MNAT1

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; OMA:MNAT1 - orthologs
Gene location (Human)
Chr.	Chromosome 14 (human)
End	60,969,965 bp
Gene location (Mouse)
Chr.	Chromosome 12 (mouse)
End	73,320,762 bp
RNA expression pattern
	Top expressed in
	Achilles tendon; ; gastrocnemius muscle; ; ganglionic eminence; ; popliteal artery; ; right uterine tube; ; sural nerve; ; ascending aorta; ; stromal cell of endometrium; ; left coronary artery; ; anterior pituitary;
	Top expressed in
	primitive streak; ; lens; ; yolk sac; ; abdominal wall; ; maxillary prominence; ; facial motor nucleus; ; seminal vesicula; ; plantaris muscle; ; otic placode; ; morula;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	ATP-dependent activity, acting on DNA; protein N-terminus binding; metal ion binding; protein binding; RNA polymerase II CTD heptapeptide repeat kinase activity; cyclin-dependent protein serine/threonine kinase activator activity; zinc ion binding;
Cellular component	nucleoplasm; nucleus; cytosol; transcription factor TFIIH holo 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 by RNA polymerase II; transcription initiation from RNA polymerase I promoter; transcription elongation from RNA polymerase II promoter; negative regulation of apoptotic process; 7-methylguanosine mRNA capping; transcription by RNA polymerase II; ventricular system development; transcription, DNA-templated; response to calcium ion; cell cycle; transcription-coupled nucleotide-excision repair; transcription initiation from RNA polymerase II promoter; cell population proliferation; DNA repair; positive regulation of transcription by RNA polymerase II; 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; protein-containing 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
	4331
	17420
	ENSG00000020426
	ENSMUSG00000021103
	P51948
	P51949
	NM_001177963; NM_002431
	NM_008612
	NP_001171434; NP_002422
	NP_032638
	Wikidata
View/Edit Human	View/Edit Mouse

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

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:

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000020426 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000021103 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ 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.
^ "Entrez Gene: MNAT1 menage a trois homolog 1, cyclin H assembly factor (Xenopus laevis)".
^ ^a ^b ^c ^d 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.
^ 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.
^ 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.
^ 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. S2CID 44625458.
^ 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.
^ 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.