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PROSITE documentation PDOC51982

Ubiquitin-like (ULD) domain profile





Description

The ubiquitin-like domain (ULD) of about 100 amino acids is found in two protein families:

  • SATB (Special AT-rich binding protein) family proteins have emerged as key regulators that integrate higher-order chromatin organization with the regulation of gene expression. SATB family chromatin organizers are involved in long-range enhancer function, extension of chromatin modifications and dynamic tethering of chromatin loops, and play diverse and important roles in regulating the dynamic equilibrium of apoptosis, cell invasion, metastasis, proliferation, angiogenesis, and immune modulation. SATB family proteins consist of ULD and CUTL (see <PDOC51983>) domains at the N terminus, a homeodomain (HD) (see <PDOC00027>) at the C terminus, and tandem CUT domains (see <PDOC51042>) in the center [1,2,3,4,5].
  • The Compass family proteins defective proventriculus (dve) from Drosophila, required for the formation of the proventriculus and proximodistal patterning of the wing disc, and dve-1 from Caenorhabditis elegans, required for embryonic development and maintenance of mitochondrial morphology. They contain the ULD domain as well as two atypical HDs [4,5,6].

The ULD domain adopts an ubiquitin-like fold comprising four antiparallel β-sheets that are flanked by four α-helices (see <PDB:3TUO>). The ULD domain of SATB1 assembles into a tetramer and the tetramerization of SATB1 is essential for recognizing specific DNA sequences (such as multiple AT-rich DNA fragments) [2,3].

The profile we developed covers the entire ULD domain.

Last update:

July 2021 / First entry.

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Technical section

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

ULD, PS51982; Ubiquitin-like (ULD) domain profile  (MATRIX)


References

1AuthorsNaik R. Galande S.
TitleSATB family chromatin organizers as master regulators of tumor progression.
SourceOncogene 38:1989-2004(2019).
PubMed ID30413763
DOI10.1038/s41388-018-0541-4

2AuthorsWang Z. Yang X. Chu X. Zhang J. Zhou H. Shen Y. Long J.
TitleThe structural basis for the oligomerization of the N-terminal domain of SATB1.
SourceNucleic. Acids. Res. 40:4193-4202(2012).
PubMed ID22241778
DOI10.1093/nar/gkr1284

3AuthorsWang Z. Yang X. Guo S. Yang Y. Su X.-C. Shen Y. Long J.
TitleCrystal structure of the ubiquitin-like domain-CUT repeat-like tandem of special AT-rich sequence binding protein 1 (SATB1) reveals a coordinating DNA-binding mechanism.
SourceJ. Biol. Chem. 289:27376-27385(2014).
PubMed ID25124042
DOI10.1074/jbc.M114.562314

4AuthorsBuerglin T.R. Cassata G.
TitleLoss and gain of domains during evolution of cut superclass homeobox genes.
SourceInt. J. Dev. Biol. 46:115-123(2002).
PubMed ID11902672

5AuthorsTakatori N. Saiga H.
TitleEvolution of CUT class homeobox genes: insights from the genome of the amphioxus, Branchiostoma floridae.
SourceInt. J. Dev. Biol. 52:969-977(2008).
PubMed ID18956327
DOI10.1387/ijdb.072541nt

6AuthorsFuss B. Hoch M.
TitleDrosophila endoderm development requires a novel homeobox gene which is a target of Wingless and Dpp signalling.
SourceMech. Dev. 79:83-97(1998).
PubMed ID10349623
DOI10.1016/s0925-4773(98)00172-5



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