST - dbPTM
PSB1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PSB1_YEAST
UniProt AC P38624
Protein Name Proteasome subunit beta type-1
Gene Name PRE3
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 215
Subcellular Localization Cytoplasm. Nucleus.
Protein Description The proteasome degrades poly-ubiquitinated proteins in the cytoplasm and in the nucleus. It is essential for the regulated turnover of proteins and for the removal of misfolded proteins. The proteasome is a multicatalytic proteinase complex that is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. It has an ATP-dependent proteolytic activity. PRE3 and PRE4 are necessary for the peptidyl-glutamyl-peptide-hydrolyzing activity.; This subunit is necessary for the peptidylglutamyl-peptide hydrolyzing activity..
Protein Sequence MNGIQVDINRLKKGEVSLGTSIMAVTFKDGVILGADSRTTTGAYIANRVTDKLTRVHDKIWCCRSGSAADTQAIADIVQYHLELYTSQYGTPSTETAASVFKELCYENKDNLTAGIIVAGYDDKNKGEVYTIPLGGSVHKLPYAIAGSGSTFIYGYCDKNFRENMSKEETVDFIKHSLSQAIKWDGSSGGVIRMVVLTAAGVERLIFYPDEYEQL
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
1Acetylation-------MNGIQVDI
-------CCCEEEEH		7.1922814378
13UbiquitinationVDINRLKKGEVSLGT
EEHHHHCCCCCCCCC		36.8724961812
37PhosphorylationGVILGADSRTTTGAY
CEEEECCCCCCCCCH		40.7227214570
52UbiquitinationIANRVTDKLTRVHDK
HHHHHHHHCCCCCCE		11.6423749301
52AcetylationIANRVTDKLTRVHDK
HHHHHHHHCCCCCCE		11.6424489116
59UbiquitinationKLTRVHDKIWCCRSG
HCCCCCCEEEECCCC		37.2223749301
91PhosphorylationLYTSQYGTPSTETAA
HHHHCCCCCCHHHHH		7.6328889911
124UbiquitinationIVAGYDDKNKGEVYT
EEEEEECCCCCEEEE		16.9817644757
126UbiquitinationAGYDDKNKGEVYTIP
EEEECCCCCEEEEEE		2.3717644757
137PhosphorylationYTIPLGGSVHKLPYA
EEEECCCEEEECCEE		28.4030377154
140UbiquitinationPLGGSVHKLPYAIAG
ECCCEEEECCEEEEC		10.6817644757
159UbiquitinationFIYGYCDKNFRENMS
EEEEEECHHHHHCCC		15.8523749301
167UbiquitinationNFRENMSKEETVDFI
HHHHCCCHHHHHHHH		21.4724961812
167AcetylationNFRENMSKEETVDFI
HHHHCCCHHHHHHHH		21.4724489116
175AcetylationEETVDFIKHSLSQAI
HHHHHHHHHHHHHHH		9.1524489116
175UbiquitinationEETVDFIKHSLSQAI
HHHHHHHHHHHHHHH		9.1524961812
183UbiquitinationHSLSQAIKWDGSSGG
HHHHHHHCCCCCCCC		52.0623749301
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 PSB1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PSB1_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 PSB1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
VAC14_YEASTVAC14physical
10688190
PSB2_YEASTPUP1physical
9087403
PSB3_YEASTPUP3physical
9087403
RHC31_YEASTAOS1physical
11595789
PSB2_YEASTPUP1physical
11595789
PSB4_YEASTPRE1genetic
9677364
BLM10_YEASTBLM10physical
16429126
ECM29_YEASTECM29physical
16429126
PSB4_YEASTPRE1physical
16429126
PSA7_YEASTPRE10physical
16429126
PSB5_YEASTPRE2physical
16429126
PSB7_YEASTPRE4physical
16429126
PSA6_YEASTPRE5physical
16429126
PSA4_YEASTPRE6physical
16429126
PSB6_YEASTPRE7physical
16429126
PSB3_YEASTPUP3physical
16429126
RPN2_YEASTRPN2physical
16429126
RPN3_YEASTRPN3physical
16429126
PSA1_YEASTSCL1physical
16429126
RPN1_YEASTRPN1physical
16429126
PRS7_YEASTRPT1physical
16429126
PSA6_YEASTPRE5physical
15687504
PSB2_YEASTPUP1genetic
10393174
PRS6B_YEASTRPT3genetic
18622397
RPN10_YEASTRPN10genetic
18622397
RPN8_YEASTRPN8genetic
18622397
RPN6_YEASTRPN6genetic
18622397
RPN12_YEASTRPN12genetic
18622397
RPN5_YEASTRPN5genetic
18622397
RPN2_YEASTRPN2genetic
18622397
PSA3_YEASTPRE9genetic
18622397
PRS6A_YEASTRPT5genetic
18622397
PRS7_YEASTRPT1genetic
18622397
PSA7_YEASTPRE10genetic
18622397
PSB2_YEASTPUP1genetic
18622397
PSA4_YEASTPRE6genetic
18622397
PSB5_YEASTPRE2genetic
18622397
PSA5_YEASTPUP2genetic
18622397
PSA6_YEASTPRE5genetic
18622397
PSA1_YEASTSCL1genetic
18622397
PSA2_YEASTPRE8genetic
18622397
PSB4_YEASTPRE1genetic
18622397
PSB7_YEASTPRE4genetic
18622397
PSB6_YEASTPRE7genetic
18622397
PSB2_YEASTPUP1genetic
23891562
PEX18_YEASTPEX18genetic
23891562
PSA7_YEASTPRE10physical
26245374
PRS7_YEASTRPT1physical
26245374
PRS6A_YEASTRPT5physical
26245374
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PSB1_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-53, 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-209 AND THR-211, ANDMASS SPECTROMETRY.

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