MNAT1

CDK-activating kinase assembly factor MAT1 is an enzyme that in humans is encoded by the MNAT1 gene.[5]

MNAT1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1G25
Identifiers
Aliases	MNAT1, CAP35, MAT1, RNF66, TFB3, CDK activating kinase assembly factor, MNAT1 component of CDK activating kinase
External IDs	OMIM: 602659 MGI: 106207 HomoloGene: 1821 GeneCards: MNAT1
Gene location (Human) Chr. Chromosome 14 (human)[1] Band 14q23.1 Start 60,734,742 bp[1] End 60,969,965 bp[1]
Gene location (Mouse) Chr. Chromosome 12 (mouse)[2] Band 12|12 C3 Start 73,123,717 bp[2] End 73,273,988 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • DNA-dependent ATPase activity • protein N-terminus binding • metal ion binding • GO:0001948 protein binding • RNA polymerase II carboxy-terminal domain kinase activity • GO:0016534 cyclin-dependent protein serine/threonine kinase activator activity • zinc ion binding Cellular component • nucleoplasm • cell nucleus • cytosol • holo TFIIH complex • cyclin-dependent protein kinase activating kinase holoenzyme complex Biological process • termination of RNA polymerase I transcription • regulation of cyclin-dependent protein serine/threonine kinase activity • regulation of transcription, DNA-templated • adult heart development • regulation of transcription from RNA polymerase II promoter • transcription initiation from RNA polymerase I promoter • transcription elongation from RNA polymerase II promoter • negative regulation of apoptotic process • 7-methylguanosine mRNA capping • transcription from RNA polymerase II promoter • ventricular system development • transcription, DNA-templated • response to calcium ion • cell cycle • transcription-coupled nucleotide-excision repair • transcription initiation from RNA polymerase II promoter • cellular proliferation • DNA repair • positive regulation of transcription from RNA polymerase II promoter • positive regulation of smooth muscle cell proliferation • protein phosphorylation • nucleotide-excision repair, preincision complex assembly • positive regulation of cyclin-dependent protein serine/threonine kinase activity • nucleotide-excision repair • macromolecular complex assembly • G1/S transition of mitotic cell cycle • negative regulation of DNA helicase activity • G2/M transition of mitotic cell cycle • transcription elongation from RNA polymerase I promoter Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	4331	17420
Ensembl	ENSG00000020426	ENSMUSG00000021103
UniProt	P51948	P51949
RefSeq (mRNA)	NM_001177963 NM_002431	NM_008612
RefSeq (protein)	NP_001171434 NP_002422	NP_032638
Location (UCSC)	Chr 14: 60.73 – 60.97 Mb	Chr 12: 73.12 – 73.27 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

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][6]

Interactions

MNAT1 has been shown to interact with:

• Cyclin H,[7][8]
• Cyclin-dependent kinase 7,[7][9]
• Estrogen receptor alpha,[7]
• MCM7,[10]
• MTA1,[7]
• P53,[11] and
• POU2F1.[12]

References

1. GRCh38: Ensembl release 89: ENSG00000020426 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000021103 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. 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.
6. "Entrez Gene: MNAT1 menage a trois homolog 1, cyclin H assembly factor (Xenopus laevis)".
7. 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.
8. 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.
9. 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.
10. 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.
11. 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.
12. 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

• Jeang KT (1998). "Tat, Tat-associated kinase, and transcription". J. Biomed. Sci. 5 (1): 24–7. doi:10.1007/BF02253352. PMID 9570510.
• Yankulov K, Bentley D (1998). "Transcriptional control: Tat cofactors and transcriptional elongation". Curr. Biol. 8 (13): R447-9. doi:10.1016/S0960-9822(98)70289-1. PMID 9651670.
• Le Goff P, Montano MM, Schodin DJ, Katzenellenbogen BS (1994). "Phosphorylation of the human estrogen receptor. Identification of hormone-regulated sites and examination of their influence on transcriptional activity". J. Biol. Chem. 269 (6): 4458–66. PMID 8308015.
• Yee A, Nichols MA, Wu L, Hall FL, Kobayashi R, Xiong Y (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.
• Tassan JP, Jaquenoud M, Fry AM, Frutiger S, Hughes GJ, Nigg EA (1995). "In vitro assembly of a functional human CDK7-cyclin H complex requires MAT1, a novel 36 kDa RING finger protein". EMBO J. 14 (22): 5608–17. doi:10.1002/j.1460-2075.1995.tb00248.x. PMC 394676. PMID 8521818.
• Blau J, Xiao H, McCracken S, O'Hare P, Greenblatt J, Bentley D (1996). "Three functional classes of transcriptional activation domain". Mol. Cell. Biol. 16 (5): 2044–55. doi:10.1128/MCB.16.5.2044. PMC 231191. PMID 8628270.
• Reardon JT, Ge H, Gibbs E, Sancar A, Hurwitz J, Pan ZQ (1996). "Isolation and characterization of two human transcription factor IIH (TFIIH)-related complexes: ERCC2/CAK and TFIIH". Proc. Natl. Acad. Sci. U.S.A. 93 (13): 6482–7. doi:10.1073/pnas.93.13.6482. PMC 39049. PMID 8692841.
• Drapkin R, Le Roy G, Cho H, Akoulitchev S, Reinberg D (1996). "Human cyclin-dependent kinase-activating kinase exists in three distinct complexes". Proc. Natl. Acad. Sci. U.S.A. 93 (13): 6488–93. doi:10.1073/pnas.93.13.6488. PMC 39050. PMID 8692842.
• Zhou Q, Sharp PA (1996). "Tat-SF1: cofactor for stimulation of transcriptional elongation by HIV-1 Tat". Science. 274 (5287): 605–10. Bibcode:1996Sci...274..605Z. doi:10.1126/science.274.5287.605. PMID 8849451.
• Parada CA, Roeder RG (1996). "Enhanced processivity of RNA polymerase II triggered by Tat-induced phosphorylation of its carboxy-terminal domain". Nature. 384 (6607): 375–8. Bibcode:1996Natur.384..375P. doi:10.1038/384375a0. PMID 8934526.
• García-Martínez LF, Ivanov D, Gaynor RB (1997). "Association of Tat with purified HIV-1 and HIV-2 transcription preinitiation complexes". J. Biol. Chem. 272 (11): 6951–8. doi:10.1074/jbc.272.11.6951. PMID 9054383.
• Marinoni JC, Roy R, Vermeulen W, Miniou P, Lutz Y, Weeda G, Seroz T, Gomez DM, Hoeijmakers JH, Egly JM (1997). "Cloning and characterization of p52, the fifth subunit of the core of the transcription/DNA repair factor TFIIH". EMBO J. 16 (5): 1093–102. doi:10.1093/emboj/16.5.1093. PMC 1169708. PMID 9118947.
• Cujec TP, Cho H, Maldonado E, Meyer J, Reinberg D, Peterlin BM (1997). "The human immunodeficiency virus transactivator Tat interacts with the RNA polymerase II holoenzyme". Mol. Cell. Biol. 17 (4): 1817–23. doi:10.1128/mcb.17.4.1817. PMC 232028. PMID 9121429.
• Rossignol M, Kolb-Cheynel I, Egly JM (1997). "Substrate specificity of the cdk-activating kinase (CAK) is altered upon association with TFIIH". EMBO J. 16 (7): 1628–37. doi:10.1093/emboj/16.7.1628. PMC 1169767. PMID 9130708.
• García-Martínez LF, Mavankal G, Neveu JM, Lane WS, Ivanov D, Gaynor RB (1997). "Purification of a Tat-associated kinase reveals a TFIIH complex that modulates HIV-1 transcription". EMBO J. 16 (10): 2836–50. doi:10.1093/emboj/16.10.2836. PMC 1169892. PMID 9184228.
• Nekhai S, Shukla RR, Kumar A (1997). "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". J. Virol. 71 (10): 7436–41. doi:10.1128/JVI.71.10.7436-7441.1997. PMC 192089. PMID 9311822.
• Cujec TP, Okamoto H, Fujinaga K, Meyer J, Chamberlin H, Morgan DO, Peterlin BM (1997). "The HIV transactivator TAT binds to the CDK-activating kinase and activates the phosphorylation of the carboxy-terminal domain of RNA polymerase II". Genes Dev. 11 (20): 2645–57. doi:10.1101/gad.11.20.2645. PMC 316603. PMID 9334327.
• Inamoto S, Segil N, Pan ZQ, Kimura M, Roeder RG (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.
• Ko LJ, Shieh SY, Chen X, Jayaraman L, Tamai K, Taya Y, Prives C, Pan ZQ (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.

External links

• Overview of all the structural information available in the PDB for UniProt: P51948 (CDK-activating kinase assembly factor MAT1) at the PDBe-KB.