RN126_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RN126_MOUSE
• UniProt AC: Q91YL2
• Protein Name: E3 ubiquitin-protein ligase RNF126 {ECO:0000305}
• Gene Name: Rnf126 {ECO:0000312|MGI:MGI:1917544}
• Organism: Mus musculus (Mouse).
• Sequence Length: 313
• Subcellular Localization: Cytoplasm . Nucleus .
• Protein Description: E3 ubiquitin-protein ligase that mediates ubiquitination oF target proteins (By similarity). Depending on the associated E2 ligase, mediates 'Lys-48'- and 'Lys-63'-linked polyubiquitination of substrates. [PubMed: 23418353 Part of a BAG6-dependent quality control process ensuring that proteins of the secretory pathway that are mislocalized to the cytosol are degraded by the proteasome (By similarity Probably acts by providing the ubiquitin ligase activity associated with the BAG6 complex and be responsible for ubiquitination of the hydrophobic mislocalized proteins and their targeting to the proteasome (By similarity May also play a role in the endosomal recycling of IGF2R, the cation-independent mannose-6-phosphate receptor (By similarity May play a role in the endosomal sorting and degradation of several membrane receptors including EGFR, FLT3, MET and CXCR4, by mediating their ubiquitination]
• Protein Sequence: MAEASPQPGRYFCHCCSVEIVPRLPDYICPRCESGFIEELPEETRNTENGSAPSTAPTDQNRQPFENVDQHLFTLPQGYSQFAFGIFDDSFEIPTFPPGAQADDGRDPESRREREHQSRHRYGARQPRARLTARRATGRHEGVPTLEGIIQQLVNGIISPAAVPSLGLGPWGVLHSNPMDYAWGANGLDTIITQLLNQFENTGPPPADKEKIQALPTVPVTEEHVGSGLECPVCKEDYALGESVRQLPCNHLFHDSCIVPWLEQHDSCPVCRKSLTGQNTATNPPGLTGVGFSSSSSSSSSSSPSNENATSNS

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	Acetylation	------MAEASPQPG ------CCCCCCCCC	22.51	-
5	Phosphorylation	---MAEASPQPGRYF ---CCCCCCCCCCEE	18.64	26824392
11	Phosphorylation	ASPQPGRYFCHCCSV CCCCCCCEECEECEE	19.24	23984901
17	Phosphorylation	RYFCHCCSVEIVPRL CEECEECEEEEECCC	28.33	22817900
29	Glutathionylation	PRLPDYICPRCESGF CCCCCCCCCCCCCCC	1.10	24333276
132	Phosphorylation	RQPRARLTARRATGR CCHHHHHHHHHHHCC	16.74	23140645
288	Phosphorylation	ATNPPGLTGVGFSSS CCCCCCCCEEECCCC	35.42	30482847
293	Phosphorylation	GLTGVGFSSSSSSSS CCCEEECCCCCCCCC	24.31	25293948
294	Phosphorylation	LTGVGFSSSSSSSSS CCEEECCCCCCCCCC	31.79	25293948
295	Phosphorylation	TGVGFSSSSSSSSSS CEEECCCCCCCCCCC	32.80	25293948
296	Phosphorylation	GVGFSSSSSSSSSSS EEECCCCCCCCCCCC	35.87	25293948
297	Phosphorylation	VGFSSSSSSSSSSSP EECCCCCCCCCCCCC	35.87	25293948
298	Phosphorylation	GFSSSSSSSSSSSPS ECCCCCCCCCCCCCC	35.87	25293948
299	Phosphorylation	FSSSSSSSSSSSPSN CCCCCCCCCCCCCCC	35.87	25293948
300	Phosphorylation	SSSSSSSSSSSPSNE CCCCCCCCCCCCCCC	35.87	25293948
301	Phosphorylation	SSSSSSSSSSPSNEN CCCCCCCCCCCCCCC	36.46	25293948
302	Phosphorylation	SSSSSSSSSPSNENA CCCCCCCCCCCCCCC	48.49	25293948
303	Phosphorylation	SSSSSSSSPSNENAT CCCCCCCCCCCCCCC	34.00	30482847
305	Phosphorylation	SSSSSSPSNENATSN CCCCCCCCCCCCCCC	59.74	25293948
310	Phosphorylation	SPSNENATSNS---- CCCCCCCCCCC----	39.77	25293948
311	Phosphorylation	PSNENATSNS----- CCCCCCCCCC-----	32.44	25293948
313	Phosphorylation	NENATSNS------- CCCCCCCC-------	41.17	25293948

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

Oops, there are no upstream regulatory protein records of RN126_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of RN126_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 RN126_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
XRCC5_HUMAN	XRCC5	physical	27895153
XRCC6_HUMAN	XRCC6	physical	27895153

Drug and Disease Associations

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