The 'PINIT' motif, of a newly identified conserved domain of the PIAS protein family, is essential for nuclear retention of PIAS3L

FEBS Lett. 2003 Nov 6;554(1-2):111-8. doi: 10.1016/s0014-5793(03)01116-5.


PIAS proteins, cytokine-dependent STAT-associated repressors, exhibit intrinsic E3-type SUMO ligase activities and form a family of transcriptional modulators. Three conserved domains have been identified so far in this protein family, the SAP box, the MIZ-Zn finger/RING module and the acidic C-terminal domain, which are essential for protein interactions, DNA binding or SUMO ligase activity. We have identified a novel conserved domain of 180 residues in PIAS proteins and shown that its 'PINIT' motif as well as other conserved motifs (in the SAP box and in the RING domain) are independently involved in nuclear retention of PIAS3L, the long form of PIAS3, that we have characterized in mouse embryonic stem cells.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Active Transport, Cell Nucleus*
  • Amino Acid Motifs
  • Amino Acid Sequence
  • Animals
  • Carrier Proteins / chemistry*
  • Carrier Proteins / genetics
  • Carrier Proteins / metabolism
  • Cell Line
  • Cloning, Molecular
  • Conserved Sequence*
  • DNA, Complementary
  • Gene Expression Regulation
  • Genetic Variation
  • Intracellular Signaling Peptides and Proteins*
  • Mice
  • Molecular Sequence Data
  • Protein Inhibitors of Activated STAT
  • Protein Structure, Tertiary
  • Sequence Alignment


  • Carrier Proteins
  • DNA, Complementary
  • Intracellular Signaling Peptides and Proteins
  • Pias3 protein, mouse
  • Protein Inhibitors of Activated STAT