Regulatory protein SWI6 - Saccharomyces cerevisiae (Baker's yeast)

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Reviewed, UniProtKB/Swiss-Prot P09959 (SWI6_YEAST)

Last modified June 16, 2009. Version 105. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Regulatory protein SWI6
Alternative name(s):
    Cell-cycle box factor subunit SWI6
    Trans-acting activator of HO endonuclease gene
    MBF subunit P90

Gene names

Name:	SWI6
Ordered Locus Names:	YLR182W
ORF Names:	L9470.8

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

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Protein attributes

Sequence length	803 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	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).
Subunit structure	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.
Subcellular location	Nucleus. Cytoplasm.
Post-translational modification	Phosphorylated by CDC28 and dephosphorylated by CDC14. Ref.7 Ref.8 Ref.9 Ref.10 Ref.12
Miscellaneous	Present with 3340 molecules/cell in log phase SD medium. Ref.6
Sequence similarities	Contains 5 ANK repeats.

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Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Domain	ANK repeat Repeat
Ligand	DNA-binding
Molecular function	Activator
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	UFP-specific transcription factor mRNA processing during unfolded protein response Inferred from mutant phenotype. Source: SGD meiosis Inferred from genetic interaction. Source: SGD positive regulation of gene-specific transcription Inferred from direct assay. Source: SGD regulation of transcription of G1/S-phase of mitotic cell cycle Traceable author statement. Source: SGD transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	MBF transcription complex Inferred from mutant phenotype. Source: SGD SBF transcription complex Inferred from direct assay. Source: SGD cytoplasm Ref.5 Inferred from direct assay. Source: SGD
Molecular function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW transcription coactivator activity Inferred from direct assay. Source: SGD
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct
	Q08270	1	EBI-18641,EBI-35014
ADH4	P10127	1	EBI-18641,EBI-2233
POL4	P25615	1	EBI-18641,EBI-6115
SWI4	P25302	2	EBI-18641,EBI-18626

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 803

803

Regulatory protein SWI6

PRO_0000067071

Regions

Repeat

318 – 346

ANK 1

Repeat

347 – 383

ANK 2

Repeat

384 – 469

ANK 3

Repeat

470 – 498

ANK 4

Repeat

499 – 514

ANK 5

Compositional bias

631 – 640

Glu-rich (acidic)

Amino acid modifications

Modified residue

133

Phosphoserine Ref.12

Modified residue

160

Phosphoserine; by CDC28 Ref.7 Ref.9 Ref.10

Modified residue

169

Phosphothreonine Ref.12

Modified residue

170

Phosphoserine Ref.12

Modified residue

176

Phosphoserine Ref.12

Modified residue

178

Phosphoserine Ref.12

Modified residue

179

Phosphothreonine Ref.8

Modified residue

182

Phosphothreonine Ref.8

Modified residue

228

Phosphoserine Ref.12

Modified residue

267

Phosphothreonine Ref.12

Modified residue

547

Phosphoserine Ref.9

Secondary structure

803

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P09959-1 [UniParc].

Last modified July 1, 1989. Version 1.
Checksum: 9B317FCACEEC493C
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FASTA

803

90,560

        10         20         30         40         50         60 
MALEEVVRYL GPHNEIPLTL TRDSETGHFL LKHFLPILQQ YHDTGNINET NPDSFPTDEE 

        70         80         90        100        110        120 
RNKLLAHYGI AVNTDDRGEL WIELEKCLQL LNMLNLFGLF QDAFEFEEPE TDQDEEDPSH 

       130        140        150        160        170        180 
SKLPENKTKS ENSKDNISSK RINNLQDMSL DSDAHRELGS PLKKLKIDTS VIDAESDSTP 

       190        200        210        220        230        240 
NTARGKPNDD INKGPSGDNE NNGTDDNDRT AGPIITFTHD LTSDFLSSPL KIMKALPSPV 

       250        260        270        280        290        300 
VNDNEQKMKL EAFLQRLLFP EIQEMPTSLN NDSSNRNSEG GSSNQQQQHV SFDSLLQEVN 

       310        320        330        340        350        360 
DAFPNTQLNL NIPVDEHGNT PLHWLTSIAN LELVKHLVKH GSNRLYGDNM GESCLVKAVK 

       370        380        390        400        410        420 
SVNNYDSGTF EALLDYLYPC LILEDSMNRT ILHHIIITSG MTGCSAAAKY YLDILMGWIV 

       430        440        450        460        470        480 
KKQNRPIQSG TNEKESKPND KNGERKDSIL ENLDLKWIIA NMLNAQDSNG DTCLNIAARL 

       490        500        510        520        530        540 
GNISIVDALL DYGADPFIAN KSGLRPVDFG AGTSKLQNTN GGDENSKMVS KGDYDGQKNG 

       550        560        570        580        590        600 
KAKKIRSQLL KNPPETTSLI NDVQNLLNSI SKDYENETVQ YNEKLEKLHK ELNEQREELA 

       610        620        630        640        650        660 
NSREQLANVK QLKDEYSLMQ EQLTNLKAGI EEEEESFREE SKKLGIIADE SSGIDWDSSE 

       670        680        690        700        710        720 
YDADEPFKVE FLSDFLEDKL QKNYEGDISK LLEAESKEQI MEQIRNQLPA EKIQSMLPPT 

       730        740        750        760        770        780 
VLLKARINAY KRNDKHLTNV LDTISTKQSE LENKFRRVLS LCLKIDENKV DNMLDGLLQA 

       790        800 
ISSEDPQDID TDEMQDFLKK HAS

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 2821408] [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. Hoheisel J.D. Nature 387:87-90(1997) [PubMed: 9169871] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	"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: 1608451] [Abstract] Cited for: CHARACTERIZATION.
[4]	"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: 10409718] [Abstract] Cited for: INTERACTION WITH STB1.
[5]	"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: 12697814] [Abstract] Cited for: NUCLEOCYTOPLASMIC SHUTTLING.
[6]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[7]	"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: 14993267] [Abstract] Cited for: PHOSPHORYLATION AT SER-160.
[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: 17330950] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-179 AND THR-182, MASS SPECTROMETRY.
[9]	"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: 17287358] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-160 AND SER-547, MASS SPECTROMETRY.
[10]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed: 17563356] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-160, MASS SPECTROMETRY.
[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: 18160399] [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: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133; THR-169; SER-170; SER-176; SER-178; SER-228 AND THR-267, MASS SPECTROMETRY.
[13]	"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: 10048928] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 188-514.
+	Additional computationally mapped references.

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Cross-references

Sequence databases

X06238 Genomic DNA. Translation: CAA29581.1.
U17246 Genomic DNA. Translation: AAB67460.1.

PIR

RGBYW6. S03161.

RefSeq

NP_013283.1.

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1SW6	X-ray	2.10	A/B	188-512	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:598N.

IntAct

P09959. 39 interactions.

Proteomic databases

PeptideAtlas

P09959.

Genome annotation databases

Ensembl

YLR182W. Saccharomyces cerevisiae. [Contig view]

GeneID

850879.

GenomeReviews

Gene locus YLR182W in contig Y13138_GR.

KEGG

sce:YLR182W.

NMPDR

fig|4932.3.peg.4293.

Organism-specific databases

CYGD

YLR182w.

SGD

S000004172. SWI6.

Yeast-GFP

Search...

Phylogenomic databases

HOGENOM

P09959.

OMA

P09959. YYLDILM.

Gene expression databases

ArrayExpress

P09959.

GermOnline

YLR182W. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR002110. ANK.
[Graphical view]

Gene3D

G3DSA:1.25.40.20. ANK. 1 hit.

Pfam

PF00023. Ank. 2 hits.
[Graphical view]

SMART

SM00248. ANK. 2 hits.
[Graphical view]

PROSITE

PS50297. ANK_REP_REGION. 2 hits.
PS50088. ANK_REPEAT. 2 hits.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

967230.

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Entry information

Entry name

SWI6_YEAST

Accession

Primary (citable) accession number: P09959

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	July 1, 1989
Last modified:	June 16, 2009
This is version 105 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)

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Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents