UniProt ID | MCRS1_MOUSE | |
---|---|---|
UniProt AC | Q99L90 | |
Protein Name | Microspherule protein 1 | |
Gene Name | Mcrs1 | |
Organism | Mus musculus (Mouse). | |
Sequence Length | 462 | |
Subcellular Localization | Nucleus . Nucleus, nucleolus . Cytoplasm . In microspherules in the nucleolus. | |
Protein Description | Modulates the transcription repressor activity of DAXX by recruiting it to the nucleolus. As part of the NSL complex it may be involved in acetylation of nucleosomal histone H4 on several lysine residues. Putative regulatory component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA replication and probably DNA repair. May also be an inhibitor of TERT telomerase activity. Binds to G-quadruplex structures in mRNA. Binds to RNA homopolymer poly(G) and poly(U).. | |
Protein Sequence | MDKDSQGLLDSSLMASGTASRSEDEESLAGQKRASSQALGTIPKRRSSSRFIKRKKFDDELVESSLAKSSTRVKGAGGVESGRCSGSEPSSSEKKKVSKAPSTPVPPSPAPTPGLTKRVKKSKQPLQVTKDLGRWKPADDLLLINAVLQTNDLTSVHLGVKFSCRFTLREVQERWYALLYDPVISKLACQAMRQLHPEAIAAIQSKALFSKAEEQLLSKVGSSSQPTLETFQDLLHTHPDAFYLARTAKALQAHWQLMKQYYLLEDQTVQPLPKGDQVLNFSDAEDLIDDSKLKDMRDEVLEHELTVADRRQKREIRQLEQELHKWQVLVDSITGMGSPDFDNQTLAVLRGRMVRYLMRSREITLGRATKDNQIDVDLSLEGPAWKISRKQGVIKLKNNGDFFIANEGRRPIYIDGRPVLCGSKWRLSNNSVVEIASLRFVFLINQDLIALIRAEAAKITPQ | |
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 |
---|---|---|---|---|---|
1 | Acetylation | -------MDKDSQGL -------CCCCCHHC | 15.13 | - | |
9 | Phosphorylation | DKDSQGLLDSSLMAS CCCCHHCCCHHHHHC | 8.41 | 24719451 | |
11 | Phosphorylation | DSQGLLDSSLMASGT CCHHCCCHHHHHCCC | 25.91 | 26643407 | |
12 | Phosphorylation | SQGLLDSSLMASGTA CHHCCCHHHHHCCCC | 23.10 | 26643407 | |
16 | Phosphorylation | LDSSLMASGTASRSE CCHHHHHCCCCCCCC | 23.78 | 23429704 | |
18 | Phosphorylation | SSLMASGTASRSEDE HHHHHCCCCCCCCCH | 20.97 | 26643407 | |
20 | Phosphorylation | LMASGTASRSEDEES HHHCCCCCCCCCHHH | 35.86 | 23429704 | |
22 | Phosphorylation | ASGTASRSEDEESLA HCCCCCCCCCHHHHH | 47.07 | 28973931 | |
27 | Phosphorylation | SRSEDEESLAGQKRA CCCCCHHHHHHHHHH | 22.82 | 26643407 | |
32 | Acetylation | EESLAGQKRASSQAL HHHHHHHHHHHHHHH | 49.35 | 7676593 | |
35 | Phosphorylation | LAGQKRASSQALGTI HHHHHHHHHHHHCCC | 27.32 | 28066266 | |
36 | Phosphorylation | AGQKRASSQALGTIP HHHHHHHHHHHCCCC | 20.63 | 28066266 | |
41 | Phosphorylation | ASSQALGTIPKRRSS HHHHHHCCCCCCCCC | 34.65 | 29899451 | |
64 | Phosphorylation | FDDELVESSLAKSST CCHHHHHHHHHCCCC | 24.15 | 22418434 | |
70 | Phosphorylation | ESSLAKSSTRVKGAG HHHHHCCCCCCCCCC | 21.37 | 22418434 | |
71 | Phosphorylation | SSLAKSSTRVKGAGG HHHHCCCCCCCCCCC | 46.72 | 22418434 | |
81 | Phosphorylation | KGAGGVESGRCSGSE CCCCCCCCCCCCCCC | 29.18 | 30635358 | |
85 | Phosphorylation | GVESGRCSGSEPSSS CCCCCCCCCCCCCHH | 43.95 | 25266776 | |
87 | Phosphorylation | ESGRCSGSEPSSSEK CCCCCCCCCCCHHHC | 30.00 | 25266776 | |
90 | Phosphorylation | RCSGSEPSSSEKKKV CCCCCCCCHHHCCCC | 42.31 | 30635358 | |
91 | Phosphorylation | CSGSEPSSSEKKKVS CCCCCCCHHHCCCCC | 53.91 | 30635358 | |
92 | Phosphorylation | SGSEPSSSEKKKVSK CCCCCCHHHCCCCCC | 58.74 | 30635358 | |
102 | Phosphorylation | KKVSKAPSTPVPPSP CCCCCCCCCCCCCCC | 50.64 | 21082442 | |
103 | Phosphorylation | KVSKAPSTPVPPSPA CCCCCCCCCCCCCCC | 27.52 | 26824392 | |
108 | Phosphorylation | PSTPVPPSPAPTPGL CCCCCCCCCCCCCCC | 27.85 | 21082442 | |
112 | Phosphorylation | VPPSPAPTPGLTKRV CCCCCCCCCCCCCCH | 31.90 | 25266776 | |
116 | Phosphorylation | PAPTPGLTKRVKKSK CCCCCCCCCCHHCCC | 23.79 | 29176673 | |
123 | Acetylation | TKRVKKSKQPLQVTK CCCHHCCCCCCEEEC | 65.89 | 23806337 | |
130 | Acetylation | KQPLQVTKDLGRWKP CCCCEEECCCCCCCC | 52.69 | 23806337 | |
268 | Phosphorylation | YYLLEDQTVQPLPKG HHCCCCCEECCCCCC | 33.17 | 23984901 | |
282 | Phosphorylation | GDQVLNFSDAEDLID CCEEECCCCHHHHCC | 34.53 | 27087446 | |
291 | Phosphorylation | AEDLIDDSKLKDMRD HHHHCCHHHHHHHHH | 35.82 | 25619855 |
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 MCRS1_MOUSE !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of MCRS1_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 MCRS1_MOUSE !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of MCRS1_MOUSE !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"The phagosomal proteome in interferon-gamma-activated macrophages."; Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.; Immunity 30:143-154(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-282, AND MASSSPECTROMETRY. | |
"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry."; Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.; J. Proteome Res. 6:250-262(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-282, AND MASSSPECTROMETRY. | |
"Phosphoproteomic analysis of the developing mouse brain."; Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.; Mol. Cell. Proteomics 3:1093-1101(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-282, AND MASSSPECTROMETRY. |