PCL6_YEAST - dbPTM
PCL6_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PCL6_YEAST
UniProt AC P40038
Protein Name PHO85 cyclin-6
Gene Name PCL6
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 420
Subcellular Localization Cytoplasm . Nucleus .
Protein Description Cyclin partner of the cyclin-dependent kinase (CDK) PHO85. Together with cyclin PCL7, controls glycogen phosphorylase and glycogen synthase activities in response to nutrient availablility. The PCL6-PHO85 cyclin-CDK holoenzyme has GLC8 kinase activity and phosphorylates and inactivates the phosphatase PP1-2 inhibitor GLC8, causing activation of PP1-2, which then dephosphorylates and activates glycogen phosphorylase. PCL6-PHO85 also phosphorylates YJL084C..
Protein Sequence MSIKGDSPSSTNASSSPKSTYSIQSDDKANLGSGNVDIRTDNSQQDSNNRRDIVVVTRVASEETLESQSSTSSMGIRPESSFNYEDASNQARVEMNNRVHGSNMNTINKYYPVRFPKNNERQLSDTNNLNEKVQGTHTVQSSTQEDKILDGDTSNSQVTPSLNIAEFPTDKLLKMLTALLTKIIKSNDRTAATNPSLTQEIENGRCLALSDNEKKYLSPVLGFRGKHVPQIGLDQYFQRIQKYCPTTNDVFLSLLVYFDRISKRCNSVTTTPKTNTAKHESPSNESSLDKANRGADKMSACNSNENNENDDSDDENTGVQRDSRAHPQMFVMDSHNIHRLIIAGITVSTKFLSDFFYSNSRYSRVGGISLQELNHLELQFLVLCDFELLISVNELQRYADLLYRFWNNAKAQSQALVTGM
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------MSIKGDSPS
------CCCCCCCCC		32.7622369663
7Phosphorylation-MSIKGDSPSSTNAS
-CCCCCCCCCCCCCC		35.0422369663
9PhosphorylationSIKGDSPSSTNASSS
CCCCCCCCCCCCCCC		54.4622369663
10PhosphorylationIKGDSPSSTNASSSP
CCCCCCCCCCCCCCC		29.1222369663
11PhosphorylationKGDSPSSTNASSSPK
CCCCCCCCCCCCCCC		38.8622369663
14PhosphorylationSPSSTNASSSPKSTY
CCCCCCCCCCCCCEE		33.1622369663
15PhosphorylationPSSTNASSSPKSTYS
CCCCCCCCCCCCEEE		48.5322369663
16PhosphorylationSSTNASSSPKSTYSI
CCCCCCCCCCCEEEE		33.5725521595
19PhosphorylationNASSSPKSTYSIQSD
CCCCCCCCEEEEECC		35.6429136822
20PhosphorylationASSSPKSTYSIQSDD
CCCCCCCEEEEECCC		27.6729136822
21PhosphorylationSSSPKSTYSIQSDDK
CCCCCCEEEEECCCC		15.7429136822
22PhosphorylationSSPKSTYSIQSDDKA
CCCCCEEEEECCCCC		17.7819823750
25PhosphorylationKSTYSIQSDDKANLG
CCEEEEECCCCCCCC		46.2119823750
28UbiquitinationYSIQSDDKANLGSGN
EEEECCCCCCCCCCC		44.1323749301
33PhosphorylationDDKANLGSGNVDIRT
CCCCCCCCCCCEECC		30.2922369663
61PhosphorylationVVVTRVASEETLESQ
EEEEEECCHHHHHCC		32.8622369663
64PhosphorylationTRVASEETLESQSST
EEECCHHHHHCCCCC		31.6022369663
67PhosphorylationASEETLESQSSTSSM
CCHHHHHCCCCCCCC		38.1723749301
69PhosphorylationEETLESQSSTSSMGI
HHHHHCCCCCCCCCC		44.8822369663
70PhosphorylationETLESQSSTSSMGIR
HHHHCCCCCCCCCCC		25.3522369663
71PhosphorylationTLESQSSTSSMGIRP
HHHCCCCCCCCCCCC		30.0222369663
72PhosphorylationLESQSSTSSMGIRPE
HHCCCCCCCCCCCCC		21.9222369663
73PhosphorylationESQSSTSSMGIRPES
HCCCCCCCCCCCCCC		22.5522369663
80PhosphorylationSMGIRPESSFNYEDA
CCCCCCCCCCCHHHC		42.8022369663
81PhosphorylationMGIRPESSFNYEDAS
CCCCCCCCCCHHHCC		18.8222369663
84PhosphorylationRPESSFNYEDASNQA
CCCCCCCHHHCCCCH		17.1122369663
88PhosphorylationSFNYEDASNQARVEM
CCCHHHCCCCHHHEH		41.6222369663
109AcetylationSNMNTINKYYPVRFP
CCCCCCCCCCCCCCC		42.1625381059
124PhosphorylationKNNERQLSDTNNLNE
CCCCCCCCCCCCCCH		33.7722369663
126PhosphorylationNERQLSDTNNLNEKV
CCCCCCCCCCCCHHH		23.7222369663
153PhosphorylationDKILDGDTSNSQVTP
CEEECCCCCCCCCCC		35.0227017623
154PhosphorylationKILDGDTSNSQVTPS
EEECCCCCCCCCCCC		38.9421440633
216PhosphorylationLSDNEKKYLSPVLGF
CCCCCCEECHHCCCC		24.3928889911
218PhosphorylationDNEKKYLSPVLGFRG
CCCCEECHHCCCCCC		15.1821440633
243PhosphorylationYFQRIQKYCPTTNDV
HHHHHHHHCCCCCHH		6.3127017623
246PhosphorylationRIQKYCPTTNDVFLS
HHHHHCCCCCHHHHH		34.3727017623
247PhosphorylationIQKYCPTTNDVFLSL
HHHHCCCCCHHHHHH		17.9827017623
253PhosphorylationTTNDVFLSLLVYFDR
CCCHHHHHHHHHHHH		14.2727017623
274PhosphorylationSVTTTPKTNTAKHES
CCCCCCCCCCCCCCC		38.7229136822
276PhosphorylationTTTPKTNTAKHESPS
CCCCCCCCCCCCCCC		42.1729136822
281PhosphorylationTNTAKHESPSNESSL
CCCCCCCCCCCHHHH		33.0919823750
283PhosphorylationTAKHESPSNESSLDK
CCCCCCCCCHHHHHH		63.6125521595
286PhosphorylationHESPSNESSLDKANR
CCCCCCHHHHHHHHH		40.2129136822
287PhosphorylationESPSNESSLDKANRG
CCCCCHHHHHHHHHH		34.1129136822
299PhosphorylationNRGADKMSACNSNEN
HHHHHHHHHCCCCCC		35.1022890988
303PhosphorylationDKMSACNSNENNEND
HHHHHCCCCCCCCCC		45.4622890988
312PhosphorylationENNENDDSDDENTGV
CCCCCCCCCCCCCHH		50.2322369663
317PhosphorylationDDSDDENTGVQRDSR
CCCCCCCCHHCCCCC		36.3622890988
323PhosphorylationNTGVQRDSRAHPQMF
CCHHCCCCCCCCCEE		33.2923749301
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 PCL6_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PCL6_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 PCL6_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PHO85_YEASTPHO85physical
11805837
ALY2_YEASTALY2physical
10688190
MMR1_YEASTMMR1physical
10688190
GLC8_YEASTGLC8genetic
12407105
WHI4_YEASTWHI4physical
11283351
CSM1_YEASTCSM1genetic
20093466
CHO2_YEASTCHO2genetic
20093466
ICE2_YEASTICE2genetic
20093466
PLMT_YEASTOPI3genetic
20093466
CSF1_YEASTCSF1genetic
20093466
YMF3_YEASTYML053Cgenetic
20093466
IDH1_YEASTIDH1genetic
20093466
RL21B_YEASTRPL21Bgenetic
20093466
CGS6_YEASTCLB6physical
20489023
AMPL_YEASTAPE1physical
20489023
PAH1_YEASTPAH1physical
20489023
PHO85_YEASTPHO85physical
20489023
SIC1_YEASTSIC1physical
20489023
HSP72_YEASTSSA2physical
23217712
HSP71_YEASTSSA1physical
23217712
VMA21_YEASTVMA21genetic
27708008
SWI6_YEASTSWI6genetic
27708008
CHO2_YEASTCHO2genetic
27708008
ICE2_YEASTICE2genetic
27708008
CSF1_YEASTCSF1genetic
27708008
RL21B_YEASTRPL21Bgenetic
27708008
CHMU_YEASTARO7genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PCL6_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 TYR-21; SER-22; SER-25;SER-61; SER-281 AND SER-312, 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-25 AND SER-281, AND MASSSPECTROMETRY.

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