SGF11_YEAST
ID SGF11_YEAST Reviewed; 99 AA.
AC Q03067; D6W3W7;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=SAGA-associated factor 11 {ECO:0000255|HAMAP-Rule:MF_03047};
DE AltName: Full=11 kDa SAGA-associated factor;
GN Name=SGF11 {ECO:0000255|HAMAP-Rule:MF_03047}; OrderedLocusNames=YPL047W;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [2]
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 [3]
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 [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [5]
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 [6]
RP IDENTIFICATION IN THE SAGA COMPLEX.
RX PubMed=15506919; DOI=10.1042/bst0320899;
RA Lee K.K., Prochasson P., Florens L., Swanson S.K., Washburn M.P.,
RA Workman J.L.;
RT "Proteomic analysis of chromatin-modifying complexes in Saccharomyces
RT cerevisiae identifies novel subunits.";
RL Biochem. Soc. Trans. 32:899-903(2004).
RN [7]
RP IDENTIFICATION IN THE SAGA COMPLEX.
RX PubMed=15282323; DOI=10.1128/mcb.24.16.7249-7259.2004;
RA Powell D.W., Weaver C.M., Jennings J.L., McAfee K.J., He Y., Weil P.A.,
RA Link A.J.;
RT "Cluster analysis of mass spectrometry data reveals a novel component of
RT SAGA.";
RL Mol. Cell. Biol. 24:7249-7259(2004).
RN [8]
RP FUNCTION IN HISTONE DEUBIQUITYLATION ACTIVITY OF THE SAGA COMPLEX,
RP IDENTIFICATION IN THE SAGA COMPLEX, AND INTERACTION WITH UBP8.
RX PubMed=15657441; DOI=10.1128/mcb.25.3.1162-1172.2005;
RA Ingvarsdottir K., Krogan N.J., Emre N.C.T., Wyce A., Thompson N.J.,
RA Emili A., Hughes T.R., Greenblatt J.F., Berger S.L.;
RT "H2B ubiquitin protease Ubp8 and Sgf11 constitute a discrete functional
RT module within the Saccharomyces cerevisiae SAGA complex.";
RL Mol. Cell. Biol. 25:1162-1172(2005).
RN [9]
RP FUNCTION IN HISTONE DEUBIQUITINATION ACTIVITY OF THE SAGA COMPLEX,
RP IDENTIFICATION IN THE SAGA COMPLEX, AND INTERACTION WITH UBP8.
RX PubMed=15657442; DOI=10.1128/mcb.25.3.1173-1182.2005;
RA Lee K.K., Florens L., Swanson S.K., Washburn M.P., Workman J.L.;
RT "The deubiquitylation activity of Ubp8 is dependent upon Sgf11 and its
RT association with the SAGA complex.";
RL Mol. Cell. Biol. 25:1173-1182(2005).
RN [10]
RP INTERACTION WITH UBP8.
RX PubMed=16611979; DOI=10.1128/mcb.26.9.3339-3352.2006;
RA Shukla A., Stanojevic N., Duan Z., Sen P., Bhaumik S.R.;
RT "Ubp8p, a histone deubiquitinase whose association with SAGA is mediated by
RT Sgf11p, differentially regulates lysine 4 methylation of histone H3 in
RT vivo.";
RL Mol. Cell. Biol. 26:3339-3352(2006).
RN [11]
RP INTERACTION WITH SUS1 AND UBP8.
RX PubMed=16855026; DOI=10.1091/mbc.e06-02-0098;
RA Koehler A., Pascual-Garcia P., Llopis A., Zapater M., Posas F., Hurt E.C.,
RA Rodriguez-Navarro S.;
RT "The mRNA export factor Sus1 is involved in Spt/Ada/Gcn5 acetyltransferase-
RT mediated H2B deubiquitinylation through its interaction with Ubp8 and
RT Sgf11.";
RL Mol. Biol. Cell 17:4228-4236(2006).
RN [12]
RP INTERACTION WITH SUS1; UBP8 AND SGF73.
RX PubMed=18488019; DOI=10.1038/ncb1733;
RA Koehler A., Schneider M., Cabal G.G., Nehrbass U., Hurt E.;
RT "Yeast Ataxin-7 links histone deubiquitination with gene gating and mRNA
RT export.";
RL Nat. Cell Biol. 10:707-715(2008).
RN [13]
RP 3D-STRUCTURE MODELING OF THE SAGA COMPLEX.
RX PubMed=15260971; DOI=10.1016/j.molcel.2004.06.005;
RA Wu P.Y., Ruhlmann C., Winston F., Schultz P.;
RT "Molecular architecture of the S. cerevisiae SAGA complex.";
RL Mol. Cell 15:199-208(2004).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) IN COMPLEX WITH SUS1; SGF73; UBP8
RP AND ZINC, AND MUTAGENESIS OF ASP-57; GLY-60; ARG-84; LEU-85; ALA-86; LEU-89
RP AND ARG-91.
RX PubMed=20434206; DOI=10.1016/j.cell.2010.04.026;
RA Kohler A., Zimmerman E., Schneider M., Hurt E., Zheng N.;
RT "Structural basis for assembly and activation of the heterotetrameric SAGA
RT histone H2B deubiquitinase module.";
RL Cell 141:606-617(2010).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 7-33 IN COMPLEX WITH SUS1, AND
RP MUTAGENESIS OF ASN-18 AND LEU-19.
RX PubMed=20007317; DOI=10.1074/jbc.m109.070839;
RA Ellisdon A.M., Jani D., Kohler A., Hurt E., Stewart M.;
RT "Structural basis for the interaction between yeast Spt-Ada-Gcn5
RT acetyltransferase (SAGA) complex components Sgf11 and Sus1.";
RL J. Biol. Chem. 285:3850-3856(2010).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (1.89 ANGSTROMS) IN COMPLEX WITH SUS1; SGF73; UBP8
RP AND ZINC.
RX PubMed=20395473; DOI=10.1126/science.1190049;
RA Samara N.L., Datta A.B., Berndsen C.E., Zhang X., Yao T., Cohen R.E.,
RA Wolberger C.;
RT "Structural insights into the assembly and function of the SAGA
RT deubiquitinating module.";
RL Science 328:1025-1029(2010).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.03 ANGSTROMS) IN COMPLEX WITH SUS1; SGF73 AND
RP UBP8.
RX PubMed=22771212; DOI=10.1016/j.str.2012.05.015;
RA Samara N.L., Ringel A.E., Wolberger C.;
RT "A role for intersubunit interactions in maintaining SAGA deubiquitinating
RT module structure and activity.";
RL Structure 20:1414-1424(2012).
RN [18]
RP STRUCTURE BY NMR OF 63-99.
RA Koehler C., Gao X., Bonnet J., Devys D., Kieffer B.;
RT "Insights into the role of SGF11 and SGF73 for the interaction between SAGA
RT and nucleosomes.";
RL Submitted (JAN-2012) to the PDB data bank.
CC -!- FUNCTION: Component of the transcription regulatory histone acetylation
CC (HAT) complex SAGA. SAGA is involved in RNA polymerase II-dependent
CC transcriptional regulation of approximately 10% of yeast genes. At the
CC promoters, SAGA is required for recruitment of the basal transcription
CC machinery. It influences RNA polymerase II transcriptional activity
CC through different activities such as TBP interaction (SPT3, SPT8 and
CC SPT20) and promoter selectivity, interaction with transcription
CC activators (GCN5, ADA2, ADA3 and TRA1), and chromatin modification
CC through histone acetylation (GCN5) and deubiquitination (UBP8). SAGA
CC acetylates nucleosomal histone H3 to some extent (to form H3K9ac,
CC H3K14ac, H3K18ac and H3K23ac). SAGA interacts with DNA via upstream
CC activating sequences (UASs). SGF11 is involved in transcriptional
CC regulation of a subset of SAGA-regulated genes. Within the SAGA
CC complex, participates in a subcomplex with SUS1, SGF73 and UBP8
CC required for deubiquitination of H2B and for the maintenance of steady-
CC state H3 methylation levels. It is required to recruit UBP8 and SUS1
CC into the SAGA complex. {ECO:0000269|PubMed:15657441,
CC ECO:0000269|PubMed:15657442}.
CC -!- SUBUNIT: Component of the 1.8 MDa SAGA complex, which consists of at
CC least of TRA1, CHD1, SPT7, TAF5, ADA3, SGF73, SPT20/ADA5, SPT8, TAF12,
CC TAF6, HFI1/ADA1, UBP8, GCN5, ADA2, SPT3, SGF29, TAF10, TAF9, SGF11 and
CC SUS1. TAF5, TAF6, TAF9, TAF19, TAF12 and ADA1 seem to be present in 2
CC copies. SAGA is built of 5 distinct domains with specialized functions.
CC Domain I (containing TRA1) probably represents the activator
CC interaction surface. Domain II (containing TAF5 and TAF6, and probably
CC TAF9 and TAF10), domain III (containing GCN5, TAF10, SPT7, TAF5 and
CC ADA1, and probably ADA2, ADA3 and TAF12), and domain IV (containing
CC HFI1/ADA1 and TAF6, and probably TAF9) are believed to play primarily
CC an architectural role. Domain III also harbors the HAT activity. Domain
CC V (containing SPT3 and SPT20, and probably SPT8) represents the TBP-
CC interacting module, which may be associated transiently with SAGA.
CC Within the SAGA complex, SUS1, SGF11, SGF73 and UBP8 form an additional
CC subcomplex of SAGA called the DUB module (deubiquitination module).
CC Interacts directly with SGF73, SUS1 and UBP8.
CC {ECO:0000269|PubMed:15282323, ECO:0000269|PubMed:15506919,
CC ECO:0000269|PubMed:15657441, ECO:0000269|PubMed:15657442,
CC ECO:0000269|PubMed:16611979, ECO:0000269|PubMed:16855026,
CC ECO:0000269|PubMed:18488019, ECO:0000269|PubMed:20007317,
CC ECO:0000269|PubMed:20395473, ECO:0000269|PubMed:20434206,
CC ECO:0000269|PubMed:22771212}.
CC -!- INTERACTION:
CC Q03067; Q6WNK7: SUS1; NbExp=12; IntAct=EBI-34550, EBI-1251050;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03047,
CC ECO:0000269|PubMed:14562095}.
CC -!- DOMAIN: The long N-terminal helix forms part of the 'assembly lobe' of
CC the SAGA deubiquitination module.
CC -!- DOMAIN: The C-terminal SGF11-type zinc-finger domain together with the
CC C-terminal catalytic domain of UBP8 forms the 'catalytic lobe' of the
CC SAGA deubiquitination module.
CC -!- MISCELLANEOUS: Present with 672 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the SGF11 family. {ECO:0000255|HAMAP-
CC Rule:MF_03047}.
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DR EMBL; U44030; AAB68174.1; -; Genomic_DNA.
DR EMBL; AY558330; AAS56656.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11383.1; -; Genomic_DNA.
DR PIR; S62029; S62029.
DR RefSeq; NP_015278.1; NM_001183861.1.
DR PDB; 2LO2; NMR; -; A=63-99.
DR PDB; 3KIK; X-ray; 2.10 A; E/F/G/H=7-33.
DR PDB; 3KJL; X-ray; 2.70 A; E/F/G/H=2-33.
DR PDB; 3M99; X-ray; 2.70 A; B=1-99.
DR PDB; 3MHH; X-ray; 2.45 A; C=1-99.
DR PDB; 3MHS; X-ray; 1.89 A; C=1-99.
DR PDB; 4FIP; X-ray; 2.69 A; C/G=1-72.
DR PDB; 4FJC; X-ray; 2.83 A; C/G=1-99.
DR PDB; 4FK5; X-ray; 2.03 A; C=1-99.
DR PDB; 4WA6; X-ray; 2.36 A; C/G=1-99.
DR PDB; 4ZUX; X-ray; 3.82 A; W/b/g/l=1-99.
DR PDB; 6AQR; X-ray; 2.10 A; C=1-99.
DR PDB; 6T9L; EM; 3.60 A; M=1-99.
DR PDBsum; 2LO2; -.
DR PDBsum; 3KIK; -.
DR PDBsum; 3KJL; -.
DR PDBsum; 3M99; -.
DR PDBsum; 3MHH; -.
DR PDBsum; 3MHS; -.
DR PDBsum; 4FIP; -.
DR PDBsum; 4FJC; -.
DR PDBsum; 4FK5; -.
DR PDBsum; 4WA6; -.
DR PDBsum; 4ZUX; -.
DR PDBsum; 6AQR; -.
DR PDBsum; 6T9L; -.
DR AlphaFoldDB; Q03067; -.
DR BMRB; Q03067; -.
DR SMR; Q03067; -.
DR BioGRID; 36133; 391.
DR ComplexPortal; CPX-656; SAGA complex.
DR ComplexPortal; CPX-675; SLIK (SAGA-like) complex.
DR DIP; DIP-39582N; -.
DR IntAct; Q03067; 25.
DR MINT; Q03067; -.
DR STRING; 4932.YPL047W; -.
DR PaxDb; Q03067; -.
DR PRIDE; Q03067; -.
DR EnsemblFungi; YPL047W_mRNA; YPL047W; YPL047W.
DR GeneID; 856060; -.
DR KEGG; sce:YPL047W; -.
DR SGD; S000005968; SGF11.
DR VEuPathDB; FungiDB:YPL047W; -.
DR eggNOG; KOG2612; Eukaryota.
DR HOGENOM; CLU_2320099_0_0_1; -.
DR InParanoid; Q03067; -.
DR OMA; SSQYFHC; -.
DR BioCyc; YEAST:G3O-33960-MON; -.
DR ChiTaRS; SGF11; yeast.
DR EvolutionaryTrace; Q03067; -.
DR PRO; PR:Q03067; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q03067; protein.
DR GO; GO:0071819; C:DUBm complex; IDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0000124; C:SAGA complex; IDA:SGD.
DR GO; GO:0046695; C:SLIK (SAGA-like) complex; IPI:ComplexPortal.
DR GO; GO:0008047; F:enzyme activator activity; IDA:SGD.
DR GO; GO:0003713; F:transcription coactivator activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0016573; P:histone acetylation; IDA:ComplexPortal.
DR GO; GO:0016578; P:histone deubiquitination; IMP:SGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:ComplexPortal.
DR HAMAP; MF_03047; Sgf11; 1.
DR InterPro; IPR013246; SAGA_su_Sgf11.
DR InterPro; IPR041216; Sgf11_N.
DR Pfam; PF08209; Sgf11; 1.
DR Pfam; PF18519; Sgf11_N; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Chromatin regulator; Metal-binding; Nucleus;
KW Reference proteome; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..99
FT /note="SAGA-associated factor 11"
FT /id="PRO_0000227805"
FT ZN_FING 71..92
FT /note="SGF11-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03047"
FT MUTAGEN 15
FT /note="I->A: Moerately decreases the affinity of SGF11 for
FT SUS1."
FT MUTAGEN 18
FT /note="N->NA: Causes a dramatic decrease in the affinity of
FT SGF11 for SUS1."
FT /evidence="ECO:0000269|PubMed:20007317"
FT MUTAGEN 19
FT /note="L->LA: Causes a dramatic decrease in the affinity of
FT SGF11 for SUS1."
FT /evidence="ECO:0000269|PubMed:20007317"
FT MUTAGEN 57
FT /note="D->A: Reduces deubiquitination activity of the SAGA
FT DUB module; when associated with A-60."
FT /evidence="ECO:0000269|PubMed:20434206"
FT MUTAGEN 60
FT /note="G->A: Reduces deubiquitination activity of the SAGA
FT DUB module; when associated with A-57."
FT /evidence="ECO:0000269|PubMed:20434206"
FT MUTAGEN 84
FT /note="R->A: No effect."
FT /evidence="ECO:0000269|PubMed:20434206"
FT MUTAGEN 85
FT /note="L->D: Strongly reduces deubiquitination activity of
FT the SAGA DUB module."
FT /evidence="ECO:0000269|PubMed:20434206"
FT MUTAGEN 86
FT /note="A->D: Moderately impairs deubiquitination activity
FT of the SAGA DUB module."
FT /evidence="ECO:0000269|PubMed:20434206"
FT MUTAGEN 89
FT /note="L->D: Strongly reduces deubiquitination activity of
FT the SAGA DUB module."
FT /evidence="ECO:0000269|PubMed:20434206"
FT MUTAGEN 91
FT /note="R->A: No effect."
FT /evidence="ECO:0000269|PubMed:20434206"
FT HELIX 8..41
FT /evidence="ECO:0007829|PDB:3MHS"
FT HELIX 66..68
FT /evidence="ECO:0007829|PDB:4FK5"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:3MHS"
FT TURN 74..76
FT /evidence="ECO:0007829|PDB:3MHS"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:3MHS"
FT HELIX 82..84
FT /evidence="ECO:0007829|PDB:3MHS"
FT HELIX 85..92
FT /evidence="ECO:0007829|PDB:3MHS"
SQ SEQUENCE 99 AA; 11285 MW; 31CBBD4CAA18F3F9 CRC64;
MTEETITIDS ISNGILNNLL TTLIQDIVAR ETTQQQLLKT RYPDLRSYYF DPNGSLDING
LQKQQESSQY IHCENCGRDV SANRLAAHLQ RCLSRGARR
