UniProt ID | SODC_HUMAN | |
---|---|---|
UniProt AC | P00441 | |
Protein Name | Superoxide dismutase [Cu-Zn] | |
Gene Name | SOD1 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 154 | |
Subcellular Localization |
Cytoplasm . Mitochondrion . Nucleus . Predominantly cytoplasmic the pathogenic variants ALS1 Arg-86 and Ala-94 gradually aggregates and accumulates in mitochondria. |
|
Protein Description | Destroys radicals which are normally produced within the cells and which are toxic to biological systems.. | |
Protein Sequence | MATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEERHVGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ | |
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 |
---|---|---|---|---|---|
2 | Acetylation | ------MATKAVCVL ------CCCEEEEEE | 20.15 | 25944712 | |
3 | Phosphorylation | -----MATKAVCVLK -----CCCEEEEEEC | 20.45 | 19299510 | |
4 | Succinylation | ----MATKAVCVLKG ----CCCEEEEEECC | 29.32 | - | |
4 | Ubiquitination | ----MATKAVCVLKG ----CCCEEEEEECC | 29.32 | - | |
4 | Glycation | ----MATKAVCVLKG ----CCCEEEEEECC | 29.32 | - | |
4 | 2-Hydroxyisobutyrylation | ----MATKAVCVLKG ----CCCEEEEEECC | 29.32 | - | |
4 | Succinylation | ----MATKAVCVLKG ----CCCEEEEEECC | 29.32 | - | |
4 | Acetylation | ----MATKAVCVLKG ----CCCEEEEEECC | 29.32 | 25953088 | |
7 | S-nitrosocysteine | -MATKAVCVLKGDGP -CCCEEEEEECCCCC | 3.38 | - | |
7 | Glutathionylation | -MATKAVCVLKGDGP -CCCEEEEEECCCCC | 3.38 | 22555962 | |
7 | S-nitrosylation | -MATKAVCVLKGDGP -CCCEEEEEECCCCC | 3.38 | 19483679 | |
7 | S-palmitoylation | -MATKAVCVLKGDGP -CCCEEEEEECCCCC | 3.38 | 23760509 | |
10 | Succinylation | TKAVCVLKGDGPVQG CEEEEEECCCCCEEE | 34.26 | 23954790 | |
10 | Ubiquitination | TKAVCVLKGDGPVQG CEEEEEECCCCCEEE | 34.26 | 21890473 | |
10 | 2-Hydroxyisobutyrylation | TKAVCVLKGDGPVQG CEEEEEECCCCCEEE | 34.26 | - | |
10 | Glycation | TKAVCVLKGDGPVQG CEEEEEECCCCCEEE | 34.26 | - | |
10 | Succinylation | TKAVCVLKGDGPVQG CEEEEEECCCCCEEE | 34.26 | - | |
10 | Acetylation | TKAVCVLKGDGPVQG CEEEEEECCCCCEEE | 34.26 | 23954790 | |
24 | Ubiquitination | GIINFEQKESNGPVK EEEEEEECCCCCCEE | 56.78 | - | |
24 | Acetylation | GIINFEQKESNGPVK EEEEEEECCCCCCEE | 56.78 | 23236377 | |
26 | Phosphorylation | INFEQKESNGPVKVW EEEEECCCCCCEEEE | 54.87 | 26437602 | |
31 | Ubiquitination | KESNGPVKVWGSIKG CCCCCCEEEEEEEEC | 35.09 | 21890473 | |
31 | Glycation | KESNGPVKVWGSIKG CCCCCCEEEEEEEEC | 35.09 | - | |
35 | Phosphorylation | GPVKVWGSIKGLTEG CCEEEEEEEECHHCC | 12.86 | 23312004 | |
37 | Glycation | VKVWGSIKGLTEGLH EEEEEEEECHHCCCC | 49.95 | - | |
37 | Ubiquitination | VKVWGSIKGLTEGLH EEEEEEEECHHCCCC | 49.95 | - | |
40 | Phosphorylation | WGSIKGLTEGLHGFH EEEEECHHCCCCEEE | 36.35 | - | |
59 | Phosphorylation | GDNTAGCTSAGPHFN CCCCCCCCCCCCCCC | 22.24 | 19299510 | |
60 | Phosphorylation | DNTAGCTSAGPHFNP CCCCCCCCCCCCCCC | 34.99 | 19299510 | |
69 | Phosphorylation | GPHFNPLSRKHGGPK CCCCCCCCHHCCCCC | 40.31 | 24275569 | |
71 | Acetylation | HFNPLSRKHGGPKDE CCCCCCHHCCCCCCC | 43.13 | 90007 | |
71 | Ubiquitination | HFNPLSRKHGGPKDE CCCCCCHHCCCCCCC | 43.13 | - | |
76 | Succinylation | SRKHGGPKDEERHVG CHHCCCCCCCCCCCC | 79.59 | 23954790 | |
76 | Sumoylation | SRKHGGPKDEERHVG CHHCCCCCCCCCCCC | 79.59 | - | |
76 | Ubiquitination | SRKHGGPKDEERHVG CHHCCCCCCCCCCCC | 79.59 | - | |
76 | Sumoylation | SRKHGGPKDEERHVG CHHCCCCCCCCCCCC | 79.59 | - | |
80 | Methylation | GGPKDEERHVGDLGN CCCCCCCCCCCCCCC | 27.95 | 115917473 | |
89 | Phosphorylation | VGDLGNVTADKDGVA CCCCCCCCCCCCCCE | 32.89 | 28450419 | |
92 | Ubiquitination | LGNVTADKDGVADVS CCCCCCCCCCCEEEE | 54.65 | - | |
92 | Succinylation | LGNVTADKDGVADVS CCCCCCCCCCCEEEE | 54.65 | - | |
92 | Succinylation | LGNVTADKDGVADVS CCCCCCCCCCCEEEE | 54.65 | - | |
99 | Phosphorylation | KDGVADVSIEDSVIS CCCCEEEEEECCEEE | 22.32 | 25159151 | |
103 | Phosphorylation | ADVSIEDSVISLSGD EEEEEECCEEEEECC | 14.46 | 25022875 | |
106 | Phosphorylation | SIEDSVISLSGDHCI EEECCEEEEECCEEE | 17.83 | 28192239 | |
108 | Phosphorylation | EDSVISLSGDHCIIG ECCEEEEECCEEEEC | 35.07 | 27251789 | |
112 | S-palmitoylation | ISLSGDHCIIGRTLV EEEECCEEEECCEEE | 2.63 | 28120938 | |
112 | Glutathionylation | ISLSGDHCIIGRTLV EEEECCEEEECCEEE | 2.63 | 22833525 | |
123 | Glycation | RTLVVHEKADDLGKG CEEEEEECHHHCCCC | 42.09 | - | |
123 | Ubiquitination | RTLVVHEKADDLGKG CEEEEEECHHHCCCC | 42.09 | 19608861 | |
123 | Succinylation | RTLVVHEKADDLGKG CEEEEEECHHHCCCC | 42.09 | 19608861 | |
123 | Succinylation | RTLVVHEKADDLGKG CEEEEEECHHHCCCC | 42.09 | - | |
123 | Malonylation | RTLVVHEKADDLGKG CEEEEEECHHHCCCC | 42.09 | 26320211 | |
123 | 2-Hydroxyisobutyrylation | RTLVVHEKADDLGKG CEEEEEECHHHCCCC | 42.09 | - | |
123 | Acetylation | RTLVVHEKADDLGKG CEEEEEECHHHCCCC | 42.09 | 19608861 | |
129 | Glycation | EKADDLGKGGNEEST ECHHHCCCCCCCCCC | 71.58 | - | |
129 | Acetylation | EKADDLGKGGNEEST ECHHHCCCCCCCCCC | 71.58 | 26051181 | |
129 | Ubiquitination | EKADDLGKGGNEEST ECHHHCCCCCCCCCC | 71.58 | - | |
135 | Phosphorylation | GKGGNEESTKTGNAG CCCCCCCCCCCCCHH | 29.08 | 28258704 | |
136 | Phosphorylation | KGGNEESTKTGNAGS CCCCCCCCCCCCHHH | 35.59 | 28258704 | |
137 | Acetylation | GGNEESTKTGNAGSR CCCCCCCCCCCHHHH | 64.81 | 26051181 | |
137 | Succinylation | GGNEESTKTGNAGSR CCCCCCCCCCCHHHH | 64.81 | - | |
137 | Ubiquitination | GGNEESTKTGNAGSR CCCCCCCCCCCHHHH | 64.81 | - | |
137 | Succinylation | GGNEESTKTGNAGSR CCCCCCCCCCCHHHH | 64.81 | - | |
138 | Phosphorylation | GNEESTKTGNAGSRL CCCCCCCCCCHHHHE | 35.44 | 26437602 | |
143 | Phosphorylation | TKTGNAGSRLACGVI CCCCCHHHHEEEEEE | 23.01 | 26437602 | |
144 | Methylation | KTGNAGSRLACGVIG CCCCHHHHEEEEEEE | 25.95 | 115917469 | |
147 | Glutathionylation | NAGSRLACGVIGIAQ CHHHHEEEEEEEEEC | 5.46 | 22555962 | |
147 | S-palmitoylation | NAGSRLACGVIGIAQ CHHHHEEEEEEEEEC | 5.46 | 26865113 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
40 | T | Phosphorylation | Kinase | MTOR | P42345 | PSP |
- | K | Ubiquitination | E3 ubiquitin ligase | AMFR | Q9UKV5 | PMID:19661182 |
- | K | Ubiquitination | E3 ubiquitin ligase | MARCHF5 | Q9NX47 | PMID:19741096 |
- | K | Ubiquitination | E3 ubiquitin ligase | RNF19A | Q9NV58 | PMID:12145308 |
- | K | Ubiquitination | E3 ubiquitin ligase | STUB1 | Q9UNE7 | PMID:15198682 |
- | K | Ubiquitination | E3 ubiquitin ligase | MARCHF8 | Q5T0T0 | PMID:22199232 |
* 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 SODC_HUMAN !! |
Kegg Disease | ||||||
---|---|---|---|---|---|---|
There are no disease associations of PTM sites. | ||||||
OMIM Disease | ||||||
105400 | Amyotrophic lateral sclerosis 1 (ALS1) | |||||
Kegg Drug | ||||||
There are no disease associations of PTM sites. | ||||||
DrugBank | ||||||
There are no disease associations of PTM sites. |
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Acetylation | |
Reference | PubMed |
"Atomic structures of wild-type and thermostable mutant recombinanthuman Cu,Zn superoxide dismutase."; Parge H.E., Hallewell R.A., Tainer J.A.; Proc. Natl. Acad. Sci. U.S.A. 89:6109-6113(1992). Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS). | |
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-123, AND MASS SPECTROMETRY. | |
Phosphorylation | |
Reference | PubMed |
"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 SER-99, AND MASSSPECTROMETRY. |