AGO2_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: AGO2_MOUSE
• UniProt AC: Q8CJG0
• Protein Name: Protein argonaute-2 {ECO:0000255|HAMAP-Rule:MF_03031}
• Gene Name: Ago2
• Organism: Mus musculus (Mouse).
• Sequence Length: 860
• Subcellular Localization: Cytoplasm, P-body . Nucleus . Translational repression of mRNAs results in their recruitment to P-bodies. Translocation to the nucleus requires IMP8.
• Protein Description: Required for RNA-mediated gene silencing (RNAi) by the RNA-induced silencing complex (RISC). The 'minimal RISC' appears to include AGO2 bound to a short guide RNA such as a microRNA (miRNA) or short interfering RNA (siRNA). These guide RNAs direct RISC to complementary mRNAs that are targets for RISC-mediated gene silencing. The precise mechanism of gene silencing depends on the degree of complementarity between the miRNA or siRNA and its target. Binding of RISC to a perfectly complementary mRNA generally results in silencing due to endonucleolytic cleavage of the mRNA specifically by AGO2. Binding of RISC to a partially complementary mRNA results in silencing through inhibition of translation, and this is independent of endonuclease activity. May inhibit translation initiation by binding to the 7-methylguanosine cap, thereby preventing the recruitment of the translation initiation factor eIF4-E. May also inhibit translation initiation via interaction with EIF6, which itself binds to the 60S ribosomal subunit and prevents its association with the 40S ribosomal subunit. The inhibition of translational initiation leads to the accumulation of the affected mRNA in cytoplasmic processing bodies (P-bodies), where mRNA degradation may subsequently occur. In some cases RISC-mediated translational repression is also observed for miRNAs that perfectly match the 3' untranslated region (3'-UTR). Can also up-regulate the translation of specific mRNAs under certain growth conditions. Binds to the AU element of the 3'-UTR of the TNF (TNF-alpha) mRNA and up-regulates translation under conditions of serum starvation. Also required for transcriptional gene silencing (TGS), in which short RNAs known as antigene RNAs or agRNAs direct the transcriptional repression of complementary promoter regions. Regulates lymphoid and erythroid development and function, and this is independent of endonuclease activity..
• Protein Sequence: MYSGAGPVLASPAPTTSPIPGYAFKPPPRPDFGTTGRTIKLQANFFEMDIPKIDIYHYELDIKPEKCPRRVNREIVEHMVQHFKTQIFGDRKPVFDGRKNLYTAMPLPIGRDKVELEVTLPGEGKDRIFKVSIKWVSCVSLQALHDALSGRLPSVPFETIQALDVVMRHLPSMRYTPVGRSFFTASEGCSNPLGGGREVWFGFHQSVRPSLWKMMLNIDVSATAFYKAQPVIEFVCEVLDFKSIEEQQKPLTDSQRVKFTKEIKGLKVEITHCGQMKRKYRVCNVTRRPASHQTFPLQQESGQTVECTVAQYFKDRHKLVLRYPHLPCLQVGQEQKHTYLPLEVCNIVAGQRCIKKLTDNQTSTMIRATARSAPDRQEEISKLMRSASFNTDPYVREFGIMVKDEMTDVTGRVLQPPSILYGGRNKAIATPVQGVWDMRNKQFHTGIEIKVWAIACFAPQRQCTEVHLKSFTEQLRKISRDAGMPIQGQPCFCKYAQGADSVEPMFRHLKNTYAGLQLVVVILPGKTPVYAEVKRVGDTVLGMATQCVQMKNVQRTTPQTLSNLCLKINVKLGGVNNILLPQGRPPVFQQPVIFLGADVTHPPAGDGKKPSIAAVVGSMDAHPNRYCATVRVQQHRQEIIQDLAAMVRELLIQFYKSTRFKPTRIIFYRDGVSEGQFQQVLHHELLAIREACIKLEKDYQPGITFIVVQKRHHTRLFCTDKNERVGKSGNIPAGTTVDTKITHPTEFDFYLCSHAGIQGTSRPSHYHVLWDDNRFSSDELQILTYQLCHTYVRCTRSVSIPAPAYYAHLVAFRARYHLVDKEHDSAEGSHTSGQSNGRDHQALAKAVQVHQDTLRTMYFA

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
2	Nitration	------MYSGAGPVL ------CCCCCCCEE	18.80	16800626
2	Nitration	------MYSGAGPVL ------CCCCCCCEE	18.80	16800626
2	Nitrated tyrosine	------MYSGAGPVL ------CCCCCCCEE	18.80	-
11	Phosphorylation	GAGPVLASPAPTTSP CCCCEECCCCCCCCC	19.89	26824392
15	Phosphorylation	VLASPAPTTSPIPGY EECCCCCCCCCCCCC	41.85	26239621
16	Phosphorylation	LASPAPTTSPIPGYA ECCCCCCCCCCCCCC	31.29	26239621
17	Phosphorylation	ASPAPTTSPIPGYAF CCCCCCCCCCCCCCC	24.26	26239621
22	Phosphorylation	TTSPIPGYAFKPPPR CCCCCCCCCCCCCCC	11.96	26643407
34	Phosphorylation	PPRPDFGTTGRTIKL CCCCCCCCCCCEEEE	26.52	26643407
35	Phosphorylation	PRPDFGTTGRTIKLQ CCCCCCCCCCEEEEE	25.66	26643407
154	Phosphorylation	ALSGRLPSVPFETIQ HHCCCCCCCCHHHHH	47.19	46103327
159	Phosphorylation	LPSVPFETIQALDVV CCCCCHHHHHHHHHH	20.83	51458725
172	Phosphorylation	VVMRHLPSMRYTPVG HHHHHCCCCCEECCC	23.42	51458731
249	Ubiquitination	KSIEEQQKPLTDSQR CCHHHHCCCCCHHHH	41.51	22790023
254	Phosphorylation	QQKPLTDSQRVKFTK HCCCCCHHHHHHHHH	18.04	28464351
256	Dimethylation	KPLTDSQRVKFTKEI CCCCHHHHHHHHHHH	37.23	-
386	Phosphorylation	EISKLMRSASFNTDP HHHHHHHHHCCCCCH	17.82	23527152
388	Phosphorylation	SKLMRSASFNTDPYV HHHHHHHCCCCCHHH	21.92	23527152
391	Phosphorylation	MRSASFNTDPYVREF HHHHCCCCCHHHHHH	36.02	28833060
394	Phosphorylation	ASFNTDPYVREFGIM HCCCCCHHHHHHCEE	18.23	28833060
426	Ubiquitination	ILYGGRNKAIATPVQ EEECCCCCCCCCCCC	39.55	22790023
470	Phosphorylation	CTEVHLKSFTEQLRK CCHHHHHHHHHHHHH	43.70	23970565
626	Phosphorylation	MDAHPNRYCATVRVQ CCCCCCCEEEEEEHH	7.96	22345495
629	Phosphorylation	HPNRYCATVRVQQHR CCCCEEEEEEHHHHH	12.80	22345495
655	Phosphorylation	RELLIQFYKSTRFKP HHHHHHHHHHCCCCC	6.40	-
701	Hydroxylation	KLEKDYQPGITFIVV HHHHCCCCCEEEEEE	29.89	-
721	Ubiquitination	TRLFCTDKNERVGKS EEEEECCCCCCCCCC	42.42	22790023
727	Ubiquitination	DKNERVGKSGNIPAG CCCCCCCCCCCCCCC	52.94	22790023
816	Phosphorylation	LVAFRARYHLVDKEH HHHHHHHEEECCCCC	9.87	25777480
825	Phosphorylation	LVDKEHDSAEGSHTS ECCCCCCCCCCCCCC	30.08	27087446
829	Phosphorylation	EHDSAEGSHTSGQSN CCCCCCCCCCCCCCC	18.33	27087446
831	Phosphorylation	DSAEGSHTSGQSNGR CCCCCCCCCCCCCCC	35.93	22817900
832	Phosphorylation	SAEGSHTSGQSNGRD CCCCCCCCCCCCCCC	29.43	22817900
835	Phosphorylation	GSHTSGQSNGRDHQA CCCCCCCCCCCCHHH	44.79	25777480

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of AGO2_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of AGO2_MOUSE !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of AGO2_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
DICER_HUMAN	DICER1	physical	12526743
LIN41_MOUSE	Trim71	physical	19898466

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Nitration

"Endogenously nitrated proteins in mouse brain: links toneurodegenerative disease.";
Sacksteder C.A., Qian W.-J., Knyushko T.V., Wang H., Chin M.H.,Lacan G., Melega W.P., Camp D.G. II, Smith R.D., Smith D.J.,Squier T.C., Bigelow D.J.;
Biochemistry 45:8009-8022(2006).
Cited for: NITRATION [LARGE SCALE ANALYSIS] AT TYR-2, AND MASS SPECTROMETRY.
PubMed: 16800626