| UniProt ID | SMN_HUMAN | |
|---|---|---|
| UniProt AC | Q16637 | |
| Protein Name | Survival motor neuron protein | |
| Gene Name | SMN1 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 294 | |
| 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 (By similarity). Under stress conditions coloc | |
| 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 | MAMSSGGSGGGVPEQEDSVLFRRGTGQSDDSDIWDDTALIKAYDKAVASFKHALKNGDICETSGKPKTTPKRKPAKKNKSQKKNTAASLQQWKVGDKCSAIWSEDGCIYPATIASIDFKRETCVVVYTGYGNREEQNLSDLLSPICEVANNIEQNAQENENESQVSTDESENSRSPGNKSDNIKPKSAPWNSFLPPPPPMPGPRLGPGKPGLKFNGPPPPPPPPPPHLLSCWLPPFPSGPPIIPPPPPICPDSLDDADALGSMLISWYMSGYHTGYYMGFRQNQKEGRCSHSLN | |
| 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 |
|---|---|---|---|---|---|
| 2 | Acetylation | ------MAMSSGGSG ------CCCCCCCCC | 13.43 | 21406692 | |
| 4 | Phosphorylation | ----MAMSSGGSGGG ----CCCCCCCCCCC | 19.12 | 23401153 | |
| 4 (in isoform 2) | Phosphorylation | - | 19.12 | - | |
| 5 | Phosphorylation | ---MAMSSGGSGGGV ---CCCCCCCCCCCC | 33.80 | 23401153 | |
| 5 (in isoform 2) | Phosphorylation | - | 33.80 | - | |
| 8 | Phosphorylation | MAMSSGGSGGGVPEQ CCCCCCCCCCCCCCC | 37.48 | 29255136 | |
| 8 (in isoform 2) | Phosphorylation | - | 37.48 | - | |
| 18 | Phosphorylation | GVPEQEDSVLFRRGT CCCCCCCCEEEECCC | 21.70 | 25159151 | |
| 18 (in isoform 2) | Phosphorylation | - | 21.70 | - | |
| 23 | Methylation | EDSVLFRRGTGQSDD CCCEEEECCCCCCCC | 39.43 | 115917285 | |
| 25 | Phosphorylation | SVLFRRGTGQSDDSD CEEEECCCCCCCCCC | 30.18 | 22167270 | |
| 25 (in isoform 2) | Phosphorylation | - | 30.18 | - | |
| 25 (in isoform 4) | Phosphorylation | - | 30.18 | - | |
| 28 | Phosphorylation | FRRGTGQSDDSDIWD EECCCCCCCCCCCCC | 44.74 | 19664994 | |
| 28 (in isoform 2) | Phosphorylation | - | 44.74 | - | |
| 28 (in isoform 4) | Phosphorylation | - | 44.74 | - | |
| 31 | Phosphorylation | GTGQSDDSDIWDDTA CCCCCCCCCCCCHHH | 35.67 | 22167270 | |
| 31 (in isoform 2) | Phosphorylation | - | 35.67 | - | |
| 31 (in isoform 4) | Phosphorylation | - | 35.67 | - | |
| 37 | Phosphorylation | DSDIWDDTALIKAYD CCCCCCHHHHHHHHH | 22.38 | 30266825 | |
| 37 (in isoform 2) | Phosphorylation | - | 22.38 | - | |
| 41 | Ubiquitination | WDDTALIKAYDKAVA CCHHHHHHHHHHHHH | 41.57 | 21890473 | |
| 41 (in isoform 2) | Ubiquitination | - | 41.57 | 21890473 | |
| 41 (in isoform 1) | Ubiquitination | - | 41.57 | 21890473 | |
| 41 (in isoform 3) | Ubiquitination | - | 41.57 | 21890473 | |
| 41 (in isoform 4) | Ubiquitination | - | 41.57 | 21890473 | |
| 43 | Phosphorylation | DTALIKAYDKAVASF HHHHHHHHHHHHHHH | 16.99 | 28152594 | |
| 45 | Acetylation | ALIKAYDKAVASFKH HHHHHHHHHHHHHHH | 31.89 | 23749302 | |
| 45 | Ubiquitination | ALIKAYDKAVASFKH HHHHHHHHHHHHHHH | 31.89 | - | |
| 45 | 2-Hydroxyisobutyrylation | ALIKAYDKAVASFKH HHHHHHHHHHHHHHH | 31.89 | - | |
| 49 | Phosphorylation | AYDKAVASFKHALKN HHHHHHHHHHHHHHH | 28.38 | 24719451 | |
| 51 | Methylation | DKAVASFKHALKNGD HHHHHHHHHHHHHCC | 26.02 | 44505113 | |
| 51 | Ubiquitination | DKAVASFKHALKNGD HHHHHHHHHHHHHCC | 26.02 | 21890473 | |
| 51 | Acetylation | DKAVASFKHALKNGD HHHHHHHHHHHHHCC | 26.02 | 25953088 | |
| 51 | Sumoylation | DKAVASFKHALKNGD HHHHHHHHHHHHHCC | 26.02 | 28112733 | |
| 51 (in isoform 1) | Ubiquitination | - | 26.02 | 21890473 | |
| 51 (in isoform 2) | Ubiquitination | - | 26.02 | 21890473 | |
| 51 (in isoform 3) | Ubiquitination | - | 26.02 | 21890473 | |
| 51 (in isoform 4) | Ubiquitination | - | 26.02 | 21890473 | |
| 55 | Methylation | ASFKHALKNGDICET HHHHHHHHHCCCCCC | 60.72 | 115980845 | |
| 55 | Ubiquitination | ASFKHALKNGDICET HHHHHHHHHCCCCCC | 60.72 | - | |
| 55 | Acetylation | ASFKHALKNGDICET HHHHHHHHHCCCCCC | 60.72 | 26051181 | |
| 62 | Phosphorylation | KNGDICETSGKPKTT HHCCCCCCCCCCCCC | 38.07 | 23927012 | |
| 63 | Phosphorylation | NGDICETSGKPKTTP HCCCCCCCCCCCCCC | 23.64 | 25159151 | |
| 65 | Acetylation | DICETSGKPKTTPKR CCCCCCCCCCCCCCC | 43.01 | 23749302 | |
| 68 | Phosphorylation | ETSGKPKTTPKRKPA CCCCCCCCCCCCCCC | 57.78 | 23927012 | |
| 69 | Phosphorylation | TSGKPKTTPKRKPAK CCCCCCCCCCCCCCC | 32.70 | 23927012 | |
| 69 (in isoform 2) | Phosphorylation | - | 32.70 | - | |
| 80 | Phosphorylation | KPAKKNKSQKKNTAA CCCCCCHHHHCCHHH | 57.54 | 22817900 | |
| 83 | Ubiquitination | KKNKSQKKNTAASLQ CCCHHHHCCHHHHHH | 52.47 | - | |
| 85 | Phosphorylation | NKSQKKNTAASLQQW CHHHHCCHHHHHHHH | 32.26 | 20873877 | |
| 88 | Phosphorylation | QKKNTAASLQQWKVG HHCCHHHHHHHHHCC | 25.01 | 20873877 | |
| 93 | Ubiquitination | AASLQQWKVGDKCSA HHHHHHHHCCCCCCE | 31.81 | - | |
| 93 | Acetylation | AASLQQWKVGDKCSA HHHHHHHHCCCCCCE | 31.81 | 26051181 | |
| 97 | Acetylation | QQWKVGDKCSAIWSE HHHHCCCCCCEEECC | 24.94 | 25953088 | |
| 109 | Phosphorylation | WSEDGCIYPATIASI ECCCCCCCEEEEEEE | 7.29 | 22817900 | |
| 119 | Acetylation | TIASIDFKRETCVVV EEEEEEECCCEEEEE | 45.64 | 69239 | |
| 127 | Phosphorylation | RETCVVVYTGYGNRE CCEEEEEEECCCCHH | 5.26 | 28152594 | |
| 128 | Phosphorylation | ETCVVVYTGYGNREE CEEEEEEECCCCHHH | 16.59 | 28152594 | |
| 130 | Phosphorylation | CVVVYTGYGNREEQN EEEEEECCCCHHHCC | 11.92 | 28152594 | |
| 139 | Phosphorylation | NREEQNLSDLLSPIC CHHHCCHHHHHHHHH | 33.49 | 20873877 | |
| 143 | Phosphorylation | QNLSDLLSPICEVAN CCHHHHHHHHHHHHH | 21.37 | 20873877 | |
| 163 | Phosphorylation | AQENENESQVSTDES HHHCCCCCCCCCCCC | 47.68 | 27251275 | |
| 166 | Phosphorylation | NENESQVSTDESENS CCCCCCCCCCCCCCC | 23.62 | 25137130 | |
| 167 | Phosphorylation | ENESQVSTDESENSR CCCCCCCCCCCCCCC | 44.95 | 25137130 | |
| 170 | Phosphorylation | SQVSTDESENSRSPG CCCCCCCCCCCCCCC | 44.91 | 25137130 | |
| 173 | Phosphorylation | STDESENSRSPGNKS CCCCCCCCCCCCCCC | 30.04 | 20873877 | |
| 175 | Phosphorylation | DESENSRSPGNKSDN CCCCCCCCCCCCCCC | 36.66 | 23663014 | |
| 179 | Ubiquitination | NSRSPGNKSDNIKPK CCCCCCCCCCCCCCC | 66.17 | - | |
| 180 | Phosphorylation | SRSPGNKSDNIKPKS CCCCCCCCCCCCCCC | 39.63 | 23663014 | |
| 184 | Ubiquitination | GNKSDNIKPKSAPWN CCCCCCCCCCCCCHH | 53.28 | - | |
| 186 | Ubiquitination | KSDNIKPKSAPWNSF CCCCCCCCCCCHHHC | 55.00 | 21890473 | |
| 186 (in isoform 1) | Ubiquitination | - | 55.00 | 21890473 | |
| 186 (in isoform 2) | Ubiquitination | - | 55.00 | 21890473 | |
| 186 (in isoform 3) | Ubiquitination | - | 55.00 | 21890473 | |
| 186 (in isoform 4) | Ubiquitination | - | 55.00 | 21890473 | |
| 187 | Phosphorylation | SDNIKPKSAPWNSFL CCCCCCCCCCHHHCC | 48.36 | 21712546 | |
| 192 | Phosphorylation | PKSAPWNSFLPPPPP CCCCCHHHCCCCCCC | 25.04 | 21712546 | |
| 204 | Methylation | PPPMPGPRLGPGKPG CCCCCCCCCCCCCCC | 59.18 | 54559453 | |
| 209 | Ubiquitination | GPRLGPGKPGLKFNG CCCCCCCCCCCCCCC | 38.76 | - | |
| 209 | Acetylation | GPRLGPGKPGLKFNG CCCCCCCCCCCCCCC | 38.76 | 26051181 | |
| 209 | Sumoylation | GPRLGPGKPGLKFNG CCCCCCCCCCCCCCC | 38.76 | 28112733 | |
| 221 (in isoform 4) | Phosphorylation | - | 60.86 | 24043423 | |
| 230 (in isoform 4) | Phosphorylation | - | 15.03 | 24043423 | |
| 234 (in isoform 4) | Phosphorylation | - | 12.18 | 24043423 | |
| 236 (in isoform 4) | Phosphorylation | - | 7.69 | 24043423 | |
| 238 (in isoform 4) | Phosphorylation | - | 65.40 | 24043423 | |
| 240 (in isoform 4) | Phosphorylation | - | 22.66 | 24043423 | |
| 242 (in isoform 4) | Phosphorylation | - | 9.21 | 24043423 | |
| 244 (in isoform 4) | Phosphorylation | - | 35.74 | 24043423 | |
| 245 (in isoform 4) | Phosphorylation | - | 43.55 | 24043423 | |
| 253 (in isoform 3) | Phosphorylation | - | 20.88 | 24043423 | |
| 262 (in isoform 3) | Phosphorylation | - | 15.97 | 24043423 | |
| 266 (in isoform 3) | Phosphorylation | - | 14.27 | 24043423 | |
| 268 (in isoform 3) | Phosphorylation | - | 3.74 | 24043423 | |
| 270 (in isoform 3) | Phosphorylation | - | 22.09 | 24043423 | |
| 272 (in isoform 3) | Phosphorylation | - | 6.73 | 24043423 | |
| 274 (in isoform 3) | Phosphorylation | - | 20.56 | 24043423 | |
| 276 (in isoform 3) | Phosphorylation | - | 7.45 | 24043423 | |
| 277 (in isoform 3) | Phosphorylation | - | 7.66 | 24043423 | |
| 292 | Phosphorylation | KEGRCSHSLN----- CCCCCCCCCC----- | 17.20 | 25849741 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
| 4 | S | Phosphorylation | Kinase | PKACA | P17612 | PSP |
| 4 | S | Phosphorylation | Kinase | PKA | - | Uniprot |
| 5 | S | Phosphorylation | Kinase | PKACA | P17612 | PSP |
| 5 | S | Phosphorylation | Kinase | PKA | - | Uniprot |
| 8 | S | Phosphorylation | Kinase | PKACA | P17612 | PSP |
| 8 | S | Phosphorylation | Kinase | PKA | - | Uniprot |
| 85 | T | Phosphorylation | Kinase | PKACA | P17612 | PSP |
| 85 | T | Phosphorylation | Kinase | PKA | - | Uniprot |
| 187 | S | Phosphorylation | Kinase | PKACA | P17612 | PSP |
| 187 | S | Phosphorylation | Kinase | PKA | - | Uniprot |
| - | K | Ubiquitination | E3 ubiquitin ligase | UCHL1 | P09936 | PMID:20713032 |
| - | K | Ubiquitination | E3 ubiquitin ligase | MIB1 | Q86YT6 | PMID:23615451 |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SMN_HUMAN !! | ||||||
* 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_HUMAN !! | ||||||
| Kegg Disease | ||||||
|---|---|---|---|---|---|---|
| There are no disease associations of PTM sites. | ||||||
| There are no disease associations of PTM sites. | ||||||
| OMIM Disease | ||||||
| 253300 | Spinal muscular atrophy 1 (SMA1) | |||||
| 253550 | Spinal muscular atrophy 2 (SMA2) | |||||
| 253400 | Spinal muscular atrophy 3 (SMA3) | |||||
| 271150 | Spinal muscular atrophy 4 (SMA4) | |||||
| Kegg Drug | ||||||
| There are no disease associations of PTM sites. | ||||||
| There are no disease associations of PTM sites. | ||||||
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Acetylation | |
| Reference | PubMed |
| "Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT THR-25; SER-28 AND SER-31, AND MASS SPECTROMETRY. | |
| Phosphorylation | |
| Reference | PubMed |
| "Identification of the phosphorylation sites in the survival motorneuron protein by protein kinase A."; Wu C.Y., Curtis A., Choi Y.S., Maeda M., Xu M.J., Berg A., Joneja U.,Mason R.W., Lee K.H., Wang W.; Biochim. Biophys. Acta 1814:1134-1139(2011). Cited for: PHOSPHORYLATION AT SER-4; SER-5; SER-8; THR-85 AND SER-187 BY PKA. | |
| "Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-25; SER-28 AND SER-31,AND MASS SPECTROMETRY. | |
| "Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4; SER-5; SER-8; THR-25;SER-28 AND SER-31, AND MASS SPECTROMETRY. | |
| "Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT THR-25; SER-28 AND SER-31, AND MASS SPECTROMETRY. | |
| "A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-25; SER-28 AND SER-31,AND MASS SPECTROMETRY. | |
| "Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8; THR-25; SER-28 ANDSER-31, AND MASS SPECTROMETRY. | |
| "Toward a global characterization of the phosphoproteome in prostatecancer cells: identification of phosphoproteins in the LNCaP cellline."; Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.; Electrophoresis 28:2027-2034(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31, AND MASSSPECTROMETRY. | |
| "Phosphoproteome analysis of the human mitotic spindle."; Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.; Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28, AND MASSSPECTROMETRY. | |
| "Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4; SER-5; SER-8; SER-28AND SER-31, AND MASS SPECTROMETRY. | |
