NAT4/YMR069W Summary Help

Standard Name NAT4 1
Systematic Name YMR069W
Alias NAA40 2
Feature Type ORF, Verified
Description N alpha-acetyl-transferase; involved in acetylation of the N-terminal residues of histones H4 and H2A (1)
Name Description N-AcetylTransferase 1
Chromosomal Location
ChrXIII:407709 to 408566 | ORF Map | GBrowse
Gbrowse
Gene Ontology Annotations All NAT4 GO evidence and references
  View Computational GO annotations for NAT4
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
High-throughput
Regulators 7 genes
Resources
Classical genetics
null
Large-scale survey
null
Resources
41 total interaction(s) for 41 unique genes/features.
Physical Interactions
  • Affinity Capture-RNA: 2
  • Affinity Capture-Western: 1
  • Biochemical Activity: 1
  • Co-fractionation: 3

Genetic Interactions
  • Negative Genetic: 27
  • Positive Genetic: 6
  • Synthetic Growth Defect: 1

Resources
Expression Summary
histogram
Resources
Length (a.a.) 285
Molecular Weight (Da) 32,334
Isoelectric Point (pI) 8.03
Localization
Phosphorylation PhosphoGRID | PhosphoPep Database
Structure
Homologs
sequence information
ChrXIII:407709 to 408566 | ORF Map | GBrowse
SGD ORF map
Last Update Coordinates: 2011-02-03 | Sequence: 1996-07-31
Subfeature details
Relative
Coordinates
Chromosomal
Coordinates
Most Recent Updates
Coordinates Sequence
CDS 1..858 407709..408566 2011-02-03 1996-07-31
Retrieve sequences
Analyze Sequence
S288C only
S288C vs. other species
S288C vs. other strains
Resources
External Links All Associated Seq | E.C. | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB
Primary SGDIDS000004673
References cited on this page View Complete Literature Guide for NAT4
1) Song OK, et al.  (2003) An Nalpha-acetyltransferase responsible for acetylation of the N-terminal residues of histones H4 and H2A. J Biol Chem 278(40):38109-12
2) Polevoda B, et al.  (2009) A synopsis of eukaryotic Nalpha-terminal acetyltransferases: nomenclature, subunits and substrates. BMC Proc 3 Suppl 6:S2