| UniProt ID | SMN_MOUSE | |
|---|---|---|
| UniProt AC | P97801 | |
| Protein Name | Survival motor neuron protein | |
| Gene Name | Smn1 | |
| Organism | Mus musculus (Mouse). | |
| Sequence Length | 288 | |
| Subcellular Localization | Nucleus, gem . Nucleus, Cajal body . Cytoplasm . Cytoplasmic granule . Perikaryon . Cell projection . Cytoplasm, myofibril, sarcomere, Z line . Colocalizes with actin and at the Z-line of skeletal muscle (PubMed:17353360). Under stress conditions col | |
| Protein Description | The SMN complex plays a catalyst role in the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. Thereby, plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP. In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the assembly of the core snRNP. Dissociation by the SMN complex of CLNS1A from the trapped Sm proteins and their transfer to an SMN-Sm complex triggers the assembly of core snRNPs and their transport to the nucleus. Ensures the correct splicing of U12 intron-containing genes that may be important for normal motor and proprioceptive neurons development. Also required for resolving RNA-DNA hybrids created by RNA polymerase II, that form R-loop in transcription terminal regions, an important step in proper transcription termination. May also play a role in the metabolism of small nucleolar ribonucleoprotein (snoRNPs).. | |
| Protein Sequence | MAMGSGGAGSEQEDTVLFRRGTGQSDDSDIWDDTALIKAYDKAVASFKHALKNGDICETPDKPKGTARRKPAKKNKSQKKNATTPLKQWKVGDKCSAVWSEDGCIYPATITSIDFKRETCVVVYTGYGNREEQNLSDLLSPTCEVANSTEQNTQENESQVSTDDSEHSSRSLRSKAHSKSKAAPWTSFLPPPPPMPGSGLGPGKPGLKFNGPPPPPPLPPPPFLPCWMPPFPSGPPIIPPPPPISPDCLDDTDALGSMLISWYMSGYHTGYYMGFRQNKKEGKCSHTN | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 5 | Phosphorylation | ---MAMGSGGAGSEQ ---CCCCCCCCCCCC | 22.44 | 23527152 | |
| 10 | Phosphorylation | MGSGGAGSEQEDTVL CCCCCCCCCCCCCEE | 35.26 | 23527152 | |
| 15 | Phosphorylation | AGSEQEDTVLFRRGT CCCCCCCCEEEECCC | 20.53 | 27742792 | |
| 22 | Phosphorylation | TVLFRRGTGQSDDSD CEEEECCCCCCCCCC | 30.18 | 24925903 | |
| 25 | Phosphorylation | FRRGTGQSDDSDIWD EECCCCCCCCCCCCC | 44.74 | 24925903 | |
| 28 | Phosphorylation | GTGQSDDSDIWDDTA CCCCCCCCCCCCHHH | 35.67 | 24925903 | |
| 34 | Phosphorylation | DSDIWDDTALIKAYD CCCCCCHHHHHHHHH | 22.38 | 24925903 | |
| 42 | Acetylation | ALIKAYDKAVASFKH HHHHHHHHHHHHHHH | 31.89 | 23806337 | |
| 59 | Phosphorylation | KNGDICETPDKPKGT HCCCCCCCCCCCCCC | 32.17 | 26824392 | |
| 66 | Phosphorylation | TPDKPKGTARRKPAK CCCCCCCCCCCCCCC | 24.10 | - | |
| 83 | Phosphorylation | KSQKKNATTPLKQWK HHHCCCCCCCHHHCC | 38.04 | 25266776 | |
| 84 | Phosphorylation | SQKKNATTPLKQWKV HHCCCCCCCHHHCCC | 24.98 | 27149854 | |
| 140 | Phosphorylation | QNLSDLLSPTCEVAN CCHHHHHCCCCHHCC | 26.01 | 25293948 | |
| 142 | Phosphorylation | LSDLLSPTCEVANST HHHHHCCCCHHCCCC | 20.23 | 25293948 | |
| 148 | Phosphorylation | PTCEVANSTEQNTQE CCCHHCCCCCCCCCC | 24.47 | 25293948 | |
| 149 | Phosphorylation | TCEVANSTEQNTQEN CCHHCCCCCCCCCCC | 41.20 | 25293948 | |
| 153 | Phosphorylation | ANSTEQNTQENESQV CCCCCCCCCCCCCCC | 36.63 | 25293948 | |
| 158 | Phosphorylation | QNTQENESQVSTDDS CCCCCCCCCCCCCCC | 47.68 | 25293948 | |
| 161 | Phosphorylation | QENESQVSTDDSEHS CCCCCCCCCCCCHHH | 20.62 | 25293948 | |
| 162 | Phosphorylation | ENESQVSTDDSEHSS CCCCCCCCCCCHHHH | 44.99 | 25293948 | |
| 165 | Phosphorylation | SQVSTDDSEHSSRSL CCCCCCCCHHHHHHH | 39.76 | 25293948 | |
| 168 | Phosphorylation | STDDSEHSSRSLRSK CCCCCHHHHHHHHHH | 24.32 | 25293948 | |
| 169 | Phosphorylation | TDDSEHSSRSLRSKA CCCCHHHHHHHHHHH | 28.00 | 25293948 | |
| 204 | Ubiquitination | GSGLGPGKPGLKFNG CCCCCCCCCCCCCCC | 38.76 | - |
| 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 SMN_MOUSE !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SMN_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 SMN_MOUSE !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| 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-28, AND MASSSPECTROMETRY. | |
| "Large-scale phosphorylation analysis of mouse liver."; Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25 AND SER-28, 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-25 AND SER-28, AND MASSSPECTROMETRY. | |
