| UniProt ID | HOT1_YEAST | |
|---|---|---|
| UniProt AC | Q03213 | |
| Protein Name | High-osmolarity-induced transcription protein 1 | |
| Gene Name | HOT1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 719 | |
| Subcellular Localization | Nucleus . | |
| Protein Description | Required for a complete transcriptional response to osmotic stress, through recruitment of HOG1 followed by pol II recruitment to the promoters of GPD1 and other HOG-dependent genes.. | |
| Protein Sequence | MSGMGIAILCIVRTKIYRITISFDYSTLMSPFFLFLMMPTTLKDGYRMNSQVNEDAIGINLDLSLPTHISPTTGSESASGSNASTLRNDGNALDGGLLRTSAAISAPTGTSQPTETIGEKLSNEERVNSNVSASNSTTAGTGRMLSQSLTNDSPSNEISTDQLKIFQRMDEMSARMIEMEESFNKLSNKIAEQNTMVLNLKQDNYKVMNKLNILLKLVAQPSARPSTNNAQNKLAIELLNSISAVSSAYLQKMQNNGSGRQHTADLCTGDSNTHSGINQHRTTNGTIDVNTNTAQLNNQFSNALNTILPDQQHNRNNVSQNINQSLPNRQLGPVINTQANQNQSQVLIHNTNTHQQVNRSPISFPNASTDKPFKLNPNGIKRRRRNTQSNNNASTNDHASAAQKPISALSPLTNSHNSTTSMNYTNSSIHSGVTSASNSFHDLNSLNNFGTTTALSLPSLALDNASFPPNQNVIPPIINNTQQPLSFSQLINQDSTTSELLPSGKSGVNTNIVNRNRASTLPSYPKPMTVKSNVDDDGYQEDDDDDGDDEGDGRDNEEDSTAEEDEVDDEIETDMKNASINKRRRSLHHKKSNSLNGRRKLHGESATKPNINSDLHYRILKAPTDVKTIWEEYDTGIRGKPSIKHLEAKYGNKWRLNKNKKTFSRRKRLYKFILNGMERGKTAQEMIETLENKRLYKDDEDGEVKKRTIGWLQESLAGI | |
| 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 | Phosphorylation | ------MSGMGIAIL ------CCCCCEEEE | 37.17 | 30377154 | |
| 17 | Phosphorylation | CIVRTKIYRITISFD EEECCCEEEEEEEEC | 9.49 | 28132839 | |
| 41 | Phosphorylation | LFLMMPTTLKDGYRM HHHHCCCCCCCCCCC | 26.41 | 27017623 | |
| 46 | Phosphorylation | PTTLKDGYRMNSQVN CCCCCCCCCCCCCCC | 19.47 | 27017623 | |
| 110 | Phosphorylation | AISAPTGTSQPTETI EEECCCCCCCCCCCH | 27.02 | 22369663 | |
| 111 | Phosphorylation | ISAPTGTSQPTETIG EECCCCCCCCCCCHH | 35.19 | 22369663 | |
| 114 | Phosphorylation | PTGTSQPTETIGEKL CCCCCCCCCCHHHHC | 37.82 | 22369663 | |
| 116 | Phosphorylation | GTSQPTETIGEKLSN CCCCCCCCHHHHCCC | 36.44 | 22369663 | |
| 122 | Phosphorylation | ETIGEKLSNEERVNS CCHHHHCCCHHHHCC | 53.95 | 22369663 | |
| 129 | Phosphorylation | SNEERVNSNVSASNS CCHHHHCCCCCCCCC | 35.43 | 22369663 | |
| 132 | Phosphorylation | ERVNSNVSASNSTTA HHHCCCCCCCCCCCC | 30.17 | 22369663 | |
| 134 | Phosphorylation | VNSNVSASNSTTAGT HCCCCCCCCCCCCCC | 24.65 | 22369663 | |
| 136 | Phosphorylation | SNVSASNSTTAGTGR CCCCCCCCCCCCCCC | 25.33 | 22369663 | |
| 137 | Phosphorylation | NVSASNSTTAGTGRM CCCCCCCCCCCCCCC | 25.56 | 22369663 | |
| 138 | Phosphorylation | VSASNSTTAGTGRML CCCCCCCCCCCCCCC | 23.94 | 22369663 | |
| 141 | Phosphorylation | SNSTTAGTGRMLSQS CCCCCCCCCCCCCCH | 21.10 | 22369663 | |
| 146 | Phosphorylation | AGTGRMLSQSLTNDS CCCCCCCCCHHCCCC | 14.37 | 22369663 | |
| 148 | Phosphorylation | TGRMLSQSLTNDSPS CCCCCCCHHCCCCCC | 33.51 | 22369663 | |
| 150 | Phosphorylation | RMLSQSLTNDSPSNE CCCCCHHCCCCCCCC | 42.08 | 28132839 | |
| 153 | Phosphorylation | SQSLTNDSPSNEIST CCHHCCCCCCCCCCH | 32.09 | 22369663 | |
| 155 | Phosphorylation | SLTNDSPSNEISTDQ HHCCCCCCCCCCHHH | 51.55 | 22369663 | |
| 159 | Phosphorylation | DSPSNEISTDQLKIF CCCCCCCCHHHHHHH | 21.54 | 22369663 | |
| 160 | Phosphorylation | SPSNEISTDQLKIFQ CCCCCCCHHHHHHHH | 33.16 | 22369663 | |
| 360 | Phosphorylation | THQQVNRSPISFPNA CCCCCCCCCCCCCCC | 22.75 | 28889911 | |
| 363 | Phosphorylation | QVNRSPISFPNASTD CCCCCCCCCCCCCCC | 37.73 | 30377154 | |
| 374 | Acetylation | ASTDKPFKLNPNGIK CCCCCCCCCCCCHHH | 56.75 | 24489116 | |
| 389 | Phosphorylation | RRRRNTQSNNNASTN HCCCCCCCCCCCCCC | 39.21 | 28889911 | |
| 395 | Phosphorylation | QSNNNASTNDHASAA CCCCCCCCCCHHHHH | 42.11 | 28889911 | |
| 510 | Phosphorylation | SGKSGVNTNIVNRNR CCCCCCCCCCCCCCC | 24.74 | 24961812 | |
| 519 | Phosphorylation | IVNRNRASTLPSYPK CCCCCCCCCCCCCCC | 27.52 | 24961812 | |
| 520 | Phosphorylation | VNRNRASTLPSYPKP CCCCCCCCCCCCCCC | 41.52 | 28152593 | |
| 523 | Phosphorylation | NRASTLPSYPKPMTV CCCCCCCCCCCCCEE | 58.12 | 21440633 | |
| 524 | Phosphorylation | RASTLPSYPKPMTVK CCCCCCCCCCCCEEE | 17.21 | 28889911 | |
| 560 | Phosphorylation | GRDNEEDSTAEEDEV CCCCCCCCCCCHHHC | 32.56 | 28889911 | |
| 579 | Phosphorylation | ETDMKNASINKRRRS HHHHHHHHHHHHHHH | 35.77 | 30377154 | |
| 608 | Acetylation | LHGESATKPNINSDL CCCCCCCCCCCCCHH | 35.47 | 24489116 |
| 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 HOT1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of HOT1_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 HOT1_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-111; SER-146; SER-153;SER-155 AND SER-360, AND MASS SPECTROMETRY. | |