UniProt ID | HEM2_YEAST | |
---|---|---|
UniProt AC | P05373 | |
Protein Name | Delta-aminolevulinic acid dehydratase | |
Gene Name | HEM2 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 342 | |
Subcellular Localization | ||
Protein Description | Catalyzes an early step in the biosynthesis of tetrapyrroles. Binds two molecules of 5-aminolevulinate per subunit, each at a distinct site, and catalyzes their condensation to form porphobilinogen.. | |
Protein Sequence | MHTAEFLETEPTEISSVLAGGYNHPLLRQWQSERQLTKNMLIFPLFISDNPDDFTEIDSLPNINRIGVNRLKDYLKPLVAKGLRSVILFGVPLIPGTKDPVGTAADDPAGPVIQGIKFIREYFPELYIICDVCLCEYTSHGHCGVLYDDGTINRERSVSRLAAVAVNYAKAGAHCVAPSDMIDGRIRDIKRGLINANLAHKTFVLSYAAKFSGNLYGPFRDAACSAPSNGDRKCYQLPPAGRGLARRALERDMSEGADGIIVKPSTFYLDIMRDASEICKDLPICAYHVSGEYAMLHAAAEKGVVDLKTIAFESHQGFLRAGARLIITYLAPEFLDWLDEEN | |
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 |
---|---|---|---|---|---|
76 | Acetylation | NRLKDYLKPLVAKGL HHHHHHHHHHHHHCC | 30.03 | 24489116 | |
170 | Ubiquitination | AVAVNYAKAGAHCVA HHHHHHHHCCCEEEC | 36.67 | 23749301 | |
225 | Phosphorylation | PFRDAACSAPSNGDR CCCCCCCCCCCCCCC | 38.19 | 28889911 | |
254 | Phosphorylation | RALERDMSEGADGII HHHHHHHCCCCCEEE | 36.85 | 22369663 | |
263 | Ubiquitination | GADGIIVKPSTFYLD CCCEEEECCCEEHHH | 23.89 | 23749301 | |
265 | Phosphorylation | DGIIVKPSTFYLDIM CEEEECCCEEHHHHH | 25.98 | 22369663 | |
266 | Phosphorylation | GIIVKPSTFYLDIMR EEEECCCEEHHHHHC | 25.48 | 22369663 | |
268 | Phosphorylation | IVKPSTFYLDIMRDA EECCCEEHHHHHCCH | 11.98 | 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 HEM2_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of HEM2_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 HEM2_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-254, AND MASSSPECTROMETRY. |