ATG12

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ATG12 autophagy related 12 homolog (S. cerevisiae)
Identifiers
Symbols ATG12 ; APG12; APG12L; HAPG12
External IDs Template:OMIM5 Template:MGI HomoloGene37953
RNA expression pattern
More reference expression data
Orthologs
Template:GNF Ortholog box
Species Human Mouse
Entrez n/a n/a
Ensembl n/a n/a
UniProt n/a n/a
RefSeq (mRNA) n/a n/a
RefSeq (protein) n/a n/a
Location (UCSC) n/a n/a
PubMed search n/a n/a

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]

References

  1. 1.0 1.1 "Entrez Gene: ATG12 ATG12 autophagy related 12 homolog (S. cerevisiae)".

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.

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