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Protein

Regulatory protein SWI6

Gene

SWI6

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

Part of a complex involved in cell-cycle-dependent transcription. SWI4 and SWI6 are required for formation of the cell-cycle box factor-DNA complex. The repeated element in the upstream region of HO (5'-CACGAAAA-3') is called the cell cycle box (CCB).

GO - Molecular functioni

  1. DNA binding Source: UniProtKB-KW
  2. RNA polymerase II transcription coactivator activity Source: SGD

GO - Biological processi

  1. positive regulation of reciprocal meiotic recombination Source: SGD
  2. positive regulation of transcription from RNA polymerase II promoter Source: SGD
  3. positive regulation of transcription from RNA polymerase II promoter in response to heat stress Source: SGD
  4. positive regulation of transcription involved in G1/S transition of mitotic cell cycle Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-32306-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Regulatory protein SWI6
Alternative name(s):
Cell-cycle box factor subunit SWI6
MBF subunit P90
Trans-acting activator of HO endonuclease gene
Gene namesi
Name:SWI6
Ordered Locus Names:YLR182W
ORF Names:L9470.8
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome XII

Organism-specific databases

CYGDiYLR182w.
SGDiS000004172. SWI6.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: SGD
  2. MBF transcription complex Source: SGD
  3. nucleus Source: SGD
  4. SBF transcription complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 803803Regulatory protein SWI6PRO_0000067071Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei149 – 1491Phosphoserine1 Publication
Modified residuei160 – 1601Phosphoserine; by CDC282 Publications
Modified residuei176 – 1761Phosphoserine2 Publications
Modified residuei179 – 1791Phosphothreonine2 Publications
Modified residuei182 – 1821Phosphothreonine2 Publications
Modified residuei547 – 5471Phosphoserine1 Publication

Post-translational modificationi

Phosphorylated by CDC28 and dephosphorylated by CDC14.5 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP09959.
PaxDbiP09959.
PeptideAtlasiP09959.

Expressioni

Gene expression databases

GenevestigatoriP09959.

Interactioni

Subunit structurei

Component of the transcription complex MCB-binding factor (MBF) composed of SWI6 and MBP1. Component of the transcription complex SCB-binding factor (SBF) composed of SWI6 and SWI4. Interacts with MSA1 and STB1.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
MBP1P396785EBI-18641,EBI-10485
SWI4P253028EBI-18641,EBI-18626

Protein-protein interaction databases

BioGridi31453. 393 interactions.
DIPiDIP-598N.
IntActiP09959. 55 interactions.
MINTiMINT-528932.
STRINGi4932.YLR182W.

Structurei

Secondary structure

1
803
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 119Combined sources
Beta strandi16 – 238Combined sources
Turni24 – 263Combined sources
Beta strandi29 – 313Combined sources
Helixi32 – 343Combined sources
Helixi35 – 4410Combined sources
Helixi47 – 493Combined sources
Helixi58 – 6811Combined sources
Beta strandi80 – 823Combined sources
Helixi84 – 9310Combined sources
Turni97 – 1004Combined sources
Helixi101 – 1033Combined sources
Beta strandi104 – 1063Combined sources
Beta strandi214 – 2163Combined sources
Turni225 – 2273Combined sources
Helixi244 – 25815Combined sources
Helixi292 – 30211Combined sources
Helixi321 – 3277Combined sources
Helixi331 – 3399Combined sources
Helixi354 – 3607Combined sources
Helixi363 – 3664Combined sources
Helixi370 – 3778Combined sources
Helixi378 – 3825Combined sources
Helixi391 – 3999Combined sources
Helixi405 – 42117Combined sources
Helixi422 – 4243Combined sources
Beta strandi427 – 4293Combined sources
Helixi448 – 4525Combined sources
Helixi455 – 4617Combined sources
Turni462 – 4643Combined sources
Helixi473 – 4808Combined sources
Helixi483 – 4919Combined sources
Helixi506 – 5094Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1SW6X-ray2.10A/B188-512[»]
2XFVX-ray1.90A/B2-126[»]
ProteinModelPortaliP09959.
SMRiP09959. Positions 2-109, 212-512.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP09959.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati318 – 34629ANK 1Add
BLAST
Repeati347 – 38337ANK 2Add
BLAST
Repeati384 – 46986ANK 3Add
BLAST
Repeati470 – 49829ANK 4Add
BLAST
Repeati499 – 51416ANK 5Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi631 – 64010Glu-rich (acidic)

Sequence similaritiesi

Contains 5 ANK repeats.PROSITE-ProRule annotation

Keywords - Domaini

ANK repeat, Repeat

Phylogenomic databases

eggNOGiCOG0666.
GeneTreeiENSGT00530000067565.
HOGENOMiHOG000057104.
InParanoidiP09959.
KOiK06648.
OMAiYYLDILM.
OrthoDBiEOG73BVP1.

Family and domain databases

Gene3Di1.25.40.20. 2 hits.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR029791. Swi6/Cdc10.
[Graphical view]
PANTHERiPTHR11707:SF17. PTHR11707:SF17. 1 hit.
PfamiPF00023. Ank. 1 hit.
[Graphical view]
SMARTiSM00248. ANK. 2 hits.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
PROSITEiPS50297. ANK_REP_REGION. 2 hits.
PS50088. ANK_REPEAT. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P09959-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MALEEVVRYL GPHNEIPLTL TRDSETGHFL LKHFLPILQQ YHDTGNINET
60 70 80 90 100
NPDSFPTDEE RNKLLAHYGI AVNTDDRGEL WIELEKCLQL LNMLNLFGLF
110 120 130 140 150
QDAFEFEEPE TDQDEEDPSH SKLPENKTKS ENSKDNISSK RINNLQDMSL
160 170 180 190 200
DSDAHRELGS PLKKLKIDTS VIDAESDSTP NTARGKPNDD INKGPSGDNE
210 220 230 240 250
NNGTDDNDRT AGPIITFTHD LTSDFLSSPL KIMKALPSPV VNDNEQKMKL
260 270 280 290 300
EAFLQRLLFP EIQEMPTSLN NDSSNRNSEG GSSNQQQQHV SFDSLLQEVN
310 320 330 340 350
DAFPNTQLNL NIPVDEHGNT PLHWLTSIAN LELVKHLVKH GSNRLYGDNM
360 370 380 390 400
GESCLVKAVK SVNNYDSGTF EALLDYLYPC LILEDSMNRT ILHHIIITSG
410 420 430 440 450
MTGCSAAAKY YLDILMGWIV KKQNRPIQSG TNEKESKPND KNGERKDSIL
460 470 480 490 500
ENLDLKWIIA NMLNAQDSNG DTCLNIAARL GNISIVDALL DYGADPFIAN
510 520 530 540 550
KSGLRPVDFG AGTSKLQNTN GGDENSKMVS KGDYDGQKNG KAKKIRSQLL
560 570 580 590 600
KNPPETTSLI NDVQNLLNSI SKDYENETVQ YNEKLEKLHK ELNEQREELA
610 620 630 640 650
NSREQLANVK QLKDEYSLMQ EQLTNLKAGI EEEEESFREE SKKLGIIADE
660 670 680 690 700
SSGIDWDSSE YDADEPFKVE FLSDFLEDKL QKNYEGDISK LLEAESKEQI
710 720 730 740 750
MEQIRNQLPA EKIQSMLPPT VLLKARINAY KRNDKHLTNV LDTISTKQSE
760 770 780 790 800
LENKFRRVLS LCLKIDENKV DNMLDGLLQA ISSEDPQDID TDEMQDFLKK

HAS
Length:803
Mass (Da):90,560
Last modified:July 1, 1989 - v1
Checksum:i9B317FCACEEC493C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X06238 Genomic DNA. Translation: CAA29581.1.
U17246 Genomic DNA. Translation: AAB67460.1.
BK006945 Genomic DNA. Translation: DAA09502.1.
PIRiS03161. RGBYW6.
RefSeqiNP_013283.1. NM_001182069.1.

Genome annotation databases

EnsemblFungiiYLR182W; YLR182W; YLR182W.
GeneIDi850879.
KEGGisce:YLR182W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X06238 Genomic DNA. Translation: CAA29581.1.
U17246 Genomic DNA. Translation: AAB67460.1.
BK006945 Genomic DNA. Translation: DAA09502.1.
PIRiS03161. RGBYW6.
RefSeqiNP_013283.1. NM_001182069.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1SW6X-ray2.10A/B188-512[»]
2XFVX-ray1.90A/B2-126[»]
ProteinModelPortaliP09959.
SMRiP09959. Positions 2-109, 212-512.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31453. 393 interactions.
DIPiDIP-598N.
IntActiP09959. 55 interactions.
MINTiMINT-528932.
STRINGi4932.YLR182W.

Proteomic databases

MaxQBiP09959.
PaxDbiP09959.
PeptideAtlasiP09959.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYLR182W; YLR182W; YLR182W.
GeneIDi850879.
KEGGisce:YLR182W.

Organism-specific databases

CYGDiYLR182w.
SGDiS000004172. SWI6.

Phylogenomic databases

eggNOGiCOG0666.
GeneTreeiENSGT00530000067565.
HOGENOMiHOG000057104.
InParanoidiP09959.
KOiK06648.
OMAiYYLDILM.
OrthoDBiEOG73BVP1.

Enzyme and pathway databases

BioCyciYEAST:G3O-32306-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP09959.
NextBioi967230.

Gene expression databases

GenevestigatoriP09959.

Family and domain databases

Gene3Di1.25.40.20. 2 hits.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR029791. Swi6/Cdc10.
[Graphical view]
PANTHERiPTHR11707:SF17. PTHR11707:SF17. 1 hit.
PfamiPF00023. Ank. 1 hit.
[Graphical view]
SMARTiSM00248. ANK. 2 hits.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
PROSITEiPS50297. ANK_REP_REGION. 2 hits.
PS50088. ANK_REPEAT. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Similarity between cell-cycle genes of budding yeast and fission yeast and the Notch gene of Drosophila."
    Breeden L., Nasmyth K.
    Nature 329:651-654(1987) [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. "A central role for SWI6 in modulating cell cycle Start-specific transcription in yeast."
    Dirick L., Moll T., Auer H., Nasmyth K.
    Nature 357:508-513(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  5. "Regulation of transcription at the Saccharomyces cerevisiae start transition by Stb1, a Swi6-binding protein."
    Ho Y., Costanzo M., Moore L., Kobayashi R., Andrews B.J.
    Mol. Cell. Biol. 19:5267-5278(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH STB1.
  6. "Cell cycle activation of the Swi6p transcription factor is linked to nucleocytoplasmic shuttling."
    Queralt E., Igual J.C.
    Mol. Cell. Biol. 23:3126-3140(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOCYTOPLASMIC SHUTTLING.
  7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  8. "Clb6/Cdc28 and Cdc14 regulate phosphorylation status and cellular localization of Swi6."
    Geymonat M., Spanos A., Wells G.P., Smerdon S.J., Sedgwick S.G.
    Mol. Cell. Biol. 24:2277-2285(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-160.
  9. "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 THR-179 AND THR-182, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  10. "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
    Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
    Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-160 AND SER-547, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "The SBF- and MBF-associated protein Msa1 is required for proper timing of G1-specific transcription in Saccharomyces cerevisiae."
    Ashe M., de Bruin R.A.M., Kalashnikova T., McDonald W.H., Yates J.R. III, Wittenberg C.
    J. Biol. Chem. 283:6040-6049(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MSA1.
  12. "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-176, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "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-149; SER-176; THR-179 AND THR-182, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "X-ray structural analysis of the yeast cell cycle regulator Swi6 reveals variations of the ankyrin fold and has implications for Swi6 function."
    Foord R., Taylor I.A., Sedgwick S.G., Smerdon S.J.
    Nat. Struct. Biol. 6:157-165(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 188-514.

Entry informationi

Entry nameiSWI6_YEAST
AccessioniPrimary (citable) accession number: P09959
Secondary accession number(s): D6VYI6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: January 7, 2015
This is version 164 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 3340 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

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 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.