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Protein

Regulatory protein SIR4

Gene

SIR4

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.1 Publication

GO - Molecular functioni

  • double-stranded DNA binding Source: SGD
  • nucleosome binding Source: SGD

GO - Biological processi

  • chromatin silencing Source: SGD
  • negative regulation of chromatin silencing involved in replicative cell aging 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-29806-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Regulatory protein SIR4
Alternative name(s):
Silent information regulator 4
Gene namesi
Name:SIR4
Synonyms:ASD1, STE9, UTH2
Ordered Locus Names:YDR227W
ORF Names:YD9934.12
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDR227W.
SGDiS000002635. SIR4.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 13581358Regulatory protein SIR4PRO_0000097769Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei692 – 6921PhosphoserineCombined sources
Cross-linki1128 – 1128Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP11978.
PeptideAtlasiP11978.

PTM databases

iPTMnetiP11978.

Interactioni

Subunit structurei

Homodimer. Interacts with MPS3, RIS1, SIR1, SIR2, SIR3, YKU80 and RAP1 C-terminus.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
NUP170P381813EBI-17237,EBI-11756
RAP1P119384EBI-17237,EBI-14821
RTT106P401612EBI-17237,EBI-29119
SIR2P067006EBI-17237,EBI-17219
SIR3P067016EBI-17237,EBI-17230
YKU80Q044372EBI-17237,EBI-8224

GO - Molecular functioni

  • nucleosome binding Source: SGD

Protein-protein interaction databases

BioGridi32279. 94 interactions.
DIPiDIP-33N.
IntActiP11978. 12 interactions.
MINTiMINT-622754.

Structurei

Secondary structure

1
1358
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi808 – 82114Combined sources
Helixi829 – 8379Combined sources
Turni846 – 8483Combined sources
Turni854 – 8574Combined sources
Turni861 – 8633Combined sources
Helixi864 – 8663Combined sources
Helixi869 – 8724Combined sources
Beta strandi879 – 8835Combined sources
Helixi1273 – 134270Combined sources
Turni1343 – 13453Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1NYHX-ray3.10A1198-1358[»]
1PL5X-ray2.50A/S1217-1358[»]
4IAOX-ray2.90C/D737-893[»]
ProteinModelPortaliP11978.
SMRiP11978. Positions 803-893, 1271-1346.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP11978.

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili1271 – 134777Add
BLAST

Keywords - Domaini

Coiled coil

Phylogenomic databases

InParanoidiP11978.
KOiK11123.
OMAiKHASENI.
OrthoDBiEOG70GMTK.

Family and domain databases

InterProiIPR031556. SIR4_SID.
[Graphical view]
PfamiPF16991. SIR4_SID. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P11978-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPNDNKTPNR SSTPKFTKKP VTPNDKIPER EEKSNEVKTP KIPLFTFAKS
60 70 80 90 100
KNYSRPSTAI HTSPHQPSDV KPTSHKQLQQ PKSSPLKKNN YNSFPHSNLE
110 120 130 140 150
KISNSKLLSL LRSKTSAGRI ESNNPSHDAS RSLASFEQTA FSRHAQQQTS
160 170 180 190 200
TFNSKPVRTI VPISTSQTNN SFLSGVKSLL SEEKIRDYSK EILGINLANE
210 220 230 240 250
QPVLEKPLKK GSADIGASVI SLTKDKSIRK DTVEEKKEEK LNIGKNFAHS
260 270 280 290 300
DSLSVPKVSA GDSGISPEES KARSPGIAKP NAIQTEVYGI NEESTNERLE
310 320 330 340 350
INQEKPVKLD ENSANSTVAS ALDTNGTSAT TETLTSKKIV PSPKKVAIDQ
360 370 380 390 400
DKITLHDEKT LAPSKHQPIT SEQKMKEDAD LKRMEILKSP HLSKSPADRP
410 420 430 440 450
QGRRNSRNFS TRDEETTKLA FLVEYEGQEN NYNSTSRSTE KKNDMNTSAK
460 470 480 490 500
NKNGENKKIG KRPPEIMSTE AHVNKVTEET TKQIQSVRID GRKVLQKVQG
510 520 530 540 550
ESHIDSRNNT LNVTPSKRPQ LGEIPNPMKK HKPNEGRTPN ISNGTINIQK
560 570 580 590 600
KLEPKEIVRD ILHTKESSNE AKKTIQNPLN KSQNTALPST HKVTQKKDIK
610 620 630 640 650
IGTNDLFQVE SAPKISSEID RENVKSKDEP VSKAVESKSL LNLFSNVLKA
660 670 680 690 700
PFIKSESKPF SSDALSKEKA NFLETIASTE KPENKTDKVS LSQPVSASKH
710 720 730 740 750
EYSDNFPVSL SQPSKKSFAN HTEDEQIEKK KICRGRMNTI ITHPGKMELV
760 770 780 790 800
YVSDSDDSSS DNDSLTDLES LSSGESNEIK VTNDLDTSAE KDQIQAGKWF
810 820 830 840 850
DPVLDWRKSD RELTKNILWR IADKTTYDKE TITDLIEQGI PKHSYLSGNP
860 870 880 890 900
LTSVTNDICS VENYETSSAF FYQQVHKKDR LQYLPLYAVS TFENTNNTEK
910 920 930 940 950
NDVTNKNINI GKHSQEQNSS SAKPSQIPTV SSPLGFEETK LSTTPTKSNR
960 970 980 990 1000
RVSHSDTNSS KPKNTKENLS KSSWRQEWLA NLKLISVSLV DEFPSELSDS
1010 1020 1030 1040 1050
DRQIINEKMQ LLKDIFANNL KSAISNNFRE SDIIILKGEI EDYPMSSEIK
1060 1070 1080 1090 1100
IYYNELQNKP DAKKARFWSF MKTQRFVSNM GFDIQKSCEP VSISTSVKPH
1110 1120 1130 1140 1150
VVEPEHMADA KIMPKDILQI TKKPLMVKNV KPSSPPDVKS LVQLSTMETK
1160 1170 1180 1190 1200
TLPEKKQFDS IFNSNKAKII PGNGKHASEN ISLSFSRPAS YGYFSVGKRV
1210 1220 1230 1240 1250
PIVEDRRVKQ LDDITDSNTT EILTSVDVLG THSQTGTQQS NMYTSTQKTE
1260 1270 1280 1290 1300
LEIDNKDSVT ECSKDMKEDG LSFVDIVLSK AASALDEKEK QLAVANEIIR
1310 1320 1330 1340 1350
SLSDEVMRNE IRITSLQGDL TFTKKCLENA RSQISEKDAK INKLMEKDFQ

VNKEIKPY
Length:1,358
Mass (Da):152,062
Last modified:October 1, 1989 - v1
Checksum:i9C698765964F094E
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti994 – 9941P → L.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M37249 Genomic DNA. Translation: AAA20881.1.
U13239 Genomic DNA. Translation: AAC33144.1.
Z48612 Genomic DNA. Translation: CAA88507.1.
BK006938 Genomic DNA. Translation: DAA12069.1.
PIRiA29360.
RefSeqiNP_010513.1. NM_001180535.1.

Genome annotation databases

EnsemblFungiiYDR227W; YDR227W; YDR227W.
GeneIDi851813.
KEGGisce:YDR227W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M37249 Genomic DNA. Translation: AAA20881.1.
U13239 Genomic DNA. Translation: AAC33144.1.
Z48612 Genomic DNA. Translation: CAA88507.1.
BK006938 Genomic DNA. Translation: DAA12069.1.
PIRiA29360.
RefSeqiNP_010513.1. NM_001180535.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1NYHX-ray3.10A1198-1358[»]
1PL5X-ray2.50A/S1217-1358[»]
4IAOX-ray2.90C/D737-893[»]
ProteinModelPortaliP11978.
SMRiP11978. Positions 803-893, 1271-1346.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32279. 94 interactions.
DIPiDIP-33N.
IntActiP11978. 12 interactions.
MINTiMINT-622754.

PTM databases

iPTMnetiP11978.

Proteomic databases

MaxQBiP11978.
PeptideAtlasiP11978.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDR227W; YDR227W; YDR227W.
GeneIDi851813.
KEGGisce:YDR227W.

Organism-specific databases

EuPathDBiFungiDB:YDR227W.
SGDiS000002635. SIR4.

Phylogenomic databases

InParanoidiP11978.
KOiK11123.
OMAiKHASENI.
OrthoDBiEOG70GMTK.

Enzyme and pathway databases

BioCyciYEAST:G3O-29806-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP11978.
NextBioi969671.
PROiP11978.

Family and domain databases

InterProiIPR031556. SIR4_SID.
[Graphical view]
PfamiPF16991. SIR4_SID. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Functional domains of SIR4, a gene required for position effect regulation in Saccharomyces cerevisiae."
    Marshall M., Mahoney D., Rose A., Hicks J.B., Broach J.R.
    Mol. Cell. Biol. 7:4441-4452(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Insertion site specificity of the transposon Tn3."
    Davies C.J., Hutchison C.A. III
    Nucleic Acids Res. 23:507-514(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
    Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
    , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
    Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. "Identification of a member of a DNA-dependent ATPase family that causes interference with silencing."
    Zhang Z., Buchman A.R.
    Mol. Cell. Biol. 17:5461-5472(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RIS1.
  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. "Separation-of-function mutants of yeast Ku80 reveal a Yku80p-Sir4p interaction involved in telomeric silencing."
    Roy R., Meier B., McAinsh A.D., Feldmann H.M., Jackson S.P.
    J. Biol. Chem. 279:86-94(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH YKU80.
  8. "A proteomic strategy for gaining insights into protein sumoylation in yeast."
    Denison C., Rudner A.D., Gerber S.A., Bakalarski C.E., Moazed D., Gygi S.P.
    Mol. Cell. Proteomics 4:246-254(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1128.
  9. "Telomere anchoring at the nuclear periphery requires the budding yeast Sad1-UNC-84 domain protein Mps3."
    Bupp J.M., Martin A.E., Stensrud E.S., Jaspersen S.L.
    J. Cell Biol. 179:845-854(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH MPS3.
  10. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces 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) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  11. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-692, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "Structure of the coiled-coil dimerization motif of Sir4 and its interaction with Sir3."
    Chang J.F., Hall B.E., Tanny J.C., Moazed D., Filman D., Ellenberger T.
    Structure 11:637-649(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 1271-1346.

Entry informationi

Entry nameiSIR4_YEAST
AccessioniPrimary (citable) accession number: P11978
Secondary accession number(s): D6VSK9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: May 11, 2016
This is version 148 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: 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.