ATG7

From Wikipedia, the free encyclopedia

ATG7 autophagy related 7 homolog (S. cerevisiae)

Identifiers

ATG7; APG7L; DKFZp434N0735; GSA7

External IDs

OMIM: 608760 MGI: 1921494 HomoloGene: 4662

Gene ontology
Molecular Function:	• catalytic activity • ubiquitin activating enzyme activity • protein binding
Cellular Component:	• cytoplasm
Biological Process:	• protein amino acid lipidation • ubiquitin cycle • autophagy • membrane fusion • protein transport • positive regulation of protein modification

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_006395 (mRNA)
NP_006386 (protein)

NM_028835 (mRNA)
NP_083111 (protein)

Location

Chr 3: 11.29 - 11.57 Mb

Chr 6: 114.64 - 114.74 Mb

Pubmed search

[1]

[2]

ATG7 autophagy related 7 homolog (S. cerevisiae), also known as ATG7, is a human gene.^[1]

This gene was identified based on homology to Pichia pastoris GSA7 and Saccharomyces cerevisiae APG7. In the yeast, the protein appears to be required for fusion of peroxisomal and vaculuolar membranes. The protein shows homlogy to the ATP-binding and catalytic sites of the E1 ubiquitin activating enzymes.^[1]

[edit] References

^ ^a ^b Entrez Gene: ATG7 ATG7 autophagy related 7 homolog (S. cerevisiae).

[edit] Further reading

Yuan W, Stromhaug PE, Dunn WA (1999). "Glucose-induced autophagy of peroxisomes in Pichia pastoris requires a unique E1-like protein.". Mol. Biol. Cell 10 (5): 1353–66. PMID 10233149.
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.
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.
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.
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.
Nemoto T, Tanida I, Tanida-Miyake E, et al. (2003). "The mouse APG10 homologue, an E2-like enzyme for Apg12p conjugation, facilitates MAP-LC3 modification.". J. Biol. Chem. 278 (41): 39517–26. doi:10.1074/jbc.C200334200. PMID 12890687.
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.
Otsuki T, Ota T, Nishikawa T, et al. (2007). "Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries.". DNA Res. 12 (2): 117–26. doi:10.1093/dnares/12.2.117. PMID 16303743.
Tanida I, Sou YS, Minematsu-Ikeguchi N, et al. (2006). "Atg8L/Apg8L is the fourth mammalian modifier of mammalian Atg8 conjugation mediated by human Atg4B, Atg7 and Atg3.". FEBS J. 273 (11): 2553–62. doi:10.1111/j.1742-4658.2006.05260.x. PMID 16704426.