UniProt ID | SODC_YEAST | |
---|---|---|
UniProt AC | P00445 | |
Protein Name | Superoxide dismutase [Cu-Zn] | |
Gene Name | SOD1 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 154 | |
Subcellular Localization | Cytoplasm . Mitochondrion intermembrane space . A small percentage (around 1-5 percent) localizes to the mitochondrial intermembrane space. | |
Protein Description | Destroys radicals which are normally produced within the cells and which are toxic to biological systems.. | |
Protein Sequence | MVQAVAVLKGDAGVSGVVKFEQASESEPTTVSYEIAGNSPNAERGFHIHEFGDATNGCVSAGPHFNPFKKTHGAPTDEVRHVGDMGNVKTDENGVAKGSFKDSLIKLIGPTSVVGRSVVIHAGQDDLGKGDTEESLKTGNAGPRPACGVIGLTN | |
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 |
---|---|---|---|---|---|
9 | Ubiquitination | VQAVAVLKGDAGVSG CEEEEEEECCCCEEC | 48.42 | 24961812 | |
15 | Phosphorylation | LKGDAGVSGVVKFEQ EECCCCEECEEEEEE | 25.59 | 22369663 | |
19 | Sumoylation | AGVSGVVKFEQASES CCEECEEEEEECCCC | 40.55 | - | |
19 | Sumoylation | AGVSGVVKFEQASES CCEECEEEEEECCCC | 40.55 | 15166219 | |
19 | Acetylation | AGVSGVVKFEQASES CCEECEEEEEECCCC | 40.55 | 24489116 | |
24 | Phosphorylation | VVKFEQASESEPTTV EEEEEECCCCCCEEE | 41.15 | 22369663 | |
26 | Phosphorylation | KFEQASESEPTTVSY EEEECCCCCCEEEEE | 46.51 | 22369663 | |
29 | Phosphorylation | QASESEPTTVSYEIA ECCCCCCEEEEEEEC | 35.46 | 22890988 | |
30 | Phosphorylation | ASESEPTTVSYEIAG CCCCCCEEEEEEECC | 20.40 | 22890988 | |
32 | Phosphorylation | ESEPTTVSYEIAGNS CCCCEEEEEEECCCC | 18.24 | 22890988 | |
33 | Phosphorylation | SEPTTVSYEIAGNSP CCCEEEEEEECCCCC | 13.66 | 22890988 | |
39 | Phosphorylation | SYEIAGNSPNAERGF EEEECCCCCCCCCCE | 20.72 | 22369663 | |
58 | Glutathionylation | FGDATNGCVSAGPHF CCCCCCCCCCCCCCC | 2.07 | 22833525 | |
69 | Acetylation | GPHFNPFKKTHGAPT CCCCCCCCCCCCCCC | 59.00 | 24489116 | |
69 | Sumoylation | GPHFNPFKKTHGAPT CCCCCCCCCCCCCCC | 59.00 | - | |
70 | Sumoylation | PHFNPFKKTHGAPTD CCCCCCCCCCCCCCC | 46.24 | 15166219 | |
70 | Sumoylation | PHFNPFKKTHGAPTD CCCCCCCCCCCCCCC | 46.24 | - | |
70 | 2-Hydroxyisobutyrylation | PHFNPFKKTHGAPTD CCCCCCCCCCCCCCC | 46.24 | - | |
71 | Phosphorylation | HFNPFKKTHGAPTDE CCCCCCCCCCCCCCC | 26.57 | 28889911 | |
76 | Phosphorylation | KKTHGAPTDEVRHVG CCCCCCCCCCCEEEC | 44.23 | 23749301 | |
89 | Succinylation | VGDMGNVKTDENGVA ECCCCCEEECCCCCC | 55.01 | 23954790 | |
89 | Acetylation | VGDMGNVKTDENGVA ECCCCCEEECCCCCC | 55.01 | 24489116 | |
90 | Phosphorylation | GDMGNVKTDENGVAK CCCCCEEECCCCCCC | 44.24 | 28889911 | |
97 | Succinylation | TDENGVAKGSFKDSL ECCCCCCCCCHHHHH | 53.32 | 23954790 | |
97 | Acetylation | TDENGVAKGSFKDSL ECCCCCCCCCHHHHH | 53.32 | 22865919 | |
97 | 2-Hydroxyisobutyrylation | TDENGVAKGSFKDSL ECCCCCCCCCHHHHH | 53.32 | - | |
99 | Phosphorylation | ENGVAKGSFKDSLIK CCCCCCCCHHHHHHH | 28.54 | 22369663 | |
101 | 2-Hydroxyisobutyrylation | GVAKGSFKDSLIKLI CCCCCCHHHHHHHHH | 48.37 | - | |
101 | Ubiquitination | GVAKGSFKDSLIKLI CCCCCCHHHHHHHHH | 48.37 | 23749301 | |
101 | Succinylation | GVAKGSFKDSLIKLI CCCCCCHHHHHHHHH | 48.37 | 23954790 | |
101 | Acetylation | GVAKGSFKDSLIKLI CCCCCCHHHHHHHHH | 48.37 | 24489116 | |
103 | Phosphorylation | AKGSFKDSLIKLIGP CCCCHHHHHHHHHCC | 32.36 | 22369663 | |
106 | Ubiquitination | SFKDSLIKLIGPTSV CHHHHHHHHHCCCCE | 39.07 | 24961812 | |
106 | Acetylation | SFKDSLIKLIGPTSV CHHHHHHHHHCCCCE | 39.07 | 24489116 | |
111 | Phosphorylation | LIKLIGPTSVVGRSV HHHHHCCCCEECCEE | 29.01 | 28889911 | |
112 | Phosphorylation | IKLIGPTSVVGRSVV HHHHCCCCEECCEEE | 20.24 | 17287358 | |
117 | Phosphorylation | PTSVVGRSVVIHAGQ CCCEECCEEEEECCC | 18.14 | 22369663 | |
129 | Acetylation | AGQDDLGKGDTEESL CCCCCCCCCCCHHHH | 61.99 | 24489116 | |
129 | 2-Hydroxyisobutyrylation | AGQDDLGKGDTEESL CCCCCCCCCCCHHHH | 61.99 | - | |
129 | Ubiquitination | AGQDDLGKGDTEESL CCCCCCCCCCCHHHH | 61.99 | 23749301 | |
129 | Succinylation | AGQDDLGKGDTEESL CCCCCCCCCCCHHHH | 61.99 | 23954790 | |
132 | Phosphorylation | DDLGKGDTEESLKTG CCCCCCCCHHHHHHC | 50.77 | 17287358 | |
135 | Phosphorylation | GKGDTEESLKTGNAG CCCCCHHHHHHCCCC | 29.00 | 20377248 | |
137 | Acetylation | GDTEESLKTGNAGPR CCCHHHHHHCCCCCC | 64.76 | 24489116 | |
137 | Ubiquitination | GDTEESLKTGNAGPR CCCHHHHHHCCCCCC | 64.76 | 23749301 | |
138 | Phosphorylation | DTEESLKTGNAGPRP CCHHHHHHCCCCCCC | 40.75 | 23749301 | |
153 | Phosphorylation | ACGVIGLTN------ CCCEEECCC------ | 33.40 | 21440633 |
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 SODC_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SODC_YEAST !! |
* 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_YEAST !! |
Kegg Drug | ||||||
---|---|---|---|---|---|---|
DrugBank | ||||||
There are no disease associations of PTM sites. |
loading...
Phosphorylation | |
Reference | PubMed |
"A multidimensional chromatography technology for in-depthphosphoproteome analysis."; Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; Mol. Cell. Proteomics 7:1389-1396(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15; SER-24; SER-26;SER-39; SER-99 AND SER-103, AND MASS SPECTROMETRY. | |
"Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases."; Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.; Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39 AND SER-99, AND MASSSPECTROMETRY. | |
"Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry."; Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.; Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99; SER-112; SER-117 ANDTHR-132, AND MASS SPECTROMETRY. | |
"Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway."; Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.; Mol. Cell. Proteomics 4:310-327(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39, AND MASSSPECTROMETRY. | |
Sumoylation | |
Reference | PubMed |
"Global analyses of sumoylated proteins in Saccharomyces cerevisiae.Induction of protein sumoylation by cellular stresses."; Zhou W., Ryan J.J., Zhou H.; J. Biol. Chem. 279:32262-32268(2004). Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-19 AND LYS-70, AND MASSSPECTROMETRY. |