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FLASH GENE
Symbol DNLZ contributors: mct/npt - updated : 07-12-2011
HGNC name DNL-type zinc finger
HGNC id 33879
Location 9q34.3      Physical location : 139.256.351 - 139.258.241
Synonym name
  • Hsp70 escort protein
  • chromosome 9 open reading frame 151
  • translocase of inner mitochondrial membrane 15 homolog (yeast)
  • Synonym symbol(s) RP11-413M3.2, C9orf151, HEP, MGC87491, TIMM15, ZIM17, bA413M3.2
    DNA
    TYPE functioning gene
    STRUCTURE 1.89 kb     3 Exon(s)
    MAPPING cloned Y linked N status provisional
    RNA
    TRANSCRIPTS type messenger
    identificationnb exonstypebpproduct
    ProteinkDaAAspecific expressionYearPubmed
    3 - 724 19.1 178 - 2011 21530495
    EXPRESSION
    Type restricted
       expressed in (based on citations)
    organ(s)
    SystemOrgan level 1Organ level 2Organ level 3Organ level 4LevelPubmedSpeciesStageRna symbol
    Digestivesalivary gland    
    Reproductivefemale systemuteruscervix  
     male systemprostate   
    Urinarykidney    
    cell lineage
    cell lines
    fluid/secretion
    at STAGE
    PROTEIN
    PHYSICAL PROPERTIES globular
    STRUCTURE
    motifs/domains
  • an N-terminal ATPase domain, predicted to constitute a mitochondrial localization signaling sequence
  • a ZBS domain required to form a stable complex with the HSPA9 ATPase domain, and ATP hydrolysis measurements reveal that the ZBS is critical for full stimulation of HSPA9 catalytic activity
  • a conserved histidine as critical for DNLZ regulation of mitochondrial HSPA9 catalytic activity
  • a C-terminal peptide-binding domain
  • HOMOLOGY
    interspecies ortholog to S. Cerevisiae Zim17
    Homologene
    FAMILY
  • hsp70 protein family
  • CATEGORY chaperone/stress
    SUBCELLULAR LOCALIZATION     intracellular
    intracellular,cytoplasm,organelle,mitochondria
    basic FUNCTION
  • exhibits limited solubility due to aggregation mediated by its ATPase domain and directly enhances chaperone solubility through interactions with this domain
  • promote chaperone solubility through interactions with the ATPase domain
  • enhances the HSPA9 rate of ATP hydrolysis
  • cochaperone that controls the rate at which HSPA9 converts between its low peptide affinity (ATP bound) and high peptide affinity (ADP bound) conformations
  • regulates the catalytic activity and solubility of the mitochondrial hsp70 chaperone HSPA9
  • CELLULAR PROCESS
    PHYSIOLOGICAL PROCESS
    PATHWAY
    metabolism
    signaling
    a component
    INTERACTION
    DNA
    RNA
    small molecule
    protein
    cell & other
    REGULATION
    ASSOCIATED DISORDERS
    ANIMAL & CELL MODELS