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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: Acetyl-coenzyme A synthetase, cytoplasmic

UniprotKB/SwissProt ID: Q9NR19 (Q9NR19)

Gene Name: ACSS2

Organism: Homo sapiens (Human)

Function: Catalyzes the synthesis of acetyl-CoA from short-chain fatty acids (PubMed:10843999, PubMed:28003429, PubMed:28552616). Acetate is the preferred substrate (PubMed:10843999, PubMed:28003429). Can also utilize propionate with a much lower affinity (By similarity). Nuclear ACSS2 promotes glucose deprivation-induced lysosomal biogenesis and autophagy, tumor cell survival and brain tumorigenesis (PubMed:28552616). Glucose deprivation results in AMPK-mediated phosphorylation of ACSS2 leading to its translocation to the nucleus where it binds to TFEB and locally produces acetyl-CoA for histone acetylation in the promoter regions of TFEB target genes thereby activating their transcription (PubMed:28552616). The regulation of genes associated with autophagy and lysosomal activity through ACSS2 is important for brain tumorigenesis and tumor survival (PubMed:28552616). Acts as a chromatin-bound transcriptional coactivator that up-regulates histone acetylation and expression of neuronal genes (By similarity). Can be recruited to the loci of memory-related neuronal genes to maintain a local acetyl-CoA pool, providing the substrate for histone acetylation and promoting the expression of specific genes, which is essential for maintaining long-term spatial memory (By similarity)

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Cytoplasm, cytosol. Cytoplasm. Nucleus

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR011904 Ac_CoA_lig
IPR032387 ACAS_N
IPR025110 AMP-bd_C
IPR045851 AMP-bd_C_sf
IPR020845 AMP-binding_CS
IPR000873 AMP-dep_synth/lig_dom
IPR042099 ANL_N_sf

The S-nitrosylation sites of Q9NR19

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 75 IAKEFYWKTP C PGPFLRYNFD