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Protein

Regulatory protein SIR3

Gene

SIR3

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.

GO - Molecular functioni

  • chromatin binding Source: SGD
  • double-stranded DNA binding Source: SGD
  • identical protein binding Source: IntAct
  • nucleosomal histone binding Source: SGD
  • nucleosome binding Source: SGD
  • single-stranded DNA binding Source: SGD

GO - Biological processi

  • chromatin silencing at silent mating-type cassette Source: SGD
  • heterochromatin assembly Source: SGD
  • negative regulation of chromatin silencing involved in replicative cell aging Source: SGD
  • nuclear-transcribed mRNA catabolic process, non-stop decay Source: SGD
  • telomere tethering at nuclear periphery Source: SGD
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-32498-MONOMER.
ReactomeiR-SCE-113510. E2F mediated regulation of DNA replication.
R-SCE-68616. Assembly of the ORC complex at the origin of replication.
R-SCE-68689. CDC6 association with the ORC:origin complex.
R-SCE-68949. Orc1 removal from chromatin.
R-SCE-68962. Activation of the pre-replicative complex.
R-SCE-69017. CDK-mediated phosphorylation and removal of Cdc6.
R-SCE-69205. G1/S-Specific Transcription.
R-SCE-69298. Association of licensing factors with the pre-replicative complex.

Names & Taxonomyi

Protein namesi
Recommended name:
Regulatory protein SIR3
Alternative name(s):
Silent information regulator 3
Gene namesi
Name:SIR3
Synonyms:CMT1, MAR2, STE8
Ordered Locus Names:YLR442C
ORF Names:L9753.10
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XII

Organism-specific databases

EuPathDBiFungiDB:YLR442C.
SGDiS000004434. SIR3.

Subcellular locationi

GO - Cellular componenti

  • chromatin silencing complex Source: SGD
  • chromosome, telomeric region Source: SGD
  • nuclear chromosome, telomeric region Source: SGD
  • nuclear heterochromatin Source: SGD
  • nuclear telomeric heterochromatin Source: SGD
  • nucleolus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi2A → G: No acetylation, reduced silencing activity. 1 Publication1
Mutagenesisi2A → Q: No acetylation, No silencing activity. 1 Publication1
Mutagenesisi2A → S: No effect. 1 Publication1
Mutagenesisi2A → T: Reduced silencing activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00000977682 – 978Regulatory protein SIR3Add BLAST977

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanine1 Publication1

Post-translational modificationi

N-terminal acetylation by NatA is important for transcriptional silencing activity.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP06701.
PRIDEiP06701.

PTM databases

iPTMnetiP06701.

Interactioni

Subunit structurei

Homodimer and interacts with SIR4 and RAP1 C-terminus. Interacts with MCM10.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
itself8EBI-17230,EBI-17230
RAP1P119382EBI-17230,EBI-14821
SIR4P119786EBI-17230,EBI-17237

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • nucleosomal histone binding Source: SGD

Protein-protein interaction databases

BioGridi31701. 99 interactors.
DIPiDIP-595N.
IntActiP06701. 22 interactors.
MINTiMINT-673027.

Structurei

Secondary structure

1978
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 4Combined sources3
Helixi5 – 8Combined sources4
Beta strandi11 – 16Combined sources6
Beta strandi18 – 20Combined sources3
Beta strandi22 – 24Combined sources3
Beta strandi27 – 30Combined sources4
Turni31 – 35Combined sources5
Beta strandi37 – 43Combined sources7
Turni44 – 46Combined sources3
Beta strandi49 – 51Combined sources3
Beta strandi55 – 60Combined sources6
Turni61 – 64Combined sources4
Beta strandi65 – 75Combined sources11
Beta strandi79 – 82Combined sources4
Beta strandi84 – 91Combined sources8
Helixi93 – 95Combined sources3
Helixi98 – 105Combined sources8
Helixi107 – 111Combined sources5
Helixi116 – 126Combined sources11
Beta strandi131 – 141Combined sources11
Helixi143 – 145Combined sources3
Beta strandi146 – 149Combined sources4
Beta strandi151 – 153Combined sources3
Turni155 – 157Combined sources3
Beta strandi159 – 163Combined sources5
Turni167 – 169Combined sources3
Beta strandi170 – 176Combined sources7
Turni179 – 181Combined sources3
Beta strandi184 – 186Combined sources3
Helixi189 – 198Combined sources10
Helixi201 – 211Combined sources11
Helixi465 – 475Combined sources11
Helixi535 – 568Combined sources34
Beta strandi574 – 578Combined sources5
Helixi583 – 598Combined sources16
Turni599 – 603Combined sources5
Beta strandi608 – 614Combined sources7
Helixi622 – 632Combined sources11
Helixi643 – 652Combined sources10
Helixi655 – 657Combined sources3
Beta strandi660 – 666Combined sources7
Beta strandi669 – 671Combined sources3
Helixi675 – 685Combined sources11
Beta strandi691 – 696Combined sources6
Helixi704 – 708Combined sources5
Helixi711 – 714Combined sources4
Beta strandi717 – 721Combined sources5
Helixi727 – 741Combined sources15
Beta strandi745 – 749Combined sources5
Beta strandi755 – 757Combined sources3
Beta strandi773 – 776Combined sources4
Helixi782 – 796Combined sources15
Helixi799 – 820Combined sources22
Beta strandi831 – 833Combined sources3
Helixi837 – 843Combined sources7
Helixi851 – 856Combined sources6
Helixi860 – 873Combined sources14
Beta strandi874 – 876Combined sources3
Beta strandi880 – 882Combined sources3
Helixi883 – 896Combined sources14
Helixi901 – 910Combined sources10
Helixi920 – 923Combined sources4
Helixi928 – 937Combined sources10
Beta strandi940 – 945Combined sources6
Beta strandi947 – 949Combined sources3
Beta strandi952 – 956Combined sources5
Helixi959 – 968Combined sources10
Helixi970 – 972Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2FL7X-ray1.85A1-229[»]
2FVUX-ray2.00A/B1-219[»]
3OWTX-ray2.00C456-481[»]
3TE6X-ray2.80A/B530-845[»]
3TU4X-ray3.00K/L1-213[»]
3ZCOX-ray2.70A840-978[»]
4JJNX-ray3.09K/L2-382[»]
4KUDX-ray3.20K/L2-219[»]
4KUIX-ray1.85A2-219[»]
4KULX-ray2.62A2-219[»]
4LD9X-ray3.31K/L2-229[»]
DisProtiDP00533.
ProteinModelPortaliP06701.
SMRiP06701.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP06701.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini48 – 188BAHPROSITE-ProRule annotationAdd BLAST141

Sequence similaritiesi

Contains 1 BAH domain.PROSITE-ProRule annotation

Phylogenomic databases

GeneTreeiENSGT00530000063498.
InParanoidiP06701.
KOiK11122.
OMAiGSANTHY.
OrthoDBiEOG092C0XFO.

Family and domain databases

InterProiIPR001025. BAH_dom.
[Graphical view]
PfamiPF01426. BAH. 1 hit.
[Graphical view]
SMARTiSM00439. BAH. 1 hit.
[Graphical view]
PROSITEiPS51038. BAH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P06701-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKTLKDLDG WQVIITDDQG RVIDDNNRRR SRKRGGENVF LKRISDGLSF
60 70 80 90 100
GKGESVIFND NVTETYSVYL IHEIRLNTLN NVVEIWVFSY LRWFELKPKL
110 120 130 140 150
YYEQFRPDLI KEDHPLEFYK DKFFNEVNKS ELYLTAELSE IWLKDFIAVG
160 170 180 190 200
QILPESQWND SSIDKIEDRD FLVRYACEPT AEKFVPIDIF QIIRRVKEME
210 220 230 240 250
PKQSDEYLKR VSVPVSGQKT NRQVMHKMGV ERSSKRLAKK PSMKKIKIEP
260 270 280 290 300
SADDDVNNGN IPSQRGTSTT HGSISPQEES VSPNISSASP SALTSPTDSS
310 320 330 340 350
KILQKRSISK ELIVSEEIPI NSSEQESDYE PNNETSVLSS KPGSKPEKTS
360 370 380 390 400
TELVDGRENF VYANNPEVSD DGGLEEETDE VSSESSDEAI IPVNKRRGAH
410 420 430 440 450
GSELSSKIRK IHIQETQEFS KNYTTETDNE MNGNGKPGIP RGNTKIHSMN
460 470 480 490 500
ENPTPEKGNA KMIDFATLSK LKKKYQIILD RFAPDNQVTD SSQLNKLTDE
510 520 530 540 550
QSSLDVAGLE DKFRKACSSS GRETILSNFN ADINLEESIR ESLQKRELLK
560 570 580 590 600
SQVEDFTRIF LPIYDSLMSS QNKLFYITNA DDSTKFQLVN DVMDELITSS
610 620 630 640 650
ARKELPIFDY IHIDALELAG MDALYEKIWF AISKENLCGD ISLEALNFYI
660 670 680 690 700
TNVPKAKKRK TLILIQNPEN LLSEKILQYF EKWISSKNSK LSIICVGGHN
710 720 730 740 750
VTIREQINIM PSLKAHFTEI KLNKVDKNEL QQMIITRLKS LLKPFHVKVN
760 770 780 790 800
DKKEMTIYNN IREGQNQKIP DNVIVINHKI NNKITQLIAK NVANVSGSTE
810 820 830 840 850
KAFKICEAAV EISKKDFVRK GGLQKGKLVV SQEMVPRYFS EAINGFKDET
860 870 880 890 900
ISKKIIGMSL LMRTFLYTLA QETEGTNRHT LALETVLIKM VKMLRDNPGY
910 920 930 940 950
KASKEIKKVI CGAWEPAITI EKLKQFSWIS VVNDLVGEKL VVVVLEEPSA
960 970
SIMVELKLPL EINYAFSMDE EFKNMDCI
Length:978
Mass (Da):111,360
Last modified:January 23, 2007 - v6
Checksum:iCA2503D7645397AC
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti74I → T in AAT93176 (PubMed:17322287).Curated1
Sequence conflicti331P → S in CAA25668 (PubMed:6098447).Curated1
Sequence conflicti335T → P in CAA25668 (PubMed:6098447).Curated1
Sequence conflicti405S → G in CAA25668 (PubMed:6098447).Curated1
Sequence conflicti421K → Q in CAA25668 (PubMed:6098447).Curated1
Sequence conflicti429 – 430NE → KK in CAA25668 (PubMed:6098447).Curated2
Sequence conflicti497L → V in CAA25668 (PubMed:6098447).Curated1
Sequence conflicti587Q → R in CAA25668 (PubMed:6098447).Curated1
Sequence conflicti597I → V in CAA25668 (PubMed:6098447).Curated1
Sequence conflicti669E → D in CAA25668 (PubMed:6098447).Curated1
Sequence conflicti704R → G in CAA25668 (PubMed:6098447).Curated1
Sequence conflicti712S → T in CAA25668 (PubMed:6098447).Curated1
Sequence conflicti726D → N in CAA25668 (PubMed:6098447).Curated1
Sequence conflicti828L → F (PubMed:6098447).Curated1
Sequence conflicti830V → L (PubMed:6098447).Curated1
Sequence conflicti925Q → K in CAA25668 (PubMed:6098447).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X01420 Genomic DNA. Translation: CAA25668.1.
U21094 Genomic DNA. Translation: AAB67522.1.
AY693157 Genomic DNA. Translation: AAT93176.1.
BK006945 Genomic DNA. Translation: DAA09743.1.
PIRiS59410. RGBYI3.
RefSeqiNP_013547.3. NM_001182330.3.

Genome annotation databases

EnsemblFungiiYLR442C; YLR442C; YLR442C.
GeneIDi851163.
KEGGisce:YLR442C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X01420 Genomic DNA. Translation: CAA25668.1.
U21094 Genomic DNA. Translation: AAB67522.1.
AY693157 Genomic DNA. Translation: AAT93176.1.
BK006945 Genomic DNA. Translation: DAA09743.1.
PIRiS59410. RGBYI3.
RefSeqiNP_013547.3. NM_001182330.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2FL7X-ray1.85A1-229[»]
2FVUX-ray2.00A/B1-219[»]
3OWTX-ray2.00C456-481[»]
3TE6X-ray2.80A/B530-845[»]
3TU4X-ray3.00K/L1-213[»]
3ZCOX-ray2.70A840-978[»]
4JJNX-ray3.09K/L2-382[»]
4KUDX-ray3.20K/L2-219[»]
4KUIX-ray1.85A2-219[»]
4KULX-ray2.62A2-219[»]
4LD9X-ray3.31K/L2-229[»]
DisProtiDP00533.
ProteinModelPortaliP06701.
SMRiP06701.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31701. 99 interactors.
DIPiDIP-595N.
IntActiP06701. 22 interactors.
MINTiMINT-673027.

PTM databases

iPTMnetiP06701.

Proteomic databases

MaxQBiP06701.
PRIDEiP06701.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYLR442C; YLR442C; YLR442C.
GeneIDi851163.
KEGGisce:YLR442C.

Organism-specific databases

EuPathDBiFungiDB:YLR442C.
SGDiS000004434. SIR3.

Phylogenomic databases

GeneTreeiENSGT00530000063498.
InParanoidiP06701.
KOiK11122.
OMAiGSANTHY.
OrthoDBiEOG092C0XFO.

Enzyme and pathway databases

BioCyciYEAST:G3O-32498-MONOMER.
ReactomeiR-SCE-113510. E2F mediated regulation of DNA replication.
R-SCE-68616. Assembly of the ORC complex at the origin of replication.
R-SCE-68689. CDC6 association with the ORC:origin complex.
R-SCE-68949. Orc1 removal from chromatin.
R-SCE-68962. Activation of the pre-replicative complex.
R-SCE-69017. CDK-mediated phosphorylation and removal of Cdc6.
R-SCE-69205. G1/S-Specific Transcription.
R-SCE-69298. Association of licensing factors with the pre-replicative complex.

Miscellaneous databases

EvolutionaryTraceiP06701.
PROiP06701.

Family and domain databases

InterProiIPR001025. BAH_dom.
[Graphical view]
PfamiPF01426. BAH. 1 hit.
[Graphical view]
SMARTiSM00439. BAH. 1 hit.
[Graphical view]
PROSITEiPS51038. BAH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSIR3_YEAST
AccessioniPrimary (citable) accession number: P06701
Secondary accession number(s): D6VZ77, E9P924
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 153 of the entry and version 6 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 1400 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XII
    Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.