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Protein

SIR4-interacting protein SIF2

Gene

SIF2

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

Antagonizes telomeric silencing in yeast. May recruit SIR4 to non-telomeric sites or repression.

GO - Molecular functioni

GO - Biological processi

  • histone deacetylation Source: SGD
  • negative regulation of chromatin silencing at telomere Source: SGD
  • negative regulation of meiotic nuclear division Source: SGD
  • positive regulation of stress-activated MAPK cascade Source: SGD
  • regulation of transcription, DNA-templated Source: SGD
  • regulation of transcription from RNA polymerase II promoter Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator

Enzyme and pathway databases

BioCyciYEAST:G3O-29065-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
SIR4-interacting protein SIF2
Gene namesi
Name:SIF2
Synonyms:EMB1
Ordered Locus Names:YBR103W
ORF Names:YBR0832
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:YBR103W.
SGDiS000000307. SIF2.

Subcellular locationi

GO - Cellular componenti

  • nucleus Source: SGD
  • Set3 complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 535535SIR4-interacting protein SIF2PRO_0000051216Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei137 – 1371PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP38262.

PTM databases

iPTMnetiP38262.

Interactioni

Subunit structurei

Homotetramer. Interacts with SIR4 N-terminal domain. Interacts with a complex composed of SIN3 and RPD3. Identified in the Set3C complex with HOS2, HST1, SNT1, CPR1, HOS4/YIL112W and SET3.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
HOS4P404804EBI-17136,EBI-8492
HST1P536852EBI-17136,EBI-8691

Protein-protein interaction databases

BioGridi32807. 220 interactions.
DIPiDIP-1377N.
IntActiP38262. 20 interactions.
MINTiMINT-391284.

Structurei

Secondary structure

1
535
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi152 – 1565Combined sources
Beta strandi161 – 1655Combined sources
Beta strandi172 – 1776Combined sources
Beta strandi181 – 1899Combined sources
Beta strandi198 – 20710Combined sources
Beta strandi223 – 2286Combined sources
Beta strandi232 – 2398Combined sources
Beta strandi244 – 2485Combined sources
Beta strandi253 – 2575Combined sources
Beta strandi264 – 2696Combined sources
Beta strandi273 – 2808Combined sources
Beta strandi285 – 2895Combined sources
Turni290 – 2934Combined sources
Beta strandi294 – 2996Combined sources
Beta strandi325 – 3284Combined sources
Beta strandi331 – 3355Combined sources
Helixi337 – 3393Combined sources
Beta strandi341 – 3455Combined sources
Beta strandi352 – 3554Combined sources
Beta strandi362 – 3687Combined sources
Turni369 – 3724Combined sources
Beta strandi373 – 3786Combined sources
Beta strandi383 – 3864Combined sources
Beta strandi388 – 3925Combined sources
Beta strandi394 – 3974Combined sources
Beta strandi404 – 4107Combined sources
Turni411 – 4133Combined sources
Beta strandi414 – 4196Combined sources
Beta strandi422 – 4287Combined sources
Turni429 – 4324Combined sources
Beta strandi433 – 4397Combined sources
Beta strandi445 – 4506Combined sources
Beta strandi454 – 4618Combined sources
Beta strandi466 – 4705Combined sources
Helixi472 – 4754Combined sources
Beta strandi496 – 5005Combined sources
Beta strandi509 – 5146Combined sources
Beta strandi518 – 52811Combined sources
Beta strandi531 – 5344Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1R5MX-ray1.55A113-535[»]
ProteinModelPortaliP38262.
SMRiP38262. Positions 1-68, 146-535.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP38262.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini4 – 3633LisHPROSITE-ProRule annotationAdd
BLAST
Repeati155 – 18632WD 1Add
BLAST
Repeati218 – 24831WD 2Add
BLAST
Repeati259 – 28931WD 3Add
BLAST
Repeati316 – 34530WD 4Add
BLAST
Repeati357 – 38731WD 5Add
BLAST
Repeati399 – 42830WD 6Add
BLAST
Repeati440 – 47031WD 7Add
BLAST
Repeati503 – 53432WD 8Add
BLAST

Domaini

The LisH domain mediates tetramerization and interaction with SNT1.1 Publication

Sequence similaritiesi

Contains 1 LisH domain.PROSITE-ProRule annotation
Contains 8 WD repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, WD repeat

Phylogenomic databases

GeneTreeiENSGT00750000117536.
HOGENOMiHOG000111162.
InParanoidiP38262.
KOiK04508.
OMAiYTESELM.
OrthoDBiEOG7B5X4Z.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
InterProiIPR006594. LisH.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF08513. LisH. 1 hit.
PF00400. WD40. 3 hits.
[Graphical view]
SMARTiSM00667. LisH. 1 hit.
SM00320. WD40. 5 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
PROSITEiPS50896. LISH. 1 hit.
PS50082. WD_REPEATS_2. 4 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P38262-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSITSEELNY LIWRYCQEMG HEVSALALQD ETRVLEFDEK YKEHIPLGTL
60 70 80 90 100
VNLVQRGILY TESELMVDSK GDISALNEHH LSEDFNLVQA LQIDKEKFPE
110 120 130 140 150
ISSEGRFTLE TNSESNKAGE DGASTVERET QEDDTNSIDS SDDLDGFVKI
160 170 180 190 200
LKEIVKLDNI VSSTWNPLDE SILAYGEKNS VARLARIVET DQEGKKYWKL
210 220 230 240 250
TIIAELRHPF ALSASSGKTT NQVTCLAWSH DGNSIVTGVE NGELRLWNKT
260 270 280 290 300
GALLNVLNFH RAPIVSVKWN KDGTHIISMD VENVTILWNV ISGTVMQHFE
310 320 330 340 350
LKETGGSSIN AENHSGDGSL GVDVEWVDDD KFVIPGPKGA IFVYQITEKT
360 370 380 390 400
PTGKLIGHHG PISVLEFNDT NKLLLSASDD GTLRIWHGGN GNSQNCFYGH
410 420 430 440 450
SQSIVSASWV GDDKVISCSM DGSVRLWSLK QNTLLALSIV DGVPIFAGRI
460 470 480 490 500
SQDGQKYAVA FMDGQVNVYD LKKLNSKSRS LYGNRDGILN PLPIPLYASY
510 520 530
QSSQDNDYIF DLSWNCAGNK ISVAYSLQEG SVVAI
Length:535
Mass (Da):59,161
Last modified:October 25, 2004 - v2
Checksum:i25C0AEA2CCEF1B07
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti396 – 3961C → S in CAA55606 (PubMed:7900426).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X78993 Genomic DNA. Translation: CAA55606.1.
Z35972 Genomic DNA. Translation: CAA85058.1.
AY693053 Genomic DNA. Translation: AAT93072.1.
BK006936 Genomic DNA. Translation: DAA07222.1.
PIRiS48268.
RefSeqiNP_009661.1. NM_001178451.1.

Genome annotation databases

EnsemblFungiiYBR103W; YBR103W; YBR103W.
GeneIDi852399.
KEGGisce:YBR103W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X78993 Genomic DNA. Translation: CAA55606.1.
Z35972 Genomic DNA. Translation: CAA85058.1.
AY693053 Genomic DNA. Translation: AAT93072.1.
BK006936 Genomic DNA. Translation: DAA07222.1.
PIRiS48268.
RefSeqiNP_009661.1. NM_001178451.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1R5MX-ray1.55A113-535[»]
ProteinModelPortaliP38262.
SMRiP38262. Positions 1-68, 146-535.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32807. 220 interactions.
DIPiDIP-1377N.
IntActiP38262. 20 interactions.
MINTiMINT-391284.

PTM databases

iPTMnetiP38262.

Proteomic databases

MaxQBiP38262.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYBR103W; YBR103W; YBR103W.
GeneIDi852399.
KEGGisce:YBR103W.

Organism-specific databases

EuPathDBiFungiDB:YBR103W.
SGDiS000000307. SIF2.

Phylogenomic databases

GeneTreeiENSGT00750000117536.
HOGENOMiHOG000111162.
InParanoidiP38262.
KOiK04508.
OMAiYTESELM.
OrthoDBiEOG7B5X4Z.

Enzyme and pathway databases

BioCyciYEAST:G3O-29065-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP38262.
PROiP38262.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
InterProiIPR006594. LisH.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF08513. LisH. 1 hit.
PF00400. WD40. 3 hits.
[Graphical view]
SMARTiSM00667. LisH. 1 hit.
SM00320. WD40. 5 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
PROSITEiPS50896. LISH. 1 hit.
PS50082. WD_REPEATS_2. 4 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Analysis of a 70 kb region on the right arm of yeast chromosome II."
    Mannhaupt G., Stucka R., Ehnle S., Vetter I., Feldmann H.
    Yeast 10:1363-1381(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. "Complete DNA sequence of yeast chromosome II."
    Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C.
    , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.
    EMBO J. 13:5795-5809(1994) [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. "Sif2p interacts with Sir4p amino-terminal domain and antagonizes telomeric silencing in yeast."
    Cockell M., Renauld H., Watt P., Gasser S.M.
    Curr. Biol. 8:787-790(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  6. "The S. cerevisiae SET3 complex includes two histone deacetylases, Hos2 and Hst1, and is a meiotic-specific repressor of the sporulation gene program."
    Pijnappel W.W.M.P., Schaft D., Roguev A., Shevchenko A., Tekotte H., Wilm M., Rigaut G., Seraphin B., Aasland R., Stewart A.F.
    Genes Dev. 15:2991-3004(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A COMPLEX WITH HOS2; HST1; SNT1; CPR1; YIL112W AND SET3.
  7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  8. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  9. "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].
  10. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "The structure of Sif2p, a WD repeat protein functioning in the SET3 corepressor complex."
    Cerna D., Wilson D.K.
    J. Mol. Biol. 351:923-935(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 113-535, SUBUNIT, DOMAINS WD REPEATS.

Entry informationi

Entry nameiSIF2_YEAST
AccessioniPrimary (citable) accession number: P38262
Secondary accession number(s): D6VQA2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 25, 2004
Last modified: July 6, 2016
This is version 157 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 1620 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 II
    Yeast (Saccharomyces cerevisiae) chromosome II: 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.