UniProt ID | AGO4_ARATH | |
---|---|---|
UniProt AC | Q9ZVD5 | |
Protein Name | Protein argonaute 4 | |
Gene Name | AGO4 | |
Organism | Arabidopsis thaliana (Mouse-ear cress). | |
Sequence Length | 924 | |
Subcellular Localization | Nucleus, nucleolus . Nucleus, nucleoplasm . Nucleus, Cajal body . Also located in AB-bodies that are distincts from the Cajal bodies and immediately adjacent to the condensed 45S ribosomal DNA (rDNA) loci (PubMed:18266474). Colocalizes with AGO4 and | |
Protein Description | 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] | |
Protein Sequence | MDSTNGNGADLESANGANGSGVTEALPPPPPVIPPNVEPVRVKTELAEKKGPVRVPMARKGFGTRGQKIPLLTNHFKVDVANLQGHFFHYSVALFYDDGRPVEQKGVGRKILDKVHQTYHSDLDGKEFAYDGEKTLFTYGALPSNKMDFSVVLEEVSATRANGNGSPNGNESPSDGDRKRLRRPNRSKNFRVEISYAAKIPLQALANAMRGQESENSQEAIRVLDIILRQHAARQGCLLVRQSFFHNDPTNCEPVGGNILGCRGFHSSFRTTQGGMSLNMDVTTTMIIKPGPVVDFLIANQNARDPYSIDWSKAKRTLKNLRVKVSPSGQEFKITGLSDKPCREQTFELKKRNPNENGEFETTEVTVADYFRDTRHIDLQYSADLPCINVGKPKRPTYIPLELCALVPLQRYTKALTTFQRSALVEKSRQKPQERMTVLSKALKVSNYDAEPLLRSCGISISSNFTQVEGRVLPAPKLKMGCGSETFPRNGRWNFNNKEFVEPTKIQRWVVVNFSARCNVRQVVDDLIKIGGSKGIEIASPFQVFEEGNQFRRAPPMIRVENMFKDIQSKLPGVPQFILCVLPDKKNSDLYGPWKKKNLTEFGIVTQCMAPTRQPNDQYLTNLLLKINAKLGGLNSMLSVERTPAFTVISKVPTIILGMDVSHGSPGQSDVPSIAAVVSSREWPLISKYRASVRTQPSKAEMIESLVKKNGTEDDGIIKELLVDFYTSSNKRKPEHIIIFRDGVSESQFNQVLNIELDQIIEACKLLDANWNPKFLLLVAQKNHHTKFFQPTSPENVPPGTIIDNKICHPKNNDFYLCAHAGMIGTTRPTHYHVLYDEIGFSADELQELVHSLSYVYQRSTSAISVVAPICYAHLAAAQLGTFMKFEDQSETSSSHGGITAPGPISVAQLPRLKDNVANSMFFC | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
166 | Phosphorylation | TRANGNGSPNGNESP CCCCCCCCCCCCCCC | 21.13 | 23776212 | |
172 | Phosphorylation | GSPNGNESPSDGDRK CCCCCCCCCCCCCHH | 33.43 | 23776212 | |
174 | Phosphorylation | PNGNESPSDGDRKRL CCCCCCCCCCCHHHC | 64.60 | 23776212 | |
636 | Phosphorylation | AKLGGLNSMLSVERT HHCCCHHHHCCCCCC | 26.58 | 30589143 | |
890 | Phosphorylation | FMKFEDQSETSSSHG CEECCCCCCCCCCCC | 55.98 | 23776212 | |
892 | Phosphorylation | KFEDQSETSSSHGGI ECCCCCCCCCCCCCC | 38.87 | 23776212 | |
893 | Phosphorylation | FEDQSETSSSHGGIT CCCCCCCCCCCCCCC | 26.28 | 23776212 | |
894 | Phosphorylation | EDQSETSSSHGGITA CCCCCCCCCCCCCCC | 33.50 | 23776212 | |
895 | Phosphorylation | DQSETSSSHGGITAP CCCCCCCCCCCCCCC | 26.39 | 23776212 | |
900 | Phosphorylation | SSSHGGITAPGPISV CCCCCCCCCCCCCCH | 30.03 | 23776212 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
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Oops, there are no upstream regulatory protein records of AGO4_ARATH !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of AGO4_ARATH !! |
* Distance = the distance between SAP position and PTM sites.
Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of AGO4_ARATH !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
RDM1_ARATH | RDM1 | physical | 20410883 | |
NRPE1_ARATH | NRPD1B | physical | 19410546 |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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