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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: Protein argonaute 4

UniprotKB/SwissProt ID: Q9ZVD5 (Q9ZVD5)

Gene Name: AGO4

Organism: Arabidopsis thaliana (Mouse-ear cress)

Function: Together with RDM3, required for transcriptional gene silencing (TGS) by DNA methylation and repressive histone modifications (H3K9me2) of several chromatin loci (PubMed:21738482). Component of the RISC complex that associate with the small interfering RNA (siRNA) pathway involved in direct cytosine methylation at endogenous DNA repeats. Forms a AGO4/NRPE1/siRNA complex in cajal body, facilitating its function in RNA-directed gene silencing of target loci. Required for CpNpG and asymmetric DNA methylation as well as histone H3 'Lys-9' methylation (H3K9me) at SUP and SN1 loci. May be not required for CpG methylation. Required for the production and maintenance of retrotransposon SN1 and Copia and ribosomal 5S 25 nucleotide siRNAs specialized in gene silencing at chromatin level. Involved in de novo methylation of FWA gene and required for the maintenance of RNA-directed DNA methylation (RdDM) triggered by inverted repeat transgenes. Interacts with miRNA miR390 and miR172, targeting respectively TAS3 and AP2 mRNAs, and mediates cleavage of miRNA targets. Associates mainly with small RNAs of 24 nucleotide in length and preferentially recruits small RNAs with a 5' terminal adenosine. Targeted by the turnip yellows virus (TuYV) protein P0 (via F-box-like domain) for probable proteasome degradation and thereby inactivating AGO4 function in RNA silencing. Required for resistance to the bacterial pathogen P.syringae. Works independently of the RdDM pathway in mediating resistance to P.syringae. RdDM is involved in viral genome methylation as an epigenetic defense against geminiviruses (PubMed:12522258, PubMed:14988555, PubMed:15242620, PubMed:16839878, PubMed:16839879, PubMed:16998468, PubMed:17869110, PubMed:17938239, PubMed:17993621, PubMed:18342361, PubMed:18596098, PubMed:19377477, PubMed:20173091)

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Nucleus, nucleolus. Nucleus, nucleoplasm. Nucleus, Cajal body

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR014811 ArgoL1
IPR032472 ArgoL2
IPR032473 Argonaute_Mid_dom
IPR032474 Argonaute_N
IPR003100 PAZ_dom
IPR036085 PAZ_dom_sf
IPR003165 Piwi
IPR045246 Piwi_ago-like
IPR012337 RNaseH-like_sf
IPR036397 RNaseH_sf

The S-nitrosylation sites of Q9ZVD5

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 482 VLPAPKLKMG C GSETFPRNGR