UniProt ID | MEP50_MOUSE | |
---|---|---|
UniProt AC | Q99J09 | |
Protein Name | Methylosome protein 50 | |
Gene Name | Wdr77 | |
Organism | Mus musculus (Mouse). | |
Sequence Length | 342 | |
Subcellular Localization | Nucleus . Cytoplasm . | |
Protein Description | Non-catalytic component of the methylosome complex, composed of PRMT5, WDR77 and CLNS1A, which modifies specific arginines to dimethylarginines in several spliceosomal Sm proteins and histones. This modification targets Sm proteins to the survival of motor neurons (SMN) complex for assembly into small nuclear ribonucleoprotein core particles. Might play a role in transcription regulation. The methylosome complex also methylates the Piwi proteins (PIWIL1, PIWIL2 and PIWIL4), methylation of Piwi proteins being required for the interaction with Tudor domain-containing proteins and subsequent localization to the meiotic nuage. [PubMed: 19584108] | |
Protein Sequence | MRKDTPPPLVPPAAREWNLPPNAPACMERQLEAARYRSDGSLLLGVSSLSGRCWVGSLWFFKDPSAAPNEGFCSAGVQTEAGVADLTWVGDKGILVASDSGAVELWELDENETLIVSKFCKYEHDDIVSTVTVLSSGTQAVSGSKDCCIKIWDLAQQVSLNSYRAHAGQVTCVAASPHKDSVFLSCSEDSRILLWDTRCPKPASQMACNASGYLPTALAWHPQQSEVFVFGDENGSVSLVDTKNASCTLSSAVHSQGVTRLVFSPHSVPLLTSLSEDCSLAVLDSSLSEVFRSRAHRDFVRDATWSPLNHSLLTTVGWDHQVIHHVVPLEPLPNPGPDSVVE | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
|
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
5 | Phosphorylation | ---MRKDTPPPLVPP ---CCCCCCCCCCCC | 40.50 | 26824392 | |
26 | Glutathionylation | LPPNAPACMERQLEA CCCCCCHHHHHHHHH | 2.57 | 24333276 | |
159 | Phosphorylation | WDLAQQVSLNSYRAH HHHHHHHCCCHHHHC | 19.93 | 25168779 | |
162 | Phosphorylation | AQQVSLNSYRAHAGQ HHHHCCCHHHHCCCE | 22.68 | 25168779 | |
163 | Phosphorylation | QQVSLNSYRAHAGQV HHHCCCHHHHCCCEE | 15.67 | 25168779 | |
171 | Phosphorylation | RAHAGQVTCVAASPH HHCCCEEEEEECCCC | 8.06 | 25168779 | |
172 | S-nitrosocysteine | AHAGQVTCVAASPHK HCCCEEEEEECCCCC | 1.74 | - | |
172 | S-nitrosylation | AHAGQVTCVAASPHK HCCCEEEEEECCCCC | 1.74 | 21278135 | |
176 | Phosphorylation | QVTCVAASPHKDSVF EEEEEECCCCCCCEE | 20.14 | 25168779 | |
247 | Glutathionylation | VDTKNASCTLSSAVH EECCCCCEEECHHHH | 4.05 | 24333276 |
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 MEP50_MOUSE !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of MEP50_MOUSE !! |
* 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 MEP50_MOUSE !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of MEP50_MOUSE !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry."; Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.; J. Proteome Res. 7:5314-5326(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-5, AND MASSSPECTROMETRY. |