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PROSITE documentation PDOC51912 [for PROSITE entry PS51912]

DMAP1-binding domain profile





Description

The DNA methyltransferase 1 (DNMT1) is a multifunctional protein that is a critical DNA methyltransferase important for chromatin structure and gene silencing as well as methyltransferase-independent transcriptional repression. DNMT1 is composed of multiple functional domains. The N-terminal regulatory region contains conserved domains, including the DNA methyltransferase-associated protein 1 (DMAP1)-binding domain, the PCNA (proliferating cell nuclear antigen) binding domain (PBD) and the replication foci targeting sequence (RFTS) which control the subnuclear localization of DNMT1. In contrast, the C-terminal portion contains a catalytic domain (see <PDOC51555>). The DMAP1-binding domain is a ~120-amino acid protein-protein interaction module that binds notably DMAP1, a transcriptional co-repressor [1,2,3].

In addition to DNMT1, a DMAP1-binding domain is found in the following proteins:

  • Animal disco-interacting protein 2 (DIP-2), that maintains morphology of mature neurons. DIP-2 consists of a DMAP1-binding domain and two adenylate- forming domains (AFDs) [4,5,6].
  • Animal N-acetylglucosamine-1-phosphotransferase subunits α (GNPTA) and γ (GNPTG), members of a complex that catalyzes the initial step in the formation of the mannose 6-phopsphate targeting signal on newly synthesized lysosomal acid hydrolases. The DMAP1-binding domain mediates the selective binding GlcNAc-1-phosphotranferase to acid hydrolases [7,8].

The DMAP1-binding domain is predicted to adopt a long helix-turn-helix structure that is rich in leucine residues [1].

The profile we developed covers the entire DMAP1-binding domain.

Last update:

January 2020 / First entry.

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Technical section

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

DMAP1_BIND, PS51912; DMAP1-binding domain profile  (MATRIX)


References

1AuthorsYoder J.A. Yen R.-W. Vertino P.M. Bestor T.H. Baylin S.B.
TitleNew 5' regions of the murine and human genes for DNA (cytosine-5)-methyltransferase.
SourceJ. Biol. Chem. 271:31092-31097(1996).
PubMed ID8940105
DOI10.1074/jbc.271.49.31092

2AuthorsRountree M.R. Bachman K.E. Baylin S.B.
TitleDNMT1 binds HDAC2 and a new co-repressor, DMAP1, to form a complex at replication foci.
SourceNat. Genet. 25:269-277(2000).
PubMed ID10888872
DOI10.1038/77023

3AuthorsMisaki T. Yamaguchi L. Sun J. Orii M. Nishiyama A. Nakanishi M.
TitleThe replication foci targeting sequence (RFTS) of DNMT1 functions as a potent histone H3 binding domain regulated by autoinhibition.
SourceBiochem. Biophys. Res. Commun. 470:741-747(2016).
PubMed ID26774338
DOI10.1016/j.bbrc.2016.01.029

4AuthorsWinnepenninckx B. Debacker K. Ramsay J. Smeets D. Smits A. FitzPatrick D.R. Kooy R.F.
TitleCGG-repeat expansion in the DIP2B gene is associated with the fragile site FRA12A on chromosome 12q13.1.
SourceAm. J. Hum. Genet. 80:221-231(2007).
PubMed ID17236128
DOI10.1086/510800

5AuthorsNitta Y. Yamazaki D. Sugie A. Hiroi M. Tabata T.
TitleDISCO Interacting Protein 2 regulates axonal bifurcation and guidance of Drosophila mushroom body neurons.
SourceDev. Biol. 421:233-244(2017).
PubMed ID27908785
DOI10.1016/j.ydbio.2016.11.015

6AuthorsNoblett N. Wu Z. Ding Z.H. Park S. Roenspies T. Flibotte S. Chisholm A.D. Jin Y. Colavita A.
TitleDIP-2 suppresses ectopic neurite sprouting and axonal regeneration in mature neurons.
SourceJ. Cell. Biol. 218:125-133(2019).
PubMed ID30396999
DOI10.1083/jcb.201804207

7AuthorsQian Y. Flanagan-Steet H. van Meel E. Steet R. Kornfeld S.A.
TitleThe DMAP interaction domain of UDP-GlcNAc:lysosomal enzyme N-acetylglucosamine-1-phosphotransferase is a substrate recognition module.
SourceProc. Natl. Acad. Sci. U. S. A. 110:10246-10251(2013).
PubMed ID23733939
DOI10.1073/pnas.1308453110

8AuthorsQian Y. van Meel E. Flanagan-Steet H. Yox A. Steet R. Kornfeld S.
TitleAnalysis of mucolipidosis II/III GNPTAB missense mutations identifies domains of UDP-GlcNAc:lysosomal enzyme GlcNAc-1-phosphotransferase involved in catalytic function and lysosomal enzyme recognition.
SourceJ. Biol. Chem. 290:3045-3056(2015).
PubMed ID25505245
DOI10.1074/jbc.M114.612507



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