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FLASH GENE
Symbol HNRNPH1 contributors: mct - updated : 16-09-2017
HGNC name heterogeneous nuclear ribonucleoprotein H1 (H)
HGNC id 5041
EXPRESSION
Type ubiquitous
   expressed in (based on citations)
organ(s)
cell lineage
cell lines
fluid/secretion
at STAGE
PROTEIN
PHYSICAL PROPERTIES
STRUCTURE
motifs/domains
  • RNA binding protein with three RNP-like (qRRM) motifs
  • conjugated RiboP
    HOMOLOGY
    Homologene
    FAMILY
  • heterogeneous nuclear ribonucleoproteins (HNRNP) family
  • CATEGORY RNA associated
    SUBCELLULAR LOCALIZATION     plasma membrane
        intracellular
    intracellular,nucleus,nucleoplasm
    basic FUNCTION
  • associated with pre-mRNAs in the nucleus and may be influencing pre-mRNA processing and other aspects of mRNA metabolism and transport
  • CELLULAR PROCESS
    PHYSIOLOGICAL PROCESS
    PATHWAY
    metabolism
    signaling
    a component
  • component of heterogeneous nuclear RNA ribonucleoprotein complex
  • INTERACTION
    DNA
    RNA binding
    small molecule
    protein
  • strong binding of HNRNPH1/HNRNPH2 to TYMP pre-mRNA, hence implicating them in TYMP splicing
  • HNRNPH1, RALY, and TFG are proteins that specifically interact with the C-terminal domain of RBFOX1 and RBFOX2
  • HNRNPH1 and TFG modulate the splicing activity of RBFOX1/2, whereas RALY had no effect
  • level of the two isoforms of NDUFB11 is regulated by three DGGGD ESS elements located in exon 2 which can bind the HNRNPH1 protein
  • PRKAA2 directly interact with the heterogeneous nuclear ribonucleoprotein H (HNRNPH1)
  • SRSF1 and HNRNPH1 antagonistically modulate splicing by binding exclusively to the target in exon 16 of COLQ
  • SRSF3 and HNRNPH1 are the first splicing factors identified which regulate the production of these functionally distinct ERBB2 splice variants and therefore maybe important for the regulation of ERBB2 signaling
  • IL7 stimulation induced the phosphorylation of the proteins STIP1, ATIC and HNRNPH1, involved in pathways related to survival, proliferation and gene expression, respectively, and increased the phosphorylation of CRKL
  • cell & other
    REGULATION
    ASSOCIATED DISORDERS
    ANIMAL & CELL MODELS