PPIL2_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PPIL2_MOUSE
• UniProt AC: Q9D787
• Protein Name: RING-type E3 ubiquitin-protein ligase PPIL2 {ECO:0000305}
• Gene Name: Ppil2 {ECO:0000312|MGI:MGI:2447857}
• Organism: Mus musculus (Mouse).
• Sequence Length: 521
• Subcellular Localization: Nucleus .
• Protein Description: Has a ubiquitin-protein ligase activity acting as an E3 ubiquitin protein ligase or as an ubiquitin-ubiquitin ligase promoting elongation of ubiquitin chains on substrates. By mediating 'Lys-48'-linked polyubiquitination of proteins could target them for proteasomal degradation. May also function as a chaperone, playing a role in transport to the cell membrane of BSG/Basigin for instance. Probable inactive PPIase with no peptidyl-prolyl cis-trans isomerase activity..
• Protein Sequence: MGKRQHQKDKMYITCAEYTHFYGGRKPDISQTSFRRLPFDHCSLSLQPFVYPVCTPEGVVFDLLNIVPWLKKYGTNPSTGEKLDGKSLIKLNFAKNSEGQYHCPVLYSVFTDNTHIVAIRTTGNVYTYEAVEQLNIKAKNLRDLLTDEPFSRQDIITLQDPTNLDKFNVSNFFHVKNNMRIIDPDEEKAKQDPSYYLKNTNSETRETLQELYKEFKGDEILAATMRPPEKKKVDQLNAAHYSTGKVSASFTSTAMVPETTHEAAVIDEDVLRYQFVKKKGYVRLHTNKGDLNLELHCDLTPKTCENFIKLCKKQYYDGTIFHRSIRNFVIQGGDPTGTGTGGESFWGKPFKDEFRPNLSHTGRGVLSMANSGPNTNKSQFFITFRSCAYLDKKHTIFGRVVGGFDTLTAMENVESDPKTDRPKEEVLICTTTVFVDPYEEADAQIAQERKKTQHQVDPEAKVKMSQPQPGNQGPQTYRQGVGKYIHPAATKRSAEEEPSTSTATPTAKKRPSRGFGDFSSW

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
86	Ubiquitination	TGEKLDGKSLIKLNF CCCCCCCCEEEEEEE	41.58	-
90	Ubiquitination	LDGKSLIKLNFAKNS CCCCEEEEEEECCCC	42.54	-
195	Phosphorylation	KAKQDPSYYLKNTNS HHHCCCCHHCCCCCH	20.43	29514104
202	Phosphorylation	YYLKNTNSETRETLQ HHCCCCCHHHHHHHH	38.00	25338131
224	Phosphorylation	GDEILAATMRPPEKK CCCEEEEECCCCCCC	14.22	22871156
367	Phosphorylation	HTGRGVLSMANSGPN CCCCCCEEECCCCCC	17.28	26160508
371	Phosphorylation	GVLSMANSGPNTNKS CCEEECCCCCCCCHH	46.20	26160508
375	Phosphorylation	MANSGPNTNKSQFFI ECCCCCCCCHHHEEE	47.35	26160508
378	Phosphorylation	SGPNTNKSQFFITFR CCCCCCHHHEEEEEH	34.00	26160508
383	Phosphorylation	NKSQFFITFRSCAYL CHHHEEEEEHHCEEC	14.08	26160508
483	Acetylation	TYRQGVGKYIHPAAT CHHCCCCCCCCHHHC	38.33	23806337
491	Acetylation	YIHPAATKRSAEEEP CCCHHHCCCCCCCCC	39.36	15630883
493	Phosphorylation	HPAATKRSAEEEPST CHHHCCCCCCCCCCC	41.40	29176673
501	Phosphorylation	AEEEPSTSTATPTAK CCCCCCCCCCCCCCC	22.00	20139300
502	Phosphorylation	EEEPSTSTATPTAKK CCCCCCCCCCCCCCC	34.34	29550500
504	Phosphorylation	EPSTSTATPTAKKRP CCCCCCCCCCCCCCC	22.66	25266776
506	Phosphorylation	STSTATPTAKKRPSR CCCCCCCCCCCCCCC	46.91	29550500

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

Oops, there are no upstream regulatory protein records of PPIL2_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of PPIL2_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 PPIL2_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of PPIL2_MOUSE !!

Drug and Disease Associations

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