| UniProt ID | HAP2_YEAST | |
|---|---|---|
| UniProt AC | P06774 | |
| Protein Name | Transcriptional activator HAP2 | |
| Gene Name | HAP2 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 265 | |
| Subcellular Localization | Nucleus. | |
| Protein Description | Acts a component of the CCAT-binding factor, which is a transcriptional activator and binds to the upstream activation site (UAS2) of the CYC1 gene and other genes involved in mitochondrial electron transport and activates their expression. Recognizes the sequence 5'-CCAAT-3'. HAP2 has primarily a structural role in the HAP complexes I and II.. | |
| Protein Sequence | MSADETDAKFHPLETDLQSDTAAATSTAAASRSPSLQEKPIEMPLDMGKAPSPRGEDQRVTNEEDLFLFNRLRASQNRVMDSLEPQQQSQYTSSSVSTMEPSADFTSFSAVTTLPPPPHQQQQQQQQQQQQQQLVVQAQYTQNQPNLQSDVLGTAIAEQPFYVNAKQYYRILKRRYARAKLEEKLRISRERKPYLHESRHKHAMRRPRGEGGRFLTAAEIKAMKSKKSGASDDPDDSHEDKKITTKIIQEQPHATSTAAAADKKT | |
| 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 |
|---|---|---|---|---|---|
| 2 | Acetylation | ------MSADETDAK ------CCHHHHHCC | 44.41 | 22814378 | |
| 2 | Phosphorylation | ------MSADETDAK ------CCHHHHHCC | 44.41 | 28889911 | |
| 6 | Phosphorylation | --MSADETDAKFHPL --CCHHHHHCCCCCC | 41.63 | 28889911 | |
| 15 | Phosphorylation | AKFHPLETDLQSDTA CCCCCCCCHHHCCHH | 50.09 | 22369663 | |
| 19 | Phosphorylation | PLETDLQSDTAAATS CCCCHHHCCHHHHHH | 44.20 | 22369663 | |
| 21 | Phosphorylation | ETDLQSDTAAATSTA CCHHHCCHHHHHHHH | 24.36 | 22369663 | |
| 25 | Phosphorylation | QSDTAAATSTAAASR HCCHHHHHHHHHHHC | 23.14 | 22369663 | |
| 26 | Phosphorylation | SDTAAATSTAAASRS CCHHHHHHHHHHHCC | 16.01 | 21440633 | |
| 27 | Phosphorylation | DTAAATSTAAASRSP CHHHHHHHHHHHCCC | 18.89 | 22369663 | |
| 31 | Phosphorylation | ATSTAAASRSPSLQE HHHHHHHHCCCCCCC | 28.67 | 22369663 | |
| 33 | Phosphorylation | STAAASRSPSLQEKP HHHHHHCCCCCCCCC | 19.15 | 22369663 | |
| 35 | Phosphorylation | AAASRSPSLQEKPIE HHHHCCCCCCCCCCC | 43.88 | 22369663 | |
| 52 | Phosphorylation | LDMGKAPSPRGEDQR CCCCCCCCCCCCCCC | 31.89 | 22369663 | |
| 228 | Phosphorylation | KAMKSKKSGASDDPD HHHHHCCCCCCCCCC | 43.24 | 28889911 | |
| 231 | Phosphorylation | KSKKSGASDDPDDSH HHCCCCCCCCCCCCH | 46.18 | 27717283 | |
| 237 | Phosphorylation | ASDDPDDSHEDKKIT CCCCCCCCHHHHHHH | 35.84 | 28889911 | |
| 257 | Phosphorylation | EQPHATSTAAAADKK CCCCCCCHHHHHHCC | 18.89 | 19823750 | |
| 265 | Phosphorylation | AAAADKKT------- HHHHHCCC------- | 49.97 | 20377248 |
| 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 HAP2_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of HAP2_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 HAP2_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-33 AND SER-35, AND MASSSPECTROMETRY. | |
