| UniProt ID | 3HAO_YEAST | |
|---|---|---|
| UniProt AC | P47096 | |
| Protein Name | 3-hydroxyanthranilate 3,4-dioxygenase {ECO:0000255|HAMAP-Rule:MF_03019} | |
| Gene Name | BNA1 {ECO:0000255|HAMAP-Rule:MF_03019} | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 177 | |
| Subcellular Localization | Cytoplasm . Nucleus . | |
| Protein Description | Catalyzes the oxidative ring opening of 3-hydroxyanthranilate to 2-amino-3-carboxymuconate semialdehyde, which spontaneously cyclizes to quinolinate.. | |
| Protein Sequence | MFNTTPINIDKWLKENEGLLKPPVNNYCLHKGGFTVMIVGGPNERTGYHINPTPEWFYQKKGSMLLKVVDETDAEPKFIDIIINEGDSYLLPGNVPHSPVRFADTVGIVVEQDRPGGENDKIRWYCSHCRQVVHESELQMLDLGTQVKEAILDFENDVEKRTCFHCKTLNYARPQSN | |
| 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 |
|---|---|---|---|---|---|
| 60 | Ubiquitination | TPEWFYQKKGSMLLK CCHHHHCCCCCEEEE | 47.96 | 23749301 | |
| 67 | Ubiquitination | KKGSMLLKVVDETDA CCCCEEEEEECCCCC | 35.93 | 23749301 | |
| 98 | Phosphorylation | LPGNVPHSPVRFADT CCCCCCCCCCCCCCE | 21.01 | 22369663 | |
| 121 | Acetylation | RPGGENDKIRWYCSH CCCCCCCCEEEEHHH | 45.83 | 24489116 | |
| 160 | Acetylation | DFENDVEKRTCFHCK HCCCCCHHCEEEEEE | 53.51 | 24489116 | |
| 167 | Ubiquitination | KRTCFHCKTLNYARP HCEEEEEEECCCCCC | 47.69 | 22817900 | |
| 167 | Acetylation | KRTCFHCKTLNYARP HCEEEEEEECCCCCC | 47.69 | 24489116 | |
| 168 | Phosphorylation | RTCFHCKTLNYARPQ CEEEEEEECCCCCCC | 26.15 | 21126336 | |
| 176 | Phosphorylation | LNYARPQSN------ CCCCCCCCC------ | 47.38 | 22369663 |
| 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 3HAO_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of 3HAO_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 3HAO_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-176, AND MASSSPECTROMETRY. | |
| "Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae."; Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.; J. Proteome Res. 6:1190-1197(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-176, AND MASSSPECTROMETRY. | |
| "Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway."; Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.; Mol. Cell. Proteomics 4:310-327(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-176, AND MASSSPECTROMETRY. | |