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Protein

SWI/SNF chromatin-remodeling complex subunit SWI1

Gene

SWI1

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

Involved in transcriptional activation. Component of the SWI/SNF complex, an ATP-dependent chromatin remodeling complex, which is required for the positive and negative regulation of gene expression of a large number of genes. It changes chromatin structure by altering DNA-histone contacts within a nucleosome, leading eventually to a change in nucleosome position, thus facilitating or repressing binding of gene-specific transcription factors.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri1241 – 125818C4-typeAdd
BLAST

GO - Molecular functioni

  • DNA binding Source: UniProtKB-KW
  • metal ion binding Source: UniProtKB-KW
  • RNA polymerase II activating transcription factor binding Source: SGD

GO - Biological processi

  • ATP-dependent chromatin remodeling Source: SGD
  • carbon catabolite activation of transcription from RNA polymerase II promoter Source: SGD
  • cellular alcohol catabolic process Source: SGD
  • DNA-dependent DNA replication Source: SGD
  • positive regulation of mating type switching Source: SGD
  • positive regulation of transcription from RNA polymerase II promoter Source: SGD
  • positive regulation of transcription from RNA polymerase II promoter in response to amino acid starvation Source: SGD
  • sucrose catabolic process Source: SGD
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator, Prion

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

BioCyciYEAST:G3O-33935-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
SWI/SNF chromatin-remodeling complex subunit SWI1
Alternative name(s):
Regulatory protein GAM3
SWI/SNF complex subunit SWI1
Transcription regulatory protein ADR6
Transcription regulatory protein SWI1
Gene namesi
Name:SWI1
Synonyms:ADR6, GAM3
Ordered Locus Names:YPL016W
ORF Names:LPA1
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XVI

Organism-specific databases

EuPathDBiFungiDB:YPL016W.
SGDiS000005937. SWI1.

Subcellular locationi

  • Nucleus PROSITE-ProRule annotation1 Publication

  • Note: While the soluble protein is nuclear, [SWI+] aggregates appear to be cytoplasmic.

GO - Cellular componenti

  • nucleus Source: SGD
  • SWI/SNF complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Amyloid, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 13141314SWI/SNF chromatin-remodeling complex subunit SWI1PRO_0000200596Add
BLAST

Proteomic databases

MaxQBiP09547.

PTM databases

iPTMnetiP09547.

Interactioni

Subunit structurei

Component of the SWI/SNF global transcription activator complex. The 1.14 MDa SWI/SNF complex is composed of 11 different subunits: one copy each of SWI1, SNF2/SWI2, SNF5, SNF12/SWP73, ARP7/SWP61, ARP9/SWP59; two copies each of SWI3, SNF6, SNF11, SWP82; and three copies of TAF14/SWP29.

GO - Molecular functioni

  • RNA polymerase II activating transcription factor binding Source: SGD

Protein-protein interaction databases

BioGridi36161. 75 interactions.
DIPiDIP-1032N.
IntActiP09547. 37 interactions.
MINTiMINT-426044.

Structurei

Secondary structure

1
1314
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi396 – 3983Combined sources
Beta strandi402 – 4054Combined sources
Helixi408 – 42215Combined sources
Beta strandi426 – 4294Combined sources
Beta strandi434 – 4374Combined sources
Helixi442 – 4476Combined sources
Turni448 – 4503Combined sources
Helixi453 – 4564Combined sources
Helixi460 – 46910Combined sources
Helixi474 – 49118Combined sources
Turni492 – 4943Combined sources
Beta strandi498 – 5025Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KKXNMR-A405-506[»]
1KN5NMR-A405-506[»]
2LI6NMR-A390-505[»]
ProteinModelPortaliP09547.
SMRiP09547. Positions 390-505.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP09547.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini406 – 49388ARIDPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 323323Prion domain (PrD)Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi337 – 524188Gln-richAdd
BLAST

Domaini

The prion domain (PrD) is a Gln/Asn (Q/N)-rich domain, which is unstructured in its native, soluble form, and which forms a parallel in-register beta-sheet in its amyloid form (By similarity). The first 37 residues of this domain are sufficient for aggregation, propagation, and transmission of the [SWI+] prion.By similarity1 Publication

Sequence similaritiesi

Belongs to the SWI1 family.Curated
Contains 1 ARID domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri1241 – 125818C4-typeAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

InParanoidiP09547.
KOiK11771.
OMAiKQYELFM.
OrthoDBiEOG7B8SCM.

Family and domain databases

Gene3Di1.10.150.60. 1 hit.
InterProiIPR001606. ARID_dom.
[Graphical view]
PfamiPF01388. ARID. 1 hit.
[Graphical view]
SMARTiSM00501. BRIGHT. 1 hit.
[Graphical view]
SUPFAMiSSF46774. SSF46774. 1 hit.
PROSITEiPS51011. ARID. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P09547-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDFFNLNNNN NNNNTTTTTT TTNNNNTNNN NTNNNNNPAN NTNNNNSTGH
60 70 80 90 100
SSNTNNNTNN NNTNTGASGV DDFQNFFDPK PFDQNLDSNN NNSNSNNNDN
110 120 130 140 150
NNSNTVASST NFTSPTAVVN NAAPANVTGG KAANFIQNQS PQFNSPYDSN
160 170 180 190 200
NSNTNLNSLS PQAILAKNSI IDSSNLPLQA QQQLYGGNNN NNSTGIANDN
210 220 230 240 250
VITPHFITNV QSISQNSSSS TPNTNSNSTP NANQQFLPFN NSASNNGNLT
260 270 280 290 300
SNQLISNYAA SNSMDRSSSA SNEFVPNTSD NNNNSNNHNM RNNSNNKTSN
310 320 330 340 350
NNNVTAVPAA TPANTNNSTS NANTVFSERA AMFAALQQKQ QQRFQALQQQ
360 370 380 390 400
QQQQQNQQQQ NQQPQQQQQQ QQNPKFLQSQ RQQQQRSILQ SLNPALQEKI
410 420 430 440 450
STELNNKQYE LFMKSLIENC KKRNMPLQSI PEIGNRKINL FYLYMLVQKF
460 470 480 490 500
GGADQVTRTQ QWSMVAQRLQ ISDYQQLESI YFRILLPYER HMISQEGIKE
510 520 530 540 550
TQAKRIFLQQ FLQELLKKVQ QQQQAAALAN ANNNINSASS APTPAAPGAS
560 570 580 590 600
VPATAAPGTE AGIVPVSANT PKSLNSNINI NVNNNNIGQQ QVKKPRKQRV
610 620 630 640 650
KKKTKKELEL ERKEREDFQK RQQKLLEDQQ RQQKLLLETK LRQQYEIELK
660 670 680 690 700
KLPKVYKRSI VRNYKPLINR LKHYNGYDIN YISKIGEKID SNKPIFLFAP
710 720 730 740 750
ELGAINLHAL SMSLQSKNLG EINTALNTLL VTSADSNLKI SLVKYPELLD
760 770 780 790 800
SLAILGMNLL SNLSQNVVPY HRNTSDYYYE DAGSNQYYVT QHDKMVDKIF
810 820 830 840 850
EKVNNNATLT PNDSNDEKVT ILVDSLTGNQ LPTPTPTEME PDLDTECFIS
860 870 880 890 900
MQSTSPAVKQ WDLLPEPIRF LPNQFPLKIH RTPYLTSLKK IKDEIDDPFT
910 920 930 940 950
KINTRGAEDP KVLINDQLST ISMILRNISF SDNNSRIMSR NFYLKRFISD
960 970 980 990 1000
LLWLVLIHPE NFTCNRKILN FKKDLVIVLS NISHLLEIAS SIDCLLILIL
1010 1020 1030 1040 1050
VISFGQPKLN PMASSSSFGS ESLTFNEFQL QWGKYQTFGV DILAKLFSLE
1060 1070 1080 1090 1100
KPNLNYFKSI LLNKNTGNNL YDRNSNNNHK DKKLLRRLLN LYNDNNKNNN
1110 1120 1130 1140 1150
NRHNLLNDVV SFLFSAIPLQ QVLSQSADPS LLIDQFSPVI SQSLTSILVI
1160 1170 1180 1190 1200
VQKILPLSNE VFEISENNSD SNSNNNGNKD SSFNFNKNLP FVWLSSEENI
1210 1220 1230 1240 1250
GSGLLKLSEI ILNINNSTSK NTLLQQQNYS KVLLPSINIS CVQLIKCLVE
1260 1270 1280 1290 1300
KSICFENCLN NDPEILKKIA SIPNLFPTDL EIFQLFTNPS VDIQIINQYQ
1310
LLYNLKNDIL TNLE
Length:1,314
Mass (Da):147,938
Last modified:July 1, 1989 - v1
Checksum:iF442D5A82013CDBD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X12493 Genomic DNA. Translation: CAA31013.1.
U33335 Genomic DNA. Translation: AAB68089.1.
BK006949 Genomic DNA. Translation: DAA11412.1.
PIRiS05728. TNBYR6.
RefSeqiNP_015309.1. NM_001183830.2.

Genome annotation databases

EnsemblFungiiYPL016W; YPL016W; YPL016W.
GeneIDi856091.
KEGGisce:YPL016W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X12493 Genomic DNA. Translation: CAA31013.1.
U33335 Genomic DNA. Translation: AAB68089.1.
BK006949 Genomic DNA. Translation: DAA11412.1.
PIRiS05728. TNBYR6.
RefSeqiNP_015309.1. NM_001183830.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KKXNMR-A405-506[»]
1KN5NMR-A405-506[»]
2LI6NMR-A390-505[»]
ProteinModelPortaliP09547.
SMRiP09547. Positions 390-505.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36161. 75 interactions.
DIPiDIP-1032N.
IntActiP09547. 37 interactions.
MINTiMINT-426044.

PTM databases

iPTMnetiP09547.

Proteomic databases

MaxQBiP09547.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYPL016W; YPL016W; YPL016W.
GeneIDi856091.
KEGGisce:YPL016W.

Organism-specific databases

EuPathDBiFungiDB:YPL016W.
SGDiS000005937. SWI1.

Phylogenomic databases

InParanoidiP09547.
KOiK11771.
OMAiKQYELFM.
OrthoDBiEOG7B8SCM.

Enzyme and pathway databases

BioCyciYEAST:G3O-33935-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP09547.
PROiP09547.

Family and domain databases

Gene3Di1.10.150.60. 1 hit.
InterProiIPR001606. ARID_dom.
[Graphical view]
PfamiPF01388. ARID. 1 hit.
[Graphical view]
SMARTiSM00501. BRIGHT. 1 hit.
[Graphical view]
SUPFAMiSSF46774. SSF46774. 1 hit.
PROSITEiPS51011. ARID. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The yeast ADR6 gene encodes homopolymeric amino acid sequences and a potential metal-binding domain."
    O'Hara P.J., Horowitz H., Eichinger G., Young E.T.
    Nucleic Acids Res. 16:10153-10169(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI."
    Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M.
    , Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J.
    Nature 387:103-105(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. "Characterization of the yeast SWI1, SWI2, and SWI3 genes, which encode a global activator of transcription."
    Peterson C.L., Herskowitz I.
    Cell 68:573-583(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  6. "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].
  7. "Newly identified prion linked to the chromatin-remodeling factor Swi1 in Saccharomyces cerevisiae."
    Du Z., Park K.W., Yu H., Fan Q., Li L.
    Nat. Genet. 40:460-465(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PRION FORMATION, PRION CURING, SUBCELLULAR LOCATION OF PRION AGGREGATES.
  8. "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].
  9. "Distinct subregions of Swi1 manifest striking differences in prion transmission and SWI/SNF function."
    Du Z., Crow E.T., Kang H.S., Li L.
    Mol. Cell. Biol. 30:4644-4655(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PRION FORMATION, AMYLOID FORMATION.
  10. "A small, glutamine-free domain propagates the [SWI(+)] prion in budding yeast."
    Crow E.T., Du Z., Li L.
    Mol. Cell. Biol. 31:3436-3444(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAIN PRION.
  11. "[SWI], the prion formed by the chromatin remodeling factor Swi1, is highly sensitive to alterations in Hsp70 chaperone system activity."
    Hines J.K., Li X., Du Z., Higurashi T., Li L., Craig E.A.
    PLoS Genet. 7:E1001309-E1001309(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PRION FORMATION.
  12. "Structural analysis of the yeast SWI/SNF chromatin remodeling complex."
    Smith C.L., Horowitz-Scherer R., Flanagan J.F., Woodcock C.L., Peterson C.L.
    Nat. Struct. Biol. 10:141-145(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: 3D-STRUCTURE MODELING OF THE SWI/SNF COMPLEX, ELECTRON MICROSCOPY OF THE SWI/SNF COMPLEX.
  13. "1H, 13C and 15N resonance assignments and secondary structure of ADR6 DNA-binding domain."
    Tu X., Wu J., Xu Y., Shi Y.
    J. Biomol. NMR 21:187-188(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 405-506.

Entry informationi

Entry nameiSWI1_YEAST
AccessioniPrimary (citable) accession number: P09547
Secondary accession number(s): D6W3Z6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: July 6, 2016
This is version 152 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

[SWI+] is the prion form of SWI1 (PubMed:18362884). [SWI+] is the result of a conformational change of the cellular SWI1 protein that becomes self-propagating and infectious. This conformational change generates a form of SWI1 that assembles into amyloid fibrils (PubMed:20679490). [SWI+]-aggregates sequester soluble SWI1, resulting in reduced growth on carbon sources other than glucose, reminiscent of a partial loss of function of the SWI/SNF chromatin-remodeling complex. [SWI+] can be cured by GdnHCl and by deletion of the molecular chaperone HSP104, which is required for [SWI+] propagation (PubMed:18362884). [SWI+] propagation is highly dependent upon the action of members of the Hsp70 molecular chaperone system, specifically the Hsp70 SSA, two of its J-protein co-chaperones, SIS1 and YDJ1, and the nucleotide exchange factors of the Hsp110 family (SSE1/2). Both under- and overexpression of components of this system initiate rapid loss of the prion from the cell population. It is speculated that prion properties of transcription factors may generate an optimized phenotypic heterogeneity that buffers yeast populations against diverse environmental insults (PubMed:21379326).3 Publications
Present with 92 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 XVI
    Yeast (Saccharomyces cerevisiae) chromosome XVI: 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.