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<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{Infobox_gene}}
{{PBB_Controls
'''CDK-activating kinase assembly factor MAT1''' is an [[enzyme]] that in humans is encoded by the ''MNAT1'' [[gene]].<ref name="pmid9465303">{{cite journal | vauthors = Eki T, Okumura K, Abe M, Kagotani K, Taguchi H, Murakami Y, Pan ZQ, Hanaoka F | title = Mapping of the human genes encoding cyclin H (CCNH) and the CDK-activating kinase (CAK) assembly factor MAT1 (MNAT1) to chromosome bands 5q13.3-q14 and 14q23, respectively | journal = Genomics | volume = 47 | issue = 1 | pages = 115–20  | date = April 1998 | pmid = 9465303 | pmc = | doi = 10.1006/geno.1997.5053 }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| 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 = PBB_Protein_MNAT1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1g25.
| PDB = {{PDB2|1g25}}
| Name = Menage a trois homolog 1, cyclin H assembly factor (Xenopus laevis)
| HGNCid = 7181
| Symbol = MNAT1
| AltSymbols =; MAT1; RNF66
| OMIM = 602659
| ECnumber = 
| Homologene = 1821
| MGIid = 106207
| GeneAtlas_image1 = PBB_GE_MNAT1_203565_s_at_tn.png
| Function = {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0000079 |text = regulation of cyclin-dependent protein kinase activity}} {{GNF_GO|id=GO:0006281 |text = DNA repair}} {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0006357 |text = regulation of transcription from RNA polymerase II promoter}} {{GNF_GO|id=GO:0006461 |text = protein complex assembly}} {{GNF_GO|id=GO:0007049 |text = cell cycle}} {{GNF_GO|id=GO:0008283 |text = cell proliferation}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 4331
    | Hs_Ensembl = ENSG00000020426
    | Hs_RefseqProtein = NP_002422
    | Hs_RefseqmRNA = NM_002431
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 14
    | Hs_GenLoc_start = 60271223
    | Hs_GenLoc_end = 60505149
    | Hs_Uniprot = P51948
    | Mm_EntrezGene = 17420
    | Mm_Ensembl = ENSMUSG00000021103
    | Mm_RefseqmRNA = NM_008612
    | Mm_RefseqProtein = NP_032638
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 12
    | Mm_GenLoc_start = 74042554
    | Mm_GenLoc_end = 74191689
    | Mm_Uniprot = Q14BS9
  }}
}}
'''Menage a trois homolog 1, cyclin H assembly factor (Xenopus laevis)''', also known as '''MNAT1''', is a human [[gene]].


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
[[Cyclin-dependent kinase | Cyclin-dependent kinases (CDKs)]], which play an essential role in cell cycle control of eukaryotic cells, are phosphorylated and thus activated by the CDK-activating kinase (CAK). CAK is a multisubunit protein that includes CDK7 (MIM 601955), cyclin H (CCNH; MIM 601953), and MAT1. MAT1 (for 'ménage à trois-1') is involved in the assembly of the CAK complex.[supplied by OMIM]<ref name="entrez">{{cite web | title = Entrez Gene: MNAT1 menage a trois homolog 1, cyclin H assembly factor (Xenopus laevis)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4331| accessdate = }}</ref>
{{PBB_Summary
| section_title =
| summary_text = Cyclin-dependent kinases (CDKs), which play an essential role in cell cycle control of eukaryotic cells, are phosphorylated and thus activated by the CDK-activating kinase (CAK). CAK is a multisubunit protein that includes CDK7 (MIM 601955), cyclin H (CCNH; MIM 601953), and MAT1. MAT1 (for 'menage a trois-1') is involved in the assembly of the CAK complex.[supplied by OMIM]<ref name="entrez">{{cite web | title = Entrez Gene: MNAT1 menage a trois homolog 1, cyclin H assembly factor (Xenopus laevis)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4331| accessdate = }}</ref>
}}


==References==
== Interactions ==
{{reflist|2}}
 
==Further reading==
MNAT1 has been shown to [[Protein-protein interaction|interact]] with:
{{div col|colwidth=20em}}
* [[Cyclin H]],<ref name = pmid12527756/><ref name = pmid17353931>{{cite journal | vauthors = Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S, McBroom-Cerajewski L, Robinson MD, O'Connor L, Li M, Taylor R, Dharsee M, Ho Y, Heilbut A, Moore L, Zhang S, Ornatsky O, Bukhman YV, Ethier M, Sheng Y, Vasilescu J, Abu-Farha M, Lambert JP, Duewel HS, Stewart II, Kuehl B, Hogue K, Colwill K, Gladwish K, Muskat B, Kinach R, Adams SL, Moran MF, Morin GB, Topaloglou T, Figeys D | title = Large-scale mapping of human protein-protein interactions by mass spectrometry | journal = Mol. Syst. Biol. | volume = 3 | issue =  | pages = 89 | year = 2007 | pmid = 17353931 | pmc = 1847948 | doi = 10.1038/msb4100134 }}</ref>
* [[Cyclin-dependent kinase 7]],<ref name = pmid12527756/><ref name = pmid8521393>{{cite journal | vauthors = Yee A, Nichols MA, Wu L, Hall FL, Kobayashi R, Xiong Y | title = Molecular cloning of CDK7-associated human MAT1, a cyclin-dependent kinase-activating kinase (CAK) assembly factor | journal = Cancer Res. | volume = 55 | issue = 24 | pages = 6058–62  | date = December 1995 | pmid = 8521393 | doi =  }}</ref>
* [[Estrogen receptor alpha]],<ref name = pmid12527756/>
* [[MCM7]],<ref name = pmid11056214>{{cite journal | vauthors = Wang Y, Xu F, Hall FL | title = The MAT1 cyclin-dependent kinase-activating kinase (CAK) assembly/targeting factor interacts physically with the MCM7 DNA licensing factor | journal = FEBS Lett. | volume = 484 | issue = 1 | pages = 17–21  | date = October 2000 | pmid = 11056214 | doi =  10.1016/s0014-5793(00)02117-7}}</ref>
* [[MTA1]],<ref name = pmid12527756>{{cite journal | vauthors = Talukder AH, Mishra SK, Mandal M, Balasenthil S, Mehta S, Sahin AA, Barnes CJ, Kumar R | title = MTA1 interacts with MAT1, a cyclin-dependent kinase-activating kinase complex ring finger factor, and regulates estrogen receptor transactivation functions | journal = J. Biol. Chem. | volume = 278 | issue = 13 | pages = 11676–85  | date = March 2003 | pmid = 12527756 | doi = 10.1074/jbc.M209570200 }}</ref>
* [[P53]],<ref name = pmid9372954>{{cite journal | vauthors = Ko LJ, Shieh SY, Chen X, Jayaraman L, Tamai K, Taya Y, Prives C, Pan ZQ | title = p53 is phosphorylated by CDK7-cyclin H in a p36MAT1-dependent manner | journal = Mol. Cell. Biol. | volume = 17 | issue = 12 | pages = 7220–9  | date = December 1997 | pmid = 9372954 | pmc = 232579 | doi =  10.1128/mcb.17.12.7220}}</ref>  and
* [[POU2F1]].<ref name = pmid9368058>{{cite journal | vauthors = Inamoto S, Segil N, Pan ZQ, Kimura M, Roeder RG | title = The cyclin-dependent kinase-activating kinase (CAK) assembly factor, MAT1, targets and enhances CAK activity on the POU domains of octamer transcription factors | journal = J. Biol. Chem. | volume = 272 | issue = 47 | pages = 29852–8  | date = November 1997 | pmid = 9368058 | doi =  10.1074/jbc.272.47.29852}}</ref>
{{Div col end}}
 
== References ==
{{reflist}}
{{Clear}}
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Jeang KT | title = Tat, Tat-associated kinase, and transcription | journal = J. Biomed. Sci. | volume = 5 | issue = 1 | pages = 24–7 | year = 1998 | pmid = 9570510 | doi = 10.1007/BF02253352 }}
| citations =
* {{cite journal | vauthors = Yankulov K, Bentley D | title = Transcriptional control: Tat cofactors and transcriptional elongation | journal = Curr. Biol. | volume = 8 | issue = 13 | pages = R447-9 | year = 1998 | pmid = 9651670 | doi = 10.1016/S0960-9822(98)70289-1 }}
*{{cite journal | author=Jeang KT |title=Tat, Tat-associated kinase, and transcription. |journal=J. Biomed. Sci. |volume=5 |issue= 1 |pages= 24-7 |year= 1998 |pmid= 9570510 |doi= }}
* {{cite journal | vauthors = Le Goff P, Montano MM, Schodin DJ, Katzenellenbogen BS | title = Phosphorylation of the human estrogen receptor. Identification of hormone-regulated sites and examination of their influence on transcriptional activity | journal = J. Biol. Chem. | volume = 269 | issue = 6 | pages = 4458–66 | year = 1994 | pmid = 8308015 | doi =  }}
*{{cite journal | author=Yankulov K, Bentley D |title=Transcriptional control: Tat cofactors and transcriptional elongation. |journal=Curr. Biol. |volume=8 |issue= 13 |pages= R447-9 |year= 1998 |pmid= 9651670 |doi= }}
* {{cite journal | vauthors = Yee A, Nichols MA, Wu L, Hall FL, Kobayashi R, Xiong Y | title = Molecular cloning of CDK7-associated human MAT1, a cyclin-dependent kinase-activating kinase (CAK) assembly factor | journal = Cancer Res. | volume = 55 | issue = 24 | pages = 6058–62 | year = 1995 | pmid = 8521393 | doi =  }}
*{{cite journal | author=Le Goff P, Montano MM, Schodin DJ, Katzenellenbogen BS |title=Phosphorylation of the human estrogen receptor. Identification of hormone-regulated sites and examination of their influence on transcriptional activity. |journal=J. Biol. Chem. |volume=269 |issue= 6 |pages= 4458-66 |year= 1994 |pmid= 8308015 |doi=  }}
* {{cite journal | vauthors = Tassan JP, Jaquenoud M, Fry AM, Frutiger S, Hughes GJ, Nigg EA | title = In vitro assembly of a functional human CDK7-cyclin H complex requires MAT1, a novel 36 kDa RING finger protein | journal = EMBO J. | volume = 14 | issue = 22 | pages = 5608–17 | year = 1995 | pmid = 8521818 | pmc = 394676 | doi =  }}
*{{cite journal | author=Yee A, Nichols MA, Wu L, ''et al.'' |title=Molecular cloning of CDK7-associated human MAT1, a cyclin-dependent kinase-activating kinase (CAK) assembly factor. |journal=Cancer Res. |volume=55 |issue= 24 |pages= 6058-62 |year= 1996 |pmid= 8521393 |doi=  }}
* {{cite journal | vauthors = Blau J, Xiao H, McCracken S, O'Hare P, Greenblatt J, Bentley D | title = Three functional classes of transcriptional activation domain | journal = Mol. Cell. Biol. | volume = 16 | issue = 5 | pages = 2044–55 | year = 1996 | pmid = 8628270 | pmc = 231191 | doi =  }}
*{{cite journal | author=Tassan JP, Jaquenoud M, Fry AM, ''et al.'' |title=In vitro assembly of a functional human CDK7-cyclin H complex requires MAT1, a novel 36 kDa RING finger protein. |journal=EMBO J. |volume=14 |issue= 22 |pages= 5608-17 |year= 1996 |pmid= 8521818 |doi=  }}
* {{cite journal | vauthors = Reardon JT, Ge H, Gibbs E, Sancar A, Hurwitz J, Pan ZQ | title = Isolation and characterization of two human transcription factor IIH (TFIIH)-related complexes: ERCC2/CAK and TFIIH | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 93 | issue = 13 | pages = 6482–7 | year = 1996 | pmid = 8692841 | pmc = 39049 | doi = 10.1073/pnas.93.13.6482 }}
*{{cite journal | author=Blau J, Xiao H, McCracken S, ''et al.'' |title=Three functional classes of transcriptional activation domain. |journal=Mol. Cell. Biol. |volume=16 |issue= 5 |pages= 2044-55 |year= 1996 |pmid= 8628270 |doi=  }}
* {{cite journal | vauthors = Drapkin R, Le Roy G, Cho H, Akoulitchev S, Reinberg D | title = Human cyclin-dependent kinase-activating kinase exists in three distinct complexes | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 93 | issue = 13 | pages = 6488–93 | year = 1996 | pmid = 8692842 | pmc = 39050 | doi = 10.1073/pnas.93.13.6488 }}
*{{cite journal | author=Reardon JT, Ge H, Gibbs E, ''et al.'' |title=Isolation and characterization of two human transcription factor IIH (TFIIH)-related complexes: ERCC2/CAK and TFIIH. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 13 |pages= 6482-7 |year= 1996 |pmid= 8692841 |doi= }}
* {{cite journal | vauthors = Zhou Q, Sharp PA | title = Tat-SF1: cofactor for stimulation of transcriptional elongation by HIV-1 Tat | journal = Science | volume = 274 | issue = 5287 | pages = 605–10 | year = 1996 | pmid = 8849451 | doi = 10.1126/science.274.5287.605 }}
*{{cite journal | author=Drapkin R, Le Roy G, Cho H, ''et al.'' |title=Human cyclin-dependent kinase-activating kinase exists in three distinct complexes. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 13 |pages= 6488-93 |year= 1996 |pmid= 8692842 |doi= }}
* {{cite journal | vauthors = Parada CA, Roeder RG | title = Enhanced processivity of RNA polymerase II triggered by Tat-induced phosphorylation of its carboxy-terminal domain | journal = Nature | volume = 384 | issue = 6607 | pages = 375–8 | year = 1996 | pmid = 8934526 | doi = 10.1038/384375a0 }}
*{{cite journal | author=Zhou Q, Sharp PA |title=Tat-SF1: cofactor for stimulation of transcriptional elongation by HIV-1 Tat. |journal=Science |volume=274 |issue= 5287 |pages= 605-10 |year= 1996 |pmid= 8849451 |doi= }}
* {{cite journal | vauthors = García-Martínez LF, Ivanov D, Gaynor RB | title = Association of Tat with purified HIV-1 and HIV-2 transcription preinitiation complexes | journal = J. Biol. Chem. | volume = 272 | issue = 11 | pages = 6951–8 | year = 1997 | pmid = 9054383 | doi = 10.1074/jbc.272.11.6951 }}
*{{cite journal | author=Parada CA, Roeder RG |title=Enhanced processivity of RNA polymerase II triggered by Tat-induced phosphorylation of its carboxy-terminal domain. |journal=Nature |volume=384 |issue= 6607 |pages= 375-8 |year= 1996 |pmid= 8934526 |doi= 10.1038/384375a0 }}
* {{cite journal | vauthors = Marinoni JC, Roy R, Vermeulen W, Miniou P, Lutz Y, Weeda G, Seroz T, Gomez DM, Hoeijmakers JH, Egly JM | title = Cloning and characterization of p52, the fifth subunit of the core of the transcription/DNA repair factor TFIIH | journal = EMBO J. | volume = 16 | issue = 5 | pages = 1093–102 | year = 1997 | pmid = 9118947 | pmc = 1169708 | doi = 10.1093/emboj/16.5.1093 }}
*{{cite journal | author=García-Martínez LF, Ivanov D, Gaynor RB |title=Association of Tat with purified HIV-1 and HIV-2 transcription preinitiation complexes. |journal=J. Biol. Chem. |volume=272 |issue= 11 |pages= 6951-8 |year= 1997 |pmid= 9054383 |doi= }}
* {{cite journal | vauthors = Cujec TP, Cho H, Maldonado E, Meyer J, Reinberg D, Peterlin BM | title = The human immunodeficiency virus transactivator Tat interacts with the RNA polymerase II holoenzyme | journal = Mol. Cell. Biol. | volume = 17 | issue = 4 | pages = 1817–23 | year = 1997 | pmid = 9121429 | pmc = 232028 | doi =  }}
*{{cite journal | author=Marinoni JC, Roy R, Vermeulen W, ''et al.'' |title=Cloning and characterization of p52, the fifth subunit of the core of the transcription/DNA repair factor TFIIH. |journal=EMBO J. |volume=16 |issue= 5 |pages= 1093-102 |year= 1997 |pmid= 9118947 |doi= 10.1093/emboj/16.5.1093 }}
* {{cite journal | vauthors = Rossignol M, Kolb-Cheynel I, Egly JM | title = Substrate specificity of the cdk-activating kinase (CAK) is altered upon association with TFIIH | journal = EMBO J. | volume = 16 | issue = 7 | pages = 1628–37 | year = 1997 | pmid = 9130708 | pmc = 1169767 | doi = 10.1093/emboj/16.7.1628 }}
*{{cite journal | author=Cujec TP, Cho H, Maldonado E, ''et al.'' |title=The human immunodeficiency virus transactivator Tat interacts with the RNA polymerase II holoenzyme. |journal=Mol. Cell. Biol. |volume=17 |issue= 4 |pages= 1817-23 |year= 1997 |pmid= 9121429 |doi=  }}
* {{cite journal | vauthors = García-Martínez LF, Mavankal G, Neveu JM, Lane WS, Ivanov D, Gaynor RB | title = Purification of a Tat-associated kinase reveals a TFIIH complex that modulates HIV-1 transcription | journal = EMBO J. | volume = 16 | issue = 10 | pages = 2836–50 | year = 1997 | pmid = 9184228 | pmc = 1169892 | doi = 10.1093/emboj/16.10.2836 }}
*{{cite journal | author=Rossignol M, Kolb-Cheynel I, Egly JM |title=Substrate specificity of the cdk-activating kinase (CAK) is altered upon association with TFIIH. |journal=EMBO J. |volume=16 |issue= 7 |pages= 1628-37 |year= 1997 |pmid= 9130708 |doi= 10.1093/emboj/16.7.1628 }}
* {{cite journal | vauthors = Nekhai S, Shukla RR, Kumar A | title = A human primary T-lymphocyte-derived human immunodeficiency virus type 1 Tat-associated kinase phosphorylates the C-terminal domain of RNA polymerase II and induces CAK activity | journal = J. Virol. | volume = 71 | issue = 10 | pages = 7436–41 | year = 1997 | pmid = 9311822 | pmc = 192089 | doi =  }}
*{{cite journal | author=García-Martínez LF, Mavankal G, Neveu JM, ''et al.'' |title=Purification of a Tat-associated kinase reveals a TFIIH complex that modulates HIV-1 transcription. |journal=EMBO J. |volume=16 |issue= 10 |pages= 2836-50 |year= 1997 |pmid= 9184228 |doi= 10.1093/emboj/16.10.2836 }}
* {{cite journal | vauthors = Cujec TP, Okamoto H, Fujinaga K, Meyer J, Chamberlin H, Morgan DO, Peterlin BM | title = The HIV transactivator TAT binds to the CDK-activating kinase and activates the phosphorylation of the carboxy-terminal domain of RNA polymerase II | journal = Genes Dev. | volume = 11 | issue = 20 | pages = 2645–57 | year = 1997 | pmid = 9334327 | pmc = 316603 | doi = 10.1101/gad.11.20.2645 }}
*{{cite journal | author=Nekhai S, Shukla RR, Kumar A |title=A human primary T-lymphocyte-derived human immunodeficiency virus type 1 Tat-associated kinase phosphorylates the C-terminal domain of RNA polymerase II and induces CAK activity. |journal=J. Virol. |volume=71 |issue= 10 |pages= 7436-41 |year= 1997 |pmid= 9311822 |doi=  }}
* {{cite journal | vauthors = Inamoto S, Segil N, Pan ZQ, Kimura M, Roeder RG | title = The cyclin-dependent kinase-activating kinase (CAK) assembly factor, MAT1, targets and enhances CAK activity on the POU domains of octamer transcription factors | journal = J. Biol. Chem. | volume = 272 | issue = 47 | pages = 29852–8 | year = 1997 | pmid = 9368058 | doi = 10.1074/jbc.272.47.29852 }}
*{{cite journal | author=Cujec TP, Okamoto H, Fujinaga K, ''et al.'' |title=The HIV transactivator TAT binds to the CDK-activating kinase and activates the phosphorylation of the carboxy-terminal domain of RNA polymerase II. |journal=Genes Dev. |volume=11 |issue= 20 |pages= 2645-57 |year= 1997 |pmid= 9334327 |doi= }}
* {{cite journal | vauthors = Ko LJ, Shieh SY, Chen X, Jayaraman L, Tamai K, Taya Y, Prives C, Pan ZQ | title = p53 is phosphorylated by CDK7-cyclin H in a p36MAT1-dependent manner | journal = Mol. Cell. Biol. | volume = 17 | issue = 12 | pages = 7220–9 | year = 1997 | pmid = 9372954 | pmc = 232579 | doi = 10.1128/mcb.17.12.7220}}
*{{cite journal | author=Inamoto S, Segil N, Pan ZQ, ''et al.'' |title=The cyclin-dependent kinase-activating kinase (CAK) assembly factor, MAT1, targets and enhances CAK activity on the POU domains of octamer transcription factors. |journal=J. Biol. Chem. |volume=272 |issue= 47 |pages= 29852-8 |year= 1997 |pmid= 9368058 |doi= }}
*{{cite journal | author=Ko LJ, Shieh SY, Chen X, ''et al.'' |title=p53 is phosphorylated by CDK7-cyclin H in a p36MAT1-dependent manner. |journal=Mol. Cell. Biol. |volume=17 |issue= 12 |pages= 7220-9 |year= 1997 |pmid= 9372954 |doi= }}
*{{cite journal  | author=Eki T, Okumura K, Abe M, ''et al.'' |title=Mapping of the human genes encoding cyclin H (CCNH) and the CDK-activating kinase (CAK) assembly factor MAT1 (MNAT1) to chromosome bands 5q13.3-q14 and 14q23, respectively. |journal=Genomics |volume=47 |issue= 1 |pages= 115-20 |year= 1998 |pmid= 9465303 |doi= 10.1006/geno.1997.5053 }}
}}
{{refend}}
{{refend}}


{{protein-stub}}
{{PDB Gallery|geneid=4331}}
{{WikiDoc Sources}}

Latest revision as of 06:42, 4 September 2017

VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

n/a

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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

CDK-activating kinase assembly factor MAT1 is an enzyme that in humans is encoded by the MNAT1 gene.[1]

Function

Cyclin-dependent kinases (CDKs), which play an essential role in cell cycle control of eukaryotic cells, are phosphorylated and thus activated by the CDK-activating kinase (CAK). CAK is a multisubunit protein that includes CDK7 (MIM 601955), cyclin H (CCNH; MIM 601953), and MAT1. MAT1 (for 'ménage à trois-1') is involved in the assembly of the CAK complex.[supplied by OMIM][2]

Interactions

MNAT1 has been shown to interact with:

References

  1. ↑ Eki T, Okumura K, Abe M, Kagotani K, Taguchi H, Murakami Y, Pan ZQ, Hanaoka F (April 1998). "Mapping of the human genes encoding cyclin H (CCNH) and the CDK-activating kinase (CAK) assembly factor MAT1 (MNAT1) to chromosome bands 5q13.3-q14 and 14q23, respectively". Genomics. 47 (1): 115–20. doi:10.1006/geno.1997.5053. PMID 9465303.
  2. ↑ "Entrez Gene: MNAT1 menage a trois homolog 1, cyclin H assembly factor (Xenopus laevis)".
  3. ↑ 3.0 3.1 3.2 3.3 Talukder AH, Mishra SK, Mandal M, Balasenthil S, Mehta S, Sahin AA, Barnes CJ, Kumar R (March 2003). "MTA1 interacts with MAT1, a cyclin-dependent kinase-activating kinase complex ring finger factor, and regulates estrogen receptor transactivation functions". J. Biol. Chem. 278 (13): 11676–85. doi:10.1074/jbc.M209570200. PMID 12527756.
  4. ↑ Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S, McBroom-Cerajewski L, Robinson MD, O'Connor L, Li M, Taylor R, Dharsee M, Ho Y, Heilbut A, Moore L, Zhang S, Ornatsky O, Bukhman YV, Ethier M, Sheng Y, Vasilescu J, Abu-Farha M, Lambert JP, Duewel HS, Stewart II, Kuehl B, Hogue K, Colwill K, Gladwish K, Muskat B, Kinach R, Adams SL, Moran MF, Morin GB, Topaloglou T, Figeys D (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Mol. Syst. Biol. 3: 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.
  5. ↑ Yee A, Nichols MA, Wu L, Hall FL, Kobayashi R, Xiong Y (December 1995). "Molecular cloning of CDK7-associated human MAT1, a cyclin-dependent kinase-activating kinase (CAK) assembly factor". Cancer Res. 55 (24): 6058–62. PMID 8521393.
  6. ↑ Wang Y, Xu F, Hall FL (October 2000). "The MAT1 cyclin-dependent kinase-activating kinase (CAK) assembly/targeting factor interacts physically with the MCM7 DNA licensing factor". FEBS Lett. 484 (1): 17–21. doi:10.1016/s0014-5793(00)02117-7. PMID 11056214.
  7. ↑ Ko LJ, Shieh SY, Chen X, Jayaraman L, Tamai K, Taya Y, Prives C, Pan ZQ (December 1997). "p53 is phosphorylated by CDK7-cyclin H in a p36MAT1-dependent manner". Mol. Cell. Biol. 17 (12): 7220–9. doi:10.1128/mcb.17.12.7220. PMC 232579. PMID 9372954.
  8. ↑ Inamoto S, Segil N, Pan ZQ, Kimura M, Roeder RG (November 1997). "The cyclin-dependent kinase-activating kinase (CAK) assembly factor, MAT1, targets and enhances CAK activity on the POU domains of octamer transcription factors". J. Biol. Chem. 272 (47): 29852–8. doi:10.1074/jbc.272.47.29852. PMID 9368058.

Further reading

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