| UniProt ID | FFT3_SCHPO | |
|---|---|---|
| UniProt AC | O42861 | |
| Protein Name | ATP-dependent helicase fft3 | |
| Gene Name | fft3 | |
| Organism | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast). | |
| Sequence Length | 922 | |
| Subcellular Localization | Nucleus. Chromosome. | |
| Protein Description | DNA helicase that possesses intrinsic ATP-dependent nucleosome-remodeling activity and is required for heterochromatin organization. Required for maintaining a heterochromatin chromatin structure at centromeres and subtelomeres by protecting these regions from euchromatin assembly. Enhances the nucleotide exchange activity of the pim1 guanine nucleotide exchange factor and abolishes histone-H3-mediated RanGAP inhibition. Involved in the construction of the centromeres.. | |
| Protein Sequence | MDGKRKIEHTADGTHYDATSNVKRKPIFPPFIADSLSEATEKANVMGGGMNSRLQILSEMSKRVQATAPISSLEHFKQLSDISPSFTSSANSINQPYNYSGSLENLVPTPSAGTPSQFMDAQNPYGAVYNALSQFSETEPKMPSYMDDEEASDSLPLSLSSQSLSSQVTNQKPAPHRLTMRERYAANNLTNGLQFTLPLSSRKTYEPEADDDSNDDMYSDDDSNADRWASRIDTAALKEEVLKYMNRCSTQDLADMTGCTLAEAEFMVAKRPFPDLESALVVKQPRPVIPKGRRGRREKTPLGPRLVGICMEIMRGYFVVDALIRQCEQLGGKIQRGIEAWGLSNTATSDEGETSLVNFDQMKSFGTPANSSFITTPPASFSPDIKLQDYQIIGINWLYLLYELKLAGILADEMGLGKTCQTIAFFSLLMDKNINGPHLVIAPASTMENWLREFAKFCPKLKIELYYGSQVEREEIRERINSNKDSYNVMLTTYRLAATSKADRLFLRNQKFNVCVYDEGHYLKNRASERYRHLMSIPADFRVLLTGTPLQNNLKELISLLAFILPHVFDYGLKSLDVIFTMKKSPESDFERALLSEQRVSRAKMMMAPFVLRRKKSQVLDALPKKTRIIEFCEFSEEERRRYDDFASKQSVNSLLDENVMKTNLDTNANLAKKKSTAGFVLVQLRKLADHPMLFRIHYKDDILRQMAKAIMNEPQYKKANELYIFEDMQYMSDIELHNLCCKFPSINSFQLKDEPWMDATKVRKLKKLLTNAVENGDRVVLFSQFTQVLDILQLVMKSLNLKFLRFDGSTQVDFRQDLIDQFYADESINVFLLSTKAGGFGINLACANMVILYDVSFNPFDDLQAEDRAHRVGQKKEVTVYKFVVKDTIEEHIQRLANAKIALDATLSGNAETVEAEDDDD | |
| 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 |
|---|---|---|---|---|---|
| 144 | Phosphorylation | ETEPKMPSYMDDEEA CCCCCCCCCCCCHHH | 29996109 | ||
| 145 | Phosphorylation | TEPKMPSYMDDEEAS CCCCCCCCCCCHHHC | 24763107 | ||
| 152 | Phosphorylation | YMDDEEASDSLPLSL CCCCHHHCCCCCCCC | 29996109 | ||
| 154 | Phosphorylation | DDEEASDSLPLSLSS CCHHHCCCCCCCCCC | 21712547 | ||
| 158 | Phosphorylation | ASDSLPLSLSSQSLS HCCCCCCCCCCCCHH | 21712547 | ||
| 160 | Phosphorylation | DSLPLSLSSQSLSSQ CCCCCCCCCCCHHHH | 24763107 | ||
| 161 | Phosphorylation | SLPLSLSSQSLSSQV CCCCCCCCCCHHHHH | 21712547 | ||
| 163 | Phosphorylation | PLSLSSQSLSSQVTN CCCCCCCCHHHHHHC | 29996109 | ||
| 165 | Phosphorylation | SLSSQSLSSQVTNQK CCCCCCHHHHHHCCC | 24763107 | ||
| 166 | Phosphorylation | LSSQSLSSQVTNQKP CCCCCHHHHHHCCCC | 29996109 | ||
| 169 | Phosphorylation | QSLSSQVTNQKPAPH CCHHHHHHCCCCCCC | 29996109 | ||
| 204 | Phosphorylation | LPLSSRKTYEPEADD EECCCCCCCCCCCCC | 27738172 | ||
| 213 | Phosphorylation | EPEADDDSNDDMYSD CCCCCCCCCCCCCCC | 28889911 | ||
| 218 | Phosphorylation | DDSNDDMYSDDDSNA CCCCCCCCCCCCCCH | 27738172 | ||
| 219 | Phosphorylation | DSNDDMYSDDDSNAD CCCCCCCCCCCCCHH | 28889911 | ||
| 230 | Phosphorylation | SNADRWASRIDTAAL CCHHHHHHHCHHHHH | 25720772 | ||
| 617 | Phosphorylation | FVLRRKKSQVLDALP HHHHHHHHHHHHHCC | 28889911 |
| 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 FFT3_SCHPO !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of FFT3_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 FFT3_SCHPO !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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