Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

NuA3 HAT complex component NTO1

Gene

NTO1

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

Functioni

Component of the NuA3 histone acetyltransferase complex, that acetylates Lys-14 of histone H3. Recruitment of NuA3 to nucleosomes requires methylated histone H3. In conjunction with the FACT complex, NuA3 may be involved in transcriptional regulation.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri263 – 31351PHD-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • methylated histone binding Source: SGD
  • zinc ion binding Source: InterPro

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciYEAST:G3O-34190-MONOMER.
ReactomeiR-SCE-114608. Platelet degranulation.
R-SCE-3214847. HATs acetylate histones.
R-SCE-6804758. Regulation of TP53 Activity through Acetylation.

Names & Taxonomyi

Protein namesi
Recommended name:
NuA3 HAT complex component NTO1
Gene namesi
Name:NTO1
Ordered Locus Names:YPR031W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XVI

Organism-specific databases

EuPathDBiFungiDB:YPR031W.
SGDiS000006235. NTO1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB-SubCell
  • NuA3a histone acetyltransferase complex Source: SGD
  • NuA3b histone acetyltransferase complex Source: SGD
  • NuA3 histone acetyltransferase complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 748748NuA3 HAT complex component NTO1PRO_0000268692Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei728 – 7281PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ12311.

PTM databases

iPTMnetiQ12311.

Interactioni

Subunit structurei

Component of the NuA3 complex, which consists of at least NTO1, SAS3, TAF14, YNG1 and EAF6.1 Publication

GO - Molecular functioni

  • methylated histone binding Source: SGD

Protein-protein interaction databases

BioGridi36209. 72 interactions.
DIPiDIP-4956N.
IntActiQ12311. 10 interactions.
MINTiMINT-510213.

Structurei

3D structure databases

ProteinModelPortaliQ12311.
SMRiQ12311. Positions 263-314, 366-442.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

Residues 156 to 543 compose a region conserved in chromatin associated proteins.1 Publication

Sequence similaritiesi

Contains 1 PHD-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri263 – 31351PHD-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

GeneTreeiENSGT00740000114866.
HOGENOMiHOG000246761.
InParanoidiQ12311.
KOiK11380.
OMAiRRCMISK.
OrthoDBiEOG7DC2D3.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR019542. Enhancer_polycomb-like_N.
IPR019786. Zinc_finger_PHD-type_CS.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF10513. EPL1. 1 hit.
[Graphical view]
SMARTiSM00249. PHD. 2 hits.
[Graphical view]
SUPFAMiSSF57903. SSF57903. 1 hit.
PROSITEiPS01359. ZF_PHD_1. 1 hit.
PS50016. ZF_PHD_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q12311-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNRGSLDDGP KLREEKHFQD FYPDLNADTL LPFIVPLVET KDNSTDTDSD
60 70 80 90 100
DISNRNNREI GSVKSVQTKE LIFKGRVTTE PLVLKKNEVE FQKCKITTNE
110 120 130 140 150
LKGKKNPYCV RFNESFISRY YHINKVRNRK SYKQQQKEFD GVEAPYFTKF
160 170 180 190 200
SSKEAPNITI STSTKSAIQK FASISPNLVN FKPQYDMDEQ DELYLHYLNK
210 220 230 240 250
RYFKDQMSHE IFEILMTTLE TEWFHIEKHI PSTNSLIARH NILRDCKNYE
260 270 280 290 300
LYGSDDGTGL SMDQACAVCL GTDSDNLNTI VFCDGCDIAV HQECYGIIFI
310 320 330 340 350
PEGKWLCRRC MISKNNFATC LMCPSHTGAF KQTDTGSWVH NICALWLPEL
360 370 380 390 400
YFSNLHYMEP IEGVQNVSVS RWKLNCYICK KKMGACIQCF QRNCFTAYHV
410 420 430 440 450
TCARRAGLYM SKGKCTIQEL ASNQFSQKYS VESFCHKHAP RGWQTSIEGI
460 470 480 490 500
NKARKYFSLL STLQTETPQH NEANDRTNSK FNKTIWKTPN QTPVAPHVFA
510 520 530 540 550
EILQKVVDFF GLANPPAGAF DICKYWSMKR ELTGGTPLTA CFENNSLGSL
560 570 580 590 600
TEEQVQTRID FANDQLEDLY RLKELTTLVK KRTQASNSLS RSRKKVFDIV
610 620 630 640 650
KSPQKYLLKI NVLDIFIKSE QFKALERLVT EPKLLVILEK CKHCDFDTVQ
660 670 680 690 700
IFKEEIMHFF EVLETLPGAS RILQTVSSKA KEQVTNLIGL IEHVDIKKLL
710 720 730 740
SRDFIINDDK IEERPWSGPV IMEEEGLSDA EELSAGEHRM LKLILNSG
Length:748
Mass (Da):86,029
Last modified:November 1, 1996 - v1
Checksum:i7D6796553BCFA06D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z49274 Genomic DNA. Translation: CAA89285.1.
Z71255 Genomic DNA. Translation: CAA95027.1.
BK006949 Genomic DNA. Translation: DAA11457.1.
PIRiS54505.
RefSeqiNP_015356.1. NM_001184128.1.

Genome annotation databases

EnsemblFungiiYPR031W; YPR031W; YPR031W.
GeneIDi856143.
KEGGisce:YPR031W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z49274 Genomic DNA. Translation: CAA89285.1.
Z71255 Genomic DNA. Translation: CAA95027.1.
BK006949 Genomic DNA. Translation: DAA11457.1.
PIRiS54505.
RefSeqiNP_015356.1. NM_001184128.1.

3D structure databases

ProteinModelPortaliQ12311.
SMRiQ12311. Positions 263-314, 366-442.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36209. 72 interactions.
DIPiDIP-4956N.
IntActiQ12311. 10 interactions.
MINTiMINT-510213.

PTM databases

iPTMnetiQ12311.

Proteomic databases

MaxQBiQ12311.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYPR031W; YPR031W; YPR031W.
GeneIDi856143.
KEGGisce:YPR031W.

Organism-specific databases

EuPathDBiFungiDB:YPR031W.
SGDiS000006235. NTO1.

Phylogenomic databases

GeneTreeiENSGT00740000114866.
HOGENOMiHOG000246761.
InParanoidiQ12311.
KOiK11380.
OMAiRRCMISK.
OrthoDBiEOG7DC2D3.

Enzyme and pathway databases

BioCyciYEAST:G3O-34190-MONOMER.
ReactomeiR-SCE-114608. Platelet degranulation.
R-SCE-3214847. HATs acetylate histones.
R-SCE-6804758. Regulation of TP53 Activity through Acetylation.

Miscellaneous databases

PROiQ12311.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR019542. Enhancer_polycomb-like_N.
IPR019786. Zinc_finger_PHD-type_CS.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF10513. EPL1. 1 hit.
[Graphical view]
SMARTiSM00249. PHD. 2 hits.
[Graphical view]
SUPFAMiSSF57903. SSF57903. 1 hit.
PROSITEiPS01359. ZF_PHD_1. 1 hit.
PS50016. ZF_PHD_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI."
    Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M.
    , Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J.
    Nature 387:103-105(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  4. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  5. "The Epc-N domain: a predicted protein-protein interaction domain found in select chromatin associated proteins."
    Perry J.
    BMC Genomics 7:6-6(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAIN, PREDICTION OF FUNCTION.
  6. "Yng1 PHD finger binding to H3 trimethylated at K4 promotes NuA3 HAT activity at K14 of H3 and transcription at a subset of targeted ORFs."
    Taverna S.D., Ilin S., Rogers R.S., Tanny J.C., Lavender H., Li H., Baker L., Boyle J., Blair L.P., Chait B.T., Patel D.J., Aitchison J.D., Tackett A.J., Allis C.D.
    Mol. Cell 24:785-796(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF THE NUA3 COMPLEX, IDENTIFICATION IN THE NUA3 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
  7. "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-728, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiNTO1_YEAST
AccessioniPrimary (citable) accession number: Q12311
Secondary accession number(s): D6W441
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: November 1, 1996
Last modified: June 8, 2016
This is version 125 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 172 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 XVI
    Yeast (Saccharomyces cerevisiae) chromosome XVI: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.