| UniProt ID | FLP1_SCHPO | |
|---|---|---|
| UniProt AC | Q9P7H1 | |
| Protein Name | Tyrosine-protein phosphatase CDC14 homolog | |
| Gene Name | clp1 | |
| Organism | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast). | |
| Sequence Length | 537 | |
| Subcellular Localization | Nucleus, nucleolus. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body. Cell septum. Localizes to kinetochores in prometaphase. Cytoplasmic retention is mediated through the binding of rad24. Tethered to the contractile ring by | |
| Protein Description | Protein phosphatase which antagonizes mitotic cyclin-dependent kinase cdc2, the inactivation of which is essential for exit from mitosis. To access its substrates, is released from nucleolar sequestration during mitosis. Plays an essential in coordinating the nuclear division cycle with cytokinesis through the cytokinesis checkpoint. Involved in chromosome segregation, where it is required for meiosis I spindle dissambly as well as for establishing two consecutive chromosome segregation phases. Allows damaged actomyosin rings to be maintained to facilitate completion of cell division in response to minor perturbation of the cell division machinery. Dephosphorylates the mitotic inducer cdc25 for its rapid degradation. Down-regulation of cdc25 activity ensures a prompt inactivation of mitotic cdc2 complexes to trigger cell division. Dephosphorylates also cdc2-phosphorylated nsk1, allowing nsk1-binding to kinetochores and spindle. Dephosphorylates ase1, which is essential for spindle midzone assembly and for continuous extension of the anaphase spindle. Tethered to the contractile ring by mid1, where it dephosphorylates cdc15.. | |
| Protein Sequence | MDYQDDGLGEMIEFLEDKLYYTSLSQPPKAELYPHMHFFTIDDELIYNPFYHDFGPLNVSHLIRFAVIVHGIMGKHRQAKKSKAIVLYSSTDTRLRANAACLLACYMVLVQNWPPHLALAPLAQAEPPFLGFRDAGYAVSDYYITIQDCVYGLWRARESSILNIRNIDVHDYETYERVENGDFNWISPKFIAFASPIQAGWNHASTRPKKLPQPFAIVLDYFVANKVKLIVRLNGPLYDKKTFENVGIRHKEMYFEDGTVPELSLVKEFIDLTEEVEEDGVIAVHCKAGLGRTGCLIGAYLIYKHCFTANEVIAYMRIMRPGMVVGPQQHWLHINQVHFRAYFYEKAMGRAIQQATAAEPLATPPRHPLNATNGTSQSNISTPLPEPTPGQPRKVSGHNPPSARRLPSASSVKFNEKLKNASKQSIQNENKASYSSYEDSEIQNDDETRTVGTPTETISVVRLRRSSSQSNIEPNGVRSPTSSPTGSPIRRTSGNRWSSGSSHSKKSAQRSVSMSSLNNTSNGRVAKPKPSKSRLIS | |
| 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 |
|---|---|---|---|---|---|
| 363 | Phosphorylation | TAAEPLATPPRHPLN HHCCCCCCCCCCCCC | 41.32 | 27738172 | |
| 381 | Phosphorylation | GTSQSNISTPLPEPT CCCCCCCCCCCCCCC | 28.37 | 27738172 | |
| 396 | Phosphorylation | PGQPRKVSGHNPPSA CCCCCCCCCCCCCHH | 37.05 | 29996109 | |
| 402 | Phosphorylation | VSGHNPPSARRLPSA CCCCCCCHHHCCCCC | 35.35 | 21712547 | |
| 408 | Phosphorylation | PSARRLPSASSVKFN CHHHCCCCCCHHHHH | 45.43 | 21712547 | |
| 410 | Phosphorylation | ARRLPSASSVKFNEK HHCCCCCCHHHHHHH | 39.75 | 25720772 | |
| 411 | Phosphorylation | RRLPSASSVKFNEKL HCCCCCCHHHHHHHH | 29.10 | 29996109 | |
| 425 | Phosphorylation | LKNASKQSIQNENKA HHHHHHHHHHCCCCC | 29.85 | 21712547 | |
| 434 | Phosphorylation | QNENKASYSSYEDSE HCCCCCCCCCCCCCC | 13.39 | 25720772 | |
| 435 | Phosphorylation | NENKASYSSYEDSEI CCCCCCCCCCCCCCC | 24.77 | 25720772 | |
| 436 | Phosphorylation | ENKASYSSYEDSEIQ CCCCCCCCCCCCCCC | 25.06 | 25720772 | |
| 450 | Phosphorylation | QNDDETRTVGTPTET CCCCCCEECCCCCCE | 30.61 | 25720772 | |
| 453 | Phosphorylation | DETRTVGTPTETISV CCCEECCCCCCEEEE | 23.77 | 28889911 | |
| 459 | Phosphorylation | GTPTETISVVRLRRS CCCCCEEEEEEEECC | 23.21 | 25720772 | |
| 466 | Phosphorylation | SVVRLRRSSSQSNIE EEEEEECCCCCCCCC | 28.10 | 25720772 | |
| 467 | Phosphorylation | VVRLRRSSSQSNIEP EEEEECCCCCCCCCC | 30.50 | 29996109 | |
| 468 | Phosphorylation | VRLRRSSSQSNIEPN EEEECCCCCCCCCCC | 38.58 | 28889911 | |
| 470 | Phosphorylation | LRRSSSQSNIEPNGV EECCCCCCCCCCCCC | 41.54 | 28889911 | |
| 479 | Phosphorylation | IEPNGVRSPTSSPTG CCCCCCCCCCCCCCC | 30.08 | 25720772 | |
| 481 | Phosphorylation | PNGVRSPTSSPTGSP CCCCCCCCCCCCCCC | 42.98 | 29996109 | |
| 482 | Phosphorylation | NGVRSPTSSPTGSPI CCCCCCCCCCCCCCC | 37.39 | 25720772 | |
| 483 | Phosphorylation | GVRSPTSSPTGSPIR CCCCCCCCCCCCCCC | 29.03 | 25720772 | |
| 513 | Phosphorylation | KSAQRSVSMSSLNNT HHHCHHCCHHHCCCC | 17.75 | 17562791 | |
| 515 | Phosphorylation | AQRSVSMSSLNNTSN HCHHCCHHHCCCCCC | 24.94 | 25720772 | |
| 516 | Phosphorylation | QRSVSMSSLNNTSNG CHHCCHHHCCCCCCC | 26.86 | 25720772 |
| 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 FLP1_SCHPO !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of FLP1_SCHPO !! | ||||||
* 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 FLP1_SCHPO !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
loading...
