≡

Midasin (MDN1)

[Edit]

MIDAS-containing protein

Midasin (MDN1)
CCC Q685
HGNC 18302
MGI 1926159
PubMed 12102729
UniProt Q9NU22
Midasin is present as a single-copy gene encoding a well-conserved protein of approximately 600 kDa in all eukaryotes for which data are available. In humans, the gene maps to 6q15 and encodes a predicted protein of 5596 residues. Sequence alignments of midasin from humans, yeast, Giardia and Encephalitozoon indicate that its domain structure comprises an N-terminal domain, followed by an AAA domain containing six tandem AAA protomers, a linker domain, an acidic domain containing 35-40% aspartate and glutamate, and a carboxy-terminal M-domain that possesses MIDAS sequence motifs and is homologous to the I-domain of integrins. Expression of hemagglutamin-tagged midasin in yeast demonstrates a polypeptide of the anticipated size that is localized principally in the nucleus.

Organism species: Homo sapiens (Human)

CATALOG NO. PRODUCT NAME APPLICATIONS
Proteins n/a Recombinant Midasin (MDN1) Recombinant Protein Customized Service Offer
Antibodies n/a Monoclonal Antibody to Midasin (MDN1) Monoclonal Antibody Customized Service Offer
n/a Polyclonal Antibody to Midasin (MDN1) Polyclonal Antibody Customized Service Offer
Assay Kits n/a CLIA Kit for Midasin (MDN1) CLIA Kit Customized Service Offer
n/a ELISA Kit for Midasin (MDN1) ELISA Kit Customized Service Offer

Organism species: Mus musculus (Mouse)

CATALOG NO. PRODUCT NAME APPLICATIONS
Proteins n/a Recombinant Midasin (MDN1) Recombinant Protein Customized Service Offer
Antibodies n/a Monoclonal Antibody to Midasin (MDN1) Monoclonal Antibody Customized Service Offer
n/a Polyclonal Antibody to Midasin (MDN1) Polyclonal Antibody Customized Service Offer
Assay Kits n/a CLIA Kit for Midasin (MDN1) CLIA Kit Customized Service Offer
n/a ELISA Kit for Midasin (MDN1) ELISA Kit Customized Service Offer
  1. "Expression and genomic analysis of midasin, a novel and highly conserved AAA protein distantly related to dynein."BMC Genomics 3:18-18(2002) [PubMed] [Europe PMC] [Abstract]
  2. "The DNA sequence and analysis of human chromosome 6." Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
  3. "Prediction of the coding sequences of unidentified human genes. VII. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."DNA Res. 4:141-150(1997) [PubMed] [Europe PMC] [Abstract]
  4. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
  5. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
  6. "A quantitative atlas of mitotic phosphorylation."Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
  7. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
  8. "Large-scale proteomics analysis of the human kinome."Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
  9. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
  10. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
  11. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
  12. "Initial characterization of the human central proteome."BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
  13. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
  14. "Systematic analysis of protein pools, isoforms, and modifications affecting turnover and subcellular localization."Mol. Cell. Proteomics 11:M111.013680.01-M111.013680.15(2012) [PubMed] [Europe PMC] [Abstract]