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P32494 (NGG1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Chromatin-remodeling complexes subunit NGG1
Alternative name(s):
Transcriptional adapter 3
Gene names
Name:NGG1
Synonyms:ADA3, SWI7
Ordered Locus Names:YDR176W
ORF Names:YD9395.09
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length702 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.8

Subunit structure

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. Ref.5 Ref.6 Ref.7 Ref.9 Ref.10 Ref.11 Ref.13

Subcellular location

Nucleus Potential.

Miscellaneous

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

Sequence similarities

Belongs to the NGG1 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 702702Chromatin-remodeling complexes subunit NGG1
PRO_0000064448

Regions

Motif606 – 61813Nuclear localization signal Potential

Amino acid modifications

Modified residue1341Phosphoserine Ref.14 Ref.15 Ref.16
Modified residue4071Phosphoserine Ref.15
Modified residue4641Phosphothreonine Ref.16

Experimental info

Sequence conflict5201K → M in AAA03542. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P32494 [UniParc].

Last modified October 1, 1993. Version 1.
Checksum: 489016BFD1C095D4

FASTA70279,282
        10         20         30         40         50         60 
MPRHGRRGKL PKGEKLPKKE GGDNTPSKLL SSMLKTLDLT FERDIGMLNG KSVRSIPNKK 

        70         80         90        100        110        120 
TLLELQSQLD SLNEILGTIA RGDQETIEAL RKIRDSKNEK QANDEKQETS NADGQHESST 

       130        140        150        160        170        180 
ATEETNIIDK GVQSPPKPPP SNEISGTIEN DVESIKQAAD NMAKEEINED KDLQVHRDQP 

       190        200        210        220        230        240 
REKRPFDSET ENRATENENT QRPDNKKQKI DVDKMENDPT VKNPKSEFVV SQTLPRAAAA 

       250        260        270        280        290        300 
LGLFNEEGLE STGEDFLKKK YNVASYPTND LKDLLPGELP DMDFSHPKPT NQIQFNTFLA 

       310        320        330        340        350        360 
FVENFFKDLS DDNLKFLKMK YIIPDSLQFD KTYDPEVNPF IIPKLGPLYT DVWFKDENDK 

       370        380        390        400        410        420 
NSAYKKPSPY SNDASTILPK KSANELDDNA LESGSISCGP LLSRLLSAVL KDDNDKSELQ 

       430        440        450        460        470        480 
SSKIIRDGGL PRTGGEDDIQ SFRNNNNDTV DMTLSQENGP SVQTPDNDID EEASFQAKLA 

       490        500        510        520        530        540 
ENKGSNGGTT STLPQQIGWI TNGINLDYPT FEERLKRELK YVGIYMNLPK DENNPNSDDP 

       550        560        570        580        590        600 
DWVTGREDDE ISAELRELQG TLKQVTKKNQ KRKAQLIPLV ERQLAWQEYS SILEDLDKQI 

       610        620        630        640        650        660 
DQAYVKRIRV PKKRKKHHTA ASNNVNTGTT SQIAQQKAAN SSLKSLLDKR QRWINKIGPL 

       670        680        690        700 
FDKPEIMKRI PNESVFKDMD QEEDEDEADV FAQNTNKDVE LN 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
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]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRS41685.
RefSeqNP_010461.3. NM_001180483.3.

3D structure databases

ProteinModelPortalP32494.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid32229. 125 interactions.
DIPDIP-774N.
IntActP32494. 33 interactions.
MINTMINT-490762.
STRING4932.YDR176W.

Proteomic databases

PaxDbP32494.
PeptideAtlasP32494.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYDR176W; YDR176W; YDR176W.
GeneID851756.
KEGGsce:YDR176W.

Organism-specific databases

CYGDYDR176w.
SGDS000002583. NGG1.

Phylogenomic databases

eggNOGNOG304305.
HOGENOMHOG000248582.
KOK11315.
OMAKRELKYI.
OrthoDBEOG7N63WV.

Enzyme and pathway databases

BioCycYEAST:G3O-29765-MONOMER.

Gene expression databases

GenevestigatorP32494.

Family and domain databases

InterProIPR019340. Histone_AcTrfase_su3.
[Graphical view]
PfamPF10198. Ada3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio969522.

Entry information

Entry nameNGG1_YEAST
AccessionPrimary (citable) accession number: P32494
Secondary accession number(s): D6VSF8
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: April 16, 2014
This is version 123 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome IV

Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families