Q60DW3 · ALFL5_ORYSJ

Function

function

Histone-binding component that specifically recognizes H3 tails trimethylated on 'Lys-4' (H3K4me3), which mark transcription start sites of virtually all active genes.

Caution

Lacks the Tyr (here Asp-212), a conserved feature of the aromatic cage required for the interaction with histone H3K4me3/2.

Features

Showing features for site.

125820406080100120140160180200220240
TypeIDPosition(s)Description
Site218Histone H3K4me3 binding
Site222Histone H3K4me3 binding
Site227Histone H3K4me3 binding

GO annotations

all annotationsall molecular functionnucleotide bindingmolecular_functionnucleic acid bindingdna bindingchromatin bindingdna-binding transcription factor activityrna bindingcytoskeletal motor activitycatalytic activitynuclease activitysignaling receptor bindingstructural molecule activitytransporter activitybindingprotein bindingtranslation factor activity, rna bindinglipid bindingkinase activitytransferase activityhydrolase activityoxygen bindingenzyme regulator activitycarbohydrate bindingsignaling receptor activitytranslation regulator activitytranscription regulator activityother molecular functionall biological processcarbohydrate metabolic processgeneration of precursor metabolites and energynucleobase-containing compound metabolic processdna metabolic processtranslationlipid metabolic processtransportresponse to stresscell cyclecell communicationsignal transductioncell-cell signalingmulticellular organism developmentcircadian rhythmbiological_processmetabolic processcatabolic processbiosynthetic processresponse to light stimulusresponse to external stimulustropismresponse to biotic stimulusresponse to abiotic stimulusresponse to endogenous stimulusembryo developmentpost-embryonic developmentfruit ripeningabscissionpollinationflower developmentcellular processprogrammed cell deathphotosynthesiscellular component organizationcell growthprotein metabolic processcellular homeostasissecondary metabolic processreproductive processcell differentiationprotein modification processgrowthepigenetic regulation of gene expressionresponse to chemicalanatomical structure developmentregulation of molecular functionother biological processall cellular componentcellular_componentextracellular regioncell wallintracellular anatomical structurenucleusnuclear envelopenucleoplasmnucleoluscytoplasmmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuscytosolribosomecytoskeletonplasma membranechloroplastplastidthylakoidmembraneexternal encapsulating structureother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentnucleus
Molecular Functionhistone binding
Molecular Functionmetal ion binding
Molecular Functiontranscription cis-regulatory region binding
Molecular Functiontranscription coregulator activity
Biological Processchromatin organization
Biological Processregulation of DNA-templated transcription

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    PHD finger protein ALFIN-LIKE 5

Gene names

    • ORF names
      OsJ_18575, P0426G01.9
    • Ordered locus names
      Os05g0419100, LOC_Os05g34640

Organism names

  • Taxonomic identifier
  • Strain
    • cv. Nipponbare
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > Liliopsida > Poales > Poaceae > BOP clade > Oryzoideae > Oryzeae > Oryzinae > Oryza > Oryza sativa

Accessions

  • Primary accession
    Q60DW3
  • Secondary accessions
    • A0A0P0WMG7

Proteomes

Genome annotation databases

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain, modified residue (large scale data).

TypeIDPosition(s)SourceDescription
ChainPRO_00004129451-258UniProtPHD finger protein ALFIN-LIKE 5
Modified residue (large scale data)171PTMeXchangePhosphoserine
Modified residue (large scale data)188PTMeXchangePhosphoserine

Proteomic databases

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for region, compositional bias, zinc finger.

TypeIDPosition(s)Description
Region143-205Disordered
Compositional bias147-169Polar residues
Compositional bias187-201Acidic residues
Zinc finger202-254PHD-type

Domain

The PHD-type zinc finger mediates the binding to H3K4me3.

Sequence similarities

Belongs to the Alfin family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    258
  • Mass (Da)
    29,105
  • Last updated
    2004-11-23 v1
  • Checksum
    FF03F6E17727CF3E
MDGGSGGPYTSRTAEEVFRDFRGRRAGMIKALTTDVEKFYQLCDPEKENLCLYGYPNETWEVTLPAEEVPPEIPEPALGINFARDGMNEKDWLALVAVHSDSWLLAVAFYFAARFGFDKEARRRLFNMINNLPTIFEVVTGAAKKQTKEKAPNSTNKPNKPSSKMQPRPESHSKAPKPPAPPKDDDESGDEYADEEEEERDNTLCGSCGTNDGKDEFWICCDSCERWYHGKCVKITPARAEHIKHYKCPDCGNKRARA

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias147-169Polar residues
Compositional bias187-201Acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AC137623
EMBL· GenBank· DDBJ
AAV25644.1
EMBL· GenBank· DDBJ
Genomic DNA
AP008211
EMBL· GenBank· DDBJ
BAF17484.1
EMBL· GenBank· DDBJ
Genomic DNA
AP014961
EMBL· GenBank· DDBJ
BAS94060.1
EMBL· GenBank· DDBJ
Genomic DNA
CM000142
EMBL· GenBank· DDBJ
EEE63756.1
EMBL· GenBank· DDBJ
Genomic DNA
AK121400
EMBL· GenBank· DDBJ
BAH00468.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

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