SDS24_YEAST - dbPTM
SDS24_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SDS24_YEAST
UniProt AC P38314
Protein Name Protein SDS24
Gene Name SDS24
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 527
Subcellular Localization Cytoplasm .
Protein Description Involved in DNA replication and cell separation during budding..
Protein Sequence MASTSNTFPPSQSNSSNNLPTSRHASIVEMLSTPPLLPHVQVNDTDDKEQPEESTPPTATAAAPGPGCAATPAPLRDEKPQFKLSAVPMTQTPSQCLSCVHAQKWQHIPLSQLIEQNKLIFVPGSISVEEAFNTLIKYHLNSIPVESFPGDMNCFTFDYNDLNSYLLLVLNKITVSNKQLTADCQNGKPVPVGEMVKLTPKNPFYKLPENESLSTVMGILGSGVHRVAITNEEMTKVKGILSQRRLIKYLWDNARSFTSLEPLLNSSLQDLHIGVLNIQSKPTSRQSRVISIQGEEPLIMGLYKMHVERISSIAVIDKQGNLLGNISVTDVKHVTRTSQYPLLHKTCRHFISVILNSRGLETGKDSFPIFHVYPSSSLARTLAKLVATKSHRLWIVQPPESSTSASSTNLTAANTAANAVSATAQSSANGATPMSKSSSSTSLNSHSPLMTAMEDPPSPRSSAIAIPPPSPASSTNTPNLFEKEYRTGKLIGVVSLTDIINLLARKQTGNKEVDPQSARRQRGSIAM
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
13PhosphorylationNTFPPSQSNSSNNLP
CCCCCCCCCCCCCCC		42.9130377154
15PhosphorylationFPPSQSNSSNNLPTS
CCCCCCCCCCCCCCC		39.4230377154
16PhosphorylationPPSQSNSSNNLPTSR
CCCCCCCCCCCCCCC		33.7130377154
21PhosphorylationNSSNNLPTSRHASIV
CCCCCCCCCCCHHHH		41.3730377154
22PhosphorylationSSNNLPTSRHASIVE
CCCCCCCCCCHHHHH		21.8228889911
26PhosphorylationLPTSRHASIVEMLST
CCCCCCHHHHHHHCC		22.5022369663
32PhosphorylationASIVEMLSTPPLLPH
HHHHHHHCCCCCCCC		37.2422369663
33PhosphorylationSIVEMLSTPPLLPHV
HHHHHHCCCCCCCCE		25.6022369663
45PhosphorylationPHVQVNDTDDKEQPE
CCEECCCCCCCCCCC		40.6829136822
54PhosphorylationDKEQPEESTPPTATA
CCCCCCCCCCCCCCC		44.5529734811
55PhosphorylationKEQPEESTPPTATAA
CCCCCCCCCCCCCCC		36.2520377248
85PhosphorylationEKPQFKLSAVPMTQT
CCCCCEEEECCCCCC		28.0119823750
90PhosphorylationKLSAVPMTQTPSQCL
EEEECCCCCCHHHHH		24.1822369663
92PhosphorylationSAVPMTQTPSQCLSC
EECCCCCCHHHHHHH		18.7522369663
94PhosphorylationVPMTQTPSQCLSCVH
CCCCCCHHHHHHHHH		36.5922369663
98PhosphorylationQTPSQCLSCVHAQKW
CCHHHHHHHHHHCCC		23.0122369663
236AcetylationITNEEMTKVKGILSQ
ECCHHHHHHHHHHCH		40.4124489116
248AcetylationLSQRRLIKYLWDNAR
HCHHHHHHHHHHCCC		38.5924489116
291PhosphorylationSRQSRVISIQGEEPL
CCCCEEEEEECCCCC		13.1527017623
332AcetylationNISVTDVKHVTRTSQ
CEEEEECEECCCCCC		34.8624489116
352PhosphorylationKTCRHFISVILNSRG
HHHHHHHHHHHHCCC		11.3629688323
357PhosphorylationFISVILNSRGLETGK
HHHHHHHCCCCCCCC		25.0429688323
364AcetylationSRGLETGKDSFPIFH
CCCCCCCCCCCCEEE		58.5824489116
384UbiquitinationSLARTLAKLVATKSH
HHHHHHHHHHHCCCC		46.7523749301
3892-HydroxyisobutyrylationLAKLVATKSHRLWIV
HHHHHHCCCCEEEEE		34.23-
406PhosphorylationPESSTSASSTNLTAA
CCCCCCCCCCCCHHH		37.1521440633
426PhosphorylationAVSATAQSSANGATP
HHHHHHHHHCCCCCC		29.0224961812
427PhosphorylationVSATAQSSANGATPM
HHHHHHHHCCCCCCC		17.4224961812
432PhosphorylationQSSANGATPMSKSSS
HHHCCCCCCCCCCCC		22.4124961812
435PhosphorylationANGATPMSKSSSSTS
CCCCCCCCCCCCCCC		30.5021440633
437PhosphorylationGATPMSKSSSSTSLN
CCCCCCCCCCCCCCC		28.3122369663
438PhosphorylationATPMSKSSSSTSLNS
CCCCCCCCCCCCCCC		31.8522369663
439PhosphorylationTPMSKSSSSTSLNSH
CCCCCCCCCCCCCCC		44.7322369663
440PhosphorylationPMSKSSSSTSLNSHS
CCCCCCCCCCCCCCC		24.7822369663
441PhosphorylationMSKSSSSTSLNSHSP
CCCCCCCCCCCCCCC		38.9022890988
442PhosphorylationSKSSSSTSLNSHSPL
CCCCCCCCCCCCCCC		27.7422369663
445PhosphorylationSSSTSLNSHSPLMTA
CCCCCCCCCCCCCCC		30.5422369663
447PhosphorylationSTSLNSHSPLMTAME
CCCCCCCCCCCCCCC		21.3922369663
451PhosphorylationNSHSPLMTAMEDPPS
CCCCCCCCCCCCCCC		30.4522890988
458PhosphorylationTAMEDPPSPRSSAIA
CCCCCCCCCCCCCEE		38.0322369663
461PhosphorylationEDPPSPRSSAIAIPP
CCCCCCCCCCEECCC		27.7520377248
462PhosphorylationDPPSPRSSAIAIPPP
CCCCCCCCCEECCCC		25.6020377248
470PhosphorylationAIAIPPPSPASSTNT
CEECCCCCCCCCCCC		38.5828152593
473PhosphorylationIPPPSPASSTNTPNL
CCCCCCCCCCCCCCC		40.8719823750
474PhosphorylationPPPSPASSTNTPNLF
CCCCCCCCCCCCCCH		27.9929734811
475PhosphorylationPPSPASSTNTPNLFE
CCCCCCCCCCCCCHH		40.3919823750
477PhosphorylationSPASSTNTPNLFEKE
CCCCCCCCCCCHHHH		17.4019823750
495PhosphorylationGKLIGVVSLTDIINL
CCEEEEEEHHHHHHH		24.1224961812
497PhosphorylationLIGVVSLTDIINLLA
EEEEEEHHHHHHHHH		20.0424961812
506AcetylationIINLLARKQTGNKEV
HHHHHHHCHHCCCCC		46.7525381059
511AcetylationARKQTGNKEVDPQSA
HHCHHCCCCCCHHHH		61.5325381059
517PhosphorylationNKEVDPQSARRQRGS
CCCCCHHHHHHHHCC		29.1821551504
524PhosphorylationSARRQRGSIAM----
HHHHHHCCCCC----		14.9017287358
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 SDS24_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SDS24_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 SDS24_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PP11_YEASTSIT4physical
16554755
SA155_YEASTSAP155physical
18467557
GPT_YEASTALG7physical
18467557
SIC1_YEASTSIC1physical
18467557
AVT5_YEASTAVT5genetic
20093466
NHP6B_YEASTNHP6Bgenetic
20093466
YCQ5_YEASTYCR015Cgenetic
20093466
YCY0_YEASTYCR090Cgenetic
20093466
MFG1_YEASTMFG1genetic
20093466
ATIF_YEASTINH1genetic
20093466
YD121_YEASTYDL121Cgenetic
20093466
PEX19_YEASTPEX19genetic
20093466
GNTK_YEASTYDR248Cgenetic
20093466
PPB_YEASTPHO8genetic
20093466
PP2C2_YEASTPTC2genetic
20093466
FRE8_YEASTFRE8genetic
20093466
PEX13_YEASTPEX13genetic
20093466
VID22_YEASTVID22genetic
20093466
NST1_YEASTNST1genetic
20093466
SAM3_YEASTSAM3genetic
20093466
MED1_YEASTMED1genetic
20093466
PP11_YEASTSIT4genetic
21360731
SWA2_YEASTSWA2genetic
20526336
SA155_YEASTSAP155physical
22615397
AVT5_YEASTAVT5genetic
27708008
YCQ5_YEASTYCR015Cgenetic
27708008
YIH1_YEASTYIH1genetic
27708008
GPR1_YEASTGPR1genetic
27708008
PEX19_YEASTPEX19genetic
27708008
MFG1_YEASTMFG1genetic
27708008
FOB1_YEASTFOB1genetic
27708008
PPB_YEASTPHO8genetic
27708008
FRE8_YEASTFRE8genetic
27708008
MSS1_YEASTMSS1genetic
27708008
NST1_YEASTNST1genetic
27708008
FABD_YEASTMCT1genetic
27708008
SAM3_YEASTSAM3genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SDS24_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-22; SER-26; THR-33;SER-94; SER-437; SER-438; SER-439; SER-440; SER-442; SER-445; SER-447;SER-458; SER-470 AND SER-524, 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-458, 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-94 AND SER-524, 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-458, AND MASSSPECTROMETRY.

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