SEPT6_MOUSE - dbPTM
SEPT6_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SEPT6_MOUSE
UniProt AC Q9R1T4
Protein Name Septin-6
Gene Name 6-Sep
Organism Mus musculus (Mouse).
Sequence Length 434
Subcellular Localization Cytoplasm. Cytoplasm, cytoskeleton, spindle. Chromosome, centromere, kinetochore. Cleavage furrow. Midbody. Cell projection, cilium, flagellum . In metaphase cells, localized within the microtubule spindle. At the metaphase plate, in close apposition
Protein Description Filament-forming cytoskeletal GTPase. Required for normal organization of the actin cytoskeleton. Involved in cytokinesis. Forms a filamentous structure with SEPT12, SEPT6, SEPT2 and probably SEPT4 at the sperm annulus which is required for the structural integrity and motility of the sperm tail during postmeiotic differentiation..
Protein Sequence MAAADIARQVGEDCRTVPLAGHVGFDSLPDQLVNKSVSQGFCFNILCVGETGLGKSTLMDTLFNTKFEGEPATHTQPGVQLQSNTYDLQESNVGLKLTIVSTVGFGDQINKEDSYKPIVEFIDAQFEAYLQEELKIRRVLHSYHDSRIHVCLYFIAPTGHSLKSLDLVTMKKLDSKVNIIPVIAKSDAISKSELAKFKIKITSELVSNGVQIYQFPTDDESVSEINGTMNAHLPFAVVGSTEEVKIGNKMMRARQYPWGTVQVENEAHCDFVKLREMLIRVNMEDLREQTHARHYELYRRCKLEEMGFKDTDPDSKPFSLQETYEAKRNEFLGELQKKEEEMRQMFVQRVKEKEAELKEAEKELHEKFDRLKKLHQEEKKKLEDKKKCLDEEMNAFKQRKAAAELLQSQGSQAGGSQTLKRDKEKKNNPWLCIE
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
2Acetylation------MAAADIARQ
------CCHHHHHHH		16.03-
27PhosphorylationAGHVGFDSLPDQLVN
CCCCCCCCCCHHHCC		39.2729899451
42S-palmitoylationKSVSQGFCFNILCVG
CCCCCCCCEEEEEEC		3.0628680068
175UbiquitinationVTMKKLDSKVNIIPV
EEHHHCCCCCCEEEE		49.2727667366
176UbiquitinationTMKKLDSKVNIIPVI
EHHHCCCCCCEEEEE		38.6822790023
192PhosphorylationKSDAISKSELAKFKI
CCCCCCHHHHHCCCE		30.9325521595
269S-palmitoylationQVENEAHCDFVKLRE
EECCCCCCCHHHHHH		5.8328680068
300UbiquitinationRHYELYRRCKLEEMG
HHHHHHHHHCHHHCC		14.3627667366
308UbiquitinationCKLEEMGFKDTDPDS
HCHHHCCCCCCCCCC		6.6327667366
309UbiquitinationKLEEMGFKDTDPDSK
CHHHCCCCCCCCCCC		54.7327667366
318UbiquitinationTDPDSKPFSLQETYE
CCCCCCCCCHHHHHH		15.1927667366
326UbiquitinationSLQETYEAKRNEFLG
CHHHHHHHHHHHHHH		12.9927667366
327UbiquitinationLQETYEAKRNEFLGE
HHHHHHHHHHHHHHH		43.7627667366
337UbiquitinationEFLGELQKKEEEMRQ
HHHHHHHHHHHHHHH		74.83-
367AcetylationAEKELHEKFDRLKKL
HHHHHHHHHHHHHHH		41.64-
387UbiquitinationKKLEDKKKCLDEEMN
HHHHHHHHHHHHHHH		45.8522790023
397UbiquitinationDEEMNAFKQRKAAAE
HHHHHHHHHHHHHHH		46.9422790023
408PhosphorylationAAAELLQSQGSQAGG
HHHHHHHHCCCCCCC		36.1625619855
411PhosphorylationELLQSQGSQAGGSQT
HHHHHCCCCCCCCHH		14.8225619855
416PhosphorylationQGSQAGGSQTLKRDK
CCCCCCCCHHHCCCH		21.0525521595
418PhosphorylationSQAGGSQTLKRDKEK
CCCCCCHHHCCCHHH		35.6225521595
432S-palmitoylationKKNNPWLCIE-----
HCCCCCCCCC-----		2.6528680068
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 SEPT6_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SEPT6_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 SEPT6_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CDC5L_HUMANCDC5Lphysical
26496610
SEPT7_HUMANSEPT7physical
26496610
IMA1_HUMANKPNA2physical
26496610
SEPT2_HUMANSEPT2physical
26496610
TAF1_HUMANTAF1physical
26496610
TAF4_HUMANTAF4physical
26496610
TAF5_HUMANTAF5physical
26496610
BAP1_HUMANBAP1physical
26496610
ADAS_HUMANAGPSphysical
26496610
DHX34_HUMANDHX34physical
26496610
RUSC2_HUMANRUSC2physical
26496610
GILT_HUMANIFI30physical
26496610
SEPT9_HUMANSEPT9physical
26496610
RFIP2_HUMANRAB11FIP2physical
26496610
SNW1_HUMANSNW1physical
26496610
TNPO3_HUMANTNPO3physical
26496610
SMBT1_HUMANSFMBT1physical
26496610
BRE1A_HUMANRNF20physical
26496610
MUC13_HUMANMUC13physical
26496610
RBM26_HUMANRBM26physical
26496610
F192A_HUMANFAM192Aphysical
26496610
PR38A_HUMANPRPF38Aphysical
26496610
SEP10_HUMANSEPT10physical
26496610
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SEPT6_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-416, AND MASSSPECTROMETRY.

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