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HTZ1 histone H2AZ [ Saccharomyces cerevisiae S288c ]

Gene ID: 854150, updated on 7-Sep-2014
Gene symbol
HTZ1
Gene description
histone H2AZ
Primary source
SGD:S000005372
Locus tag
YOL012C
Gene type
protein coding
RNA name
histone H2AZ
RefSeq status
PROVISIONAL
Organism
Saccharomyces cerevisiae S288c (strain: S288c)
Lineage
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
Also known as
HTA3
See HTZ1 in MapViewer
Location:
chromosome: XV
Exon count:
1
Sequence:
Chromosome: XV; NC_001147.6 (303579..303983, complement)

Chromosome XV - NC_001147.6Genomic Context describing neighboring genes Neighboring gene hypothetical protein Neighboring gene tRNA Neighboring gene E3 ubiquitin-protein ligase HRD1 Neighboring gene Plb3p Neighboring gene Rcl1p

GeneRIFs: Gene References Into FunctionsWhat's a GeneRIF?

Products Interactant Other Gene Complex Source Pubs Description

Homology

Gene Ontology Provided by GO

Function Evidence Code Pubs
DNA binding IEA
Inferred from Electronic Annotation
more info
 
chromatin binding IDA
Inferred from Direct Assay
more info
PubMed 
chromatin binding IGI
Inferred from Genetic Interaction
more info
PubMed 
chromatin binding ISS
Inferred from Sequence or Structural Similarity
more info
PubMed 
protein heterodimerization activity IEA
Inferred from Electronic Annotation
more info
 
Process Evidence Code Pubs
chromatin modification IEA
Inferred from Electronic Annotation
more info
 
chromatin remodeling IMP
Inferred from Mutant Phenotype
more info
 
chromatin silencing at silent mating-type cassette IGI
Inferred from Genetic Interaction
more info
PubMed 
chromatin silencing at silent mating-type cassette IPI
Inferred from Physical Interaction
more info
PubMed 
nuclear-transcribed mRNA catabolic process, non-stop decay IMP
Inferred from Mutant Phenotype
more info
PubMed 
nucleosome assembly IEA
Inferred from Electronic Annotation
more info
 
regulation of transcription from RNA polymerase II promoter IGI
Inferred from Genetic Interaction
more info
PubMed 
regulation of transcription from RNA polymerase II promoter IMP
Inferred from Mutant Phenotype
more info
PubMed 
regulation of transcription, DNA-templated IEA
Inferred from Electronic Annotation
more info
 
transcription, DNA-templated IEA
Inferred from Electronic Annotation
more info
 
Component Evidence Code Pubs
chromosome IEA
Inferred from Electronic Annotation
more info
 
nuclear chromatin IDA
Inferred from Direct Assay
more info
PubMed 
nuclear chromatin IPI
Inferred from Physical Interaction
more info
PubMed 
nucleosome IEA
Inferred from Electronic Annotation
more info
 
nucleus IDA
Inferred from Direct Assay
more info
 
nucleus IEA
Inferred from Electronic Annotation
more info
 
Names
histone H2AZ
NP_014631.1
  • Histone variant H2AZ; exchanged for histone H2A in nucleosomes by the SWR1 complex; involved in transcriptional regulation through prevention of the spread of silent heterochromatin; Htz1p-containing nucleosomes facilitate RNA Pol II passage by affecting correct assembly and modification status of RNA Pol II elongation complexes and by favoring efficient nucleosome remodeling

Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

  1. NC_001147.6 

    Range
    303579..303983
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NM_001183266.1NP_014631.1  histone H2AZ [Saccharomyces cerevisiae S288c]

    See proteins identical to NP_014631.1

    Status: PROVISIONAL

    UniProtKB/Swiss-Prot
    Q12692
    Conserved Domains (2) summary
    PTZ00017
    Location:7134
    Blast Score: 421
    PTZ00017; histone H2A; Provisional
    cd00074
    Location:11126
    Blast Score: 404
    H2A; Histone 2A; H2A is a subunit of the nucleosome. The nucleosome is an octamer containing two H2A, H2B, H3, and H4 subunits. The H2A subunit performs essential roles in maintaining structural integrity of the nucleosome, chromatin condensation, and binding ...