| UniProt ID | ACA1_YEAST | |
|---|---|---|
| UniProt AC | P39970 | |
| Protein Name | ATF/CREB activator 1 | |
| Gene Name | ACA1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 489 | |
| Subcellular Localization | Nucleus . | |
| Protein Description | Transcriptional activator of promoters containing ATF/CREB sites. Can independently stimulate transcription through ATF/CREB sites. Important for a variety of biological functions including growth on non-optimal carbon sources. Regulates the expression of COS8. Has efficient silencing blocking activities.. | |
| Protein Sequence | MDYKHNFATSPDSFLDGRQNPLLYTDFLSSNKELIYKQPSGPGLVDSAYNFHHQNSLHDRSVQENLGPMFQPFGVDISHLPITNPPIFQSSLPAFDQPVYKRRISISNGQISQLGEDLETVENLYNCQPPILSSKAQQNPNPQQVANPSAAIYPSFSSNELQNVPQPHEQATVIPEAAPQTGSKNIYAAMTPYDSNIKLNIPAVAATCDIPSATPSIPSGDSTMNQAYINMQLRLQAQMQTKAWKNAQLNVHPCTPASNSSVSSSSSCQNINDHNIENQSVHSSISHGVNHHTVNNSCQNAELNISSSLPYESKCPDVNLTHANSKPQYKDATSALKNNINSEKDVHTAPFSSMHTTATFQIKQEARPQKIENNTAGLKDGAKAWKRARLLERNRIAASKCRQRKKMSQLQLQREFDQISKENTMMKKKIENYEKLVQKMKKISRLHMQECTINGGNNSYQSLQNKDSDVNGFLKMIEEMIRSSSLYDE | |
| 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 |
|---|---|---|---|---|---|
| 25 | Phosphorylation | RQNPLLYTDFLSSNK CCCCCHHHCCHHCCC | 21.90 | 28889911 | |
| 29 | Phosphorylation | LLYTDFLSSNKELIY CHHHCCHHCCCEEEE | 31.68 | 28889911 | |
| 105 | Phosphorylation | PVYKRRISISNGQIS CCEEEEEEECCCCHH | 20.39 | 21440633 | |
| 191 | Phosphorylation | KNIYAAMTPYDSNIK CCEEEEECCCCCCCC | 17.61 | 24961812 | |
| 193 | Phosphorylation | IYAAMTPYDSNIKLN EEEEECCCCCCCCCC | 23.88 | 24961812 | |
| 195 | Phosphorylation | AAMTPYDSNIKLNIP EEECCCCCCCCCCCC | 34.31 | 24961812 | |
| 375 | Phosphorylation | PQKIENNTAGLKDGA CCCCCCCCCCCHHHH | 33.41 | 29734811 | |
| 400 | Acetylation | RNRIAASKCRQRKKM HHHHHHHHHHHHHHH | 28.80 | 25381059 | |
| 444 | Phosphorylation | VQKMKKISRLHMQEC HHHHHHHHHHHCEEE | 37.35 | 29136822 | |
| 459 | Phosphorylation | TINGGNNSYQSLQNK EEECCCCCCHHHHCC | 28.66 | 29136822 | |
| 460 | Phosphorylation | INGGNNSYQSLQNKD EECCCCCCHHHHCCC | 12.30 | 29136822 | |
| 462 | Phosphorylation | GGNNSYQSLQNKDSD CCCCCCHHHHCCCCC | 24.56 | 29136822 | |
| 483 | Phosphorylation | MIEEMIRSSSLYDE- HHHHHHHHCCCCCC- | 17.22 | 28889911 | |
| 484 | Phosphorylation | IEEMIRSSSLYDE-- HHHHHHHCCCCCC-- | 17.95 | 28889911 | |
| 485 | Phosphorylation | EEMIRSSSLYDE--- HHHHHHCCCCCC--- | 31.99 | 28889911 | |
| 487 | Phosphorylation | MIRSSSLYDE----- HHHHCCCCCC----- | 21.70 | 28889911 |
| 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 ACA1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ACA1_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 ACA1_YEAST !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| RGT1_YEAST | RGT1 | genetic | 20959818 | |
| URE2_YEAST | URE2 | genetic | 20959818 | |
| EAF5_YEAST | EAF5 | genetic | 20959818 | |
| SIN3_YEAST | SIN3 | genetic | 20959818 | |
| DOA1_YEAST | DOA1 | genetic | 20959818 | |
| BAS1_YEAST | BAS1 | genetic | 20959818 | |
| UBP3_YEAST | UBP3 | genetic | 20959818 | |
| REI1_YEAST | REI1 | genetic | 21127252 | |
| SPC72_YEAST | SPC72 | physical | 22875988 | |
| ARE1_YEAST | ARE1 | physical | 22875988 | |
| ACA1_YEAST | ACA1 | physical | 22875988 | |
| SPR3_YEAST | SPR3 | physical | 22875988 | |
| HOS4_YEAST | HOS4 | physical | 22875988 | |
| SGM1_YEAST | SGM1 | physical | 22875988 | |
| RNA1_YEAST | RNA1 | physical | 22875988 | |
| NST1_YEAST | NST1 | physical | 22875988 | |
| BNI1_YEAST | BNI1 | physical | 22875988 | |
| RLF2_YEAST | RLF2 | physical | 22875988 | |
| BUD31_YEAST | BUD31 | genetic | 27708008 | |
| ELP2_YEAST | ELP2 | genetic | 27708008 | |
| YHA8_YEAST | YHL008C | genetic | 27708008 | |
| GSH1_YEAST | GSH1 | genetic | 27708008 | |
| SRL3_YEAST | SRL3 | genetic | 27708008 | |
| METK1_YEAST | SAM1 | genetic | 27708008 |
| 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-105, AND MASSSPECTROMETRY. | |