ID   NGG1_YEAST              Reviewed;         702 AA.
AC   P32494; D6VSF8;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   27-MAR-2024, entry version 191.
DE   RecName: Full=Chromatin-remodeling complexes subunit NGG1;
DE   AltName: Full=Transcriptional adapter 3;
GN   Name=NGG1; Synonyms=ADA3, SWI7; OrderedLocusNames=YDR176W;
GN   ORFNames=YD9395.09;
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].
RX   PubMed=8262068; DOI=10.1002/j.1460-2075.1993.tb06221.x;
RA   Brandl C.J., Furlanetto A.M., Martens J.A., Hamilton K.S.;
RT   "Characterization of NGG1, a novel yeast gene required for glucose
RT   repression of GAL4p-regulated transcription.";
RL   EMBO J. 12:5255-5265(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=8413201; DOI=10.1128/mcb.13.10.5981-5989.1993;
RA   Pina B., Berger S.L., Marcus G.A., Silverman N., Agapite J., Guarente L.;
RT   "ADA3: a gene, identified by resistance to GAL4-VP16, with properties
RT   similar to and different from those of ADA2.";
RL   Mol. Cell. Biol. 13:5981-5989(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169867;
RA   Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA   Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA   Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA   Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA   Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA   Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA   Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA   Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA   Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA   Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA   Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA   Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA   Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA   Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA   Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA   Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA   Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA   Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA   Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA   Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA   Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA   Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA   Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA   Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA   Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA   Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA   Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA   Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA   Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA   Mewes H.-W., Zollner A., Zaccaria P.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL   Nature 387:75-78(1997).
RN   [4]
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   [5]
RP   IDENTIFICATION IN THE ADA/GCN5 COMPLEX.
RC   STRAIN=ATCC MYA-3516 / BWG1-7A;
RX   PubMed=9154821; DOI=10.1128/mcb.17.6.3220;
RA   Horiuchi J., Silverman N., Pina B., Marcus G.A., Guarente L.;
RT   "ADA1, a novel component of the ADA/GCN5 complex, has broader effects than
RT   GCN5, ADA2, or ADA3.";
RL   Mol. Cell. Biol. 17:3220-3228(1997).
RN   [6]
RP   IDENTIFICATION IN THE SAGA COMPLEX, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RX   PubMed=9674426; DOI=10.1016/s0092-8674(00)81220-9;
RA   Grant P.A., Schieltz D., Pray-Grant M.G., Steger D.J., Reese J.C.,
RA   Yates J.R. III, Workman J.L.;
RT   "A subset of TAF(II)s are integral components of the SAGA complex required
RT   for nucleosome acetylation and transcriptional stimulation.";
RL   Cell 94:45-53(1998).
RN   [7]
RP   IDENTIFICATION IN A SAGA COMPLEX WITH SPT7; HFI1; SPT8; GCN5; SPT20; SPT2;
RP   ADA2 AND TRA1.
RX   PubMed=9885573; DOI=10.1016/s1097-2765(00)80300-7;
RA   Grant P.A., Schieltz D., Pray-Grant M.G., Yates J.R. III, Workman J.L.;
RT   "The ATM-related cofactor Tra1 is a component of the purified SAGA
RT   complex.";
RL   Mol. Cell 2:863-867(1998).
RN   [8]
RP   FUNCTION IN HISTONE ACETYLATION AT THE SAGA COMPLEX, AND FUNCTION IN
RP   HISTONE ACETYLATION AT THE ADA COMPLEX.
RX   PubMed=10026213; DOI=10.1074/jbc.274.9.5895;
RA   Grant P.A., Eberharter A., John S., Cook R.G., Turner B.M., Workman J.L.;
RT   "Expanded lysine acetylation specificity of Gcn5 in native complexes.";
RL   J. Biol. Chem. 274:5895-5900(1999).
RN   [9]
RP   IDENTIFICATION IN THE ADA COMPLEX, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=10490601; DOI=10.1128/mcb.19.10.6621;
RA   Eberharter A., Sterner D.E., Schieltz D., Hassan A., Yates J.R. III,
RA   Berger S.L., Workman J.L.;
RT   "The ADA complex is a distinct histone acetyltransferase complex in
RT   Saccharomyces cerevisiae.";
RL   Mol. Cell. Biol. 19:6621-6631(1999).
RN   [10]
RP   IDENTIFICATION IN THE SLIK COMPLEX.
RX   PubMed=12446794; DOI=10.1128/mcb.22.24.8774-8786.2002;
RA   Pray-Grant M.G., Schieltz D., McMahon S.J., Wood J.M., Kennedy E.L.,
RA   Cook R.G., Workman J.L., Yates J.R. III, Grant P.A.;
RT   "The novel SLIK histone acetyltransferase complex functions in the yeast
RT   retrograde response pathway.";
RL   Mol. Cell. Biol. 22:8774-8786(2002).
RN   [11]
RP   IDENTIFICATION IN THE SALSA COMPLEX.
RX   PubMed=12186975; DOI=10.1073/pnas.182021199;
RA   Sterner D.E., Belotserkovskaya R., Berger S.L.;
RT   "SALSA, a variant of yeast SAGA, contains truncated Spt7, which correlates
RT   with activated transcription.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:11622-11627(2002).
RN   [12]
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   [13]
RP   IDENTIFICATION IN THE SLIK COMPLEX.
RX   PubMed=15647753; DOI=10.1038/nature03242;
RA   Pray-Grant M.G., Daniel J.A., Schieltz D., Yates J.R. III, Grant P.A.;
RT   "Chd1 chromodomain links histone H3 methylation with SAGA- and SLIK-
RT   dependent acetylation.";
RL   Nature 433:434-438(2005).
RN   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-134, 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   [15]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-134 AND SER-407, AND
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   [16]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-134 AND THR-464, AND
RP   IDENTIFICATION BY 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   [17]
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).
CC   -!- FUNCTION: Transcription regulator. Could inhibit GAL4 DNA-binding or
CC       its ability to activate transcription. Functions as a component of the
CC       transcription regulatory histone acetylation (HAT) complexes SAGA,
CC       SALSA, SLIK and ADA. 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). SALSA, an altered form of SAGA, may be
CC       involved in positive transcriptional regulation. SLIK is proposed to
CC       have partly overlapping functions with SAGA. It preferentially
CC       acetylates methylated histone H3, at least after activation at the
CC       GAL1-10 locus. ADA preferentially acetylates nucleosomal histones H3
CC       (at 'Lys-14' and 'Lys-18') and H2B. {ECO:0000269|PubMed:10026213}.
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       Component of the SALSA complex, which consists of at least TRA1, SPT7
CC       (C-terminal truncated form), TAF5, ADA3, SPT20, TAF12, TAF6, HFI1,
CC       GCN5, ADA2 and SPT3. Component of the SLIK complex, which consists of
CC       at least TRA1, CHD1, SPT7, TAF5, ADA3, SPT20, RTG2, TAF12, TAF6, HFI1,
CC       UBP8, GCN5, ADA2, SPT3, SGF29, TAF10 and TAF9. Component of the
CC       ADA/GCN5 complex that consists of HFI1/ADA1, ADA2, ADA3, SPT20/ADA5 and
CC       GCN5 and is probably a subcomplex of SAGA. Component of the 0.8 MDa ADA
CC       complex, which at least consists of ADA2, ADA3, AHC1 and GCN5.
CC       {ECO:0000269|PubMed:10490601, ECO:0000269|PubMed:12186975,
CC       ECO:0000269|PubMed:12446794, ECO:0000269|PubMed:15647753,
CC       ECO:0000269|PubMed:9154821, ECO:0000269|PubMed:9674426,
CC       ECO:0000269|PubMed:9885573}.
CC   -!- INTERACTION:
CC       P32494; Q02336: ADA2; NbExp=28; IntAct=EBI-2192, EBI-2186;
CC       P32494; Q12060: HFI1; NbExp=5; IntAct=EBI-2192, EBI-8287;
CC       P32494; P25554: SGF29; NbExp=5; IntAct=EBI-2192, EBI-21678;
CC       P32494; P38915: SPT8; NbExp=7; IntAct=EBI-2192, EBI-17964;
CC       P32494; P38811: TRA1; NbExp=3; IntAct=EBI-2192, EBI-24638;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- MISCELLANEOUS: Present with 2470 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the NGG1 family. {ECO:0000305}.
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DR   EMBL; L12137; AAA21684.1; -; Genomic_DNA.
DR   EMBL; L21189; AAA03542.1; ALT_SEQ; Unassigned_DNA.
DR   EMBL; Z46727; CAA86681.1; -; Genomic_DNA.
DR   EMBL; BK006938; DAA12018.1; -; Genomic_DNA.
DR   PIR; S41685; S41685.
DR   RefSeq; NP_010461.3; NM_001180483.3.
DR   AlphaFoldDB; P32494; -.
DR   BioGRID; 32229; 180.
DR   ComplexPortal; CPX-608; ADA complex.
DR   ComplexPortal; CPX-656; SAGA complex.
DR   ComplexPortal; CPX-675; SLIK (SAGA-like) complex.
DR   DIP; DIP-774N; -.
DR   IntAct; P32494; 37.
DR   MINT; P32494; -.
DR   STRING; 4932.YDR176W; -.
DR   iPTMnet; P32494; -.
DR   MaxQB; P32494; -.
DR   PaxDb; 4932-YDR176W; -.
DR   PeptideAtlas; P32494; -.
DR   DNASU; 851756; -.
DR   EnsemblFungi; YDR176W_mRNA; YDR176W; YDR176W.
DR   GeneID; 851756; -.
DR   KEGG; sce:YDR176W; -.
DR   AGR; SGD:S000002583; -.
DR   SGD; S000002583; NGG1.
DR   VEuPathDB; FungiDB:YDR176W; -.
DR   eggNOG; KOG4191; Eukaryota.
DR   GeneTree; ENSGT00390000008947; -.
DR   HOGENOM; CLU_016102_1_0_1; -.
DR   InParanoid; P32494; -.
DR   OMA; WQEYSSI; -.
DR   OrthoDB; 1331541at2759; -.
DR   BioCyc; YEAST:G3O-29765-MONOMER; -.
DR   BioGRID-ORCS; 851756; 0 hits in 10 CRISPR screens.
DR   PRO; PR:P32494; -.
DR   Proteomes; UP000002311; Chromosome IV.
DR   RNAct; P32494; Protein.
DR   GO; GO:0140671; C:ADA complex; IDA:SGD.
DR   GO; GO:0005634; C:nucleus; NAS:ComplexPortal.
DR   GO; GO:0000124; C:SAGA complex; IDA:SGD.
DR   GO; GO:0046695; C:SLIK (SAGA-like) complex; IDA:SGD.
DR   GO; GO:0003713; F:transcription coactivator activity; IBA:GO_Central.
DR   GO; GO:0006325; P:chromatin organization; IDA:SGD.
DR   GO; GO:0006338; P:chromatin remodeling; IEA:GOC.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:ComplexPortal.
DR   InterPro; IPR019340; Histone_AcTrfase_su3.
DR   PANTHER; PTHR13556:SF2; TRANSCRIPTIONAL ADAPTER 3; 1.
DR   PANTHER; PTHR13556; TRANSCRIPTIONAL ADAPTER 3-RELATED; 1.
DR   Pfam; PF10198; Ada3; 1.
PE   1: Evidence at protein level;
KW   Chromatin regulator; Nucleus; Phosphoprotein; Reference proteome;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..702
FT                   /note="Chromatin-remodeling complexes subunit NGG1"
FT                   /id="PRO_0000064448"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          90..224
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          611..636
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          672..702
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           606..618
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        90..112
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        113..129
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        158..221
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        621..636
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         134
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT   MOD_RES         407
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MOD_RES         464
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   CONFLICT        520
FT                   /note="K -> M (in Ref. 2; AAA03542)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   702 AA;  79282 MW;  489016BFD1C095D4 CRC64;
     MPRHGRRGKL PKGEKLPKKE GGDNTPSKLL SSMLKTLDLT FERDIGMLNG KSVRSIPNKK
     TLLELQSQLD SLNEILGTIA RGDQETIEAL RKIRDSKNEK QANDEKQETS NADGQHESST
     ATEETNIIDK GVQSPPKPPP SNEISGTIEN DVESIKQAAD NMAKEEINED KDLQVHRDQP
     REKRPFDSET ENRATENENT QRPDNKKQKI DVDKMENDPT VKNPKSEFVV SQTLPRAAAA
     LGLFNEEGLE STGEDFLKKK YNVASYPTND LKDLLPGELP DMDFSHPKPT NQIQFNTFLA
     FVENFFKDLS DDNLKFLKMK YIIPDSLQFD KTYDPEVNPF IIPKLGPLYT DVWFKDENDK
     NSAYKKPSPY SNDASTILPK KSANELDDNA LESGSISCGP LLSRLLSAVL KDDNDKSELQ
     SSKIIRDGGL PRTGGEDDIQ SFRNNNNDTV DMTLSQENGP SVQTPDNDID EEASFQAKLA
     ENKGSNGGTT STLPQQIGWI TNGINLDYPT FEERLKRELK YVGIYMNLPK DENNPNSDDP
     DWVTGREDDE ISAELRELQG TLKQVTKKNQ KRKAQLIPLV ERQLAWQEYS SILEDLDKQI
     DQAYVKRIRV PKKRKKHHTA ASNNVNTGTT SQIAQQKAAN SSLKSLLDKR QRWINKIGPL
     FDKPEIMKRI PNESVFKDMD QEEDEDEADV FAQNTNKDVE LN
//