| UniProt ID | BCA1_YEAST | |
|---|---|---|
| UniProt AC | P38891 | |
| Protein Name | Branched-chain-amino-acid aminotransferase, mitochondrial | |
| Gene Name | BAT1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 393 | |
| Subcellular Localization | Mitochondrion matrix . | |
| Protein Description | Involved in the biosynthesis of the 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 the amino donors. Appears to be involved in the regulation of the transition from G1 to S phase in the cell cycle. High copy suppressor of a temperature-sensitive mutation in the ABC transporter, ATM1.. | |
| Protein Sequence | MLQRHSLKLGKFSIRTLATGAPLDASKLKITRNPNPSKPRPNEELVFGQTFTDHMLTIPWSAKEGWGTPHIKPYGNLSLDPSACVFHYAFELFEGLKAYRTPQNTITMFRPDKNMARMNKSAARICLPTFESEELIKLTGKLIEQDKHLVPQGNGYSLYIRPTMIGTSKGLGVGTPSEALLYVITSPVGPYYKTGFKAVRLEATDYATRAWPGGVGDKKLGANYAPCILPQLQAAKRGYQQNLWLFGPEKNITEVGTMNVFFVFLNKVTGKKELVTAPLDGTILEGVTRDSVLTLARDKLDPQEWDINERYYTITEVATRAKQGELLEAFGSGTAAVVSPIKEIGWNNEDIHVPLLPGEQCGALTKQVAQWIADIQYGRVNYGNWSKTVADLN | |
| 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 |
|---|---|---|---|---|---|
| 11 | Acetylation | RHSLKLGKFSIRTLA CCCCCCCCCCHHHHC | 46.50 | 25381059 | |
| 113 | Acetylation | ITMFRPDKNMARMNK EEEECCCHHHHHCCH | 51.83 | 24489116 | |
| 121 | Phosphorylation | NMARMNKSAARICLP HHHHCCHHHHHHHHC | 23.35 | 21440633 | |
| 132 | Phosphorylation | ICLPTFESEELIKLT HHHCCCCCHHHHHHH | 31.98 | 27017623 | |
| 137 | Acetylation | FESEELIKLTGKLIE CCCHHHHHHHHHHHH | 53.25 | 25381059 | |
| 141 | Acetylation | ELIKLTGKLIEQDKH HHHHHHHHHHHCCCC | 40.85 | 24489116 | |
| 147 | Acetylation | GKLIEQDKHLVPQGN HHHHHCCCCCCCCCC | 38.23 | 24489116 | |
| 186 | Phosphorylation | ALLYVITSPVGPYYK HEEHECCCCCCCCCC | 13.38 | 28889911 | |
| 193 | Acetylation | SPVGPYYKTGFKAVR CCCCCCCCCCCEEEE | 36.01 | 24489116 | |
| 197 | Acetylation | PYYKTGFKAVRLEAT CCCCCCCEEEEEEEE | 47.52 | 24489116 | |
| 218 | Acetylation | WPGGVGDKKLGANYA CCCCCCCCCCCCCCC | 43.92 | 24489116 | |
| 219 | N6-(pyridoxal phosphate)lysine | PGGVGDKKLGANYAP CCCCCCCCCCCCCCC | 57.82 | - | |
| 219 | Other | PGGVGDKKLGANYAP CCCCCCCCCCCCCCC | 57.82 | - | |
| 236 | Acetylation | LPQLQAAKRGYQQNL HHHHHHHHCHHCCCE | 49.74 | 25381059 | |
| 267 | Ubiquitination | VFFVFLNKVTGKKEL EEEEEEECCCCCEEE | 43.23 | 22817900 | |
| 271 | Ubiquitination | FLNKVTGKKELVTAP EEECCCCCEEEEECC | 33.44 | 22817900 | |
| 272 | Ubiquitination | LNKVTGKKELVTAPL EECCCCCEEEEECCC | 58.59 | 22817900 | |
| 291 | Phosphorylation | LEGVTRDSVLTLARD EECCCHHHHHHHHHH | 18.74 | 22369663 | |
| 294 | Phosphorylation | VTRDSVLTLARDKLD CCHHHHHHHHHHCCC | 19.06 | 22369663 | |
| 299 | Acetylation | VLTLARDKLDPQEWD HHHHHHHCCCHHHCC | 49.60 | 24489116 | |
| 299 | Succinylation | VLTLARDKLDPQEWD HHHHHHHCCCHHHCC | 49.60 | 23954790 | |
| 315 | Phosphorylation | NERYYTITEVATRAK CCCEEEHHHHHHHHH | 19.33 | 28889911 | |
| 322 | Ubiquitination | TEVATRAKQGELLEA HHHHHHHHHCCHHHH | 56.39 | 19722269 | |
| 342 | Acetylation | AAVVSPIKEIGWNNE EEEEECCHHHCCCCC | 46.81 | 25381059 | |
| 387 | Acetylation | VNYGNWSKTVADLN- ECCCCHHCCHHCCC- | 38.34 | 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 BCA1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of BCA1_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 BCA1_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 SER-186 AND THR-315, ANDMASS SPECTROMETRY. | |
