SIR4_YEAST - dbPTM
SIR4_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SIR4_YEAST
UniProt AC P11978
Protein Name Regulatory protein SIR4
Gene Name SIR4
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 1358
Subcellular Localization Nucleus.
Protein Description The proteins SIR1 through SIR4 are required for transcriptional repression of the silent mating type loci, HML and HMR. [PubMed: 18039933 The proteins SIR2 through SIR4 repress mulitple loci by modulating chromatin structure]
Protein Sequence MPNDNKTPNRSSTPKFTKKPVTPNDKIPEREEKSNEVKTPKIPLFTFAKSKNYSRPSTAIHTSPHQPSDVKPTSHKQLQQPKSSPLKKNNYNSFPHSNLEKISNSKLLSLLRSKTSAGRIESNNPSHDASRSLASFEQTAFSRHAQQQTSTFNSKPVRTIVPISTSQTNNSFLSGVKSLLSEEKIRDYSKEILGINLANEQPVLEKPLKKGSADIGASVISLTKDKSIRKDTVEEKKEEKLNIGKNFAHSDSLSVPKVSAGDSGISPEESKARSPGIAKPNAIQTEVYGINEESTNERLEINQEKPVKLDENSANSTVASALDTNGTSATTETLTSKKIVPSPKKVAIDQDKITLHDEKTLAPSKHQPITSEQKMKEDADLKRMEILKSPHLSKSPADRPQGRRNSRNFSTRDEETTKLAFLVEYEGQENNYNSTSRSTEKKNDMNTSAKNKNGENKKIGKRPPEIMSTEAHVNKVTEETTKQIQSVRIDGRKVLQKVQGESHIDSRNNTLNVTPSKRPQLGEIPNPMKKHKPNEGRTPNISNGTINIQKKLEPKEIVRDILHTKESSNEAKKTIQNPLNKSQNTALPSTHKVTQKKDIKIGTNDLFQVESAPKISSEIDRENVKSKDEPVSKAVESKSLLNLFSNVLKAPFIKSESKPFSSDALSKEKANFLETIASTEKPENKTDKVSLSQPVSASKHEYSDNFPVSLSQPSKKSFANHTEDEQIEKKKICRGRMNTIITHPGKMELVYVSDSDDSSSDNDSLTDLESLSSGESNEIKVTNDLDTSAEKDQIQAGKWFDPVLDWRKSDRELTKNILWRIADKTTYDKETITDLIEQGIPKHSYLSGNPLTSVTNDICSVENYETSSAFFYQQVHKKDRLQYLPLYAVSTFENTNNTEKNDVTNKNINIGKHSQEQNSSSAKPSQIPTVSSPLGFEETKLSTTPTKSNRRVSHSDTNSSKPKNTKENLSKSSWRQEWLANLKLISVSLVDEFPSELSDSDRQIINEKMQLLKDIFANNLKSAISNNFRESDIIILKGEIEDYPMSSEIKIYYNELQNKPDAKKARFWSFMKTQRFVSNMGFDIQKSCEPVSISTSVKPHVVEPEHMADAKIMPKDILQITKKPLMVKNVKPSSPPDVKSLVQLSTMETKTLPEKKQFDSIFNSNKAKIIPGNGKHASENISLSFSRPASYGYFSVGKRVPIVEDRRVKQLDDITDSNTTEILTSVDVLGTHSQTGTQQSNMYTSTQKTELEIDNKDSVTECSKDMKEDGLSFVDIVLSKAASALDEKEKQLAVANEIIRSLSDEVMRNEIRITSLQGDLTFTKKCLENARSQISEKDAKINKLMEKDFQVNKEIKPY
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
7Phosphorylation-MPNDNKTPNRSSTP
-CCCCCCCCCCCCCC
31.8619779198
12PhosphorylationNKTPNRSSTPKFTKK
CCCCCCCCCCCCCCC
45.5521440633
22PhosphorylationKFTKKPVTPNDKIPE
CCCCCCCCCCCCCCH
25.5420377248
39PhosphorylationEKSNEVKTPKIPLFT
HHCCCCCCCCCCCEE
34.6821440633
57PhosphorylationSKNYSRPSTAIHTSP
CCCCCCCCCCCCCCC
29.3927017623
62PhosphorylationRPSTAIHTSPHQPSD
CCCCCCCCCCCCCCC
37.5317287358
63PhosphorylationPSTAIHTSPHQPSDV
CCCCCCCCCCCCCCC
13.2621440633
83PhosphorylationKQLQQPKSSPLKKNN
HHCCCCCCCCCCCCC
43.8220377248
84PhosphorylationQLQQPKSSPLKKNNY
HCCCCCCCCCCCCCC
40.1420377248
91PhosphorylationSPLKKNNYNSFPHSN
CCCCCCCCCCCCCCC
22.9028889911
93PhosphorylationLKKNNYNSFPHSNLE
CCCCCCCCCCCCCHH
29.7830377154
135PhosphorylationDASRSLASFEQTAFS
HHHHHHHHHHHHHHH
34.3130377154
168PhosphorylationVPISTSQTNNSFLSG
EECCCCCCCCCHHHH
35.8124961812
171PhosphorylationSTSQTNNSFLSGVKS
CCCCCCCCHHHHHHH
29.6328889911
174PhosphorylationQTNNSFLSGVKSLLS
CCCCCHHHHHHHHCC
39.2624961812
177AcetylationNSFLSGVKSLLSEEK
CCHHHHHHHHCCHHH
38.6225381059
181PhosphorylationSGVKSLLSEEKIRDY
HHHHHHCCHHHHHHH
49.3430377154
218PhosphorylationGSADIGASVISLTKD
CCCCCCCEEEHHHCC
18.1230377154
221PhosphorylationDIGASVISLTKDKSI
CCCCEEEHHHCCCCC
28.0330377154
250PhosphorylationIGKNFAHSDSLSVPK
CCCCCCCCCCCCCCC
26.0130377154
252PhosphorylationKNFAHSDSLSVPKVS
CCCCCCCCCCCCCCC
26.0921551504
254PhosphorylationFAHSDSLSVPKVSAG
CCCCCCCCCCCCCCC
40.0830377154
266PhosphorylationSAGDSGISPEESKAR
CCCCCCCCHHHHHCC
29.7728889911
274PhosphorylationPEESKARSPGIAKPN
HHHHHCCCCCCCCCC
32.1325752575
285PhosphorylationAKPNAIQTEVYGINE
CCCCCEEEEEECCCC
22.7019779198
342PhosphorylationTSKKIVPSPKKVAID
CCCCCCCCCCEEEEC
38.1625752575
389PhosphorylationKRMEILKSPHLSKSP
HHHHHHHCCCCCCCC
17.6919823750
393PhosphorylationILKSPHLSKSPADRP
HHHCCCCCCCCCCCC
28.2219779198
395PhosphorylationKSPHLSKSPADRPQG
HCCCCCCCCCCCCCC
23.1928889911
502PhosphorylationLQKVQGESHIDSRNN
HHHHCCCCCCCCCCC
32.3527017623
506PhosphorylationQGESHIDSRNNTLNV
CCCCCCCCCCCEEEC
35.9828889911
514PhosphorylationRNNTLNVTPSKRPQL
CCCEEECCCCCCCCC
22.2922369663
516PhosphorylationNTLNVTPSKRPQLGE
CEEECCCCCCCCCCC
31.7528889911
567PhosphorylationDILHTKESSNEAKKT
HHHHCCCCCHHHHHH
39.7728889911
582PhosphorylationIQNPLNKSQNTALPS
HCCCCCHHCCCCCCC
27.8219779198
585PhosphorylationPLNKSQNTALPSTHK
CCCHHCCCCCCCCCC
23.1819779198
589PhosphorylationSQNTALPSTHKVTQK
HCCCCCCCCCCCCCC
43.9519779198
611PhosphorylationNDLFQVESAPKISSE
CCCEEECCCCCCCCC
51.5222369663
637PhosphorylationPVSKAVESKSLLNLF
CCHHHHHCHHHHHHH
22.4221440633
639PhosphorylationSKAVESKSLLNLFSN
HHHHHCHHHHHHHHH
47.5722369663
661PhosphorylationKSESKPFSSDALSKE
CCCCCCCCCCCCCHH
35.5227214570
690PhosphorylationENKTDKVSLSQPVSA
CCCCCCCCCCCCCCC
28.2221440633
692PhosphorylationKTDKVSLSQPVSASK
CCCCCCCCCCCCCCC
25.5725521595
696PhosphorylationVSLSQPVSASKHEYS
CCCCCCCCCCCCCCC
33.2430377154
709PhosphorylationYSDNFPVSLSQPSKK
CCCCCCCCCCCCCCC
23.6521440633
711PhosphorylationDNFPVSLSQPSKKSF
CCCCCCCCCCCCCCC
32.3220377248
714PhosphorylationPVSLSQPSKKSFANH
CCCCCCCCCCCCCCC
45.1121440633
717PhosphorylationLSQPSKKSFANHTED
CCCCCCCCCCCCCCH
33.0730377154
787PhosphorylationKVTNDLDTSAEKDQI
EEECCCCCHHHHHHH
36.8122369663
788PhosphorylationVTNDLDTSAEKDQIQ
EECCCCCHHHHHHHH
33.8122369663
925PhosphorylationNSSSAKPSQIPTVSS
CCCCCCHHHCCCCCC
39.7824961812
929PhosphorylationAKPSQIPTVSSPLGF
CCHHHCCCCCCCCCC
34.3528889911
931PhosphorylationPSQIPTVSSPLGFEE
HHHCCCCCCCCCCCC
28.8121440633
932PhosphorylationSQIPTVSSPLGFEET
HHCCCCCCCCCCCCC
21.5820377248
939PhosphorylationSPLGFEETKLSTTPT
CCCCCCCCCCCCCCC
30.0424961812
943PhosphorylationFEETKLSTTPTKSNR
CCCCCCCCCCCCCCC
47.4328889911
944PhosphorylationEETKLSTTPTKSNRR
CCCCCCCCCCCCCCC
26.1125521595
946PhosphorylationTKLSTTPTKSNRRVS
CCCCCCCCCCCCCCC
45.0428889911
953PhosphorylationTKSNRRVSHSDTNSS
CCCCCCCCCCCCCCC
18.5728889911
957PhosphorylationRRVSHSDTNSSKPKN
CCCCCCCCCCCCCCC
39.7628889911
961AcetylationHSDTNSSKPKNTKEN
CCCCCCCCCCCHHHH
60.8925381059
983UbiquitinationQEWLANLKLISVSLV
HHHHHHCCEEEEEHH
43.5115699485
1008UbiquitinationDRQIINEKMQLLKDI
HHHHHHHHHHHHHHH
27.7115699485
1013UbiquitinationNEKMQLLKDIFANNL
HHHHHHHHHHHHHHH
58.3215699485
1037UbiquitinationESDIIILKGEIEDYP
HHCEEEEECCCCCCC
44.0515699485
1043PhosphorylationLKGEIEDYPMSSEIK
EECCCCCCCCCCEEE
6.5028132839
1053PhosphorylationSSEIKIYYNELQNKP
CCEEEEEHHHHHCCC
12.9728132839
1087PhosphorylationMGFDIQKSCEPVSIS
CCCEEECCCCEEEEE
13.8227017623
1092PhosphorylationQKSCEPVSISTSVKP
ECCCCEEEEECCCCC
22.8727017623
1094PhosphorylationSCEPVSISTSVKPHV
CCCEEEEECCCCCCC
13.7127017623
1128UbiquitinationTKKPLMVKNVKPSSP
CCCCEEEECCCCCCC
41.9015542864
1128SumoylationTKKPLMVKNVKPSSP
CCCCEEEECCCCCCC
41.9015542864
1128SumoylationTKKPLMVKNVKPSSP
CCCCEEEECCCCCCC
41.90-
1133PhosphorylationMVKNVKPSSPPDVKS
EEECCCCCCCCCHHH
50.1620377248
1134PhosphorylationVKNVKPSSPPDVKSL
EECCCCCCCCCHHHH
49.3217330950
1140PhosphorylationSSPPDVKSLVQLSTM
CCCCCHHHHHHHHHC
33.3528889911
1215PhosphorylationVKQLDDITDSNTTEI
CCCHHHCCCCCCCEE
40.1329688323
1217PhosphorylationQLDDITDSNTTEILT
CHHHCCCCCCCEEEE
27.6829688323
1219PhosphorylationDDITDSNTTEILTSV
HHCCCCCCCEEEEEE
29.7429688323
1220PhosphorylationDITDSNTTEILTSVD
HCCCCCCCEEEEEEE
25.8629688323
1224PhosphorylationSNTTEILTSVDVLGT
CCCCEEEEEEEEEEC
32.1629688323
1225PhosphorylationNTTEILTSVDVLGTH
CCCEEEEEEEEEECC
16.9329688323
1231PhosphorylationTSVDVLGTHSQTGTQ
EEEEEEECCCCCCCH
17.7529688323
1233PhosphorylationVDVLGTHSQTGTQQS
EEEEECCCCCCCHHH
29.3129688323
1235PhosphorylationVLGTHSQTGTQQSNM
EEECCCCCCCHHHCC
45.2529688323
1237PhosphorylationGTHSQTGTQQSNMYT
ECCCCCCCHHHCCEE
27.1629688323
1240PhosphorylationSQTGTQQSNMYTSTQ
CCCCCHHHCCEECCC
17.4729688323
1243PhosphorylationGTQQSNMYTSTQKTE
CCHHHCCEECCCEEE
11.2029688323
1244PhosphorylationTQQSNMYTSTQKTEL
CHHHCCEECCCEEEE
17.9629688323
1245PhosphorylationQQSNMYTSTQKTELE
HHHCCEECCCEEEEE
16.0229688323
1246PhosphorylationQSNMYTSTQKTELEI
HHCCEECCCEEEEEE
26.7029688323
1283PhosphorylationIVLSKAASALDEKEK
HHHHHHHHCCCHHHH
33.9430377154

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
-KUbiquitinationE3 ubiquitin ligaseSAN1P22470
PMID:22199232

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SIR4_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 SIR4_YEAST !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PMM_YEASTSEC53physical
11805837
SIR3_YEASTSIR3physical
11805837
BLM10_YEASTBLM10physical
11805837
IMA1_YEASTSRP1physical
11805837
SIR2_YEASTSIR2physical
11805837
SIR2_YEASTSIR2physical
8752220
SIR2_YEASTSIR2physical
9122169
SIR3_YEASTSIR3physical
8752220
SIR3_YEASTSIR3physical
9122169
UBP3_YEASTUBP3physical
8752220
SIR2_YEASTSIR2physical
12024030
SIR2_YEASTSIR2physical
11500379
RAP1_YEASTRAP1physical
7744964
SIR3_YEASTSIR3physical
12791253
RAP1_YEASTRAP1physical
12080091
H4_YEASTHHF1physical
8647429
H3_YEASTHHT1physical
8647429
H4_YEASTHHF1physical
7867066
H3_YEASTHHT1physical
7867066
ESC1_YEASTESC1physical
12417731
SIR4_YEASTSIR4physical
10757754
ZDS2_YEASTZDS2physical
14742666
KU80_YEASTYKU80physical
14551211
SIR2_YEASTSIR2physical
15282295
SIR3_YEASTSIR3physical
15282295
SIR4_YEASTSIR4physical
1946372
SIR3_YEASTSIR3genetic
9742128
RAD52_YEASTRAD52genetic
9278054
SAN1_YEASTSAN1genetic
2471670
SUM1_YEASTSUM1genetic
3905506
NEJ1_YEASTNEJ1genetic
11676923
SAN1_YEASTSAN1genetic
15078868
SIR3_YEASTSIR3genetic
3325825
SIR3_YEASTSIR3physical
16554755
GSP1_YEASTGSP1physical
16956377
SIR2_YEASTSIR2physical
16956377
RT106_YEASTRTT106physical
17410207
MPS3_YEASTMPS3physical
18039933
SIR4_YEASTSIR4physical
14636601
KU70_YEASTYKU70genetic
19047366
SIR4_YEASTSIR4physical
19217406
SIR2_YEASTSIR2physical
19217406
SIR3_YEASTSIR3physical
19217406
H2A1_YEASTHTA1physical
19217406
H2B1_YEASTHTB1physical
19217406
H3_YEASTHHT1physical
19217406
H4_YEASTHHF1physical
19217406
SIR3_YEASTSIR3genetic
3023863
SIR2_YEASTSIR2physical
19782027
SUM1_YEASTSUM1physical
18086891
NMA2_YEASTNMA2physical
18086891
CHD1_YEASTCHD1physical
18086891
ESC1_YEASTESC1physical
18086891
NU157_YEASTNUP157physical
18086891
CSM1_YEASTCSM1physical
21664583
CHZ1_YEASTCHZ1physical
20008511
RRS1_YEASTRRS1physical
21822217
EBP2_YEASTEBP2physical
21822217
MPS3_YEASTMPS3physical
21822217
SIR1_YEASTSIR1physical
21822217
SIF2_YEASTSIF2physical
21822217
SIR4_YEASTSIR4physical
21822217
SIR3_YEASTSIR3physical
21822217
RAP1_YEASTRAP1physical
21822217
KU70_YEASTYKU70physical
21822217
ESC1_YEASTESC1physical
21822217
SIR2_YEASTSIR2physical
21822217
SIR3_YEASTSIR3physical
21896656
SIR2_YEASTSIR2physical
21896656
SIR2_YEASTSIR2physical
22654676
SIR3_YEASTSIR3physical
22654676
H4_YEASTHHF1physical
22654676
KU80_YEASTYKU80physical
22654676
SIR1_YEASTSIR1physical
22654676
SIF2_YEASTSIF2physical
22654676
SIR1_YEASTSIR1genetic
22654676
NTR2_YEASTNTR2physical
22875988
NUF2_YEASTNUF2physical
22875988
SMT3_YEASTSMT3genetic
23417015
RAP1_YEASTRAP1genetic
23417015
SIR3_YEASTSIR3physical
23299941
SIR2_YEASTSIR2physical
23299941
NU170_YEASTNUP170physical
23452847
SIR2_YEASTSIR2physical
26319015
NSE3_YEASTNSE3physical
27564449
SIR1_YEASTSIR1genetic
28188183
SIR1_YEASTSIR1physical
28188183
DOT1_YEASTDOT1genetic
26587833
NU170_YEASTNUP170physical
28883038
PO152_YEASTPOM152physical
28883038
NU192_YEASTNUP192physical
28883038
NU157_YEASTNUP157physical
28883038
NU188_YEASTNUP188physical
28883038
NIC96_YEASTNIC96physical
28883038
NU145_YEASTNUP145physical
28883038
NU133_YEASTNUP133physical
28883038
NUP84_YEASTNUP84physical
28883038

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SIR4_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-274; SER-342; SER-692;SER-709; SER-711; SER-788 AND SER-1134, 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-1134, 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 THR-62, AND MASSSPECTROMETRY.
Sumoylation
ReferencePubMed
"A proteomic strategy for gaining insights into protein sumoylation inyeast.";
Denison C., Rudner A.D., Gerber S.A., Bakalarski C.E., Moazed D.,Gygi S.P.;
Mol. Cell. Proteomics 4:246-254(2005).
Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1128, AND MASS SPECTROMETRY.

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