UniProt ID | GABAT_YEAST | |
---|---|---|
UniProt AC | P17649 | |
Protein Name | 4-aminobutyrate aminotransferase | |
Gene Name | UGA1 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 471 | |
Subcellular Localization | Cytoplasm . | |
Protein Description | Required for the degradation of gamma-aminobutyric acid (GABA), which is important for utilization of GABA as nitrogen source and for oxidative stress tolerance. Deaminates GABA to succinate semialdehyde, which in turn is converted to succinate by the succinate-semialdehyde dehydrogenase UGA2. Cannot transaminate beta-alanine (BAL).. | |
Protein Sequence | MSICEQYYPEEPTKPTVKTESIPGPESQKQLKELGEVFDTRPAYFLADYEKSLGNYITDVDGNTYLDLYAQISSIALGYNNPALIKAAQSPEMIRALVDRPALGNFPSKDLDKILKQILKSAPKGQDHVWSGLSGADANELAFKAAFIYYRAKQRGYDADFSEKENLSVMDNDAPGAPHLAVLSFKRAFHGRLFASGSTTCSKPIHKLDFPAFHWPHAEYPSYQYPLDENSDANRKEDDHCLAIVEELIKTWSIPVAALIIEPIQSEGGDNHASKYFLQKLRDITLKYNVVYIIDEVQTGVGATGKLWCHEYADIQPPVDLVTFSKKFQSAGYFFHDPKFIPNKPYRQFNTWCGEPARMIIAGAIGQEISDKKLTEQCSRVGDYLFKKLEGLQKKYPENFQNLRGKGRGTFIAWDLPTGEKRDLLLKKLKLNGCNVGGCAVHAVRLRPSLTFEEKHADIFIEALAKSVNEL | |
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 |
---|---|---|---|---|---|
2 | Phosphorylation | ------MSICEQYYP ------CCCCCCCCC | 35.63 | 30377154 | |
8 | Phosphorylation | MSICEQYYPEEPTKP CCCCCCCCCCCCCCC | 12.12 | 30377154 | |
13 | Phosphorylation | QYYPEEPTKPTVKTE CCCCCCCCCCCCCCC | 53.59 | 30377154 | |
16 | Phosphorylation | PEEPTKPTVKTESIP CCCCCCCCCCCCCCC | 35.87 | 30377154 | |
19 | Phosphorylation | PTKPTVKTESIPGPE CCCCCCCCCCCCCHH | 30.54 | 22369663 | |
21 | Phosphorylation | KPTVKTESIPGPESQ CCCCCCCCCCCHHHH | 39.04 | 22369663 | |
27 | Phosphorylation | ESIPGPESQKQLKEL CCCCCHHHHHHHHHH | 45.90 | 22369663 | |
90 | Phosphorylation | ALIKAAQSPEMIRAL HHHHHHCCHHHHHHH | 20.35 | 25752575 | |
109 | Acetylation | ALGNFPSKDLDKILK CCCCCCHHHHHHHHH | 63.65 | 24489116 | |
326 | N6-(pyridoxal phosphate)lysine | VDLVTFSKKFQSAGY CEEEEECHHHHHCCC | 54.11 | - | |
326 | Other | VDLVTFSKKFQSAGY CEEEEECHHHHHCCC | 54.11 | - | |
339 | Acetylation | GYFFHDPKFIPNKPY CCCCCCCCCCCCCCC | 63.08 | 24489116 | |
344 | Acetylation | DPKFIPNKPYRQFNT CCCCCCCCCCCCCCC | 37.76 | 22865919 | |
451 | Phosphorylation | VRLRPSLTFEEKHAD EEECCCCCCHHHHHH | 33.08 | 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 GABAT_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of GABAT_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 GABAT_YEAST !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
DCE_YEAST | GAD1 | genetic | 21371425 | |
G3P2_YEAST | TDH2 | genetic | 21623372 | |
COX7_YEAST | COX7 | genetic | 21623372 | |
UGA2_YEAST | UGA2 | genetic | 23447388 | |
CDC48_YEAST | CDC48 | genetic | 27708008 | |
TFB1_YEAST | TFB1 | genetic | 27708008 | |
GPI19_YEAST | GPI19 | genetic | 27708008 | |
ACT_YEAST | ACT1 | genetic | 27708008 | |
CDC20_YEAST | CDC20 | genetic | 27708008 | |
RRN7_YEAST | RRN7 | genetic | 27708008 | |
KTHY_YEAST | CDC8 | genetic | 27708008 | |
DCP2_YEAST | DCP2 | genetic | 27708008 | |
SEC12_YEAST | SEC12 | genetic | 27708008 | |
CH10_YEAST | HSP10 | genetic | 27708008 | |
RPB2_YEAST | RPB2 | genetic | 27708008 |
Kegg Drug | ||||||
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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-90, AND MASSSPECTROMETRY. |