SEPT7_MOUSE - dbPTM
SEPT7_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SEPT7_MOUSE
UniProt AC O55131
Protein Name Septin-7
Gene Name 7-Sep
Organism Mus musculus (Mouse).
Sequence Length 436
Subcellular Localization Cytoplasm . Chromosome, centromere, kinetochore. Cytoplasm, cytoskeleton, spindle. Cleavage furrow. Midbody. Cytoplasm, cytoskeleton, cilium axoneme. Cell projection, cilium, flagellum . Distributed throughout the cytoplasm in prometaphase cells. Ass
Protein Description Filament-forming cytoskeletal GTPase. Required for normal organization of the actin cytoskeleton. Required for normal progress through mitosis. Involved in cytokinesis. Required for normal association of CENPE with the kinetochore. Plays a role in ciliogenesis and collective cell movements. 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 (By similarity)..
Protein Sequence MSVSARSAAAEERSVNCGTMAQPKNLEGYVGFANLPNQVYRKSVKRGFEFTLMVVGESGLGKSTLINSLFLTDLYSPEYPGPSHRIKKTVQVEQSKVLIKEGGVQLLLTIVDTPGFGDAVDNSNCWQPVIDYIDSKFEDYLNAESRVNRRQMPDNRVQCCLYFIAPSGHGLKPLDIEFMKRLHEKVNIIPLIAKADTLTPEECQQFKKQIMKEIQEHKIKIYEFPETDDEEENKLVKKIKDRLPLAVVGSNTIIEVNGKRVRGRQYPWGVAEVENGEHCDFTILRNMLIRTHMQDLKDVTNNVHYENYRSRKLAAVTYNGVDNNKNKGQLTKSPLAQMEEERREHVAKMKKMEMEMEQVFEMKVKEKVQKLKDSEAELQRRHEQMKKNLEAQHKELEEKRRQFEEEKANWEAQQRILEQQNSSRTLEKNKKKGKIF
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------MSVSARSAA
------CCHHHHHHH		25.44-
2Phosphorylation------MSVSARSAA
------CCHHHHHHH		25.4429514104
4Phosphorylation----MSVSARSAAAE
----CCHHHHHHHHH		15.6229514104
7Phosphorylation-MSVSARSAAAEERS
-CCHHHHHHHHHHHC		23.2129514104
29PhosphorylationQPKNLEGYVGFANLP
CCCCCCCCCEECCCC		6.5018563927
63PhosphorylationGESGLGKSTLINSLF
CCCCCCHHHHHHHHH		27.0125177544
64PhosphorylationESGLGKSTLINSLFL
CCCCCHHHHHHHHHC		34.8329899451
72PhosphorylationLINSLFLTDLYSPEY
HHHHHHCCCCCCCCC		19.3423984901
75PhosphorylationSLFLTDLYSPEYPGP
HHHCCCCCCCCCCCC		25.6226239621
76PhosphorylationLFLTDLYSPEYPGPS
HHCCCCCCCCCCCCC		20.6725177544
79PhosphorylationTDLYSPEYPGPSHRI
CCCCCCCCCCCCCCC		19.5126745281
83PhosphorylationSPEYPGPSHRIKKTV
CCCCCCCCCCCEEEE		31.1719060867
96UbiquitinationTVQVEQSKVLIKEGG
EEEEECCEEEEEECC		40.53-
96AcetylationTVQVEQSKVLIKEGG
EEEEECCEEEEEECC		40.5322826441
140PhosphorylationIDSKFEDYLNAESRV
HHHHHHHHHCHHHHC		8.4820415495
180AcetylationPLDIEFMKRLHEKVN
CCCHHHHHHHHHHHC		58.0722635047
185AcetylationFMKRLHEKVNIIPLI
HHHHHHHHHCCHHHH		29.8122826441
185UbiquitinationFMKRLHEKVNIIPLI
HHHHHHHHHCCHHHH		29.81-
194AcetylationNIIPLIAKADTLTPE
CCHHHHHCCCCCCHH		39.5422826441
197PhosphorylationPLIAKADTLTPEECQ
HHHHCCCCCCHHHHH		37.0729514104
207AcetylationPEECQQFKKQIMKEI
HHHHHHHHHHHHHHH		39.16129113
207UbiquitinationPEECQQFKKQIMKEI
HHHHHHHHHHHHHHH		39.16-
212UbiquitinationQFKKQIMKEIQEHKI
HHHHHHHHHHHHCCC		53.98-
220AcetylationEIQEHKIKIYEFPET
HHHHCCCEEEECCCC		44.0022826441
227PhosphorylationKIYEFPETDDEEENK
EEEECCCCCCHHHHH		49.3325521595
234UbiquitinationTDDEEENKLVKKIKD
CCCHHHHHHHHHHHH		58.92-
234AcetylationTDDEEENKLVKKIKD
CCCHHHHHHHHHHHH		58.9223236377
259UbiquitinationTIIEVNGKRVRGRQY
EEEEECCEEECCCCC		42.38-
279S-palmitoylationEVENGEHCDFTILRN
EEECCCCCCHHHHHH		3.9128680068
297UbiquitinationRTHMQDLKDVTNNVH
HHHHHHHHHHCCCCC		59.44-
312UbiquitinationYENYRSRKLAAVTYN
CCCHHHCCEEEEEEC		43.66-
317PhosphorylationSRKLAAVTYNGVDNN
HCCEEEEEECCCCCC		13.4225367039
318PhosphorylationRKLAAVTYNGVDNNK
CCEEEEEECCCCCCC		11.8820116462
325UbiquitinationYNGVDNNKNKGQLTK
ECCCCCCCCCCCCCC		67.31-
331PhosphorylationNKNKGQLTKSPLAQM
CCCCCCCCCCHHHHC		22.9125159016
332UbiquitinationKNKGQLTKSPLAQME
CCCCCCCCCHHHHCH		59.68-
333PhosphorylationNKGQLTKSPLAQMEE
CCCCCCCCHHHHCHH		21.6525521595
351UbiquitinationEHVAKMKKMEMEMEQ
HHHHHHHHHHHHHHH		36.27-
372AcetylationKEKVQKLKDSEAELQ
HHHHHHHCHHHHHHH		67.2623806337
372UbiquitinationKEKVQKLKDSEAELQ
HHHHHHHCHHHHHHH		67.26-
394UbiquitinationKNLEAQHKELEEKRR
HHHHHHHHHHHHHHH		52.49-
407UbiquitinationRRQFEEEKANWEAQQ
HHHHHHHHHHHHHHH		50.75-
422PhosphorylationRILEQQNSSRTLEKN
HHHHHHHHHHHHHHH		19.5025521595
423PhosphorylationILEQQNSSRTLEKNK
HHHHHHHHHHHHHHH		36.5125521595
425PhosphorylationEQQNSSRTLEKNKKK
HHHHHHHHHHHHHHC		41.0124925903
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
425TPhosphorylationKinaseTAOK2Q9UL54
GPS
425TPhosphorylationKinaseTAO2Q6ZQ29
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SEPT7_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 SEPT7_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SEPT2_MOUSESept2physical
11739749
SEPT5_MOUSESept5physical
11739749
SEPT2_HUMANSEPT2physical
26496610
MKNK1_HUMANMKNK1physical
26496610
SEPT9_HUMANSEPT9physical
26496610
SCMH1_HUMANSCMH1physical
26496610
SEPT6_HUMANSEPT6physical
26496610
SEPT8_HUMANSEPT8physical
26496610
BORG4_HUMANCDC42EP4physical
26496610
CXXC1_HUMANCXXC1physical
26496610
SEP11_HUMANSEPT11physical
26496610
CPEB2_HUMANCPEB2physical
26496610
SEP10_HUMANSEPT10physical
26496610
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SEPT7_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-333 AND THR-425, ANDMASS SPECTROMETRY.
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.;
Immunity 30:143-154(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-425, AND MASSSPECTROMETRY.
"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry.";
Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
J. Proteome Res. 6:250-262(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-227, AND MASSSPECTROMETRY.
"Large-scale identification and evolution indexing of tyrosinephosphorylation sites from murine brain.";
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
J. Proteome Res. 7:311-318(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-29, AND MASSSPECTROMETRY.

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