| UniProt ID | ACT_YEAST | |
|---|---|---|
| UniProt AC | P60010 | |
| Protein Name | Actin | |
| Gene Name | ACT1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 375 | |
| Subcellular Localization | Cytoplasm, cytoskeleton. | |
| Protein Description | Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.. | |
| Protein Sequence | MDSEVAALVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGIMVGMGQKDSYVGDEAQSKRGILTLRYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPMNPKSNREKMTQIMFETFNVPAFYVSIQAVLSLYSSGRTTGIVLDSGDGVTHVVPIYAGFSLPHAILRIDLAGRDLTDYLMKILSERGYSFSTTAEREIVRDIKEKLCYVALDFEQEMQTAAQSSSIEKSYELPDGQVITIGNERFRAPEALFHPSVLGLESAGIDQTTYNSIMKCDVDVRKELYGNIVMSGGTTMFPGIAERMQKEITALAPSSMKVKIIAPPERKYSVWIGGSILASLTTFQQMWISKQEYDESGPSIVHHKCF | |
| 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 |
|---|---|---|---|---|---|
| 1 | Acetylation | -------MDSEVAAL -------CCCCCEEE | 13.28 | 22814378 | |
| 3 | Phosphorylation | -----MDSEVAALVI -----CCCCCEEEEE | 32.45 | 24909858 | |
| 14 | Phosphorylation | ALVIDNGSGMCKAGF EEEEECCCCCEEECC | 29.61 | 24909858 | |
| 18 | Ubiquitination | DNGSGMCKAGFAGDD ECCCCCEEECCCCCC | 42.52 | 17644757 | |
| 33 | Phosphorylation | APRAVFPSIVGRPRH CCHHHCHHHCCCCCC | 20.59 | 21440633 | |
| 50 | Succinylation | IMVGMGQKDSYVGDE EEEECCCCCCCCCCH | 42.80 | 23954790 | |
| 50 | Ubiquitination | IMVGMGQKDSYVGDE EEEECCCCCCCCCCH | 42.80 | 23749301 | |
| 50 | Acetylation | IMVGMGQKDSYVGDE EEEECCCCCCCCCCH | 42.80 | 24489116 | |
| 50 | 2-Hydroxyisobutyrylation | IMVGMGQKDSYVGDE EEEECCCCCCCCCCH | 42.80 | - | |
| 52 | Phosphorylation | VGMGQKDSYVGDEAQ EECCCCCCCCCCHHH | 28.84 | 23749301 | |
| 53 | Phosphorylation | GMGQKDSYVGDEAQS ECCCCCCCCCCHHHH | 20.70 | 23749301 | |
| 60 | Phosphorylation | YVGDEAQSKRGILTL CCCCHHHHCCCEEEE | 31.22 | 23749301 | |
| 61 | 2-Hydroxyisobutyrylation | VGDEAQSKRGILTLR CCCHHHHCCCEEEEE | 42.43 | - | |
| 61 | Acetylation | VGDEAQSKRGILTLR CCCHHHHCCCEEEEE | 42.43 | 25381059 | |
| 61 | Ubiquitination | VGDEAQSKRGILTLR CCCHHHHCCCEEEEE | 42.43 | 23749301 | |
| 84 | Ubiquitination | TNWDDMEKIWHHTFY CCHHHHHHHHHHHHH | 44.45 | 23749301 | |
| 113 | Ubiquitination | TEAPMNPKSNREKMT EECCCCCCCCHHHHH | 56.19 | 23749301 | |
| 113 | Acetylation | TEAPMNPKSNREKMT EECCCCCCCCHHHHH | 56.19 | 24489116 | |
| 113 | 2-Hydroxyisobutyrylation | TEAPMNPKSNREKMT EECCCCCCCCHHHHH | 56.19 | - | |
| 113 | Succinylation | TEAPMNPKSNREKMT EECCCCCCCCHHHHH | 56.19 | 23954790 | |
| 118 | Ubiquitination | NPKSNREKMTQIMFE CCCCCHHHHHHHHHH | 43.97 | 22817900 | |
| 191 | Ubiquitination | DLTDYLMKILSERGY CHHHHHHHHHHHCCC | 37.59 | 23749301 | |
| 191 | Acetylation | DLTDYLMKILSERGY CHHHHHHHHHHHCCC | 37.59 | 24489116 | |
| 199 | Phosphorylation | ILSERGYSFSTTAER HHHHCCCCCCCCHHH | 18.62 | 22369663 | |
| 201 | Phosphorylation | SERGYSFSTTAEREI HHCCCCCCCCHHHHH | 20.93 | 28889911 | |
| 203 | Phosphorylation | RGYSFSTTAEREIVR CCCCCCCCHHHHHHH | 25.89 | 25752575 | |
| 215 | Ubiquitination | IVRDIKEKLCYVALD HHHHHHHHHHEEECC | 38.56 | 17644757 | |
| 238 | Ubiquitination | AQSSSIEKSYELPDG HHHCCCCEEEECCCC | 57.58 | 17644757 | |
| 239 | Phosphorylation | QSSSIEKSYELPDGQ HHCCCCEEEECCCCC | 15.85 | 25521595 | |
| 284 | Ubiquitination | TTYNSIMKCDVDVRK CHHHHHHCCCCCCHH | 26.13 | 17644757 | |
| 291 | Ubiquitination | KCDVDVRKELYGNIV CCCCCCHHHHCCCEE | 52.50 | 17644757 | |
| 291 | Acetylation | KCDVDVRKELYGNIV CCCCCCHHHHCCCEE | 52.50 | 25381059 | |
| 303 | Phosphorylation | NIVMSGGTTMFPGIA CEEECCCCCCCCCHH | 20.72 | 27017623 | |
| 304 | Phosphorylation | IVMSGGTTMFPGIAE EEECCCCCCCCCHHH | 21.79 | 21440633 | |
| 315 | Ubiquitination | GIAERMQKEITALAP CHHHHHHHHHHHHCC | 41.56 | 23749301 | |
| 315 | 2-Hydroxyisobutyrylation | GIAERMQKEITALAP CHHHHHHHHHHHHCC | 41.56 | - | |
| 315 | Acetylation | GIAERMQKEITALAP CHHHHHHHHHHHHCC | 41.56 | 24489116 | |
| 318 | Phosphorylation | ERMQKEITALAPSSM HHHHHHHHHHCCCCC | 19.40 | 22369663 | |
| 323 | Phosphorylation | EITALAPSSMKVKII HHHHHCCCCCEEEEE | 37.14 | 22369663 | |
| 324 | Phosphorylation | ITALAPSSMKVKIIA HHHHCCCCCEEEEEC | 22.89 | 22369663 | |
| 326 | Ubiquitination | ALAPSSMKVKIIAPP HHCCCCCEEEEECCC | 42.18 | 23749301 | |
| 326 | Acetylation | ALAPSSMKVKIIAPP HHCCCCCEEEEECCC | 42.18 | 24489116 | |
| 328 | 2-Hydroxyisobutyrylation | APSSMKVKIIAPPER CCCCCEEEEECCCCC | 23.91 | - | |
| 328 | Ubiquitination | APSSMKVKIIAPPER CCCCCEEEEECCCCC | 23.91 | 23749301 | |
| 328 | Acetylation | APSSMKVKIIAPPER CCCCCEEEEECCCCC | 23.91 | 24489116 | |
| 373 | Acetylation | GPSIVHHKCF----- CCCCCCCCCC----- | 23.58 | 24489116 |
| 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 ACT_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ACT_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 ACT_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Acetylation | |
| Reference | PubMed |
| "Unusual metabolism of the yeast actin amino terminus."; Cook R.K., Sheff D.R., Rubenstein P.A.; J. Biol. Chem. 266:16825-16833(1991). Cited for: ACETYLATION AT MET-1, AND PROTEIN SEQUENCE OF N-TERMINUS. | |
| 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-199; SER-201; SER-323AND SER-324, AND MASS SPECTROMETRY. | |
