| UniProt ID | HCM1_YEAST | |
|---|---|---|
| UniProt AC | P25364 | |
| Protein Name | Forkhead transcription factor HCM1 | |
| Gene Name | HCM1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 564 | |
| Subcellular Localization | Cytoplasm. Nucleus. | |
| Protein Description | Transcription factor regulating the cell cycle specific transcription of a spindle pole body (SPB) calmodulin binding protein SPC110. Required for full induction of SPC110 transcription in late G1. Binds to DNA consensus sequence 5'-[AT]AA[TC]AAACAA[AT]-3'. Dosage dependent suppressor of calmodulin mutants which have specific defects in SPB assembly.. | |
| Protein Sequence | MMNEDISIIDGHNSFLTEKSTVLLTQAKRTLEDEKEMITPPSSTVRKTMKEVNKRPSHPLSPDHSSPIAPSKAKRQRSDTCARSNGNLTLEEILQSLERRRINGELAKKPPYSYATLICLAILQSQEGKLTLSQIYHWIHVHFPYYKQKDASWQNSIRHNLSLNDAFIKTEKSCDGKGHFWEVRPGAETKFFKGENRGYEFVKDSLQDIGKYFEIDSTLDELEQVESGEGNDDLPDEEEREEAGKFPSIEIQLNSSPILRVSQLHHIPQLKTDNSVLNPHENLESMRNMIENDVNNIDSLEPPYVMKKYHTSLGLPSLVNAKDHFQAGVKNNNITQANRFNTLPITSAKSPQNFRKYFTSFNSNFEDLSPLRSNVGAGSLLDPLPYSPLKLYDQKNLALMSKPQSQQSYSNSQLPPPPSSHGSDLLKTPKMRHSDGLEKTPSRLISTPKDGNSILRKWQTPSHLFEDLYCSPLFRAIETPIRYITTPGGTLETQISPRKSSAPDVLTSATNSKFASSGLFGVDVYSVWKRATEKISDGNNTTDSNQKHHPYHNHPSNDSGNEKN | |
| 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 |
|---|---|---|---|---|---|
| 21 | Phosphorylation | SFLTEKSTVLLTQAK CHHCHHHHHHHHHHC | 26.66 | 30377154 | |
| 25 | Phosphorylation | EKSTVLLTQAKRTLE HHHHHHHHHHCHHHH | 23.48 | 30377154 | |
| 39 | Phosphorylation | EDEKEMITPPSSTVR HHHHHHCCCCHHHHH | 28.03 | 25752575 | |
| 42 | Phosphorylation | KEMITPPSSTVRKTM HHHCCCCHHHHHHHH | 39.58 | 21126336 | |
| 57 | Phosphorylation | KEVNKRPSHPLSPDH HHHHCCCCCCCCCCC | 41.59 | 21440633 | |
| 61 | Phosphorylation | KRPSHPLSPDHSSPI CCCCCCCCCCCCCCC | 32.50 | 21440633 | |
| 65 | Phosphorylation | HPLSPDHSSPIAPSK CCCCCCCCCCCCCCH | 45.23 | 21440633 | |
| 66 | Phosphorylation | PLSPDHSSPIAPSKA CCCCCCCCCCCCCHH | 19.53 | 21440633 | |
| 71 | Phosphorylation | HSSPIAPSKAKRQRS CCCCCCCCHHHHHCC | 35.90 | 19823750 | |
| 89 | Phosphorylation | ARSNGNLTLEEILQS HHHCCCCCHHHHHHH | 35.80 | 28889911 | |
| 272 | Phosphorylation | HHIPQLKTDNSVLNP CCCCCCCCCCCCCCH | 49.35 | 27017623 | |
| 275 | Phosphorylation | PQLKTDNSVLNPHEN CCCCCCCCCCCHHHC | 30.69 | 27017623 | |
| 311 | Phosphorylation | YVMKKYHTSLGLPSL CHHHHHHCCCCCCCH | 23.66 | 21551504 | |
| 312 | Phosphorylation | VMKKYHTSLGLPSLV HHHHHHCCCCCCCHH | 13.71 | 25752575 | |
| 335 | Phosphorylation | GVKNNNITQANRFNT CCCCCCCCCCCCCCC | 24.61 | 24961812 | |
| 342 | Phosphorylation | TQANRFNTLPITSAK CCCCCCCCCCCCCCC | 31.06 | 25752575 | |
| 346 | Phosphorylation | RFNTLPITSAKSPQN CCCCCCCCCCCCCHH | 22.23 | 24961812 | |
| 347 | Phosphorylation | FNTLPITSAKSPQNF CCCCCCCCCCCCHHH | 34.12 | 24961812 | |
| 350 | Phosphorylation | LPITSAKSPQNFRKY CCCCCCCCCHHHHHH | 31.28 | 28889911 | |
| 356 | Ubiquitination | KSPQNFRKYFTSFNS CCCHHHHHHHHHCCC | 40.35 | 17644757 | |
| 369 | Phosphorylation | NSNFEDLSPLRSNVG CCCCCCCCCHHCCCC | 33.92 | 24909858 | |
| 386 | Phosphorylation | SLLDPLPYSPLKLYD CCCCCCCCCCCEECC | 30.51 | 22890988 | |
| 387 | Phosphorylation | LLDPLPYSPLKLYDQ CCCCCCCCCCEECCC | 23.09 | 22890988 | |
| 405 | Phosphorylation | ALMSKPQSQQSYSNS HHCCCCCHHCCCCCC | 38.42 | 19823750 | |
| 408 | Phosphorylation | SKPQSQQSYSNSQLP CCCCHHCCCCCCCCC | 23.92 | 19823750 | |
| 409 | Phosphorylation | KPQSQQSYSNSQLPP CCCHHCCCCCCCCCC | 13.92 | 19823750 | |
| 410 | Phosphorylation | PQSQQSYSNSQLPPP CCHHCCCCCCCCCCC | 34.94 | 19823750 | |
| 412 | Phosphorylation | SQQSYSNSQLPPPPS HHCCCCCCCCCCCCC | 27.44 | 19823750 | |
| 419 | Phosphorylation | SQLPPPPSSHGSDLL CCCCCCCCCCCCCCC | 40.52 | 19823750 | |
| 420 | Phosphorylation | QLPPPPSSHGSDLLK CCCCCCCCCCCCCCC | 37.33 | 19823750 | |
| 423 | Phosphorylation | PPPSSHGSDLLKTPK CCCCCCCCCCCCCCC | 21.47 | 19823750 | |
| 428 | Phosphorylation | HGSDLLKTPKMRHSD CCCCCCCCCCCCCCC | 28.28 | 19823750 | |
| 440 | Phosphorylation | HSDGLEKTPSRLIST CCCCCCCCCCCEEEC | 19.68 | 28889911 | |
| 446 | Phosphorylation | KTPSRLISTPKDGNS CCCCCEEECCCCCCH | 43.16 | 21440633 | |
| 447 | Phosphorylation | TPSRLISTPKDGNSI CCCCEEECCCCCCHH | 27.62 | 28889911 | |
| 453 | Phosphorylation | STPKDGNSILRKWQT ECCCCCCHHHHHCCC | 28.64 | 25704821 | |
| 479 | Phosphorylation | PLFRAIETPIRYITT HHHHHHCCCCEEEEC | 20.22 | 19684113 | |
| 485 | Phosphorylation | ETPIRYITTPGGTLE CCCCEEEECCCCCEE | 20.29 | 19684113 | |
| 486 | Phosphorylation | TPIRYITTPGGTLET CCCEEEECCCCCEEE | 15.46 | 24909858 | |
| 496 | Phosphorylation | GTLETQISPRKSSAP CCEEEECCCCCCCCC | 14.61 | 21082442 | |
| 499 | Ubiquitination | ETQISPRKSSAPDVL EEECCCCCCCCCCHH | 52.74 | 17644757 | |
| 500 | Phosphorylation | TQISPRKSSAPDVLT EECCCCCCCCCCHHH | 32.77 | 21440633 | |
| 501 | Phosphorylation | QISPRKSSAPDVLTS ECCCCCCCCCCHHHH | 47.02 | 25752575 | |
| 507 | Phosphorylation | SSAPDVLTSATNSKF CCCCCHHHHHCCCCC | 19.03 | 27017623 | |
| 525 | Phosphorylation | GLFGVDVYSVWKRAT CCCCCCHHHHHHHHH | 7.95 | 21440633 | |
| 526 | Phosphorylation | LFGVDVYSVWKRATE CCCCCHHHHHHHHHC | 22.73 | 27017623 |
| 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 HCM1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of HCM1_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 HCM1_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 THR-39; SER-312; THR-342;SER-387; SER-496 AND SER-501, AND MASS SPECTROMETRY. | |
