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Sep. 10, 2014:
A total of 174 experimentally verified S-nitrosylation sites on 94 S-nitrosylated proteins from individualized human colorectal cancer tissues using a label-free quantitation strategy.

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Protein Name: Ubiquitin-like modifier-activating enzyme ATG7

UniprotKB/SwissProt ID: Q9D906 (Q9D906)

Gene Name: Atg7

Organism: Mus musculus (Mouse)

Function: E1-like activating enzyme involved in the 2 ubiquitin-like systems required for cytoplasm to vacuole transport (Cvt) and autophagy. Activates ATG12 for its conjugation with ATG5 as well as the ATG8 family proteins for their conjugation with phosphatidylethanolamine. Both systems are needed for the ATG8 association to Cvt vesicles and autophagosomes membranes. Facilitates LC3-I lipidation with phosphatidylethanolamine to form LC3-II which is found on autophagosomal membranes (By similarity). Required for autophagic death induced by caspase-8 inhibition. Required for mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. Modulates p53/TP53 activity to regulate cell cycle and survival during metabolic stress. Also plays a key role in the maintenance of axonal homeostasis, the prevention of axonal degeneration, the maintenance of hematopoietic stem cells, the formation of Paneth cell granules, as well as in adipose differentiation. Plays a role in regulating the liver clock and glucose metabolism by mediating the autophagic degradation of CRY1 (clock repressor) in a time-dependent manner (PubMed:29937374)

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Cytoplasm. Preautophagosomal structure

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR006285 Atg7
IPR032197 Atg7_N
IPR042522 Atg7_N_1
IPR042523 Atg7_N_2
IPR045886 ThiF/MoeB/HesA
IPR000594 ThiF_NAD_FAD-bd
IPR035985 Ubiquitin-activating_enz

The S-nitrosylation sites of Q9D906

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 354 LDLDKVVSVK C LLLGAGTLGC