Metallothionein 2A

MT2A

Available structures

Human UniProt search: PDBe RCSB

List of PDB id codes
1MHU, 2MHU

Identifiers

MT2A, MT2, Metallothionein 2A

External IDs

HomoloGene: 136536 GeneCards: MT2A

Gene ontology
Molecular function	• zinc ion binding • protein binding • drug binding • metal ion binding
Cellular component	• cytoplasm • perinuclear region of cytoplasm • cytosol • nucleus
Biological process	• response to metal ion • cellular response to drug • cellular response to interleukin-3 • cellular response to erythropoietin • negative regulation of growth • cellular response to zinc ion • interferon-gamma-mediated signaling pathway • cellular copper ion homeostasis
Sources:Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse


4502


n/a


ENSG00000125148


n/a


P02795


n/a

RefSeq (mRNA)


NM_005953


n/a

RefSeq (protein)


NP_005944.1


n/a

Location (UCSC)

Chr 16: 56.61 – 56.61 Mb

n/a

PubMed search

^[1]

n/a

View/Edit Human

Metallothionein-2 is a protein that in humans is encoded by the MT2A gene.^[2]^[3]

Interactions

Metallothionein 2A has been shown to interact with Protein kinase D1.^[4]

References

↑ "Human PubMed Reference:".
↑ Karin M, Richards RI (Dec 1982). "Human metallothionein genes--primary structure of the metallothionein-II gene and a related processed gene". Nature. 299 (5886): 797–802. doi:10.1038/299797a0. PMID 7133118.
↑ "Entrez Gene: MT2A metallothionein 2A".
↑ Rao, Prema S; Jaggi Meena; Smith David J; Hemstreet George P; Balaji K C (Oct 2003). "Metallothionein 2A interacts with the kinase domain of PKCmu in prostate cancer". Biochem. Biophys. Res. Commun. United States. 310 (3): 1032–8. doi:10.1016/j.bbrc.2003.09.118. ISSN 0006-291X. PMID 14550308.

Further reading

Kissling MM, Kägi HR (1977). "Primary structure of human hepatic metallothionein.". FEBS Lett. 82 (2): 247–50. doi:10.1016/0014-5793(77)80594-2. PMID 913597.
Yamazaki S, Nakanishi M, Hamamoto T, et al. (1993). "Expression of human metallothionein-II fusion protein in Escherichia coli.". Biochem. Int. 28 (3): 451–60. PMID 1339282.
Messerle BA, Schäffer A, Vasák M, et al. (1992). "Comparison of the solution conformations of human [Zn7]-metallothionein-2 and [Cd7]-metallothionein-2 using nuclear magnetic resonance spectroscopy.". J. Mol. Biol. 225 (2): 433–43. doi:10.1016/0022-2836(92)90930-I. PMID 1593628.
Zafarullah M, Martel-Pelletier J, Cloutier JM, et al. (1992). "Expression of c-fos, c-jun, jun-B, metallothionein and metalloproteinase genes in human chondrocyte.". FEBS Lett. 306 (2-3): 169–72. doi:10.1016/0014-5793(92)80992-P. PMID 1633872.
Messerle BA, Schäffer A, Vasák M, et al. (1990). "Three-dimensional structure of human [113Cd7]metallothionein-2 in solution determined by nuclear magnetic resonance spectroscopy.". J. Mol. Biol. 214 (3): 765–79. doi:10.1016/0022-2836(90)90291-S. PMID 2388267.
Duguid JR, Bohmont CW, Liu NG, Tourtellotte WW (1989). "Changes in brain gene expression shared by scrapie and Alzheimer disease.". Proc. Natl. Acad. Sci. U.S.A. 86 (18): 7260–4. doi:10.1073/pnas.86.18.7260. PMC 298037. PMID 2780570.
Karin M, Haslinger A, Heguy A, et al. (1987). "Metal-responsive elements act as positive modulators of human metallothionein-IIA enhancer activity.". Mol. Cell. Biol. 7 (2): 606–13. PMC 365115. PMID 3821726.
Karin M, Haslinger A, Holtgreve H, et al. (1984). "Characterization of DNA sequences through which cadmium and glucocorticoid hormones induce human metallothionein-IIA gene.". Nature. 308 (5959): 513–9. doi:10.1038/308513a0. PMID 6323998.
Schmidt CJ, Hamer DH, McBride OW (1984). "Chromosomal location of human metallothionein genes: implications for Menkes' disease.". Science. 224 (4653): 1104–6. doi:10.1126/science.6719135. PMID 6719135.
Karin M, Richards RI (1982). "Human metallothionein genes: molecular cloning and sequence analysis of the mRNA.". Nucleic Acids Res. 10 (10): 3165–73. doi:10.1093/nar/10.10.3165. PMC 320698. PMID 6896577.
Lambert E, Kille P, Swaminathan R (1996). "Cloning and sequencing a novel metallothionein I isoform expressed in human reticulocytes.". FEBS Lett. 389 (2): 210–2. doi:10.1016/0014-5793(96)00587-X. PMID 8766831.
Woo ES, Dellapiazza D, Wang AS, Lazo JS (1999). "Energy-dependent nuclear binding dictates metallothionein localization.". J. Cell. Physiol. 182 (1): 69–76. doi:10.1002/(SICI)1097-4652(200001)182:1<69::AID-JCP8>3.0.CO;2-9. PMID 10567918.
Jiang LJ, Vasák M, Vallee BL, Maret W (2000). "Zinc transfer potentials of the alpha - and beta-clusters of metallothionein are affected by domain interactions in the whole molecule.". Proc. Natl. Acad. Sci. U.S.A. 97 (6): 2503–8. doi:10.1073/pnas.97.6.2503. PMC 15958. PMID 10716985.
Garrett SH, Sens MA, Shukla D, et al. (2000). "Metallothionein isoform 1 and 2 gene expression in the human prostate: downregulation of MT-1X in advanced prostate cancer.". Prostate. 43 (2): 125–35. doi:10.1002/(SICI)1097-0045(20000501)43:2<125::AID-PROS7>3.0.CO;2-S. PMID 10754528.
Ebert MP, Günther T, Hoffmann J, et al. (2000). "Expression of metallothionein II in intestinal metaplasia, dysplasia, and gastric cancer.". Cancer Res. 60 (7): 1995–2001. PMID 10766190.
Toyama M, Yamashita M, Hirayama N, Murooka Y (2003). "Interactions of arsenic with human metallothionein-2.". J. Biochem. 132 (2): 217–21. doi:10.1093/oxfordjournals.jbchem.a003213. PMID 12153718.
Sun X, Kang YJ (2002). "Prior increase in metallothionein levels is required to prevent doxorubicin cardiotoxicity.". Exp. Biol. Med. (Maywood). 227 (8): 652–7. PMID 12192109.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
Izmailova E, Bertley FM, Huang Q, et al. (2003). "HIV-1 Tat reprograms immature dendritic cells to express chemoattractants for activated T cells and macrophages.". Nat. Med. 9 (2): 191–7. doi:10.1038/nm822. PMID 12539042.

PDB gallery

1mhu: THE THREE-DIMENSIONAL STRUCTURE OF HUMAN [113CD7] METALLOTHIONEIN-2 IN SOLUTION DETERMINED BY NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY
1mrb: THREE-DIMENSIONAL STRUCTURE OF RABBIT LIVER CD7 METALLOTHIONEIN-2A IN AQUEOUS SOLUTION DETERMINED BY NUCLEAR MAGNETIC RESONANCE
1mrt: CONFORMATION OF CD-7 METALLOTHIONEIN-2 FROM RAT LIVER IN AQUEOUS SOLUTION DETERMINED BY NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY
2mhu: THE THREE-DIMENSIONAL STRUCTURE OF HUMAN [113CD7] METALLOTHIONEIN-2 IN SOLUTION DETERMINED BY NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY

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