| UniProt ID | BCA2_YEAST | |
|---|---|---|
| UniProt AC | P47176 | |
| Protein Name | Branched-chain-amino-acid aminotransferase, cytosolic | |
| Gene Name | BAT2 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 376 | |
| Subcellular Localization | Cytoplasm . | |
| Protein Description | Catalyzes the first reaction in the catabolism of the essential branched chain amino acids leucine, isoleucine, and valine. Catalyzes the formation of methionine from 2-keto-4-methylthiobutyrate (KMTB) in the methionine salvage pathway primarily using branched chain amino acids (leucine, isoleucine, and valine) as well as lysine and proline as the amino donors. Involved in cell cycle regulation.. | |
| Protein Sequence | MTLAPLDASKVKITTTQHASKPKPNSELVFGKSFTDHMLTAEWTAEKGWGTPEIKPYQNLSLDPSAVVFHYAFELFEGMKAYRTVDNKITMFRPDMNMKRMNKSAQRICLPTFDPEELITLIGKLIQQDKCLVPEGKGYSLYIRPTLIGTTAGLGVSTPDRALLYVICCPVGPYYKTGFKAVRLEATDYATRAWPGGCGDKKLGANYAPCVLPQLQAASRGYQQNLWLFGPNNNITEVGTMNAFFVFKDSKTGKKELVTAPLDGTILEGVTRDSILNLAKERLEPSEWTISERYFTIGEVTERSKNGELLEAFGSGTAAIVSPIKEIGWKGEQINIPLLPGEQTGPLAKEVAQWINGIQYGETEHGNWSRVVTDLN | |
| 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 |
|---|---|---|---|---|---|
| 33 | Phosphorylation | SELVFGKSFTDHMLT CEEEEECCCCCCEEE | 33.48 | 22369663 | |
| 35 | Phosphorylation | LVFGKSFTDHMLTAE EEEECCCCCCEEEEE | 31.89 | 20377248 | |
| 51 | Phosphorylation | TAEKGWGTPEIKPYQ HHHCCCCCCCCCCCC | 15.96 | 22369663 | |
| 202 | N6-(pyridoxal phosphate)lysine | PGGCGDKKLGANYAP CCCCCCCCCCCCCCC | 57.82 | - | |
| 202 | Other | PGGCGDKKLGANYAP CCCCCCCCCCCCCCC | 57.82 | - | |
| 252 | Phosphorylation | FVFKDSKTGKKELVT EEEECCCCCCEEEEE | 59.18 | 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 BCA2_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of BCA2_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 BCA2_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| 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 THR-51, AND MASSSPECTROMETRY. | |
