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 | ||
|
* 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 |
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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 | ||||||
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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-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. |