DMAP1: Difference between revisions

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{{Infobox_gene}}
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'''DNA methyltransferase 1-associated protein 1''' is an [[enzyme]] that in humans is encoded by the ''DMAP1'' [[gene]].<ref name="pmid10888872">{{cite journal | vauthors = Rountree MR, Bachman KE, Baylin SB | title = DNMT1 binds HDAC2 and a new co-repressor, DMAP1, to form a complex at replication foci | journal = Nat Genet | volume = 25 | issue = 3 | pages = 269–77 |date=Aug 2000 | pmid = 10888872 | pmc =  | doi = 10.1038/77023 }}</ref><ref name="pmid10718198">{{cite journal | vauthors = Nagase T, Kikuno R, Ishikawa KI, Hirosawa M, Ohara O | title = Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro | journal = DNA Res | volume = 7 | issue = 1 | pages = 65–73 |date=Apr 2000 | pmid = 10718198 | pmc = | doi =10.1093/dnares/7.1.65  }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: DMAP1 DNA methyltransferase 1 associated protein 1| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=55929| accessdate = }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
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| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = DNA methyltransferase 1 associated protein 1
| HGNCid = 18291
| Symbol = DMAP1
| AltSymbols =; EAF2; DKFZp686L09142; DNMAP1; DNMTAP1; FLJ11543; KIAA1425; SWC4
| OMIM = 605077
| ECnumber = 
| Homologene = 41311
| MGIid = 1913483
| Function = {{GNF_GO|id=GO:0003677 |text = DNA binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008168 |text = methyltransferase activity}} {{GNF_GO|id=GO:0016564 |text = transcription repressor activity}} {{GNF_GO|id=GO:0016740 |text = transferase activity}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0001558 |text = regulation of cell growth}} {{GNF_GO|id=GO:0006306 |text = DNA methylation}} {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0016481 |text = negative regulation of transcription}} {{GNF_GO|id=GO:0016568 |text = chromatin modification}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 55929
    | Hs_Ensembl = ENSG00000178028
    | Hs_RefseqProtein = NP_001029195
    | Hs_RefseqmRNA = NM_001034023
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 1
    | Hs_GenLoc_start = 44451712
    | Hs_GenLoc_end = 44458940
    | Hs_Uniprot = Q9NPF5
    | Mm_EntrezGene = 66233
    | Mm_Ensembl = ENSMUSG00000009640
    | Mm_RefseqmRNA = NM_023178
    | Mm_RefseqProtein = NP_075667
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 4
    | Mm_GenLoc_start = 117172613
    | Mm_GenLoc_end = 117180205
    | Mm_Uniprot = Q9JI44
  }}
}}
'''DNA methyltransferase 1 associated protein 1''', also known as '''DMAP1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: DMAP1 DNA methyltransferase 1 associated protein 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=55929| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
This gene encodes a subunit of several, distinct complexes involved in the repression or activation of transcription. The encoded protein can independently repress transcription and is targeted to replication foci throughout S phase by interacting directly with the N-terminus of DNA methyltransferase 1. During late S phase, histone deacetylase 2 is added to this complex, providing a means to deacetylate histones in transcriptionally inactive heterochromatin following replication. The encoded protein is also a component of the nucleosome acetyltransferase of H4 complex and interacts with the transcriptional corepressor tumor susceptibility gene 101 and the pro-apoptotic death-associated protein 6, among others. Alternatively spliced transcript variants encoding the same protein have been described.<ref name="entrez" />
{{PBB_Summary
 
| section_title =
== Interactions ==
| summary_text = This gene encodes a subunit of several, distinct complexes involved in the repression or activation of transcription. The encoded protein can independently repress transcription and is targeted to replication foci throughout S phase by interacting directly with the N-terminus of DNA methyltransferase 1. During late S phase, histone deacetylase 2 is added to this complex, providing a means to deacetylate histones in transcriptionally inactive heterochromatin following replication. The encoded protein is also a component of the nucleosome acetyltransferase of H4 complex and interacts with the transcriptional corepressor tumor susceptibility gene 101 and the pro-apoptotic death-associated protein 6, among others. Alternatively spliced transcript variants encoding the same protein have been described.<ref name="entrez">{{cite web | title = Entrez Gene: DMAP1 DNA methyltransferase 1 associated protein 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=55929| accessdate = }}</ref>
 
}}
DMAP1 has been shown to [[Protein-protein interaction|interact]] with:
* [[C19orf2]],<ref name = pmid15367675>{{cite journal | date = Oct 2004 | vauthors = Delgermaa L, Hayashi N, Dorjsuren D, Nomura T, Thuy le TT, Murakami S | title = Subcellular localization of RPB5-mediating protein and its putative functional partner | journal = Mol. Cell. Biol. | volume = 24 | issue = 19 | pages = 8556–66 | pmid = 15367675 | pmc = 516735 | doi = 10.1128/MCB.24.19.8556-8566.2004}}</ref>
* [[DNMT1]],<ref name = autogenerated1>{{cite journal | date = Jul 2000 | vauthors = Rountree MR, Bachman KE, Baylin SB | title = DNMT1 binds HDAC2 and a new co-repressor, DMAP1, to form a complex at replication foci | journal = Nat. Genet. | volume = 25 | issue = 3 | pages = 269–77 | pmid = 10888872 | doi = 10.1038/77023}}</ref>
* [[ING1]],<ref name = pmid14665632>{{cite journal | date = Mar 2004 | vauthors = Xin H, Yoon HG, Singh PB, Wong J, Qin J | title = Components of a pathway maintaining histone modification and heterochromatin protein 1 binding at the pericentric heterochromatin in Mammalian cells | journal = J. Biol. Chem. | volume = 279 | issue = 10 | pages = 9539–46 | pmid = 14665632 | doi = 10.1074/jbc.M311587200}}</ref> and
* [[RGS6]]<ref name = pmid14734556>{{cite journal | date = Apr 2004 | vauthors = Liu Z, Fisher RA | title = RGS6 interacts with DMAP1 and DNMT1 and inhibits DMAP1 transcriptional repressor activity | journal = J. Biol. Chem. | volume = 279 | issue = 14 | pages = 14120–8 | pmid = 14734556 | doi = 10.1074/jbc.M309547200}}</ref>


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
*{{cite journal  | vauthors=Doyon Y, Côté J |title=The highly conserved and multifunctional NuA4 HAT complex. |journal=Curr. Opin. Genet. Dev. |volume=14 |issue= 2 |pages= 147–54 |year= 2004 |pmid= 15196461 |doi= 10.1016/j.gde.2004.02.009 }}
| citations =
*{{cite journal  | vauthors=Hartley JL, Temple GF, Brasch MA |title=DNA cloning using in vitro site-specific recombination. |journal=Genome Res. |volume=10 |issue= 11 |pages= 1788–95 |year= 2001 |pmid= 11076863 |doi=10.1101/gr.143000  | pmc=310948 }}
*{{cite journal  | author=Doyon Y, Côté J |title=The highly conserved and multifunctional NuA4 HAT complex. |journal=Curr. Opin. Genet. Dev. |volume=14 |issue= 2 |pages= 147-54 |year= 2004 |pmid= 15196461 |doi= 10.1016/j.gde.2004.02.009 }}
*{{cite journal  | vauthors=Wiemann S, Weil B, Wellenreuther R |title=Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. |journal=Genome Res. |volume=11 |issue= 3 |pages= 422–35 |year= 2001 |pmid= 11230166 |doi= 10.1101/gr.GR1547R  | pmc=311072 |display-authors=etal}}
*{{cite journal  | author=Nagase T, Kikuno R, Ishikawa KI, ''et al.'' |title=Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro. |journal=DNA Res. |volume=7 |issue= 1 |pages= 65-73 |year= 2000 |pmid= 10718198 |doi=  }}
*{{cite journal  | vauthors=Yang CS, Weiner H |title=Yeast two-hybrid screening identifies binding partners of human Tom34 that have ATPase activity and form a complex with Tom34 in the cytosol. |journal=Arch. Biochem. Biophys. |volume=400 |issue= 1 |pages= 105–10 |year= 2002 |pmid= 11913976 |doi= 10.1006/abbi.2002.2778 }}
*{{cite journal  | author=Rountree MR, Bachman KE, Baylin SB |title=DNMT1 binds HDAC2 and a new co-repressor, DMAP1, to form a complex at replication foci. |journal=Nat. Genet. |volume=25 |issue= 3 |pages= 269-77 |year= 2000 |pmid= 10888872 |doi= 10.1038/77023 }}
*{{cite journal  | vauthors=Strausberg RL, Feingold EA, Grouse LH |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241 |display-authors=etal}}
*{{cite journal  | author=Hartley JL, Temple GF, Brasch MA |title=DNA cloning using in vitro site-specific recombination. |journal=Genome Res. |volume=10 |issue= 11 |pages= 1788-95 |year= 2001 |pmid= 11076863 |doi=  }}
*{{cite journal  | vauthors=Cai Y, Jin J, Tomomori-Sato C |title=Identification of new subunits of the multiprotein mammalian TRRAP/TIP60-containing histone acetyltransferase complex. |journal=J. Biol. Chem. |volume=278 |issue= 44 |pages= 42733–6 |year= 2003 |pmid= 12963728 |doi= 10.1074/jbc.C300389200 |display-authors=etal}}
*{{cite journal  | author=Wiemann S, Weil B, Wellenreuther R, ''et al.'' |title=Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. |journal=Genome Res. |volume=11 |issue= 3 |pages= 422-35 |year= 2001 |pmid= 11230166 |doi= 10.1101/gr.154701 }}
*{{cite journal  | vauthors=Xin H, Yoon HG, Singh PB |title=Components of a pathway maintaining histone modification and heterochromatin protein 1 binding at the pericentric heterochromatin in Mammalian cells. |journal=J. Biol. Chem. |volume=279 |issue= 10 |pages= 9539–46 |year= 2004 |pmid= 14665632 |doi= 10.1074/jbc.M311587200 |display-authors=etal}}
*{{cite journal  | author=Yang CS, Weiner H |title=Yeast two-hybrid screening identifies binding partners of human Tom34 that have ATPase activity and form a complex with Tom34 in the cytosol. |journal=Arch. Biochem. Biophys. |volume=400 |issue= 1 |pages= 105-10 |year= 2002 |pmid= 11913976 |doi= 10.1006/abbi.2002.2778 }}
*{{cite journal  | vauthors=Ota T, Suzuki Y, Nishikawa T |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 |display-authors=etal}}
*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal  | vauthors=Liu Z, Fisher RA |title=RGS6 interacts with DMAP1 and DNMT1 and inhibits DMAP1 transcriptional repressor activity. |journal=J. Biol. Chem. |volume=279 |issue= 14 |pages= 14120–8 |year= 2004 |pmid= 14734556 |doi= 10.1074/jbc.M309547200 }}
*{{cite journal  | author=Cai Y, Jin J, Tomomori-Sato C, ''et al.'' |title=Identification of new subunits of the multiprotein mammalian TRRAP/TIP60-containing histone acetyltransferase complex. |journal=J. Biol. Chem. |volume=278 |issue= 44 |pages= 42733-6 |year= 2003 |pmid= 12963728 |doi= 10.1074/jbc.C300389200 }}
*{{cite journal  | vauthors=Doyon Y, Selleck W, Lane WS |title=Structural and functional conservation of the NuA4 histone acetyltransferase complex from yeast to humans. |journal=Mol. Cell. Biol. |volume=24 |issue= 5 |pages= 1884–96 |year= 2004 |pmid= 14966270 |doi=10.1128/MCB.24.5.1884-1896.2004  | pmc=350560 |display-authors=etal}}
*{{cite journal  | author=Xin H, Yoon HG, Singh PB, ''et al.'' |title=Components of a pathway maintaining histone modification and heterochromatin protein 1 binding at the pericentric heterochromatin in Mammalian cells. |journal=J. Biol. Chem. |volume=279 |issue= 10 |pages= 9539-46 |year= 2004 |pmid= 14665632 |doi= 10.1074/jbc.M311587200 }}
*{{cite journal  | vauthors=Muromoto R, Sugiyama K, Takachi A |title=Physical and functional interactions between Daxx and DNA methyltransferase 1-associated protein, DMAP1. |journal=J. Immunol. |volume=172 |issue= 5 |pages= 2985–93 |year= 2004 |pmid= 14978102 |doi=  10.4049/jimmunol.172.5.2985|display-authors=etal}}
*{{cite journal  | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40-5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
*{{cite journal  | vauthors=Muromoto R, Sugiyama K, Yamamoto T |title=Physical and functional interactions between Daxx and TSG101. |journal=Biochem. Biophys. Res. Commun. |volume=316 |issue= 3 |pages= 827–33 |year= 2004 |pmid= 15033475 |doi= 10.1016/j.bbrc.2004.02.126 |display-authors=etal}}
*{{cite journal  | author=Liu Z, Fisher RA |title=RGS6 interacts with DMAP1 and DNMT1 and inhibits DMAP1 transcriptional repressor activity. |journal=J. Biol. Chem. |volume=279 |issue= 14 |pages= 14120-8 |year= 2004 |pmid= 14734556 |doi= 10.1074/jbc.M309547200 }}
*{{cite journal  | vauthors=Ballif BA, Villén J, Beausoleil SA |title=Phosphoproteomic analysis of the developing mouse brain. |journal=Mol. Cell. Proteomics |volume=3 |issue= 11 |pages= 1093–101 |year= 2005 |pmid= 15345747 |doi= 10.1074/mcp.M400085-MCP200 |display-authors=etal}}
*{{cite journal  | author=Doyon Y, Selleck W, Lane WS, ''et al.'' |title=Structural and functional conservation of the NuA4 histone acetyltransferase complex from yeast to humans. |journal=Mol. Cell. Biol. |volume=24 |issue= 5 |pages= 1884-96 |year= 2004 |pmid= 14966270 |doi=  }}
*{{cite journal  | vauthors=Delgermaa L, Hayashi N, Dorjsuren D |title=Subcellular localization of RPB5-mediating protein and its putative functional partner. |journal=Mol. Cell. Biol. |volume=24 |issue= 19 |pages= 8556–66 |year= 2004 |pmid= 15367675 |doi= 10.1128/MCB.24.19.8556-8566.2004 | pmc=516735 |display-authors=etal}}
*{{cite journal  | author=Muromoto R, Sugiyama K, Takachi A, ''et al.'' |title=Physical and functional interactions between Daxx and DNA methyltransferase 1-associated protein, DMAP1. |journal=J. Immunol. |volume=172 |issue= 5 |pages= 2985-93 |year= 2004 |pmid= 14978102 |doi=  }}
*{{cite journal  | vauthors=Gerhard DS, Wagner L, Feingold EA |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 | pmc=528928 |display-authors=etal}}
*{{cite journal  | author=Muromoto R, Sugiyama K, Yamamoto T, ''et al.'' |title=Physical and functional interactions between Daxx and TSG101. |journal=Biochem. Biophys. Res. Commun. |volume=316 |issue= 3 |pages= 827-33 |year= 2004 |pmid= 15033475 |doi= 10.1016/j.bbrc.2004.02.126 }}
*{{cite journal  | vauthors=Wiemann S, Arlt D, Huber W |title=From ORFeome to biology: a functional genomics pipeline. |journal=Genome Res. |volume=14 |issue= 10B |pages= 2136–44 |year= 2004 |pmid= 15489336 |doi= 10.1101/gr.2576704 | pmc=528930 |display-authors=etal}}
*{{cite journal  | author=Ballif BA, Villén J, Beausoleil SA, ''et al.'' |title=Phosphoproteomic analysis of the developing mouse brain. |journal=Mol. Cell Proteomics |volume=3 |issue= 11 |pages= 1093-101 |year= 2005 |pmid= 15345747 |doi= 10.1074/mcp.M400085-MCP200 }}
*{{cite journal  | vauthors=Cai Y, Jin J, Florens L |title=The mammalian YL1 protein is a shared subunit of the TRRAP/TIP60 histone acetyltransferase and SRCAP complexes. |journal=J. Biol. Chem. |volume=280 |issue= 14 |pages= 13665–70 |year= 2005 |pmid= 15647280 |doi= 10.1074/jbc.M500001200 |display-authors=etal}}
*{{cite journal  | author=Delgermaa L, Hayashi N, Dorjsuren D, ''et al.'' |title=Subcellular localization of RPB5-mediating protein and its putative functional partner. |journal=Mol. Cell. Biol. |volume=24 |issue= 19 |pages= 8556-66 |year= 2004 |pmid= 15367675 |doi= 10.1128/MCB.24.19.8556-8566.2004 }}
*{{cite journal  | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
*{{cite journal  | author=Wiemann S, Arlt D, Huber W, ''et al.'' |title=From ORFeome to biology: a functional genomics pipeline. |journal=Genome Res. |volume=14 |issue= 10B |pages= 2136-44 |year= 2004 |pmid= 15489336 |doi= 10.1101/gr.2576704 }}
*{{cite journal  | author=Cai Y, Jin J, Florens L, ''et al.'' |title=The mammalian YL1 protein is a shared subunit of the TRRAP/TIP60 histone acetyltransferase and SRCAP complexes. |journal=J. Biol. Chem. |volume=280 |issue= 14 |pages= 13665-70 |year= 2005 |pmid= 15647280 |doi= 10.1074/jbc.M500001200 }}
}}
{{refend}}
{{refend}}


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Latest revision as of 18:32, 30 August 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

DNA methyltransferase 1-associated protein 1 is an enzyme that in humans is encoded by the DMAP1 gene.[1][2][3]

Function

This gene encodes a subunit of several, distinct complexes involved in the repression or activation of transcription. The encoded protein can independently repress transcription and is targeted to replication foci throughout S phase by interacting directly with the N-terminus of DNA methyltransferase 1. During late S phase, histone deacetylase 2 is added to this complex, providing a means to deacetylate histones in transcriptionally inactive heterochromatin following replication. The encoded protein is also a component of the nucleosome acetyltransferase of H4 complex and interacts with the transcriptional corepressor tumor susceptibility gene 101 and the pro-apoptotic death-associated protein 6, among others. Alternatively spliced transcript variants encoding the same protein have been described.[3]

Interactions

DMAP1 has been shown to interact with:

References

  1. ↑ Rountree MR, Bachman KE, Baylin SB (Aug 2000). "DNMT1 binds HDAC2 and a new co-repressor, DMAP1, to form a complex at replication foci". Nat Genet. 25 (3): 269–77. doi:10.1038/77023. PMID 10888872.
  2. ↑ Nagase T, Kikuno R, Ishikawa KI, Hirosawa M, Ohara O (Apr 2000). "Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro". DNA Res. 7 (1): 65–73. doi:10.1093/dnares/7.1.65. PMID 10718198.
  3. ↑ 3.0 3.1 "Entrez Gene: DMAP1 DNA methyltransferase 1 associated protein 1".
  4. ↑ Delgermaa L, Hayashi N, Dorjsuren D, Nomura T, Thuy le TT, Murakami S (Oct 2004). "Subcellular localization of RPB5-mediating protein and its putative functional partner". Mol. Cell. Biol. 24 (19): 8556–66. doi:10.1128/MCB.24.19.8556-8566.2004. PMC 516735. PMID 15367675.
  5. ↑ Rountree MR, Bachman KE, Baylin SB (Jul 2000). "DNMT1 binds HDAC2 and a new co-repressor, DMAP1, to form a complex at replication foci". Nat. Genet. 25 (3): 269–77. doi:10.1038/77023. PMID 10888872.
  6. ↑ Xin H, Yoon HG, Singh PB, Wong J, Qin J (Mar 2004). "Components of a pathway maintaining histone modification and heterochromatin protein 1 binding at the pericentric heterochromatin in Mammalian cells". J. Biol. Chem. 279 (10): 9539–46. doi:10.1074/jbc.M311587200. PMID 14665632.
  7. ↑ Liu Z, Fisher RA (Apr 2004). "RGS6 interacts with DMAP1 and DNMT1 and inhibits DMAP1 transcriptional repressor activity". J. Biol. Chem. 279 (14): 14120–8. doi:10.1074/jbc.M309547200. PMID 14734556.

Further reading


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