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FLASH GENE
Symbol IST1 contributors: mct - updated : 22-01-2020
HGNC name increased sodium tolerance 1 homolog
HGNC id 28977
EXPRESSION
Type
   expressed in (based on citations)
organ(s)
cell lineage
cell lines
fluid/secretion
at STAGE
PROTEIN
PHYSICAL PROPERTIES
STRUCTURE
motifs/domains
  • N-terminal domain (IST1NTD) reveals an ESCRT-III subunit-like fold, implicating IST1 as a divergent ESCRT-III family member
  • a microtubule interacting and transport (MIT) domain interacting motif (MIM) necessary for its interaction with VPS4A, LIP5 and other MIT domain-containing proteins, namely, MITD1, AMSH, UBPY, and Spastin
  • IST1 terminus contains two distinct MIT interacting motifs (MIM1 and MIM2) that wrap around and bind in different groves of the MIT helical bundle
  • HOMOLOGY
    interspecies homolog to yeast S.cerevisiae Ynl265c
    Homologene
    FAMILY
  • IST1 family
  • CATEGORY unknown/unspecified
    SUBCELLULAR LOCALIZATION     intracellular
    intracellular,cytoplasm,organelle,endoplasmic reticulum
    intracellular,cytoplasm,cytosolic,vesicle
    text colocalizes with IST1 at the midbody, and depletion of IST1 in cells by small interfering RNA significantly decreases the number of cells where spartin is present at midbodies
    basic FUNCTION
  • positive modulator of the ESCRT pathway
  • MIM activity of IST1 is essential for cytokinesis, suggesting possible mechanisms to explain its role in the last step of mammalian cell division
  • with CHMP1A act together to recruit and modulate specific VPS4A and VPS4B activities required during the final stages of cell division
  • new positive modulator of the ESCRT pathway
  • CELLULAR PROCESS
    PHYSIOLOGICAL PROCESS
    PATHWAY
    metabolism
    signaling
    a component
    INTERACTION
    DNA
    RNA
    small molecule
    protein
  • binds the late-acting ESCRT proteins Did2p/charged MVB protein (CHMP) 1 and VPS4A, VPS4B and exhibits synthetic vacuolar protein sorting defects when combined with mutations in the VTA1/CHMP5 complex
  • IST1 interaction is important for spartin recruitment to the midbody and that spartin participates in cytokinesis
  • CHMP1B and IST1 directly interacted with a tandem repeat of MIT domains of CAPN7 and autolytic activity of CAPN7 was enhanced by IST1
  • strong interactions of MITD1 with CHMP1B, CHMP2A, and IST1
  • role of MITD1 in negatively regulating the interaction of IST1 with VPS4A
  • a tandem MIT domain of VTA1, can bind MIM elements within both CHMP1A and IST1, implying that the complexes probably interact directly in cells
  • efficient abscission during cytokinesis requires proper function of the ESCRT-III protein IST1, which binds to the microtubule interacting and trafficking (MIT) domains of VPS4A, VTA1, and SPART via its C-terminal MIT-interacting motif (MIM)
  • cell & other
    REGULATION
    ASSOCIATED DISORDERS
    ANIMAL & CELL MODELS