| UniProt ID | SSN3_YEAST | |
|---|---|---|
| UniProt AC | P39073 | |
| Protein Name | Meiotic mRNA stability protein kinase SSN3 | |
| Gene Name | SSN3 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 555 | |
| Subcellular Localization | Nucleus . | |
| Protein Description | Component of the SRB8-11 complex. The SRB8-11 complex is a regulatory module of the Mediator complex which is itself involved in regulation of basal and activated RNA polymerase II-dependent transcription. The SRB8-11 complex may be involved in the transcriptional repression of a subset of genes regulated by Mediator. It may inhibit the association of the Mediator complex with RNA polymerase II to form the holoenzyme complex. The SRB8-11 complex phosphorylates the C-terminal domain (CTD) of the largest subunit of RNA polymerase II RPB1 at serines 2 and 5. The SSN3/SRB10 and SSN8/SRB11 kinase-cyclin pair may also positively and negatively regulate numerous transcriptional activators in response to changes in nutritional and physiological conditions. Phosphorylates GCN4, promoting its ubiquitin-mediated degradation, and MSN2, promoting its nuclear exclusion. Phosphorylates STE12, thereby promoting its degradation and inhibition of filamentous growth. Phosphorylates GAL4, and this phosphorylation is required for efficient galactose-inducible transcription. Also phosphorylates BDF1 and the TAF2 subunit of the TFIID complex.. | |
| Protein Sequence | MYNGKDRAQNSYQPMYQRPMQVQGQQQAQSFVGKKNTIGSVHGKAPMLMANNDVFTIGPYRARKDRMRVSVLEKYEVIGYIAAGTYGKVYKAKRQINSGTNSANGSSLNGTNAKIPQFDSTQPKSSSSMDMQANTNALRRNLLKDEGVTPGRIRTTREDVSPHYNSQKQTLIKKPLTVFYAIKKFKTEKDGVEQLHYTGISQSACREMALCRELHNKHLTTLVEIFLERKCVHMVYEYAEHDLLQIIHFHSHPEKRMIPPRMVRSIMWQLLDGVSYLHQNWVLHRDLKPANIMVTIDGCVKIGDLGLARKFHNMLQTLYTGDKVVVTIWYRAPELLLGARHYTPAVDLWSVGCIFAELIGLQPIFKGEEAKLDSKKTVPFQVNQLQRILEVLGTPDQKIWPYLEKYPEYDQITKFPKYRDNLATWYHSAGGRDKHALSLLYHLLNYDPIKRIDAFNALEHKYFTESDIPVSENVFEGLTYKYPARRIHTNDNDIMNLGSRTKNNTQASGITAGAAANALGGLGVNRRILAAAAAAAAAVSGNNASDEPSRKKNRR | |
| 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 |
|---|---|---|---|---|---|
| 44 | Acetylation | TIGSVHGKAPMLMAN CCCCCCCCCCEEECC | 34.14 | 24489116 | |
| 98 | Phosphorylation | KAKRQINSGTNSANG HHHHCCCCCCCCCCC | 48.93 | 29136822 | |
| 100 | Phosphorylation | KRQINSGTNSANGSS HHCCCCCCCCCCCCC | 26.31 | 29136822 | |
| 102 | Phosphorylation | QINSGTNSANGSSLN CCCCCCCCCCCCCCC | 23.97 | 29136822 | |
| 106 | Phosphorylation | GTNSANGSSLNGTNA CCCCCCCCCCCCCCC | 31.31 | 29136822 | |
| 107 | Phosphorylation | TNSANGSSLNGTNAK CCCCCCCCCCCCCCC | 27.53 | 29136822 | |
| 111 | Phosphorylation | NGSSLNGTNAKIPQF CCCCCCCCCCCCCCC | 30.81 | 29136822 | |
| 149 | Phosphorylation | LLKDEGVTPGRIRTT HHHCCCCCCCCCCCC | 30.77 | 24961812 | |
| 155 | Phosphorylation | VTPGRIRTTREDVSP CCCCCCCCCHHHCCC | 28.03 | 24961812 | |
| 156 | Phosphorylation | TPGRIRTTREDVSPH CCCCCCCCHHHCCCC | 23.39 | 24961812 | |
| 161 | Phosphorylation | RTTREDVSPHYNSQK CCCHHHCCCCCCCCC | 20.48 | 21440633 | |
| 540 | Phosphorylation | AAAAAAVSGNNASDE HHHHHHHHCCCCCCC | 30.95 | 19684113 |
| 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 SSN3_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SSN3_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 SSN3_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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