SEPT5_MOUSE - dbPTM
SEPT5_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SEPT5_MOUSE
UniProt AC Q9Z2Q6
Protein Name Septin-5
Gene Name 5-Sep
Organism Mus musculus (Mouse).
Sequence Length 369
Subcellular Localization Cytoplasm. Cytoplasm, cytoskeleton.
Protein Description Filament-forming cytoskeletal GTPase (By similarity). Involved in cytokinesis (Potential). May play a role in platelet secretion..
Protein Sequence MSTGLRYKSKLATPEDKQDIDKQYVGFATLPNQVHRKSVKKGFDFTLMVAGESGLGKSTLVHSLFLTDLYKDRKLLSAEERINQTVEILKHTVDIEEKGVKLKLTIVDTPGFGDAVNNSECWKPITDYVDQQFEQYFRDESGLNRKNIQDNRVHCCLYFISPFGHGLRPVDVGFMKALHEKVNIVPLIAKADCLVPSEIRKLKDRIREEIDKFGIHVYQFPECDSDEDEDFKQQDRELKESAPFAVIGSNTVVEAKGQRVRGRLYPWGIVEVENQAHCDFVKLRNMLIRTHMHDLKDVTCDVHYENYRAHCIQQMTSKLTQDSRMESPIPILPLPTPDAETEKLIRMKDEELRRMQEMLQKMKQQMQDQ
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
2Phosphorylation------MSTGLRYKS
------CCCCCHHHC		31.0522324799
3Phosphorylation-----MSTGLRYKSK
-----CCCCCHHHCC		38.6522324799
13PhosphorylationRYKSKLATPEDKQDI
HHHCCCCCHHHHHCC		37.3325521595
17UbiquitinationKLATPEDKQDIDKQY
CCCCHHHHHCCCHHH		48.4827667366
24PhosphorylationKQDIDKQYVGFATLP
HHCCCHHHCEEEECC		14.3119737024
29PhosphorylationKQYVGFATLPNQVHR
HHHCEEEECCCHHHH		40.2529899451
59PhosphorylationESGLGKSTLVHSLFL
CCCCCHHHHHHHHHH		35.9628576409
67PhosphorylationLVHSLFLTDLYKDRK
HHHHHHHHHHHHCHH		19.3428576409
70PhosphorylationSLFLTDLYKDRKLLS
HHHHHHHHHCHHHHC		17.4128576409
71UbiquitinationLFLTDLYKDRKLLSA
HHHHHHHHCHHHHCH		59.3522790023
98UbiquitinationHTVDIEEKGVKLKLT
HHCCHHHHCEEEEEE		57.1022790023
158PhosphorylationNRVHCCLYFISPFGH
CCEEEEEEEECCCCC		5.74-
161PhosphorylationHCCLYFISPFGHGLR
EEEEEEECCCCCCCC		12.32-
168MethylationSPFGHGLRPVDVGFM
CCCCCCCCCCCHHHH		33.5124129315
181UbiquitinationFMKALHEKVNIVPLI
HHHHHHHHCCCHHHH		29.8122790023
190UbiquitinationNIVPLIAKADCLVPS
CCHHHHHCCCCCCHH		37.4522790023
197PhosphorylationKADCLVPSEIRKLKD
CCCCCCHHHHHHHHH		37.87-
218PhosphorylationDKFGIHVYQFPECDS
HHHCEEEEECCCCCC		7.1225619855
225PhosphorylationYQFPECDSDEDEDFK
EECCCCCCCCCCHHH		55.3425521595
239UbiquitinationKQQDRELKESAPFAV
HHHHHHHHHHCCEEE		44.8922790023
251PhosphorylationFAVIGSNTVVEAKGQ
EEEECCCCEEEECCE		27.8525521595
256UbiquitinationSNTVVEAKGQRVRGR
CCCEEEECCEEECCE		41.9122790023
265PhosphorylationQRVRGRLYPWGIVEV
EEECCEEECCCEEEE		8.7919607848
278S-palmitoylationEVENQAHCDFVKLRN
EEECCCCCCHHHHHH		4.9428680068
296UbiquitinationRTHMHDLKDVTCDVH
HHCCCCCCCCCCCCC		57.1022790023
296AcetylationRTHMHDLKDVTCDVH
HHCCCCCCCCCCCCC		57.1022826441
318UbiquitinationCIQQMTSKLTQDSRM
HHHHHHHHCCCCCCC		46.5222790023
320PhosphorylationQQMTSKLTQDSRMES
HHHHHHCCCCCCCCC		33.7826643407
323PhosphorylationTSKLTQDSRMESPIP
HHHCCCCCCCCCCCC		24.5726643407
327PhosphorylationTQDSRMESPIPILPL
CCCCCCCCCCCCCCC		20.8425521595
336PhosphorylationIPILPLPTPDAETEK
CCCCCCCCCCHHHHH		41.2924925903
341PhosphorylationLPTPDAETEKLIRMK
CCCCCHHHHHHHHHC		39.8925619855
343AcetylationTPDAETEKLIRMKDE
CCCHHHHHHHHHCHH		57.5422902405
343UbiquitinationTPDAETEKLIRMKDE
CCCHHHHHHHHHCHH		57.5422790023
348UbiquitinationTEKLIRMKDEELRRM
HHHHHHHCHHHHHHH		52.7327667366
361UbiquitinationRMQEMLQKMKQQMQD
HHHHHHHHHHHHHHC		44.0727667366
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
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 SEPT5_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SEPT5_MOUSE !!
Disease-associated PTM Sites based on SAP

* 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 SEPT5_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SEPT2_MOUSESept2physical
11739749
SEPT7_MOUSESept7physical
11739749
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SEPT5_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-225, AND MASSSPECTROMETRY.
"Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations.";
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
Mol. Cell. Proteomics 6:283-293(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-327, AND MASSSPECTROMETRY.
"Phosphoproteomic analysis of the developing mouse brain.";
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
Mol. Cell. Proteomics 3:1093-1101(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-327 AND THR-336, ANDMASS SPECTROMETRY.

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