SWI6_SCHPO
ID SWI6_SCHPO Reviewed; 328 AA.
AC P40381;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Chromatin-associated protein swi6;
GN Name=swi6; ORFNames=SPAC664.01c, SPAC824.10c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=8200530; DOI=10.1016/0378-1119(94)90619-x;
RA Lorentz A., Ostermann K., Fleck O., Schmidt H.;
RT "Switching gene swi6, involved in repression of silent mating-type loci in
RT fission yeast, encodes a homologue of chromatin-associated proteins from
RT Drosophila and mammals.";
RL Gene 143:139-143(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP INTERACTION WITH PSC3.
RX PubMed=11780129; DOI=10.1038/ncb739;
RA Nonaka N., Kitajima T., Yokobayashi S., Xiao G., Yamamoto M.,
RA Grewal S.I.S., Watanabe Y.;
RT "Recruitment of cohesin to heterochromatic regions by Swi6/HP1 in fission
RT yeast.";
RL Nat. Cell Biol. 4:89-93(2002).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24; SER-220; SER-227; THR-240
RP AND SER-246, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
RN [5]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH HRK1.
RX PubMed=20929775; DOI=10.1126/science.1194498;
RA Yamagishi Y., Honda T., Tanno Y., Watanabe Y.;
RT "Two histone marks establish the inner centromere and chromosome bi-
RT orientation.";
RL Science 330:239-243(2010).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 261-328.
RX PubMed=10801440; DOI=10.1016/s0960-9822(00)00467-x;
RA Cowieson N.P., Partridge J.F., Allshire R.C., McLaughlin P.J.;
RT "Dimerisation of a chromo shadow domain and distinctions from the
RT chromodomain as revealed by structural analysis.";
RL Curr. Biol. 10:517-525(2000).
CC -!- FUNCTION: Recognizes and binds histone H3 tails methylated at 'Lys-9',
CC leading to epigenetic repression. Involved in the repression of the
CC silent mating-type loci MAT2 and MAT3. May compact MAT2/3 into a
CC heterochromatin-like conformation which represses the transcription of
CC these silent cassettes.
CC -!- SUBUNIT: Interacts with histone H3 methylated at 'Lys-9'. Interacts
CC with the cohesin subunit psc3 and with hrk1.
CC {ECO:0000269|PubMed:11780129, ECO:0000269|PubMed:20929775}.
CC -!- INTERACTION:
CC P40381; O94717: ers1; NbExp=3; IntAct=EBI-926939, EBI-15977565;
CC P40381; O59836: him1; NbExp=2; IntAct=EBI-926939, EBI-908382;
CC P40381; O14139: hrp3; NbExp=2; IntAct=EBI-926939, EBI-7414157;
CC P40381; P50582: hsk1; NbExp=2; IntAct=EBI-926939, EBI-908476;
CC P40381; Q9P7A0: sgo1; NbExp=3; IntAct=EBI-926939, EBI-989427;
CC P40381; P40381: swi6; NbExp=4; IntAct=EBI-926939, EBI-926939;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:20929775}.
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DR EMBL; X71783; CAA50668.1; -; Genomic_DNA.
DR EMBL; CU329670; CAB57340.1; -; Genomic_DNA.
DR PIR; T39111; T39111.
DR RefSeq; NP_593449.1; NM_001018882.2.
DR PDB; 1E0B; X-ray; 1.90 A; A/B=261-328.
DR PDB; 2RSO; NMR; -; A=55-142.
DR PDBsum; 1E0B; -.
DR PDBsum; 2RSO; -.
DR AlphaFoldDB; P40381; -.
DR BMRB; P40381; -.
DR SMR; P40381; -.
DR BioGRID; 278129; 148.
DR DIP; DIP-35736N; -.
DR IntAct; P40381; 10.
DR MINT; P40381; -.
DR STRING; 4896.SPAC664.01c.1; -.
DR iPTMnet; P40381; -.
DR MaxQB; P40381; -.
DR PaxDb; P40381; -.
DR PRIDE; P40381; -.
DR EnsemblFungi; SPAC664.01c.1; SPAC664.01c.1:pep; SPAC664.01c.
DR GeneID; 2541633; -.
DR KEGG; spo:SPAC664.01c; -.
DR PomBase; SPAC664.01c; swi6.
DR VEuPathDB; FungiDB:SPAC664.01c; -.
DR eggNOG; KOG1911; Eukaryota.
DR HOGENOM; CLU_045874_5_0_1; -.
DR InParanoid; P40381; -.
DR OMA; IYLTWKN; -.
DR PhylomeDB; P40381; -.
DR Reactome; R-SPO-73772; RNA Polymerase I Promoter Escape.
DR Reactome; R-SPO-983231; Factors involved in megakaryocyte development and platelet production.
DR EvolutionaryTrace; P40381; -.
DR PRO; PR:P40381; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0000785; C:chromatin; IDA:PomBase.
DR GO; GO:0034507; C:chromosome, centromeric outer repeat region; IDA:PomBase.
DR GO; GO:0099115; C:chromosome, subtelomeric region; IDA:PomBase.
DR GO; GO:0000779; C:condensed chromosome, centromeric region; IDA:PomBase.
DR GO; GO:0000792; C:heterochromatin; IDA:PomBase.
DR GO; GO:1990342; C:heterochromatin island; IDA:PomBase.
DR GO; GO:0031934; C:mating-type region heterochromatin; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005721; C:pericentric heterochromatin; IDA:PomBase.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0042393; F:histone binding; IDA:PomBase.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0035064; F:methylated histone binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IDA:PomBase.
DR GO; GO:0006325; P:chromatin organization; IMP:PomBase.
DR GO; GO:0007534; P:gene conversion at mating-type locus; IMP:PomBase.
DR GO; GO:0033696; P:heterochromatin boundary formation; IMP:PomBase.
DR GO; GO:0007533; P:mating type switching; IMP:PomBase.
DR GO; GO:1990758; P:mitotic sister chromatid biorientation; IMP:PomBase.
DR GO; GO:0071962; P:mitotic sister chromatid cohesion, centromeric; IMP:PomBase.
DR GO; GO:0044820; P:mitotic telomere tethering at nuclear periphery; IMP:PomBase.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0090053; P:positive regulation of pericentric heterochromatin assembly; IMP:CACAO.
DR GO; GO:0030466; P:silent mating-type cassette heterochromatin assembly; IMP:PomBase.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR023780; Chromo_domain.
DR InterPro; IPR008251; Chromo_shadow_dom.
DR InterPro; IPR023779; Chromodomain_CS.
DR Pfam; PF00385; Chromo; 1.
DR Pfam; PF01393; Chromo_shadow; 1.
DR SMART; SM00298; CHROMO; 1.
DR SMART; SM00300; ChSh; 1.
DR SUPFAM; SSF54160; SSF54160; 2.
DR PROSITE; PS00598; CHROMO_1; 1.
DR PROSITE; PS50013; CHROMO_2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Repressor; Transcription; Transcription regulation.
FT CHAIN 1..328
FT /note="Chromatin-associated protein swi6"
FT /id="PRO_0000080217"
FT DOMAIN 81..143
FT /note="Chromo 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00053"
FT DOMAIN 267..328
FT /note="Chromo 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00053"
FT REGION 1..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 132..259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..29
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..69
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..194
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..214
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..229
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 220
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 227
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 240
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 246
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT STRAND 83..91
FT /evidence="ECO:0007829|PDB:2RSO"
FT STRAND 98..104
FT /evidence="ECO:0007829|PDB:2RSO"
FT STRAND 113..116
FT /evidence="ECO:0007829|PDB:2RSO"
FT HELIX 118..122
FT /evidence="ECO:0007829|PDB:2RSO"
FT HELIX 125..135
FT /evidence="ECO:0007829|PDB:2RSO"
FT TURN 268..272
FT /evidence="ECO:0007829|PDB:1E0B"
FT STRAND 273..281
FT /evidence="ECO:0007829|PDB:1E0B"
FT STRAND 287..293
FT /evidence="ECO:0007829|PDB:1E0B"
FT STRAND 298..302
FT /evidence="ECO:0007829|PDB:1E0B"
FT HELIX 303..309
FT /evidence="ECO:0007829|PDB:1E0B"
FT HELIX 311..319
FT /evidence="ECO:0007829|PDB:1E0B"
SQ SEQUENCE 328 AA; 37293 MW; F505CC8AC5E75EAB CRC64;
MKKGGVRSYR RSSTSKRSVI DDDSEPELPS MTKEAIASHK ADSGSSDNEV ESDHESKSSS
KKLKENAKEE EGGEEEEEDE YVVEKVLKHR MARKGGGYEY LLKWEGYDDP SDNTWSSEAD
CSGCKQLIEA YWNEHGGRPE PSKRKRTARP KKPEAKEPSP KSRKTDEDKH DKDSNEKIED
VNEKTIKFAD KSQEEFNENG PPSGQPNGHI ESDNESKSPS QKESNESEDI QIAETPSNVT
PKKKPSPEVP KLPDNRELTV KQVENYDSWE DLVSSIDTIE RKDDGTLEIY LTWKNGAISH
HPSTITNKKC PQKMLQFYES HLTFRENE
