| UniProt ID | CHR2_SCHPO | |
|---|---|---|
| UniProt AC | O94486 | |
| Protein Name | Chitin synthase regulatory factor 2 | |
| Gene Name | chr2 | |
| Organism | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast). | |
| Sequence Length | 512 | |
| Subcellular Localization |
Membrane Lipid-anchor . |
|
| Protein Description | Involved in chitin biosynthesis.. | |
| Protein Sequence | MLVSNGGTGSAHEWDRTTIDYDIEPSSDTHAIEISSNDDYLHPLAQFKKSEEFDEVPTNTLIHEVPSFSDSASNIQSQRNLSPFKELEIVSKKKSEQTFSSAVDFSAINVKNLNLKSGLFDPEPPSYDPDYAFNQRSLQSDPGSDEMFRNFKKSISLEELKSSYKLASAEMCEPETRLSFLQLALQAEKSSSRRNREYVARKKEEAFDYLTSFVSQGNSFFGYSEALYLLAVCYGTGALRTEINEKEAYRLYKMAADLNHVQAAYRVAICLQMGFGVTQNTEEAIHYFFRAASGQHVGAMHRMALIYFRGLMSVKRDPVKAMYYLNLGALEADHEFPQALYDLAELYEHGSSYLDGLLELSPRKAFVLYHIAAKYGLKDAQLRVARCFELGQLECDINLVRSFVWYRRLARKRNPEAMWKLSQFYLNGVDDVIYPNPELANEWAKAAAYKNHHLASTFVQDVGKEDVFEKTSITISNEERKSRNSESLPKKKKRLSMLSFKRSKNRESCIIS | |
| 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 |
|---|---|---|---|---|---|
| 50 | Phosphorylation | PLAQFKKSEEFDEVP CHHHHCCCCCCCCCC | 42.84 | 21712547 | |
| 58 | Phosphorylation | EEFDEVPTNTLIHEV CCCCCCCCCCEEEEC | 46.11 | 29996109 | |
| 60 | Phosphorylation | FDEVPTNTLIHEVPS CCCCCCCCEEEECCC | 29.57 | 29996109 | |
| 67 | Phosphorylation | TLIHEVPSFSDSASN CEEEECCCCCCCCHH | 42.43 | 21712547 | |
| 69 | Phosphorylation | IHEVPSFSDSASNIQ EEECCCCCCCCHHHH | 34.69 | 29996109 | |
| 71 | Phosphorylation | EVPSFSDSASNIQSQ ECCCCCCCCHHHHHH | 32.19 | 21712547 | |
| 73 | Phosphorylation | PSFSDSASNIQSQRN CCCCCCCHHHHHHCC | 38.12 | 29996109 | |
| 77 | Phosphorylation | DSASNIQSQRNLSPF CCCHHHHHHCCCCCC | 27.58 | 27738172 | |
| 82 | Phosphorylation | IQSQRNLSPFKELEI HHHHCCCCCCHHHEE | 31.66 | 28889911 | |
| 91 | Phosphorylation | FKELEIVSKKKSEQT CHHHEEEEECCCCCC | 44.40 | 25720772 | |
| 95 | Phosphorylation | EIVSKKKSEQTFSSA EEEEECCCCCCHHHC | 43.76 | 24763107 | |
| 98 | Phosphorylation | SKKKSEQTFSSAVDF EECCCCCCHHHCCCH | 22.79 | 24763107 | |
| 100 | Phosphorylation | KKSEQTFSSAVDFSA CCCCCCHHHCCCHHH | 22.30 | 21712547 | |
| 101 | Phosphorylation | KSEQTFSSAVDFSAI CCCCCHHHCCCHHHC | 28.28 | 24763107 | |
| 471 | Phosphorylation | KEDVFEKTSITISNE CHHHHHHHEEEECHH | 20.40 | 21712547 | |
| 472 | Phosphorylation | EDVFEKTSITISNEE HHHHHHHEEEECHHH | 28.89 | 21712547 | |
| 476 | Phosphorylation | EKTSITISNEERKSR HHHEEEECHHHHHHC | 29.55 | 28889911 | |
| 482 | Phosphorylation | ISNEERKSRNSESLP ECHHHHHHCCCCCCC | 42.80 | 24763107 | |
| 485 | Phosphorylation | EERKSRNSESLPKKK HHHHHCCCCCCCHHH | 27.70 | 28889911 | |
| 487 | Phosphorylation | RKSRNSESLPKKKKR HHHCCCCCCCHHHHH | 50.20 | 21712547 | |
| 496 | Phosphorylation | PKKKKRLSMLSFKRS CHHHHHHHHHHHHCC | 23.01 | 24763107 | |
| 499 | Phosphorylation | KKRLSMLSFKRSKNR HHHHHHHHHHCCCCC | 21.78 | 24763107 | |
| 509 | Methylation | RSKNRESCIIS---- CCCCCCCCCCC---- | 2.47 | - | |
| 509 | Farnesylation | RSKNRESCIIS---- CCCCCCCCCCC---- | 2.47 | - |
| 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 CHR2_SCHPO !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CHR2_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 CHR2_SCHPO !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of CHR2_SCHPO !! | ||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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