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P06701

- SIR3_YEAST

UniProt

P06701 - SIR3_YEAST

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Protein

Regulatory protein SIR3

Gene

SIR3

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - 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

  1. chromatin binding Source: SGD
  2. double-stranded DNA binding Source: SGD
  3. identical protein binding Source: IntAct
  4. nucleosomal histone binding Source: SGD
  5. nucleosome binding Source: SGD
  6. protein homodimerization activity Source: SGD
  7. single-stranded DNA binding Source: SGD

GO - Biological processi

  1. chromatin silencing at silent mating-type cassette Source: SGD
  2. heterochromatin assembly Source: SGD
  3. negative regulation of chromatin silencing involved in replicative cell aging Source: SGD
  4. nuclear-transcribed mRNA catabolic process, non-stop decay Source: SGD
  5. 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.

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
ProteomesiUP000002311: Chromosome XII

Organism-specific databases

SGDiS000004434. SIR3.

Subcellular locationi

GO - Cellular componenti

  1. chromatin silencing complex Source: SGD
  2. chromosome, telomeric region Source: SGD
  3. nuclear chromosome, telomeric region Source: SGD
  4. nuclear heterochromatin Source: SGD
  5. nuclear telomeric heterochromatin Source: SGD
  6. nucleolus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi2 – 21A → G: No acetylation, reduced silencing activity. 1 Publication
Mutagenesisi2 – 21A → Q: No acetylation, No silencing activity. 1 Publication
Mutagenesisi2 – 21A → S: No effect. 1 Publication
Mutagenesisi2 – 21A → T: Reduced silencing activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 978977Regulatory protein SIR3PRO_0000097768Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication

Post-translational modificationi

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

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP06701.
PaxDbiP06701.
PeptideAtlasiP06701.

Expressioni

Gene expression databases

GenevestigatoriP06701.

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

Protein-protein interaction databases

BioGridi31701. 96 interactions.
DIPiDIP-595N.
IntActiP06701. 22 interactions.
MINTiMINT-673027.
STRINGi4932.YLR442C.

Structurei

Secondary structure

1
978
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 43Combined sources
Helixi5 – 84Combined sources
Beta strandi11 – 166Combined sources
Beta strandi18 – 203Combined sources
Beta strandi22 – 243Combined sources
Beta strandi27 – 304Combined sources
Turni31 – 355Combined sources
Beta strandi37 – 437Combined sources
Turni44 – 463Combined sources
Beta strandi49 – 513Combined sources
Beta strandi55 – 606Combined sources
Turni61 – 644Combined sources
Beta strandi65 – 7511Combined sources
Beta strandi79 – 824Combined sources
Beta strandi84 – 918Combined sources
Helixi93 – 953Combined sources
Helixi98 – 1058Combined sources
Helixi107 – 1115Combined sources
Helixi116 – 12611Combined sources
Beta strandi131 – 14111Combined sources
Helixi143 – 1453Combined sources
Beta strandi146 – 1494Combined sources
Beta strandi151 – 1533Combined sources
Turni155 – 1573Combined sources
Beta strandi159 – 1635Combined sources
Turni167 – 1693Combined sources
Beta strandi170 – 1767Combined sources
Turni179 – 1813Combined sources
Beta strandi184 – 1863Combined sources
Helixi189 – 19810Combined sources
Helixi201 – 21111Combined sources
Helixi465 – 47511Combined sources
Helixi535 – 56834Combined sources
Beta strandi574 – 5785Combined sources
Helixi583 – 59816Combined sources
Turni599 – 6035Combined sources
Beta strandi608 – 6147Combined sources
Helixi622 – 63211Combined sources
Helixi643 – 65210Combined sources
Helixi655 – 6573Combined sources
Beta strandi660 – 6667Combined sources
Beta strandi669 – 6713Combined sources
Helixi675 – 68511Combined sources
Beta strandi691 – 6966Combined sources
Helixi704 – 7085Combined sources
Helixi711 – 7144Combined sources
Beta strandi717 – 7215Combined sources
Helixi727 – 74115Combined sources
Beta strandi745 – 7495Combined sources
Beta strandi755 – 7573Combined sources
Beta strandi773 – 7764Combined sources
Helixi782 – 79615Combined sources
Helixi799 – 82022Combined sources
Beta strandi831 – 8333Combined sources
Helixi837 – 8437Combined sources
Helixi851 – 8566Combined sources
Helixi860 – 87314Combined sources
Beta strandi874 – 8763Combined sources
Beta strandi880 – 8823Combined sources
Helixi883 – 89614Combined sources
Helixi901 – 91010Combined sources
Helixi920 – 9234Combined sources
Helixi928 – 93710Combined sources
Beta strandi940 – 9456Combined sources
Beta strandi947 – 9493Combined sources
Beta strandi952 – 9565Combined sources
Helixi959 – 96810Combined sources
Helixi970 – 9723Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 2-215, 530-844.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP06701.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini48 – 188141BAHPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 BAH domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG1474.
GeneTreeiENSGT00770000121601.
InParanoidiP06701.
KOiK11122.
OMAiYLIHEIR.
OrthoDBiEOG7ZWD9N.

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti74 – 741I → T in AAT93176. (PubMed:17322287)Curated
Sequence conflicti331 – 3311P → S in CAA25668. (PubMed:6098447)Curated
Sequence conflicti335 – 3351T → P in CAA25668. (PubMed:6098447)Curated
Sequence conflicti405 – 4051S → G in CAA25668. (PubMed:6098447)Curated
Sequence conflicti421 – 4211K → Q in CAA25668. (PubMed:6098447)Curated
Sequence conflicti429 – 4302NE → KK in CAA25668. (PubMed:6098447)Curated
Sequence conflicti497 – 4971L → V in CAA25668. (PubMed:6098447)Curated
Sequence conflicti587 – 5871Q → R in CAA25668. (PubMed:6098447)Curated
Sequence conflicti597 – 5971I → V in CAA25668. (PubMed:6098447)Curated
Sequence conflicti669 – 6691E → D in CAA25668. (PubMed:6098447)Curated
Sequence conflicti704 – 7041R → G in CAA25668. (PubMed:6098447)Curated
Sequence conflicti712 – 7121S → T in CAA25668. (PubMed:6098447)Curated
Sequence conflicti726 – 7261D → N in CAA25668. (PubMed:6098447)Curated
Sequence conflicti828 – 8281L → F(PubMed:6098447)Curated
Sequence conflicti830 – 8301V → L(PubMed:6098447)Curated
Sequence conflicti925 – 9251Q → K in CAA25668. (PubMed:6098447)Curated

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 .
PIRi S59410. RGBYI3.
RefSeqi NP_013547.3. NM_001182330.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2FL7 X-ray 1.85 A 1-229 [» ]
2FVU X-ray 2.00 A/B 1-219 [» ]
3OWT X-ray 2.00 C 456-481 [» ]
3TE6 X-ray 2.80 A/B 530-845 [» ]
3TU4 X-ray 3.00 K/L 1-213 [» ]
3ZCO X-ray 2.70 A 840-978 [» ]
4JJN X-ray 3.09 K/L 2-382 [» ]
4KUD X-ray 3.20 K/L 2-219 [» ]
4KUI X-ray 1.85 A 2-219 [» ]
4KUL X-ray 2.62 A 2-219 [» ]
4LD9 X-ray 3.31 K/L 2-229 [» ]
DisProti DP00533.
ProteinModelPortali P06701.
SMRi P06701. Positions 2-215, 530-844.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 31701. 96 interactions.
DIPi DIP-595N.
IntActi P06701. 22 interactions.
MINTi MINT-673027.
STRINGi 4932.YLR442C.

Proteomic databases

MaxQBi P06701.
PaxDbi P06701.
PeptideAtlasi P06701.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YLR442C ; YLR442C ; YLR442C .
GeneIDi 851163.
KEGGi sce:YLR442C.

Organism-specific databases

SGDi S000004434. SIR3.

Phylogenomic databases

eggNOGi COG1474.
GeneTreei ENSGT00770000121601.
InParanoidi P06701.
KOi K11122.
OMAi YLIHEIR.
OrthoDBi EOG7ZWD9N.

Enzyme and pathway databases

BioCyci YEAST:G3O-32498-MONOMER.

Miscellaneous databases

EvolutionaryTracei P06701.
NextBioi 967960.

Gene expression databases

Genevestigatori P06701.

Family and domain databases

InterProi IPR001025. BAH_dom.
[Graphical view ]
Pfami PF01426. BAH. 1 hit.
[Graphical view ]
SMARTi SM00439. BAH. 1 hit.
[Graphical view ]
PROSITEi PS51038. BAH. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of two genes required for the position-effect control of yeast mating-type genes."
    Shore D., Squire M., Nasmyth K.A.
    EMBO J. 3:2817-2823(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."
    Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H.
    , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.
    Nature 387:87-90(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. "Activation of an MAP kinase cascade leads to Sir3p hyperphosphorylation and strengthens transcriptional silencing."
    Stone E.M., Pillus L.
    J. Cell Biol. 135:571-583(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION.
  6. "The molecular biology of the SIR proteins."
    Gasser S.M., Cockell M.M.
    Gene 279:1-16(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  8. "Importance of the sir3 N terminus and its acetylation for yeast transcriptional silencing."
    Wang X., Connelly J.J., Wang C.L., Sternglanz R.
    Genetics 168:547-551(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF ALA-2, ACETYLATION AT ALA-2.
  9. "Dual roles for Mcm10 in DNA replication initiation and silencing at the mating-type loci."
    Douglas N.L., Dozier S.K., Donato J.J.
    Mol. Biol. Rep. 32:197-204(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MCM10.
  10. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Structure of the Sir3 protein bromo adjacent homology (BAH) domain from S. cerevisiae at 1.95 A resolution."
    Hou Z., Danzer J.R., Fox C.A., Keck J.L.
    Protein Sci. 15:1182-1186(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 2-229.

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 26, 2014
This is version 136 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

External Data

Dasty 3