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Protein

Chromatin-associated protein swi6

Gene

swi6

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Recognizes and binds histone H3 tails methylated at 'Lys-9', leading to epigenetic repression. Involved in the repression of the silent mating-type loci MAT2 and MAT3. May compact MAT2/3 into a heterochromatin-like conformation which represses the transcription of these silent cassettes.

GO - Molecular functioni

  • methylated histone binding Source: PomBase
  • nucleosomal DNA binding Source: PomBase
  • nucleosomal histone binding Source: PomBase
  • RNA binding Source: PomBase

GO - Biological processi

  • cellular protein localization Source: PomBase
  • chromatin remodeling Source: PomBase
  • chromatin silencing at centromere Source: PomBase
  • chromatin silencing at centromere outer repeat region Source: PomBase
  • chromatin silencing at silent mating-type cassette Source: PomBase
  • chromatin silencing at telomere Source: PomBase
  • chromosome passenger complex localization to kinetochore Source: PomBase
  • donor selection Source: PomBase
  • gene conversion at mating-type locus Source: PomBase
  • mating type switching Source: PomBase
  • mitotic sister chromatid cohesion Source: PomBase
  • mitotic sister chromatid segregation Source: PomBase
  • protein localization to chromosome, centromeric region Source: PomBase
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Names & Taxonomyi

Protein namesi
Recommended name:
Chromatin-associated protein swi6
Gene namesi
Name:swi6
ORF Names:SPAC664.01c, SPAC824.10c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC664.01c.
PomBaseiSPAC664.01c. swi6.

Subcellular locationi

  • Nucleus 1 Publication

GO - Cellular componenti

  • chromosome, centromeric outer repeat region Source: PomBase
  • chromosome, telomeric region Source: GOC
  • condensed nuclear chromosome, centromeric region Source: PomBase
  • mating-type region heterochromatin Source: PomBase
  • mitotic spindle pole body Source: PomBase
  • nuclear chromatin Source: PomBase
  • nuclear heterochromatin Source: PomBase
  • nuclear pericentric heterochromatin Source: PomBase
  • nuclear subtelomeric heterochromatin Source: PomBase
  • nucleus Source: PomBase
  • pericentric heterochromatin Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 328328Chromatin-associated protein swi6PRO_0000080217Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei24 – 241Phosphoserine1 Publication
Modified residuei220 – 2201Phosphoserine1 Publication
Modified residuei227 – 2271Phosphoserine1 Publication
Modified residuei240 – 2401Phosphothreonine1 Publication
Modified residuei246 – 2461Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP40381.

PTM databases

iPTMnetiP40381.

Interactioni

Subunit structurei

Interacts with histone H3 methylated at 'Lys-9'. Interacts with the cohesin subunit psc3 and with hrk1.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
him1O598362EBI-926939,EBI-908382
hrp3O141392EBI-926939,EBI-7414157
hsk1P505822EBI-926939,EBI-908476

GO - Molecular functioni

  • methylated histone binding Source: PomBase
  • nucleosomal DNA binding Source: PomBase
  • nucleosomal histone binding Source: PomBase

Protein-protein interaction databases

BioGridi278129. 135 interactions.
DIPiDIP-35736N.
IntActiP40381. 6 interactions.
MINTiMINT-1571275.

Structurei

Secondary structure

1
328
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi83 – 919Combined sources
Beta strandi98 – 1047Combined sources
Beta strandi113 – 1164Combined sources
Helixi118 – 1225Combined sources
Helixi125 – 13511Combined sources
Turni268 – 2725Combined sources
Beta strandi273 – 2819Combined sources
Beta strandi287 – 2937Combined sources
Beta strandi298 – 3025Combined sources
Helixi303 – 3097Combined sources
Helixi311 – 3199Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1E0BX-ray1.90A/B261-328[»]
2RSONMR-A55-142[»]
ProteinModelPortaliP40381.
SMRiP40381. Positions 266-324.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP40381.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini81 – 14363Chromo 1PROSITE-ProRule annotationAdd
BLAST
Domaini267 – 32862Chromo 2PROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi74 – 807Poly-Glu

Sequence similaritiesi

Contains 2 chromo domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

InParanoidiP40381.
OMAiGYLVKWK.
OrthoDBiEOG7Z3FHM.
PhylomeDBiP40381.

Family and domain databases

InterProiIPR000953. Chromo/shadow_dom.
IPR023780. Chromo_domain.
IPR008251. Chromo_shadow_dom.
IPR016197. Chromodomain-like.
IPR023779. Chromodomain_CS.
[Graphical view]
PfamiPF00385. Chromo. 1 hit.
PF01393. Chromo_shadow. 1 hit.
[Graphical view]
SMARTiSM00298. CHROMO. 1 hit.
SM00300. ChSh. 1 hit.
[Graphical view]
SUPFAMiSSF54160. SSF54160. 2 hits.
PROSITEiPS00598. CHROMO_1. 1 hit.
PS50013. CHROMO_2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P40381-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKGGVRSYR RSSTSKRSVI DDDSEPELPS MTKEAIASHK ADSGSSDNEV
60 70 80 90 100
ESDHESKSSS KKLKENAKEE EGGEEEEEDE YVVEKVLKHR MARKGGGYEY
110 120 130 140 150
LLKWEGYDDP SDNTWSSEAD CSGCKQLIEA YWNEHGGRPE PSKRKRTARP
160 170 180 190 200
KKPEAKEPSP KSRKTDEDKH DKDSNEKIED VNEKTIKFAD KSQEEFNENG
210 220 230 240 250
PPSGQPNGHI ESDNESKSPS QKESNESEDI QIAETPSNVT PKKKPSPEVP
260 270 280 290 300
KLPDNRELTV KQVENYDSWE DLVSSIDTIE RKDDGTLEIY LTWKNGAISH
310 320
HPSTITNKKC PQKMLQFYES HLTFRENE
Length:328
Mass (Da):37,293
Last modified:February 1, 1995 - v1
Checksum:iF505CC8AC5E75EAB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X71783 Genomic DNA. Translation: CAA50668.1.
CU329670 Genomic DNA. Translation: CAB57340.1.
PIRiT39111.
RefSeqiNP_593449.1. NM_001018882.2.

Genome annotation databases

EnsemblFungiiSPAC664.01c.1; SPAC664.01c.1:pep; SPAC664.01c.
GeneIDi2541633.
KEGGispo:SPAC664.01c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X71783 Genomic DNA. Translation: CAA50668.1.
CU329670 Genomic DNA. Translation: CAB57340.1.
PIRiT39111.
RefSeqiNP_593449.1. NM_001018882.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1E0BX-ray1.90A/B261-328[»]
2RSONMR-A55-142[»]
ProteinModelPortaliP40381.
SMRiP40381. Positions 266-324.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi278129. 135 interactions.
DIPiDIP-35736N.
IntActiP40381. 6 interactions.
MINTiMINT-1571275.

PTM databases

iPTMnetiP40381.

Proteomic databases

MaxQBiP40381.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC664.01c.1; SPAC664.01c.1:pep; SPAC664.01c.
GeneIDi2541633.
KEGGispo:SPAC664.01c.

Organism-specific databases

EuPathDBiFungiDB:SPAC664.01c.
PomBaseiSPAC664.01c. swi6.

Phylogenomic databases

InParanoidiP40381.
OMAiGYLVKWK.
OrthoDBiEOG7Z3FHM.
PhylomeDBiP40381.

Miscellaneous databases

EvolutionaryTraceiP40381.
NextBioi20802726.
PROiP40381.

Family and domain databases

InterProiIPR000953. Chromo/shadow_dom.
IPR023780. Chromo_domain.
IPR008251. Chromo_shadow_dom.
IPR016197. Chromodomain-like.
IPR023779. Chromodomain_CS.
[Graphical view]
PfamiPF00385. Chromo. 1 hit.
PF01393. Chromo_shadow. 1 hit.
[Graphical view]
SMARTiSM00298. CHROMO. 1 hit.
SM00300. ChSh. 1 hit.
[Graphical view]
SUPFAMiSSF54160. SSF54160. 2 hits.
PROSITEiPS00598. CHROMO_1. 1 hit.
PS50013. CHROMO_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Switching gene swi6, involved in repression of silent mating-type loci in fission yeast, encodes a homologue of chromatin-associated proteins from Drosophila and mammals."
    Lorentz A., Ostermann K., Fleck O., Schmidt H.
    Gene 143:139-143(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  2. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  3. "Recruitment of cohesin to heterochromatic regions by Swi6/HP1 in fission yeast."
    Nonaka N., Kitajima T., Yokobayashi S., Xiao G., Yamamoto M., Grewal S.I.S., Watanabe Y.
    Nat. Cell Biol. 4:89-93(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PSC3.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24; SER-220; SER-227; THR-240 AND SER-246, IDENTIFICATION BY MASS SPECTROMETRY.
  5. "Two histone marks establish the inner centromere and chromosome bi-orientation."
    Yamagishi Y., Honda T., Tanno Y., Watanabe Y.
    Science 330:239-243(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH HRK1.
  6. "Dimerisation of a chromo shadow domain and distinctions from the chromodomain as revealed by structural analysis."
    Cowieson N.P., Partridge J.F., Allshire R.C., McLaughlin P.J.
    Curr. Biol. 10:517-525(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 261-328.

Entry informationi

Entry nameiSWI6_SCHPO
AccessioniPrimary (citable) accession number: P40381
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: May 11, 2016
This is version 142 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. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  3. SIMILARITY comments
    Index of protein domains and families

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.