ATG12

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ATG12 autophagy related 12 homolog (S. cerevisiae)
Identifiers
Symbol(s) ATG12; APG12; APG12L; HAPG12
External IDs OMIM: 609608 MGI1914776 HomoloGene37953
RNA expression pattern

More reference expression data

Orthologs
Human Mouse
Entrez 9140 67526
Ensembl ENSG00000145782 ENSMUSG00000032905
Uniprot O94817 Q9CQY1
Refseq NM_004707 (mRNA)
NP_004698 (protein)
NM_026217 (mRNA)
NP_080493 (protein)
Location Chr 5: 115.19 - 115.21 Mb Chr 18: 46.86 - 46.87 Mb
Pubmed search [1] [2]

ATG12 autophagy related 12 homolog (S. cerevisiae), also known as ATG12, is a human gene.[1]

Autophagy is a process of bulk protein degradation in which cytoplasmic components, including organelles, are enclosed in double-membrane structures called autophagosomes and delivered to lysosomes or vacuoles for degradation. ATG12 is the human homolog of a yeast protein involved in autophagy (Mizushima et al., 1998).[supplied by OMIM][1]

[edit] References

[edit] Further reading

  • Prigione A, Cortopassi G (2007). "Mitochondrial DNA deletions and chloramphenicol treatment stimulate the autophagic transcript ATG12.". Autophagy 3 (4): 377–80. PMID 17457038. 
  • Ewing RM, Chu P, Elisma F, et al. (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry.". Mol. Syst. Biol. 3: 89. doi:10.1038/msb4100134. PMID 17353931. 
  • Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network.". Nature 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514. 
  • Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMID 15489334. 
  • Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039. 
  • Mizushima N, Kuma A, Kobayashi Y, et al. (2004). "Mouse Apg16L, a novel WD-repeat protein, targets to the autophagic isolation membrane with the Apg12-Apg5 conjugate.". J. Cell. Sci. 116 (Pt 9): 1679–88. PMID 12665549. 
  • Mizushima N, Yoshimori T, Ohsumi Y (2003). "Mouse Apg10 as an Apg12-conjugating enzyme: analysis by the conjugation-mediated yeast two-hybrid method.". FEBS Lett. 532 (3): 450–4. PMID 12482611. 
  • 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. PMID 12477932. 
  • Tanida I, Nishitani T, Nemoto T, et al. (2002). "Mammalian Apg12p, but not the Apg12p.Apg5p conjugate, facilitates LC3 processing.". Biochem. Biophys. Res. Commun. 296 (5): 1164–70. PMID 12207896. 
  • Tanida I, Tanida-Miyake E, Nishitani T, et al. (2002). "Murine Apg12p has a substrate preference for murine Apg7p over three Apg8p homologs.". Biochem. Biophys. Res. Commun. 292 (1): 256–62. PMID 11890701. 
  • Tanida I, Tanida-Miyake E, Komatsu M, et al. (2002). "Human Apg3p/Aut1p homologue is an authentic E2 enzyme for multiple substrates, GATE-16, GABARAP, and MAP-LC3, and facilitates the conjugation of hApg12p to hApg5p.". J. Biol. Chem. 277 (16): 13739–44. doi:10.1074/jbc.M200385200. PMID 11825910. 
  • Mizushima N, Sugita H, Yoshimori T, Ohsumi Y (1999). "A new protein conjugation system in human. The counterpart of the yeast Apg12p conjugation system essential for autophagy.". J. Biol. Chem. 273 (51): 33889–92. PMID 9852036. 
  • Ueno K, Kumagai T, Kijima T, et al. (1998). "Cloning and tissue expression of cDNAs from chromosome 5q21-22 which is frequently deleted in advanced lung cancer.". Hum. Genet. 102 (1): 63–8. PMID 9490301. 
  • Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery.". Genome Res. 6 (9): 791–806. PMID 8889548.