| UniProt ID | SEPT9_RAT | |
|---|---|---|
| UniProt AC | Q9QZR6 | |
| Protein Name | Septin-9 | |
| Gene Name | 9-Sep | |
| Organism | Rattus norvegicus (Rat). | |
| Sequence Length | 564 | |
| Subcellular Localization | Cytoplasm, cytoskeleton . In embryonic fibroblasts, associated with actin stress fibers. No apparent co-distribution with microtubules, but some colocalization with vimentin filaments in the perinuclear region. | |
| Protein Description | Filament-forming cytoskeletal GTPase (By similarity). May play a role in cytokinesis (Potential).. | |
| Protein Sequence | MERDRITALKRSFEVEEIEPPNSTPPRRVQTPLLRATVASSSQKFQDLGVKNSEPAARLVDTLSQRSPKPSLRRVDLAGAKAPEPMSRRTELSIDISSKQVESTASTPGPSRFGLKRAEVLGHKTPEPVPRRTEITIVKPQESGLRRVETPASKAPEGSAMPVTDAAPKRVEIQVPKPAEAPNCPLPPQTLENSEAPMSQLQSRLEPRPPVTEVPYRNQEDSEVAPSCVVDMADNPRDAMLKQAPVSRNEKAPVDFGYVGIDSILEQMRRKAMKQGFEFNIMVVGQSGLGKSTLINTLFKSKISRKSVQPISEERIPKTIEIKSITHDIEEKGVRMKLTVIDTPGFGDHINNENCWQPIMKFINDQYEKYLQEEVNINRKKRIPDTRVHCCLYFIPATGHSLRPLDIEFMKRLSKVVNIVPVIAKADTLTLEERVYFKQRITSDLLSNGIDVYPQKEFDEAEDRLVNEKFREMIPFAVVGSDHEYQVNGKRILGRKTKWGTIEVENTTHCEFAYLRDLLIRTHMQNIKDITSNIHFEAYRVKRLNEGNSAMANGIEKEPETQEM | |
| 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 |
|---|---|---|---|---|---|
| 1 | Acetylation | -------MERDRITA -------CCHHHHHH | 9.58 | - | |
| 12 | Phosphorylation | RITALKRSFEVEEIE HHHHHHHCEEEEECC | 24.95 | 24259510 | |
| 23 | Phosphorylation | EEIEPPNSTPPRRVQ EECCCCCCCCCCCCC | 48.33 | 27097102 | |
| 24 | Phosphorylation | EIEPPNSTPPRRVQT ECCCCCCCCCCCCCC | 43.91 | 27097102 | |
| 31 | Phosphorylation | TPPRRVQTPLLRATV CCCCCCCCHHHHHHH | 17.04 | 29779826 | |
| 37 | Phosphorylation | QTPLLRATVASSSQK CCHHHHHHHCCCCHH | 15.35 | 25575281 | |
| 40 | Phosphorylation | LLRATVASSSQKFQD HHHHHHCCCCHHHHH | 26.62 | 23984901 | |
| 41 | Phosphorylation | LRATVASSSQKFQDL HHHHHCCCCHHHHHH | 27.35 | 23984901 | |
| 42 | Phosphorylation | RATVASSSQKFQDLG HHHHCCCCHHHHHHC | 34.59 | 25403869 | |
| 44 | Acetylation | TVASSSQKFQDLGVK HHCCCCHHHHHHCCC | 47.11 | 22902405 | |
| 62 | Phosphorylation | PAARLVDTLSQRSPK HHHHHHHHHHHCCCC | 22.34 | 25403869 | |
| 64 | Phosphorylation | ARLVDTLSQRSPKPS HHHHHHHHHCCCCCC | 26.16 | 27097102 | |
| 67 | Phosphorylation | VDTLSQRSPKPSLRR HHHHHHCCCCCCCCC | 29.64 | 28689409 | |
| 71 | Phosphorylation | SQRSPKPSLRRVDLA HHCCCCCCCCCHHCC | 40.40 | 25403869 | |
| 90 | Phosphorylation | PEPMSRRTELSIDIS CCCCCCCEEEEEECC | 39.92 | 27097102 | |
| 93 | Phosphorylation | MSRRTELSIDISSKQ CCCCEEEEEECCCCC | 16.39 | 27097102 | |
| 97 | Phosphorylation | TELSIDISSKQVEST EEEEEECCCCCCCCC | 27.95 | 30181290 | |
| 98 | Phosphorylation | ELSIDISSKQVESTA EEEEECCCCCCCCCC | 27.69 | 30181290 | |
| 103 | Phosphorylation | ISSKQVESTASTPGP CCCCCCCCCCCCCCC | 30.34 | 23984901 | |
| 104 | Phosphorylation | SSKQVESTASTPGPS CCCCCCCCCCCCCCC | 15.89 | 23984901 | |
| 106 | Phosphorylation | KQVESTASTPGPSRF CCCCCCCCCCCCCHH | 34.91 | 23984901 | |
| 107 | Phosphorylation | QVESTASTPGPSRFG CCCCCCCCCCCCHHC | 29.78 | 22108457 | |
| 111 | Phosphorylation | TASTPGPSRFGLKRA CCCCCCCCHHCCCHH | 46.27 | 23984901 | |
| 125 | Phosphorylation | AEVLGHKTPEPVPRR HHHCCCCCCCCCCCC | 27.49 | 23298284 | |
| 139 | Acetylation | RTEITIVKPQESGLR CCEEEEECCCCCCCC | 36.81 | 22902405 | |
| 150 | Phosphorylation | SGLRRVETPASKAPE CCCCCCCCCHHHCCC | 22.69 | 29779826 | |
| 153 | Phosphorylation | RRVETPASKAPEGSA CCCCCCHHHCCCCCC | 30.47 | 16641100 | |
| 258 | Phosphorylation | KAPVDFGYVGIDSIL CCCCCCCCCCHHHHH | 8.76 | - | |
| 307 | Phosphorylation | KSKISRKSVQPISEE HCCCCCCCCCCCCHH | 25.52 | 29779826 | |
| 312 | Phosphorylation | RKSVQPISEERIPKT CCCCCCCCHHHCCCE | 39.84 | 25403869 | |
| 332 | Acetylation | ITHDIEEKGVRMKLT EECCHHHHCCEEEEE | 50.33 | 22902405 | |
| 332 | Ubiquitination | ITHDIEEKGVRMKLT EECCHHHHCCEEEEE | 50.33 | - | |
| 428 | Phosphorylation | PVIAKADTLTLEERV HEEEECCCCCHHHHH | 26.88 | 23984901 | |
| 430 | Phosphorylation | IAKADTLTLEERVYF EEECCCCCHHHHHHH | 33.93 | 23984901 |
| 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 SEPT9_RAT !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SEPT9_RAT !! | ||||||
* 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 SEPT9_RAT !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of SEPT9_RAT !! | ||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:regulation of aquaporin-2 phosphorylation at two sites."; Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.; Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-31 AND THR-150, AND MASSSPECTROMETRY. | |