O13801 · DRI1_SCHPO

Function

function

Mediates heterochromatin assembly by promoting RNAi-mediated heterochromatin silencing and histone deacetylation (PubMed:33693625).
Binds pericetromeric transcripts and recruits the RNA-induced transcriptional silencing (RITS) complex to heterochromatin (PubMed:33693625).
Recruits sir2 to chromatin to promote deacetylation of 'Lys-9' of histone H3 (PubMed:33693625).

Miscellaneous

Shown to localize to the nucleolus in PMID:16823372 by overexpression of a C-terminally tagged allele, however this allele was subsequently shown to be non-functional in PMID:33693625.

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentchromosome
Cellular Componentcytoplasm
Cellular Componentnucleus
Cellular Componentprotein aggregate center
Molecular Functionmetal ion binding
Molecular FunctionmRNA binding
Molecular FunctionRNA binding
Biological Processcellular response to heat
Biological Processcellular response to temperature stimulus
Biological Processchromatin organization
Biological Processregulation of heterochromatin formation
Biological Processregulatory ncRNA-mediated gene silencing

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    RNA-binding protein involved in heterochromatin assembly dri1
  • Alternative names
    • Dpb4-interacting, RRM, and IDR-containing factor

Gene names

    • Name
      dri1
    • Synonyms
      nrp1
    • ORF names
      SPAC17H9.04c

Organism names

Accessions

  • Primary accession
    O13801

Proteomes

Organism-specific databases

Subcellular Location

Keywords

Phenotypes & Variants

Disruption phenotype

Abolishes siRNA production from the centromeric outer repeat region (PubMed:33693625).
Decreases H3K9 methylation and impairs heterochromatin silencing; simultaneous disruption of dpb4 exacerbates the effect (PubMed:33693625).

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 7 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

PTM/Processing

Features

Showing features for chain, modified residue.

Type
IDPosition(s)Description
ChainPRO_00003141021-604RNA-binding protein involved in heterochromatin assembly dri1
Modified residue184Phosphoserine
Modified residue437Phosphoserine

Keywords

Proteomic databases

PTM databases

Interaction

Subunit

Interacts with dpb4 (PubMed:33693625).
Interacts with chp1 (PubMed:33693625).

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain, zinc finger.

Type
IDPosition(s)Description
Domain244-322RRM
Zinc finger343-372RanBP2-type 1
Zinc finger445-476RanBP2-type 2
Zinc finger560-588RanBP2-type 3

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    604
  • Mass (Da)
    66,396
  • Last updated
    1998-01-01 v1
  • Checksum
    F4DE6C459D062716
MSKLPSPTMPLPESVGDLVVLHFETNLDDHGISIGRAPCEIHEICWVILDGKTLEKQHCESCSIREDSSRHGICGSASSLTEAIFTLDNSIQERLNFQGKPFTFVVMNGRELRVLLPKEARDQGITLPSYMRHPRLFDLSSEYAKWQIRMGAVPPYTITLSHIFGKLDVDSLPPITESKAIELSPSDAPYITKGLTQCWRLANATTLLLRKAEKDSRGHSLPSVLTQPINCQADARSFYAERSKIVHVAGLTNDVTQLELESWFTNHGVHPVALWTLKTPEPYKSTGTGFVLFASHEDAADALAFNGYCLGDRMLEIIPSSTKVLDKASDILIPFPSSKNRPRPGDWNCPMCGFSNFQRRTSCFRCSFPGPTHVSAATGSNTFSPDFPYGNSYGNGSSHFIANYGGSVHHSNENTMQSDLQHQNGNNAVNHHHSSRSFGGNVPFRAGDWKCGSEGCGYHNFAKNVCCLRCGASRATAAVVADHASGPVNGSYSHNSYSHIPPVMSTSPPNHSVYPYSQLSINSVTANHGQNFGGQNGGNVSRFDDHGRFKEVSRPSVTTDQGDWLCECGFTNFRRRSNCLRCNAPHYSNMQIPASLPSDFNAYV

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CU329670
EMBL· GenBank· DDBJ
CAB11213.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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