AGO4_ARATH - dbPTM
AGO4_ARATH - PTM Information in dbPTM
Basic Information of Protein
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
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
166PhosphorylationTRANGNGSPNGNESP
CCCCCCCCCCCCCCC
21.1323776212
172PhosphorylationGSPNGNESPSDGDRK
CCCCCCCCCCCCCHH
33.4323776212
174PhosphorylationPNGNESPSDGDRKRL
CCCCCCCCCCCHHHC
64.6023776212
636PhosphorylationAKLGGLNSMLSVERT
HHCCCHHHHCCCCCC
26.5830589143
890PhosphorylationFMKFEDQSETSSSHG
CEECCCCCCCCCCCC
55.9823776212
892PhosphorylationKFEDQSETSSSHGGI
ECCCCCCCCCCCCCC
38.8723776212
893PhosphorylationFEDQSETSSSHGGIT
CCCCCCCCCCCCCCC
26.2823776212
894PhosphorylationEDQSETSSSHGGITA
CCCCCCCCCCCCCCC
33.5023776212
895PhosphorylationDQSETSSSHGGITAP
CCCCCCCCCCCCCCC
26.3923776212
900PhosphorylationSSSHGGITAPGPISV
CCCCCCCCCCCCCCH
30.0323776212

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of AGO4_ARATH !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AGO4_ARATH !!

Disease-associated PTM Sites based on SAP

* 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 !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RDM1_ARATHRDM1physical
20410883
NRPE1_ARATHNRPD1Bphysical
19410546

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of AGO4_ARATH

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Related Literatures of Post-Translational Modification

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