PLM2_YEAST - dbPTM
PLM2_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PLM2_YEAST
UniProt AC Q04383
Protein Name Protein PLM2
Gene Name PLM2
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 521
Subcellular Localization Nucleus .
Protein Description Binds to the promoters of genes with functions important for the G1/S (start) transition; primarily genes involved in DNA synthesis and repair, chromosome segregation, nuclear division and transcription..
Protein Sequence MSHLFPPSSPVAGKPLESPQKEPGKLANTSVLTLGRKRYNYELEEYPTPDPSSSIGRQSSPVKDITSRLNETKSALSSPSKQEKVLAGPIEIELDASDPSRLAIGRKKSVCNIILPCRKNISRQHAFISYAADRNEIKLECNGTNGLSVHLPYSMQLHLVKPFPTRNFYKLVAEEPLTSQNTKQSHGKTLQKNQNFISFVLAKGETVTFPYIQGSFINFTGVTVCLSLKKVAPYPGDGNNNFDEENSTETEDELCLLTTTSDDFSWQKETPSMKFVPVEHSPRTEQISKPLLIASPALVKNSPISYRTTPQTSFVINQPSTPKKLKRKSISLKNNTIQETPLPKDKIIGTLSASTRSGGINEEESFAAVAKKTKELSSTTAIVSPAQKRLKTSLNIIPEISRSLSERGIRFDDLVHVLCNHLAFSNLQQTPLSQLQNINSNTSQLSKDELKKVLETISCIGIIVREGKDASGKPLEDEYYYDVENDDSDERKILYNSLKGRSRLRSCRKKHKQYFWKRPTK
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
8PhosphorylationMSHLFPPSSPVAGKP
CCCCCCCCCCCCCCC		47.7328889911
9PhosphorylationSHLFPPSSPVAGKPL
CCCCCCCCCCCCCCC		29.2128889911
29PhosphorylationEPGKLANTSVLTLGR
CCCCCCCCEEEEECC		18.0127017623
30PhosphorylationPGKLANTSVLTLGRK
CCCCCCCEEEEECCE		18.2230377154
52PhosphorylationEYPTPDPSSSIGRQS
CCCCCCCCCCCCCCC		44.0627017623
53PhosphorylationYPTPDPSSSIGRQSS
CCCCCCCCCCCCCCC		31.2228889911
54PhosphorylationPTPDPSSSIGRQSSP
CCCCCCCCCCCCCCC		33.1428889911
59PhosphorylationSSSIGRQSSPVKDIT
CCCCCCCCCCHHHHH		34.9421440633
60PhosphorylationSSIGRQSSPVKDITS
CCCCCCCCCHHHHHH		25.9317563356
74PhosphorylationSRLNETKSALSSPSK
HHHHHHHHHHCCCCH		41.6927017623
77PhosphorylationNETKSALSSPSKQEK
HHHHHHHCCCCHHHC		39.6628889911
78PhosphorylationETKSALSSPSKQEKV
HHHHHHCCCCHHHCC		33.7617563356
80PhosphorylationKSALSSPSKQEKVLA
HHHHCCCCHHHCCCC		49.2528889911
97PhosphorylationIEIELDASDPSRLAI
EEEEECCCCHHHEEC		50.1227017623
109PhosphorylationLAIGRKKSVCNIILP
EECCCCCCCCEEEEE		34.6330377154
130PhosphorylationRQHAFISYAADRNEI
HHHEEEEEEECCCEE		10.8628132839
179PhosphorylationVAEEPLTSQNTKQSH
HEECCCCCCCCHHHC		29.1720190278
182PhosphorylationEPLTSQNTKQSHGKT
CCCCCCCCHHHCCCE		23.8730377154
281PhosphorylationKFVPVEHSPRTEQIS
EEEECCCCCCCHHCC		11.5420190278
284PhosphorylationPVEHSPRTEQISKPL
ECCCCCCCHHCCCCE		35.3120377248
288PhosphorylationSPRTEQISKPLLIAS
CCCCHHCCCCEEEEC		28.1027717283
295PhosphorylationSKPLLIASPALVKNS
CCCEEEECHHHHCCC		12.0525533186
302PhosphorylationSPALVKNSPISYRTT
CHHHHCCCCCCCCCC		20.2125752575
308PhosphorylationNSPISYRTTPQTSFV
CCCCCCCCCCCCEEE		34.3028889911
309PhosphorylationSPISYRTTPQTSFVI
CCCCCCCCCCCEEEE		12.3727017623
313PhosphorylationYRTTPQTSFVINQPS
CCCCCCCEEEECCCC		16.5728889911
320PhosphorylationSFVINQPSTPKKLKR
EEEECCCCCCHHHCC		47.8030377154
321PhosphorylationFVINQPSTPKKLKRK
EEECCCCCCHHHCCC		45.9025752575
329PhosphorylationPKKLKRKSISLKNNT
CHHHCCCEEECCCCC		22.8029136822
331PhosphorylationKLKRKSISLKNNTIQ
HHCCCEEECCCCCCC		40.1429136822
333AcetylationKRKSISLKNNTIQET
CCCEEECCCCCCCCC		41.1625381059
336PhosphorylationSISLKNNTIQETPLP
EEECCCCCCCCCCCC		33.1729136822
340PhosphorylationKNNTIQETPLPKDKI
CCCCCCCCCCCCCCE		17.4727017623
352PhosphorylationDKIIGTLSASTRSGG
CCEEEEEECCCCCCC		21.7330377154
355PhosphorylationIGTLSASTRSGGINE
EEEEECCCCCCCCCH		28.6827017623
384PhosphorylationSSTTAIVSPAQKRLK
CCCEEECCHHHHHHH		14.3825533186
405PhosphorylationPEISRSLSERGIRFD
HHHHHHHHHHCCCHH		26.8830377154
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 PLM2_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PLM2_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 PLM2_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
YK58_YEASTYKR078Wphysical
16554755
SUS1_YEASTSUS1genetic
17314980
ARO1_YEASTARO1genetic
17314980
RGP1_YEASTRGP1genetic
17314980
RTG3_YEASTRTG3genetic
17314980
HXT1_YEASTHXT1physical
18467557
PPZ1_YEASTPPZ1physical
18467557
PDR12_YEASTPDR12physical
18467557
YL413_YEASTINA1physical
18467557
MUP1_YEASTMUP1physical
18467557
TCB3_YEASTTCB3physical
18467557
YG169_YEASTLSO2physical
18467557
KEX1_YEASTKEX1physical
18467557
RCK2_YEASTRCK2physical
18467557
ARB1_YEASTARB1physical
18467557
TPO1_YEASTTPO1physical
18467557
SFK1_YEASTSFK1physical
18467557
KES1_YEASTKES1physical
18467557
MEP3_YEASTMEP3physical
18467557
TPO4_YEASTTPO4physical
18467557
TPO2_YEASTTPO2physical
18467557
COPD_YEASTRET2physical
18467557
COPB2_YEASTSEC27physical
18467557
HNM1_YEASTHNM1physical
18467557
WSC2_YEASTWSC2physical
18467557
FLC1_YEASTFLC1physical
18467557
QDR2_YEASTQDR2physical
18467557
SNA3_YEASTSNA3physical
18467557
YOR1_YEASTYOR1physical
18467557
DIP5_YEASTDIP5physical
18467557
PP11_YEASTSIT4genetic
19269370
SWI5_YEASTSWI5genetic
19269370
MNN10_YEASTMNN10genetic
19269370
CAX4_YEASTCAX4genetic
19269370
BCK1_YEASTBCK1genetic
19269370
MNN11_YEASTMNN11genetic
19269370
IME1_YEASTIME1genetic
19269370
SWI6_YEASTSWI6genetic
19269370
CDC5_YEASTCDC5genetic
19269370
PP2C1_YEASTPTC1genetic
21127252
TEC1_YEASTTEC1genetic
21127252
KCS1_YEASTKCS1genetic
21127252
HCM1_YEASTHCM1genetic
21127252
CSN12_YEASTYJR084Wgenetic
27708008
NCBP2_YEASTCBC2genetic
27708008
ELO2_YEASTELO2genetic
27708008
ODO2_YEASTKGD2genetic
27708008
DAL81_YEASTDAL81genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PLM2_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; SER-54; SER-77;SER-78; SER-179; SER-281; SER-295; SER-302; THR-308; SER-313; THR-321AND SER-384, 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-60; SER-78; SER-281 ANDSER-384, AND MASS SPECTROMETRY.
"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-281 AND SER-295, ANDMASS SPECTROMETRY.

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