SIF2_YEAST
ID SIF2_YEAST Reviewed; 535 AA.
AC P38262; D6VQA2;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 2.
DT 03-AUG-2022, entry version 197.
DE RecName: Full=SIR4-interacting protein SIF2;
GN Name=SIF2; Synonyms=EMB1; OrderedLocusNames=YBR103W; ORFNames=YBR0832;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7900426; DOI=10.1002/yea.320101014;
RA Mannhaupt G., Stucka R., Ehnle S., Vetter I., Feldmann H.;
RT "Analysis of a 70 kb region on the right arm of yeast chromosome II.";
RL Yeast 10:1363-1381(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP CHARACTERIZATION.
RX PubMed=9651685; DOI=10.1016/s0960-9822(98)70304-5;
RA Cockell M., Renauld H., Watt P., Gasser S.M.;
RT "Sif2p interacts with Sir4p amino-terminal domain and antagonizes telomeric
RT silencing in yeast.";
RL Curr. Biol. 8:787-790(1998).
RN [6]
RP IDENTIFICATION IN A COMPLEX WITH HOS2; HST1; SNT1; CPR1; YIL112W AND SET3.
RX PubMed=11711434; DOI=10.1101/gad.207401;
RA Pijnappel W.W.M.P., Schaft D., Roguev A., Shevchenko A., Tekotte H.,
RA Wilm M., Rigaut G., Seraphin B., Aasland R., Stewart A.F.;
RT "The S. cerevisiae SET3 complex includes two histone deacetylases, Hos2 and
RT Hst1, and is a meiotic-specific repressor of the sporulation gene
RT program.";
RL Genes Dev. 15:2991-3004(2001).
RN [7]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 113-535, SUBUNIT, AND DOMAINS WD
RP REPEATS.
RX PubMed=16051270; DOI=10.1016/j.jmb.2005.06.025;
RA Cerna D., Wilson D.K.;
RT "The structure of Sif2p, a WD repeat protein functioning in the SET3
RT corepressor complex.";
RL J. Mol. Biol. 351:923-935(2005).
CC -!- FUNCTION: Antagonizes telomeric silencing in yeast. May recruit SIR4 to
CC non-telomeric sites or repression.
CC -!- SUBUNIT: Homotetramer. Interacts with SIR4 N-terminal domain. Interacts
CC with a complex composed of SIN3 and RPD3. Identified in the Set3C
CC complex with HOS2, HST1, SNT1, CPR1, HOS4/YIL112W and SET3.
CC {ECO:0000269|PubMed:11711434, ECO:0000269|PubMed:16051270}.
CC -!- INTERACTION:
CC P38262; P40480: HOS4; NbExp=5; IntAct=EBI-17136, EBI-8492;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- DOMAIN: The LisH domain mediates tetramerization and interaction with
CC SNT1. {ECO:0000269|PubMed:16051270}.
CC -!- MISCELLANEOUS: Present with 1620 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; X78993; CAA55606.1; -; Genomic_DNA.
DR EMBL; Z35972; CAA85058.1; -; Genomic_DNA.
DR EMBL; AY693053; AAT93072.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07222.1; -; Genomic_DNA.
DR PIR; S48268; S48268.
DR RefSeq; NP_009661.1; NM_001178451.1.
DR PDB; 1R5M; X-ray; 1.55 A; A=113-535.
DR PDBsum; 1R5M; -.
DR AlphaFoldDB; P38262; -.
DR SMR; P38262; -.
DR BioGRID; 32807; 495.
DR ComplexPortal; CPX-1342; SET3C histone deacetylase complex.
DR DIP; DIP-1377N; -.
DR IntAct; P38262; 35.
DR MINT; P38262; -.
DR STRING; 4932.YBR103W; -.
DR iPTMnet; P38262; -.
DR MaxQB; P38262; -.
DR PaxDb; P38262; -.
DR PRIDE; P38262; -.
DR EnsemblFungi; YBR103W_mRNA; YBR103W; YBR103W.
DR GeneID; 852399; -.
DR KEGG; sce:YBR103W; -.
DR SGD; S000000307; SIF2.
DR VEuPathDB; FungiDB:YBR103W; -.
DR eggNOG; KOG0273; Eukaryota.
DR GeneTree; ENSGT00940000153421; -.
DR HOGENOM; CLU_007609_1_1_1; -.
DR InParanoid; P38262; -.
DR OMA; KWNKCGN; -.
DR BioCyc; YEAST:G3O-29065-MON; -.
DR Reactome; R-SCE-3214815; HDACs deacetylate histones.
DR EvolutionaryTrace; P38262; -.
DR PRO; PR:P38262; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P38262; protein.
DR GO; GO:0000118; C:histone deacetylase complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0070210; C:Rpd3L-Expanded complex; HDA:SGD.
DR GO; GO:0034967; C:Set3 complex; IDA:SGD.
DR GO; GO:0003714; F:transcription corepressor activity; IBA:GO_Central.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IC:ComplexPortal.
DR GO; GO:0009267; P:cellular response to starvation; IC:ComplexPortal.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0016575; P:histone deacetylation; IDA:ComplexPortal.
DR GO; GO:0045835; P:negative regulation of meiotic nuclear division; IDA:ComplexPortal.
DR GO; GO:0032874; P:positive regulation of stress-activated MAPK cascade; IMP:SGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:SGD.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR024977; Apc4_WD40_dom.
DR InterPro; IPR045183; Ebi-like.
DR InterPro; IPR006594; LisH.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR22846; PTHR22846; 1.
DR Pfam; PF12894; ANAPC4_WD40; 1.
DR Pfam; PF08513; LisH; 1.
DR Pfam; PF00400; WD40; 2.
DR SMART; SM00667; LisH; 1.
DR SMART; SM00320; WD40; 5.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS50896; LISH; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 4.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chromatin regulator; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; WD repeat.
FT CHAIN 1..535
FT /note="SIR4-interacting protein SIF2"
FT /id="PRO_0000051216"
FT DOMAIN 4..36
FT /note="LisH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00126"
FT REPEAT 155..186
FT /note="WD 1"
FT REPEAT 218..248
FT /note="WD 2"
FT REPEAT 259..289
FT /note="WD 3"
FT REPEAT 316..345
FT /note="WD 4"
FT REPEAT 357..387
FT /note="WD 5"
FT REPEAT 399..428
FT /note="WD 6"
FT REPEAT 440..470
FT /note="WD 7"
FT REPEAT 503..534
FT /note="WD 8"
FT REGION 104..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 105..120
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..135
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 137
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT CONFLICT 396
FT /note="C -> S (in Ref. 1; CAA55606)"
FT /evidence="ECO:0000305"
FT STRAND 152..156
FT /evidence="ECO:0007829|PDB:1R5M"
FT STRAND 161..165
FT /evidence="ECO:0007829|PDB:1R5M"
FT STRAND 172..177
FT /evidence="ECO:0007829|PDB:1R5M"
FT STRAND 181..189
FT /evidence="ECO:0007829|PDB:1R5M"
FT STRAND 198..207
FT /evidence="ECO:0007829|PDB:1R5M"
FT STRAND 223..228
FT /evidence="ECO:0007829|PDB:1R5M"
FT STRAND 232..239
FT /evidence="ECO:0007829|PDB:1R5M"
FT STRAND 244..248
FT /evidence="ECO:0007829|PDB:1R5M"
FT STRAND 253..257
FT /evidence="ECO:0007829|PDB:1R5M"
FT STRAND 264..269
FT /evidence="ECO:0007829|PDB:1R5M"
FT STRAND 273..280
FT /evidence="ECO:0007829|PDB:1R5M"
FT STRAND 285..289
FT /evidence="ECO:0007829|PDB:1R5M"
FT TURN 290..293
FT /evidence="ECO:0007829|PDB:1R5M"
FT STRAND 294..299
FT /evidence="ECO:0007829|PDB:1R5M"
FT STRAND 325..328
FT /evidence="ECO:0007829|PDB:1R5M"
FT STRAND 331..335
FT /evidence="ECO:0007829|PDB:1R5M"
FT HELIX 337..339
FT /evidence="ECO:0007829|PDB:1R5M"
FT STRAND 341..345
FT /evidence="ECO:0007829|PDB:1R5M"
FT STRAND 352..355
FT /evidence="ECO:0007829|PDB:1R5M"
FT STRAND 362..368
FT /evidence="ECO:0007829|PDB:1R5M"
FT TURN 369..372
FT /evidence="ECO:0007829|PDB:1R5M"
FT STRAND 373..378
FT /evidence="ECO:0007829|PDB:1R5M"
FT STRAND 383..386
FT /evidence="ECO:0007829|PDB:1R5M"
FT STRAND 388..392
FT /evidence="ECO:0007829|PDB:1R5M"
FT STRAND 394..397
FT /evidence="ECO:0007829|PDB:1R5M"
FT STRAND 404..410
FT /evidence="ECO:0007829|PDB:1R5M"
FT TURN 411..413
FT /evidence="ECO:0007829|PDB:1R5M"
FT STRAND 414..419
FT /evidence="ECO:0007829|PDB:1R5M"
FT STRAND 422..428
FT /evidence="ECO:0007829|PDB:1R5M"
FT TURN 429..432
FT /evidence="ECO:0007829|PDB:1R5M"
FT STRAND 433..439
FT /evidence="ECO:0007829|PDB:1R5M"
FT STRAND 445..450
FT /evidence="ECO:0007829|PDB:1R5M"
FT STRAND 454..461
FT /evidence="ECO:0007829|PDB:1R5M"
FT STRAND 466..470
FT /evidence="ECO:0007829|PDB:1R5M"
FT HELIX 472..475
FT /evidence="ECO:0007829|PDB:1R5M"
FT STRAND 496..500
FT /evidence="ECO:0007829|PDB:1R5M"
FT STRAND 509..514
FT /evidence="ECO:0007829|PDB:1R5M"
FT STRAND 518..528
FT /evidence="ECO:0007829|PDB:1R5M"
FT STRAND 531..534
FT /evidence="ECO:0007829|PDB:1R5M"
SQ SEQUENCE 535 AA; 59161 MW; 25C0AEA2CCEF1B07 CRC64;
MSITSEELNY LIWRYCQEMG HEVSALALQD ETRVLEFDEK YKEHIPLGTL VNLVQRGILY
TESELMVDSK GDISALNEHH LSEDFNLVQA LQIDKEKFPE ISSEGRFTLE TNSESNKAGE
DGASTVERET QEDDTNSIDS SDDLDGFVKI LKEIVKLDNI VSSTWNPLDE SILAYGEKNS
VARLARIVET DQEGKKYWKL TIIAELRHPF ALSASSGKTT NQVTCLAWSH DGNSIVTGVE
NGELRLWNKT GALLNVLNFH RAPIVSVKWN KDGTHIISMD VENVTILWNV ISGTVMQHFE
LKETGGSSIN AENHSGDGSL GVDVEWVDDD KFVIPGPKGA IFVYQITEKT PTGKLIGHHG
PISVLEFNDT NKLLLSASDD GTLRIWHGGN GNSQNCFYGH SQSIVSASWV GDDKVISCSM
DGSVRLWSLK QNTLLALSIV DGVPIFAGRI SQDGQKYAVA FMDGQVNVYD LKKLNSKSRS
LYGNRDGILN PLPIPLYASY QSSQDNDYIF DLSWNCAGNK ISVAYSLQEG SVVAI
