PIWL2_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PIWL2_MOUSE
• UniProt AC: Q8CDG1
• Protein Name: Piwi-like protein 2 {ECO:0000305}
• Gene Name: Piwil2 {ECO:0000312|MGI:MGI:1930036}
• Organism: Mus musculus (Mouse).
• Sequence Length: 971
• Subcellular Localization: Cytoplasm . Present in chromatoid body. Probable component of the meiotic nuage, also named P granule, a germ-cell-specific organelle required to repress transposon activity during meiosis (PubMed:20439430).
• Protein Description: Endoribonuclease that plays a central role during spermatogenesis by repressing transposable elements and preventing their mobilization, which is essential for the germline integrity. [PubMed: 11578866]
• Protein Sequence: MDPVRPLFRGPTPVHPSQCVRMPGCWPQAPRPLEPAWGRAGPAGRGLVFRKPEDSSPPLQPVQKDSVGLVSMFRGMGLDTAFRPPSKREVPPLGRGVLGRGLSANMVRKDREEPRSSLPDPSVLAAGDSKLAEASVGWSRMLGRGSSEVSLLPLGRAASSIGRGMDKPPSAFGLTARDPPRLPQPPALSPTSLHSADPPPVLTMERKEKELLVKQGSKGTPQSLGLNLIKIQCHNEAVYQYHVTFSPSVECKSMRFGMLKDHQSVTGNVTAFDGSILYLPVKLQQVVELKSQRKTDDAEISIKIQLTKILEPCSDLCIPFYNVVFRRVMKLLDMKLVGRNFYDPTSAMVLQQHRLQIWPGYAASIRRTDGGLFLLADVSHKVIRNDSVLDVMHAIYQQNKEHFQDECSKLLVGSIVITRYNNRTYRIDDVDWNKTPKDSFVMSDGKEITFLEYYSKNYGITVKEDDQPLLIHRPSERQNNHGMLLKGEILLLPELSFMTGIPEKMKKDFRAMKDLTQQINLSPKQHHGALECLLQRISQNETASNELTRWGLSLHKDVHKIEGRLLPMERINLRNTSFVTSEDLNWVKEVTRDASILTIPMHFWALFYPKRAMDQARELVNMLEKIAGPIGMRISPPAWVELKDDRIETYIRTIQSLLGVEGKIQMVVCIIMGTRDDLYGAIKKLCCVQSPVPSQVINVRTIGQPTRLRSVAQKILLQMNCKLGGELWGVDIPLKQLMVIGMDVYHDPSRGMRSVVGFVASINLTLTKWYSRVVFQMPHQEIVDSLKLCLVGSLKKYYEVNHCLPEKIVVYRDGVSDGQLKTVANYEIPQLQKCFEAFDNYHPKMVVFVVQKKISTNLYLAAPDHFVTPSPGTVVDHTITSCEWVDFYLLAHHVRQGCGIPTHYICVLNTANLSPDHMQRLTFKLCHMYWNWPGTIRVPAPCKYAHKLAFLSGQILHHEPAIQLCGNLFFL

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
45	Methylation	GRAGPAGRGLVFRKP CCCCCCCCCCEEECC	37.06	19918066
45	Symmetric dimethylarginine	GRAGPAGRGLVFRKP CCCCCCCCCCEEECC	37.06	-
74	Dimethylation	VGLVSMFRGMGLDTA HHHHHHHCCCCCCCC	26.08	-
74	Methylation	VGLVSMFRGMGLDTA HHHHHHHCCCCCCCC	26.08	22996915
83	Symmetric dimethylarginine	MGLDTAFRPPSKREV CCCCCCCCCCCCCCC	39.49	-
83	Methylation	MGLDTAFRPPSKREV CCCCCCCCCCCCCCC	39.49	19918066
95	Symmetric dimethylarginine	REVPPLGRGVLGRGL CCCCCCCCCCCCCCC	39.47	-
95	Methylation	REVPPLGRGVLGRGL CCCCCCCCCCCCCCC	39.47	19584108
100	Methylation	LGRGVLGRGLSANMV CCCCCCCCCCCHHCC	38.42	19584108
100	Dimethylation	LGRGVLGRGLSANMV CCCCCCCCCCCHHCC	38.42	-
144	Symmetric dimethylarginine	GWSRMLGRGSSEVSL HHHHHCCCCCCCEEE	37.55	-
144	Methylation	GWSRMLGRGSSEVSL HHHHHCCCCCCCEEE	37.55	19918066
156	Symmetric dimethylarginine	VSLLPLGRAASSIGR EEEECCCHHHHHHCC	34.36	-
156	Methylation	VSLLPLGRAASSIGR EEEECCCHHHHHHCC	34.36	19918066
163	Dimethylation	RAASSIGRGMDKPPS HHHHHHCCCCCCCCH	35.28	-
163	Methylation	RAASSIGRGMDKPPS HHHHHHCCCCCCCCH	35.28	19584108
170	Phosphorylation	RGMDKPPSAFGLTAR CCCCCCCHHCCCCCC	44.77	-
189	Phosphorylation	LPQPPALSPTSLHSA CCCCCCCCCCCCCCC	28.39	19060867
191	Phosphorylation	QPPALSPTSLHSADP CCCCCCCCCCCCCCC	40.31	25293948
192	Phosphorylation	PPALSPTSLHSADPP CCCCCCCCCCCCCCC	27.71	25293948
195	Phosphorylation	LSPTSLHSADPPPVL CCCCCCCCCCCCCEE	39.39	25293948
220	Phosphorylation	VKQGSKGTPQSLGLN HHCCCCCCCCHHCCE	23.14	30165576
223	Phosphorylation	GSKGTPQSLGLNLIK CCCCCCCHHCCEEEE	26.13	30165576
361	Phosphorylation	RLQIWPGYAASIRRT CCCCCCCCCEEEEEC	8.56	28978645
364	Phosphorylation	IWPGYAASIRRTDGG CCCCCCEEEEECCCE	14.41	28978645
549	Methylation	TASNELTRWGLSLHK CHHHHHHHHHHHHHC	37.78	19584108
549	Dimethylation	TASNELTRWGLSLHK CHHHHHHHHHHHHHC	37.78	-
706	Phosphorylation	VRTIGQPTRLRSVAQ EEECCCCHHHHHHHH	34.15	21659604
710	Phosphorylation	GQPTRLRSVAQKILL CCCHHHHHHHHHHHH	26.79	21659604

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

Oops, there are no upstream regulatory protein records of PIWL2_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of PIWL2_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 PIWL2_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of PIWL2_MOUSE !!

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Methylation

"Loss of the Mili-interacting Tudor domain-containing protein-1activates transposons and alters the Mili-associated small RNAprofile.";
Reuter M., Chuma S., Tanaka T., Franz T., Stark A., Pillai R.S.;
Nat. Struct. Mol. Biol. 16:639-646(2009).
Cited for: METHYLATION AT ARG-74, SUBCELLULAR LOCATION, AND INTERACTION WITHTDRD1.
PubMed: 19465913

"Proteomic analysis of murine Piwi proteins reveals a role forarginine methylation in specifying interaction with Tudor familymembers.";
Vagin V.V., Wohlschlegel J., Qu J., Jonsson Z., Huang X., Chuma S.,Girard A., Sachidanandam R., Hannon G.J., Aravin A.A.;
Genes Dev. 23:1749-1762(2009).
Cited for: METHYLATION AT ARG-74; ARG-95; ARG-100; ARG-163 AND ARG-549,SUBCELLULAR LOCATION, INTERACTION WITH TDRD1; PRMT5 AND WDR77, ANDMUTAGENESIS OF ARG-9; ARG-39; ARG-45 AND ARG-74.
PubMed: 19584108