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PROSITE documentation PDOC51414 [for PROSITE entry PS51414]

HSR domain profile





Description

The following proteins share a nuclear dot (DT) targeting and dimerization domain of ~100 amino acids [1,2,3]:

  • Mammalian nuclear autoantigen Sp-100, a constituent of nuclear domains known as nuclear dots (NDs) or promyelocytic leukemia (PML) bodies. It may play a role in the control of gene expression.
  • Murine Sp100-rs, a murine-truncated Sp-100 homologue, which is expressed from a highly amplified gene. In some mice strains, the amplification has progressed to such extremely high copy numbers that the amplified gene locus is visible as a homogeneously staining region (HSR) on the corresponding murine chromosome.
  • Mammalian nuclear body protein SP140-like or LySp100B protein.
  • Mammalian Sp110 nuclear body protein.
  • Vertebrate AutoImmune REgulator (AIRE) protein, a transcription regulator predominantly expressed in thymus medullary epithelial cells. It subcellularly localizes to nuclear dots.

As this domain comprises most of the sequence of the truncated murine Sp100-rs protein, it was termed HSR domain [2]. The HSR domain, which has also been named ASS (AIRE, Sp-100 and Sp140) domain [3], can also be found N-terminally in association with other domains, such as SAND (see <PDOC50864>), PHD finger (see <PDOC50016>) and Bromo (see <PDOC00550>), The HSR domain is predicted to be predominantly α-helical [1,2,3].

The profile we developed covers the entire HSR domain.

Last update:

December 2008 / First entry.

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Technical section

PROSITE method (with tools and information) covered by this documentation:

HSR, PS51414; HSR domain profile  (MATRIX)


References

1AuthorsGibson T.J. Ramu C. Gemuend C. Aasland R.
TitleThe APECED polyglandular autoimmune syndrome protein, AIRE-1, contains the SAND domain and is probably a transcription factor.
SourceTrends Biochem. Sci. 23:242-244(1998).
PubMed ID9697411

2AuthorsSternsdorf T. Jensen K. Reich B. Will H.
TitleThe nuclear dot protein sp100, characterization of domains necessary for dimerization, subcellular localization, and modification by small ubiquitin-like modifiers.
SourceJ. Biol. Chem. 274:12555-12566(1999).
PubMed ID10212234

3AuthorsMittaz L. Rossier C. Heino M. Peterson P. Krohn K.J.E. Gos A. Morris M.A. Kudoh J. Shimizu N. Antonarakis S.E. Scott H.S.
TitleIsolation and characterization of the mouse Aire gene.
SourceBiochem. Biophys. Res. Commun. 255:483-490(1999).
PubMed ID10049735
DOI10.1006/bbrc.1999.0223



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