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P32494

- NGG1_YEAST

UniProt

P32494 - NGG1_YEAST

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Protein

Chromatin-remodeling complexes subunit NGG1

Gene

NGG1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Transcription regulator. Could inhibit GAL4 DNA-binding or its ability to activate transcription. Functions as component of the transcription regulatory histone acetylation (HAT) complexes SAGA, SALSA, SLIK and ADA. SAGA is involved in RNA polymerase II-dependent transcriptional regulation of approximately 10% of yeast genes. At the promoters, SAGA is required for recruitment of the basal transcription machinery. It influences RNA polymerase II transcriptional activity through different activities such as TBP interaction (SPT3, SPT8 and SPT20) and promoter selectivity, interaction with transcription activators (GCN5, ADA2, ADA3 and TRA1), and chromatin modification through histone acetylation (GCN5) and deubiquitination (UBP8). SAGA acetylates nucleosomal histone H3 to some extent (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac). SAGA interacts with DNA via upstream activating sequences (UASs). SALSA, an altered form of SAGA, may be involved in positive transcriptional regulation. SLIK is proposed to have partly overlapping functions with SAGA. It preferentially acetylates methylated histone H3, at least after activation at the GAL1-10 locus. ADA preferentially acetylates nucleosomal histones H3 (at 'Lys-14' and 'Lys-18') and H2B.1 Publication

GO - Biological processi

  1. chromatin modification Source: SGD
  2. histone acetylation Source: SGD
  3. regulation of transcription, DNA-templated Source: UniProtKB-KW
  4. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator

Keywords - Biological processi

Transcription, Transcription regulation

Enzyme and pathway databases

BioCyciYEAST:G3O-29765-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Chromatin-remodeling complexes subunit NGG1
Alternative name(s):
Transcriptional adapter 3
Gene namesi
Name:NGG1
Synonyms:ADA3, SWI7
Ordered Locus Names:YDR176W
ORF Names:YD9395.09
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome IV

Organism-specific databases

CYGDiYDR176w.
SGDiS000002583. NGG1.

Subcellular locationi

Nucleus Curated

GO - Cellular componenti

  1. Ada2/Gcn5/Ada3 transcription activator complex Source: SGD
  2. SAGA complex Source: SGD
  3. SLIK (SAGA-like) complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 702702Chromatin-remodeling complexes subunit NGG1PRO_0000064448Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei134 – 1341Phosphoserine3 Publications
Modified residuei407 – 4071Phosphoserine1 Publication
Modified residuei464 – 4641Phosphothreonine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP32494.
PaxDbiP32494.
PeptideAtlasiP32494.

Expressioni

Gene expression databases

GenevestigatoriP32494.

Interactioni

Subunit structurei

Component of the 1.8 MDa SAGA complex, which consists of at least of TRA1, CHD1, SPT7, TAF5, ADA3, SGF73, SPT20/ADA5, SPT8, TAF12, TAF6, HFI1/ADA1, UBP8, GCN5, ADA2, SPT3, SGF29, TAF10, TAF9, SGF11 and SUS1. TAF5, TAF6, TAF9, TAF19, TAF12 and ADA1 seem to be present in 2 copies. SAGA is built of 5 distinct domains with specialized functions. Domain I (containing TRA1) probably represents the activator interaction surface. Domain II (containing TAF5 and TAF6, and probably TAF9 and TAF10), domain III (containing GCN5, TAF10, SPT7, TAF5 and ADA1, and probably ADA2, ADA3 and TAF12), and domain IV (containing HFI1/ADA1 and TAF6, and probably TAF9) are believed to play primarily an architectural role. Domain III also harbors the HAT activity. Domain V (containing SPT3 and SPT20, and probably SPT8) represents the TBP-interacting module, which may be associated transiently with SAGA. Component of the SALSA complex, which consists of at least TRA1, SPT7 (C-terminal truncated form), TAF5, ADA3, SPT20, TAF12, TAF6, HFI1, GCN5, ADA2 and SPT3. Component of the SLIK complex, which consists of at least TRA1, CHD1, SPT7, TAF5, ADA3, SPT20, RTG2, TAF12, TAF6, HFI1, UBP8, GCN5, ADA2, SPT3, SGF29, TAF10 and TAF9. Component of the ADA/GCN5 complex that consists of HFI1/ADA1, ADA2, ADA3, SPT20/ADA5 and GCN5 and is probably a subcomplex of SAGA. Component of the 0.8 MDa ADA complex, which at least consists of ADA2, ADA3, AHC1 and GCN5.7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ADA2Q0233625EBI-2192,EBI-2186
HFI1Q120605EBI-2192,EBI-8287
SGF29P255545EBI-2192,EBI-21678
SPT8P389157EBI-2192,EBI-17964
TRA1P388113EBI-2192,EBI-24638

Protein-protein interaction databases

BioGridi32229. 125 interactions.
DIPiDIP-774N.
IntActiP32494. 33 interactions.
MINTiMINT-490762.
STRINGi4932.YDR176W.

Structurei

3D structure databases

ProteinModelPortaliP32494.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi606 – 61813Nuclear localization signalSequence AnalysisAdd
BLAST

Sequence similaritiesi

Belongs to the NGG1 family.Curated

Phylogenomic databases

eggNOGiNOG304305.
HOGENOMiHOG000248582.
InParanoidiP32494.
KOiK11315.
OMAiKRELKYI.
OrthoDBiEOG7N63WV.

Family and domain databases

InterProiIPR019340. Histone_AcTrfase_su3.
[Graphical view]
PfamiPF10198. Ada3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P32494-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPRHGRRGKL PKGEKLPKKE GGDNTPSKLL SSMLKTLDLT FERDIGMLNG
60 70 80 90 100
KSVRSIPNKK TLLELQSQLD SLNEILGTIA RGDQETIEAL RKIRDSKNEK
110 120 130 140 150
QANDEKQETS NADGQHESST ATEETNIIDK GVQSPPKPPP SNEISGTIEN
160 170 180 190 200
DVESIKQAAD NMAKEEINED KDLQVHRDQP REKRPFDSET ENRATENENT
210 220 230 240 250
QRPDNKKQKI DVDKMENDPT VKNPKSEFVV SQTLPRAAAA LGLFNEEGLE
260 270 280 290 300
STGEDFLKKK YNVASYPTND LKDLLPGELP DMDFSHPKPT NQIQFNTFLA
310 320 330 340 350
FVENFFKDLS DDNLKFLKMK YIIPDSLQFD KTYDPEVNPF IIPKLGPLYT
360 370 380 390 400
DVWFKDENDK NSAYKKPSPY SNDASTILPK KSANELDDNA LESGSISCGP
410 420 430 440 450
LLSRLLSAVL KDDNDKSELQ SSKIIRDGGL PRTGGEDDIQ SFRNNNNDTV
460 470 480 490 500
DMTLSQENGP SVQTPDNDID EEASFQAKLA ENKGSNGGTT STLPQQIGWI
510 520 530 540 550
TNGINLDYPT FEERLKRELK YVGIYMNLPK DENNPNSDDP DWVTGREDDE
560 570 580 590 600
ISAELRELQG TLKQVTKKNQ KRKAQLIPLV ERQLAWQEYS SILEDLDKQI
610 620 630 640 650
DQAYVKRIRV PKKRKKHHTA ASNNVNTGTT SQIAQQKAAN SSLKSLLDKR
660 670 680 690 700
QRWINKIGPL FDKPEIMKRI PNESVFKDMD QEEDEDEADV FAQNTNKDVE

LN
Length:702
Mass (Da):79,282
Last modified:October 1, 1993 - v1
Checksum:i489016BFD1C095D4
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti520 – 5201K → M in AAA03542. (PubMed:8413201)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L12137 Genomic DNA. Translation: AAA21684.1.
L21189 Unassigned DNA. Translation: AAA03542.1. Sequence problems.
Z46727 Genomic DNA. Translation: CAA86681.1.
BK006938 Genomic DNA. Translation: DAA12018.1.
PIRiS41685.
RefSeqiNP_010461.3. NM_001180483.3.

Genome annotation databases

EnsemblFungiiYDR176W; YDR176W; YDR176W.
GeneIDi851756.
KEGGisce:YDR176W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L12137 Genomic DNA. Translation: AAA21684.1 .
L21189 Unassigned DNA. Translation: AAA03542.1 . Sequence problems.
Z46727 Genomic DNA. Translation: CAA86681.1 .
BK006938 Genomic DNA. Translation: DAA12018.1 .
PIRi S41685.
RefSeqi NP_010461.3. NM_001180483.3.

3D structure databases

ProteinModelPortali P32494.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 32229. 125 interactions.
DIPi DIP-774N.
IntActi P32494. 33 interactions.
MINTi MINT-490762.
STRINGi 4932.YDR176W.

Proteomic databases

MaxQBi P32494.
PaxDbi P32494.
PeptideAtlasi P32494.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YDR176W ; YDR176W ; YDR176W .
GeneIDi 851756.
KEGGi sce:YDR176W.

Organism-specific databases

CYGDi YDR176w.
SGDi S000002583. NGG1.

Phylogenomic databases

eggNOGi NOG304305.
HOGENOMi HOG000248582.
InParanoidi P32494.
KOi K11315.
OMAi KRELKYI.
OrthoDBi EOG7N63WV.

Enzyme and pathway databases

BioCyci YEAST:G3O-29765-MONOMER.

Miscellaneous databases

NextBioi 969522.

Gene expression databases

Genevestigatori P32494.

Family and domain databases

InterProi IPR019340. Histone_AcTrfase_su3.
[Graphical view ]
Pfami PF10198. Ada3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of NGG1, a novel yeast gene required for glucose repression of GAL4p-regulated transcription."
    Brandl C.J., Furlanetto A.M., Martens J.A., Hamilton K.S.
    EMBO J. 12:5255-5265(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "ADA3: a gene, identified by resistance to GAL4-VP16, with properties similar to and different from those of ADA2."
    Pina B., Berger S.L., Marcus G.A., Silverman N., Agapite J., Guarente L.
    Mol. Cell. Biol. 13:5981-5989(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
  3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
    Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
    , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
    Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. "ADA1, a novel component of the ADA/GCN5 complex, has broader effects than GCN5, ADA2, or ADA3."
    Horiuchi J., Silverman N., Pina B., Marcus G.A., Guarente L.
    Mol. Cell. Biol. 17:3220-3228(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE ADA/GCN5 COMPLEX.
    Strain: ATCC MYA-3516 / BWG1-7A.
  6. "A subset of TAF(II)s are integral components of the SAGA complex required for nucleosome acetylation and transcriptional stimulation."
    Grant P.A., Schieltz D., Pray-Grant M.G., Steger D.J., Reese J.C., Yates J.R. III, Workman J.L.
    Cell 94:45-53(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE SAGA COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
  7. "The ATM-related cofactor Tra1 is a component of the purified SAGA complex."
    Grant P.A., Schieltz D., Pray-Grant M.G., Yates J.R. III, Workman J.L.
    Mol. Cell 2:863-867(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A SAGA COMPLEX WITH SPT7; HFI1; SPT8; GCN5; SPT20; SPT2; ADA2 AND TRA1.
  8. "Expanded lysine acetylation specificity of Gcn5 in native complexes."
    Grant P.A., Eberharter A., John S., Cook R.G., Turner B.M., Workman J.L.
    J. Biol. Chem. 274:5895-5900(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN HISTONE ACETYLATION AT THE SAGA COMPLEX, FUNCTION IN HISTONE ACETYLATION AT THE ADA COMPLEX.
  9. "The ADA complex is a distinct histone acetyltransferase complex in Saccharomyces cerevisiae."
    Eberharter A., Sterner D.E., Schieltz D., Hassan A., Yates J.R. III, Berger S.L., Workman J.L.
    Mol. Cell. Biol. 19:6621-6631(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE ADA COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
  10. "The novel SLIK histone acetyltransferase complex functions in the yeast retrograde response pathway."
    Pray-Grant M.G., Schieltz D., McMahon S.J., Wood J.M., Kennedy E.L., Cook R.G., Workman J.L., Yates J.R. III, Grant P.A.
    Mol. Cell. Biol. 22:8774-8786(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE SLIK COMPLEX.
  11. "SALSA, a variant of yeast SAGA, contains truncated Spt7, which correlates with activated transcription."
    Sterner D.E., Belotserkovskaya R., Berger S.L.
    Proc. Natl. Acad. Sci. U.S.A. 99:11622-11627(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE SALSA COMPLEX.
  12. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  13. "Chd1 chromodomain links histone H3 methylation with SAGA- and SLIK-dependent acetylation."
    Pray-Grant M.G., Daniel J.A., Schieltz D., Yates J.R. III, Grant P.A.
    Nature 433:434-438(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE SLIK COMPLEX.
  14. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
    Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
    J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-134, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  15. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-134 AND SER-407, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-134 AND THR-464, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "Molecular architecture of the S. cerevisiae SAGA complex."
    Wu P.Y., Ruhlmann C., Winston F., Schultz P.
    Mol. Cell 15:199-208(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: 3D-STRUCTURE MODELING OF THE SAGA COMPLEX.

Entry informationi

Entry nameiNGG1_YEAST
AccessioniPrimary (citable) accession number: P32494
Secondary accession number(s): D6VSF8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: October 29, 2014
This is version 127 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 2470 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

External Data

Dasty 3