PAR32_YEAST - dbPTM
PAR32_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PAR32_YEAST
UniProt AC Q12515
Protein Name Protein PAR32
Gene Name PAR32
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 295
Subcellular Localization Cytoplasm .
Protein Description Involved in resistance to cisplatin..
Protein Sequence MATFNPQNEMENQARVQEYKVSTGRGGAGNIHKSMSKPSPVLLPLKSNSKTVANNNNNGSNQEKVPRFAIGRGGAGNIFHDPHLTRSAQQLDSNDNINYNDVINDIDDYISPITSDMVDEGGSNPVTNTRSRISATRSHQSLHATTSSPNNNAPIVVGRGGAGNIFFNKKKVASNGGNEEDEIRGGNIEDEDTINANEDNLFVVTSNGNALAAIKSTSKKPKNKLKGKSAPEKFAIGRGGAGNIISPKSSRNTINHNLNDDDEDKFNLKDDNGKEKKKKKKKKSGFFSSLKTMFN
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
2Acetylation------MATFNPQNE
------CCCCCCHHH		22.3922814378
20UbiquitinationQARVQEYKVSTGRGG
HHHHEEEEECCCCCC		29.0223749301
22PhosphorylationRVQEYKVSTGRGGAG
HHEEEEECCCCCCCC		22.4623749301
34PhosphorylationGAGNIHKSMSKPSPV
CCCCCCCCCCCCCCC		17.7122369663
35OxidationAGNIHKSMSKPSPVL
CCCCCCCCCCCCCCE		7.7215665377
36PhosphorylationGNIHKSMSKPSPVLL
CCCCCCCCCCCCCEE		48.8022369663
37UbiquitinationNIHKSMSKPSPVLLP
CCCCCCCCCCCCEEE		40.6523749301
39PhosphorylationHKSMSKPSPVLLPLK
CCCCCCCCCCEEECC		31.2322369663
46AcetylationSPVLLPLKSNSKTVA
CCCEEECCCCCCEEC		45.7325381059
47PhosphorylationPVLLPLKSNSKTVAN
CCEEECCCCCCEECC		54.7617330950
49PhosphorylationLLPLKSNSKTVANNN
EEECCCCCCEECCCC		36.4719684113
50UbiquitinationLPLKSNSKTVANNNN
EECCCCCCEECCCCC		51.7923749301
60PhosphorylationANNNNNGSNQEKVPR
CCCCCCCCCCCCCCC		37.1523749301
64UbiquitinationNNGSNQEKVPRFAIG
CCCCCCCCCCCEEEC		48.0123749301
123PhosphorylationDMVDEGGSNPVTNTR
HCCCCCCCCCCCCCC		49.1428889911
131PhosphorylationNPVTNTRSRISATRS
CCCCCCCHHHEECCC		31.7424909858
134PhosphorylationTNTRSRISATRSHQS
CCCCHHHEECCCCCC		23.6017330950
136PhosphorylationTRSRISATRSHQSLH
CCHHHEECCCCCCCE		26.3917330950
138PhosphorylationSRISATRSHQSLHAT
HHHEECCCCCCCEEE		22.8622369663
141PhosphorylationSATRSHQSLHATTSS
EECCCCCCCEEECCC		19.3922369663
145PhosphorylationSHQSLHATTSSPNNN
CCCCCEEECCCCCCC		19.2322369663
146PhosphorylationHQSLHATTSSPNNNA
CCCCEEECCCCCCCC		28.1722369663
147PhosphorylationQSLHATTSSPNNNAP
CCCEEECCCCCCCCC		39.1722369663
148PhosphorylationSLHATTSSPNNNAPI
CCEEECCCCCCCCCE		29.5622369663
174PhosphorylationFNKKKVASNGGNEED
ECCHHCCCCCCCCCC		38.7124909858
205PhosphorylationEDNLFVVTSNGNALA
CCCEEEEECCCCEEE		15.9228132839
206PhosphorylationDNLFVVTSNGNALAA
CCEEEEECCCCEEEH		31.0028889911
233AcetylationKGKSAPEKFAIGRGG
CCCCCCCCCCCCCCC		38.7524489116
246PhosphorylationGGAGNIISPKSSRNT
CCCCCCCCCCCCCCC		23.6022369663
249PhosphorylationGNIISPKSSRNTINH
CCCCCCCCCCCCCCC		37.6022369663
250PhosphorylationNIISPKSSRNTINHN
CCCCCCCCCCCCCCC		35.3622369663
253PhosphorylationSPKSSRNTINHNLND
CCCCCCCCCCCCCCC		23.2624930733
284PhosphorylationKKKKKKKSGFFSSLK
HHHHHHHHCCHHHHH		50.1122369663
288PhosphorylationKKKSGFFSSLKTMFN
HHHHCCHHHHHHHCC		32.2821440633
289PhosphorylationKKSGFFSSLKTMFN-
HHHCCHHHHHHHCC-		28.8221440633
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 PAR32_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PAR32_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 PAR32_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of PAR32_YEAST !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PAR32_YEAST

loading...

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-36; SER-39; SER-123;THR-146; SER-148; SER-246 AND SER-284, 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 SER-39 AND SER-141, 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-36; SER-39; SER-47;SER-147 AND SER-246, 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-39 AND SER-246, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory