MNAT1

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Menage a trois homolog 1, cyclin H assembly factor (Xenopus laevis)
Image:PBB Protein MNAT1 image.jpg
PDB rendering based on 1g25.
Available structures:
For the file format that describes the 3D structures of molecules found in the Protein Data Bank, see Protein Data Bank (file format).

The Protein Data Bank (PDB) is a repository for 3-D structural data of proteins and nucleic acids. These data, typically obtained by X-ray crystallography or NMR spectroscopy, are submitted by biologists and biochemists from around the world, are released into the public domain, and can be accessed for free.

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Contents

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Proteins Nucleic Acids Protein/NA complexes Other Total
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NMR 5665 781 134 7 6587
Electron microscopy 105 10 38 0 153
Other 80 4 4 2 90
Total 42073 1778 1860 33 45744

Note that theoretical models are no longer accepted in the PDB.

22461 structures in the PDB have a structure factor file. 3138 structures in the PDB have an NMR restraint file.

The current breakdown of holdings is updated weekly.

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References

Printed

  • H.M. Berman, K. Henrick, H. Nakamura (2003): Announcing the worldwide Protein Data Bank. Nature Structural Biology 10 (12), p. 980 PMID 14634627.
  • H.M. Berman, J. Westbrook, Z. Feng, G. Gilliland, T.N. Bhat, H. Weissig, I.N. Shindyalov, P.E. Bourne: The Protein Data Bank. Nucleic Acids Research, 28 pp. 235-242 (2000). PMID 10592235
  • Bernstein FC, Koetzle TF, Williams GJ, Meyer Jr EF, Brice MD, Rodgers JR, Kennard O, Shimanouchi T, Tasumi M. The Protein Data Bank: a computer-based archival file for macromolecular structures. J Mol Biol 1977;112:535-542. PMID 875032.
  • E.F. Meyer “The First Years of the Protein Data Bank“, Protein Science 6:1591-1597 (1997)
  • Sussman, JL, Lin, D, Jiang, J, Manning, NO, Prilusky, J, Ritter, O & Abola, EE. Protein data bank (PDB): a database of 3D structural information of biological macromolecules. Acta Cryst 1998; D54:1078-1084. PMID 10089483.

Online

Other external links

Links to enzyme database data

  • [1] The best mapping is provided by Kim Henrick's group at EBI as part of the MSD SIFTS initiative.
  • [2] PDB provide a mapping on their beta site, but it is at the whole PDB level not chain level.
  • [3] Search at BRENDA enzyme database portal.
  • [4] PDBSProtEC:

Molecular graphic visualisation tools

Identifiers
Symbol(s) MNAT1; MAT1; RNF66
External IDs OMIM: 602659 MGI: 106207 Homologene: 1821
RNA expression pattern

Image:PBB GE MNAT1 203565 s at tn.png

More reference expression data

Orthologs
Human Mouse
Entrez 4331 17420
Ensembl ENSG00000020426 ENSMUSG00000021103
Uniprot P51948 Q14BS9
Refseq NM_002431 (mRNA)
NP_002422 (protein) 		NM_008612 (mRNA)
NP_032638 (protein)
Location Chr 14: 60.27 - 60.51 Mb Chr 12: 74.04 - 74.19 Mb
Pubmed search [5] [6]

Menage a trois homolog 1, cyclin H assembly factor (Xenopus laevis), also known as MNAT1, is a human gene.


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][1]


References

Further reading

  • Jeang KT (1998). "Tat, Tat-associated kinase, and transcription.". J. Biomed. Sci. 5 (1): 24-7. PMID 9570510.
  • Yankulov K, Bentley D (1998). "Transcriptional control: Tat cofactors and transcriptional elongation.". Curr. Biol. 8 (13): R447-9. 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, et al. (1996). "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, et al. (1996). "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. PMID 8521818.
  • Blau J, Xiao H, McCracken S, et al. (1996). "Three functional classes of transcriptional activation domain.". Mol. Cell. Biol. 16 (5): 2044-55. PMID 8628270.
  • Reardon JT, Ge H, Gibbs E, et al. (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. PMID 8692841.
  • Drapkin R, Le Roy G, Cho H, et al. (1996). "Human cyclin-dependent kinase-activating kinase exists in three distinct complexes.". Proc. Natl. Acad. Sci. U.S.A. 93 (13): 6488-93. PMID 8692842.
  • Zhou Q, Sharp PA (1996). "Tat-SF1: cofactor for stimulation of transcriptional elongation by HIV-1 Tat.". Science 274 (5287): 605-10. 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. 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. PMID 9054383.
  • Marinoni JC, Roy R, Vermeulen W, et al. (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. PMID 9118947.
  • Cujec TP, Cho H, Maldonado E, et al. (1997). "The human immunodeficiency virus transactivator Tat interacts with the RNA polymerase II holoenzyme.". Mol. Cell. Biol. 17 (4): 1817-23. 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. PMID 9130708.
  • García-Martínez LF, Mavankal G, Neveu JM, et al. (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. 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. PMID 9311822.
  • Cujec TP, Okamoto H, Fujinaga K, et al. (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. PMID 9334327.
  • Inamoto S, Segil N, Pan ZQ, et al. (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. PMID 9368058.
  • Ko LJ, Shieh SY, Chen X, et al. (1997). "p53 is phosphorylated by CDK7-cyclin H in a p36MAT1-dependent manner.". Mol. Cell. Biol. 17 (12): 7220-9. PMID 9372954.
  • Eki T, Okumura K, Abe M, et al. (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.
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