SIR3_YEAST - dbPTM
SIR3_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SIR3_YEAST
UniProt AC P06701
Protein Name Regulatory protein SIR3
Gene Name SIR3
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 978
Subcellular Localization Nucleus.
Protein Description The proteins SIR1 through SIR4 are required for transcriptional repression of the silent mating type loci, HML and HMR. The proteins SIR2 through SIR4 repress mulitple loci by modulating chromatin structure. Involves the compaction of chromatin fiber into a more condensed form..
Protein Sequence MAKTLKDLDGWQVIITDDQGRVIDDNNRRRSRKRGGENVFLKRISDGLSFGKGESVIFNDNVTETYSVYLIHEIRLNTLNNVVEIWVFSYLRWFELKPKLYYEQFRPDLIKEDHPLEFYKDKFFNEVNKSELYLTAELSEIWLKDFIAVGQILPESQWNDSSIDKIEDRDFLVRYACEPTAEKFVPIDIFQIIRRVKEMEPKQSDEYLKRVSVPVSGQKTNRQVMHKMGVERSSKRLAKKPSMKKIKIEPSADDDVNNGNIPSQRGTSTTHGSISPQEESVSPNISSASPSALTSPTDSSKILQKRSISKELIVSEEIPINSSEQESDYEPNNETSVLSSKPGSKPEKTSTELVDGRENFVYANNPEVSDDGGLEEETDEVSSESSDEAIIPVNKRRGAHGSELSSKIRKIHIQETQEFSKNYTTETDNEMNGNGKPGIPRGNTKIHSMNENPTPEKGNAKMIDFATLSKLKKKYQIILDRFAPDNQVTDSSQLNKLTDEQSSLDVAGLEDKFRKACSSSGRETILSNFNADINLEESIRESLQKRELLKSQVEDFTRIFLPIYDSLMSSQNKLFYITNADDSTKFQLVNDVMDELITSSARKELPIFDYIHIDALELAGMDALYEKIWFAISKENLCGDISLEALNFYITNVPKAKKRKTLILIQNPENLLSEKILQYFEKWISSKNSKLSIICVGGHNVTIREQINIMPSLKAHFTEIKLNKVDKNELQQMIITRLKSLLKPFHVKVNDKKEMTIYNNIREGQNQKIPDNVIVINHKINNKITQLIAKNVANVSGSTEKAFKICEAAVEISKKDFVRKGGLQKGKLVVSQEMVPRYFSEAINGFKDETISKKIIGMSLLMRTFLYTLAQETEGTNRHTLALETVLIKMVKMLRDNPGYKASKEIKKVICGAWEPAITIEKLKQFSWISVVNDLVGEKLVVVVLEEPSASIMVELKLPLEINYAFSMDEEFKNMDCI
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------MAKTLKDLD
------CCCCCHHCC		17.3415454564
216PhosphorylationKRVSVPVSGQKTNRQ
HHCCCCCCCCCCHHH		29.4527017623
263PhosphorylationVNNGNIPSQRGTSTT
CCCCCCCCCCCCCCC		28.8127214570
267PhosphorylationNIPSQRGTSTTHGSI
CCCCCCCCCCCCCCC		25.7023749301
275PhosphorylationSTTHGSISPQEESVS
CCCCCCCCCCCCCCC		23.4123749301
280PhosphorylationSISPQEESVSPNISS
CCCCCCCCCCCCCCC		27.4319779198
282PhosphorylationSPQEESVSPNISSAS
CCCCCCCCCCCCCCC		22.8523749301
286PhosphorylationESVSPNISSASPSAL
CCCCCCCCCCCCHHC		26.8823749301
287PhosphorylationSVSPNISSASPSALT
CCCCCCCCCCCHHCC		29.0323749301
289PhosphorylationSPNISSASPSALTSP
CCCCCCCCCHHCCCC		22.7221440633
291PhosphorylationNISSASPSALTSPTD
CCCCCCCHHCCCCCC		33.1523749301
294PhosphorylationSASPSALTSPTDSSK
CCCCHHCCCCCCHHH		32.1723749301
295PhosphorylationASPSALTSPTDSSKI
CCCHHCCCCCCHHHH		27.0123749301
315PhosphorylationISKELIVSEEIPINS
CCCEEEEEEECCCCC		23.6319823750
322PhosphorylationSEEIPINSSEQESDY
EEECCCCCCCCCCCC		35.6520377248
323PhosphorylationEEIPINSSEQESDYE
EECCCCCCCCCCCCC		38.5221440633
327PhosphorylationINSSEQESDYEPNNE
CCCCCCCCCCCCCCC		45.2321440633
329PhosphorylationSSEQESDYEPNNETS
CCCCCCCCCCCCCCC		42.4320377248
335PhosphorylationDYEPNNETSVLSSKP
CCCCCCCCCCCCCCC		26.6819823750
336PhosphorylationYEPNNETSVLSSKPG
CCCCCCCCCCCCCCC		18.1921440633
339PhosphorylationNNETSVLSSKPGSKP
CCCCCCCCCCCCCCC		33.8719779198
340PhosphorylationNETSVLSSKPGSKPE
CCCCCCCCCCCCCCC		38.4121440633
344PhosphorylationVLSSKPGSKPEKTST
CCCCCCCCCCCCCCC		54.2721440633
402PhosphorylationKRRGAHGSELSSKIR
CCCCCCHHHHHHHHH		26.0430377154
425PhosphorylationEFSKNYTTETDNEMN
HHHCCCCCCCCCCCC		26.9123749301
427PhosphorylationSKNYTTETDNEMNGN
HCCCCCCCCCCCCCC		41.8721440633
448PhosphorylationRGNTKIHSMNENPTP
CCCCCEEECCCCCCC		27.1222890988
454PhosphorylationHSMNENPTPEKGNAK
EECCCCCCCCCCCCC		56.5125521595
467PhosphorylationAKMIDFATLSKLKKK
CCEECHHHHHHHHHH		31.4030377154
469PhosphorylationMIDFATLSKLKKKYQ
EECHHHHHHHHHHHH		31.4230377154
474AcetylationTLSKLKKKYQIILDR
HHHHHHHHHHEEHHC		40.5825381059
489PhosphorylationFAPDNQVTDSSQLNK
CCCCCCCCCHHHHHH		22.0230377154
491PhosphorylationPDNQVTDSSQLNKLT
CCCCCCCHHHHHHHC		15.6030377154
492PhosphorylationDNQVTDSSQLNKLTD
CCCCCCHHHHHHHCC		41.3127214570
502PhosphorylationNKLTDEQSSLDVAGL
HHHCCCCCCCCCCCC		30.7128889911
503PhosphorylationKLTDEQSSLDVAGLE
HHCCCCCCCCCCCCH		28.4330377154
692PhosphorylationSSKNSKLSIICVGGH
HCCCCCEEEEEECCC		17.4028889911
736PhosphorylationELQQMIITRLKSLLK
HHHHHHHHHHHHHHC		21.0126447709
820AcetylationSKKDFVRKGGLQKGK
CHHHHHHCCCCCCCC		52.6225381059
825AcetylationVRKGGLQKGKLVVSQ
HHCCCCCCCCEEECH		64.1625381059
867PhosphorylationLLMRTFLYTLAQETE
HHHHHHHHHHHHHCC		8.7729650682
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 SIR3_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 SIR3_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SYSC_YEASTSES1physical
11805837
CBS_YEASTCYS4physical
11805837
ILV5_YEASTILV5physical
11805837
RIR2_YEASTRNR2physical
11805837
GAS1_YEASTGAS1physical
11805837
VATA_YEASTVMA1physical
11805837
UBP8_YEASTUBP8physical
11805837
EF1G2_YEASTTEF4physical
11805837
SAHH_YEASTSAH1physical
11805837
SIR1_YEASTSIR1physical
11805837
ADH6_YEASTADH6physical
11805837
QCR1_YEASTCOR1physical
11805837
YM71_YEASTYMR226Cphysical
11805837
SIR4_YEASTSIR4physical
8752220
SIR4_YEASTSIR4physical
9122169
SIR2_YEASTSIR2physical
9122169
H4_YEASTHHF1physical
8779721
H3_YEASTHHT1physical
8779721
H2A1_YEASTHTA1physical
8779721
H2B1_YEASTHTB1physical
8779721
RAP1_YEASTRAP1physical
8779721
SIR4_YEASTSIR4physical
8779721
H4_YEASTHHF1physical
7867066
H3_YEASTHHT1physical
7867066
H4_YEASTHHF1physical
8647429
H3_YEASTHHT1physical
8647429
RAP1_YEASTRAP1physical
11689698
RAP1_YEASTRAP1physical
7958893
SIR3_YEASTSIR3physical
11689698
SIR3_YEASTSIR3physical
7958893
SIR4_YEASTSIR4physical
11689698
SIR4_YEASTSIR4physical
7958893
SIR4_YEASTSIR4physical
8830766
DOT1_YEASTDOT1physical
12080090
RAP1_YEASTRAP1physical
10835378
SIR4_YEASTSIR4physical
10835378
RAD7_YEASTRAD7physical
10835378
H3_YEASTHHT1physical
10835378
H4_YEASTHHF1physical
10835378
SIR4_YEASTSIR4physical
9150138
H4_YEASTHHF1physical
11714726
H4_YEASTHHF1physical
11447281
H3_YEASTHHT1physical
11447281
RAP1_YEASTRAP1physical
12080091
MCM10_YEASTMCM10physical
16085704
SIR4_YEASTSIR4physical
15907466
SIR2_YEASTSIR2physical
15907466
SIR3_YEASTSIR3physical
15907466
SIR4_YEASTSIR4physical
15899856
SIR2_YEASTSIR2physical
15899856
SIR1_YEASTSIR1genetic
10835377
RAD52_YEASTRAD52genetic
9278054
HPR1_YEASTHPR1genetic
8647430
SAN1_YEASTSAN1genetic
2471670
SUM1_YEASTSUM1genetic
11063674
SUM1_YEASTSUM1genetic
3905506
SUM1_YEASTSUM1genetic
2403645
SUM1_YEASTSUM1genetic
2199314
SIR4_YEASTSIR4genetic
9707122
HMO1_YEASTHMO1physical
16554755
SIR1_YEASTSIR1genetic
16581798
SIR3_YEASTSIR3physical
16717101
SIR4_YEASTSIR4physical
16717101
RPD3_YEASTRPD3genetic
10082585
SIR3_YEASTSIR3physical
17176117
H4_YEASTHHF1physical
18158898
H3_YEASTHHT1physical
18158898
SIR4_YEASTSIR4physical
17925448
SIR1_YEASTSIR1physical
18045995
H4_YEASTHHF1physical
18158899
H2A1_YEASTHTA1physical
18158899
H2A2_YEASTHTA2physical
18158899
H2B1_YEASTHTB1physical
18158899
H2B2_YEASTHTB2physical
18158899
H3_YEASTHHT1physical
18158899
H3_YEASTHHT1physical
18391024
COM1_YEASTSAE2physical
18719252
RMR1_YEASTRMR1physical
18719252
SIR2_YEASTSIR2physical
18794362
SIR4_YEASTSIR4physical
18794362
ASF2_YEASTASF2physical
18794362
SIR3_YEASTSIR3physical
18794362
H3_YEASTHHT1physical
18794362
H4_YEASTHHF1physical
18794362
HSP72_YEASTSSA2physical
19536198
SSB1_YEASTSSB1physical
19536198
DOT1_YEASTDOT1genetic
18562671
H2A1_YEASTHTA1physical
19217406
H2B1_YEASTHTB1physical
19217406
H3_YEASTHHT1physical
19217406
H4_YEASTHHF1physical
19217406
SIR1_YEASTSIR1genetic
19273586
DOT1_YEASTDOT1genetic
19273586
H3_YEASTHHT1physical
19273586
SIR1_YEASTSIR1genetic
2005909
RAD50_YEASTRAD50genetic
20348017
CSM1_YEASTCSM1physical
21664583
LRS4_YEASTLRS4genetic
21664583
CHZ1_YEASTCHZ1physical
20008511
SIR1_YEASTSIR1genetic
21896656
SIR3_YEASTSIR3physical
21896656
H32_XENLAhist2h3cphysical
22096199
H4_XENLAhist1h4aphysical
22096199
H2B11_XENLAhist1h2bjphysical
22096199
H4_YEASTHHF1physical
22654676
SIR3_YEASTSIR3physical
23299941
H2B1_YEASTHTB1genetic
20713692
H2B11_XENLAhist1h2bjphysical
23934150
H4_XENLAhist1h4aphysical
23934150
H32_XENLAhist2h3cphysical
23934150
H3_YEASTHHT1physical
23650358
SNF2_YEASTSNF2physical
25453095
SIR4_YEASTSIR4physical
25453095
ARP9_YEASTARP9physical
25453095
SIR4_YEASTSIR4genetic
28188183
SIR1_YEASTSIR1genetic
28188183
SIR1_YEASTSIR1physical
28188183
ARP5_YEASTARP5genetic
25691465
RAD52_YEASTRAD52genetic
26205667
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SIR3_YEAST

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Importance of the sir3 N terminus and its acetylation for yeasttranscriptional silencing.";
Wang X., Connelly J.J., Wang C.L., Sternglanz R.;
Genetics 168:547-551(2004).
Cited for: MUTAGENESIS OF ALA-2, AND ACETYLATION AT ALA-2.
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-502, AND MASSSPECTROMETRY.

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