SEPT9_MOUSE - dbPTM
SEPT9_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SEPT9_MOUSE
UniProt AC Q80UG5
Protein Name Septin-9
Gene Name 9-Sep
Organism Mus musculus (Mouse).
Sequence Length 583
Subcellular Localization Cytoplasm, cytoskeleton . In an epithelial cell line, concentrates at cell-cell contact areas. After TGF-beta1 treatment and induction of epithelial to mesenchymal transition, colocalizes with actin stress fibers.
Protein Description Filament-forming cytoskeletal GTPase (By similarity). May play a role in cytokinesis (Potential)..
Protein Sequence MKKSYSGVTRTSSGRLRRLADPTGPALKRSFEVEEIEPPNSTPPRRVQTPLLRATVASSSQKFQDLGVKNSEPAARLVDSLSQRSPKPSLRRVELAGAKAPEPMSRRTEISIDISSKQVESTASAAGPSRFGLKRAEVLGHKTPEPVPRRTEITIVKPQESVLRRVETPASKIPEGSAVPATDAAPKRVEIQVPKPAEAPNCPLPSQTLENSEAPMSQLQSRLEPRPSVAEVPYRNQEDSEVTPSCVGDMADNPRDAMLKQAPASRNEKAPMEFGYVGIDSILEQMRRKAMKQGFEFNIMVVGQSGLGKSTLINTLFKSKISRKSVQPTSEERIPKTIEIKSITHDIEEKGVRMKLTVIDTPGFGDHINNENCWQPIMKFINDQYEKYLQEEVNINRKKRIPDTRVHCCLYFIPATGHSLRPLDIEFMKRLSKVVNIVPVIAKADTLTLEERVYFKQRITADLLSNGIDVYPQKEFDEDAEDRLVNEKFREMIPFAVVGSDHEYQVNGKRILGRKTKWGTIEVENTTHCEFAYLRDLLIRTHMQNIKDITSNIHFEAYRVKRLNEGNSAMANGIEKEPEAQEM
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
1Acetylation-------MKKSYSGV
-------CCCCCCCC		12.76-
2 (in isoform 3)Phosphorylation-50.8826824392
6Phosphorylation--MKKSYSGVTRTSS
--CCCCCCCCCCCCC		33.6021183079
13PhosphorylationSGVTRTSSGRLRRLA
CCCCCCCCCCCCCCC		27.5923140645
23PhosphorylationLRRLADPTGPALKRS
CCCCCCCCCHHHHEE		57.2424719451
23 (in isoform 3)Phosphorylation-57.2425266776
30PhosphorylationTGPALKRSFEVEEIE
CCHHHHEEEEEEECC		24.9525521595
41PhosphorylationEEIEPPNSTPPRRVQ
EECCCCCCCCCCCCC		48.3323984901
42PhosphorylationEIEPPNSTPPRRVQT
ECCCCCCCCCCCCCC		43.9123527152
49PhosphorylationTPPRRVQTPLLRATV
CCCCCCCCHHHHHHH		17.0426824392
55PhosphorylationQTPLLRATVASSSQK
CCHHHHHHHCCCCHH		15.3526643407
58PhosphorylationLLRATVASSSQKFQD
HHHHHHCCCCHHHHH		26.6226239621
59PhosphorylationLRATVASSSQKFQDL
HHHHHCCCCHHHHHH		27.3527087446
60PhosphorylationRATVASSSQKFQDLG
HHHHCCCCHHHHHHC		34.5927087446
62AcetylationTVASSSQKFQDLGVK
HHCCCCHHHHHHCCC		47.1123806337
71PhosphorylationQDLGVKNSEPAARLV
HHHCCCCCHHHHHHH		38.9629514104
80PhosphorylationPAARLVDSLSQRSPK
HHHHHHHHHHHCCCC		23.5722942356
82PhosphorylationARLVDSLSQRSPKPS
HHHHHHHHHCCCCCC		27.7426824392
85PhosphorylationVDSLSQRSPKPSLRR
HHHHHHCCCCCCCHH		29.6427087446
87MalonylationSLSQRSPKPSLRRVE
HHHHCCCCCCCHHHH		48.7826320211
89PhosphorylationSQRSPKPSLRRVELA
HHCCCCCCCHHHHHC		40.4027087446
111PhosphorylationMSRRTEISIDISSKQ
CCCCEEEEEECCHHH		14.1522817900
121PhosphorylationISSKQVESTASAAGP
CCHHHHHCHHHCCCC		30.3429899451
122PhosphorylationSSKQVESTASAAGPS
CHHHHHCHHHCCCCC		15.8929514104
124PhosphorylationKQVESTASAAGPSRF
HHHHCHHHCCCCCHH		20.8125521595
143PhosphorylationAEVLGHKTPEPVPRR
HHHCCCCCCCCCCCC		27.4926824392
151O-linked_GlycosylationPEPVPRRTEITIVKP
CCCCCCCCEEEEECC		32.7855413681
151PhosphorylationPEPVPRRTEITIVKP
CCCCCCCCEEEEECC		32.7822871156
154PhosphorylationVPRRTEITIVKPQES
CCCCCEEEEECCHHH		17.3129899451
161PhosphorylationTIVKPQESVLRRVET
EEECCHHHHHHHCCC		22.6226824392
168PhosphorylationSVLRRVETPASKIPE
HHHHHCCCCHHHCCC		22.6930352176
171PhosphorylationRRVETPASKIPEGSA
HHCCCCHHHCCCCCC		32.1123984901
177PhosphorylationASKIPEGSAVPATDA
HHHCCCCCCCCCCCC		25.1623984901
182PhosphorylationEGSAVPATDAAPKRV
CCCCCCCCCCCCCEE		21.7923984901
228PhosphorylationSRLEPRPSVAEVPYR
HHCCCCCCCCCCCCC		34.9325521595
234PhosphorylationPSVAEVPYRNQEDSE
CCCCCCCCCCCCCCC		27.6321082442
243PhosphorylationNQEDSEVTPSCVGDM
CCCCCCCCCCHHHHC		12.8729514104
245PhosphorylationEDSEVTPSCVGDMAD
CCCCCCCCHHHHCCC		16.4529514104
260UbiquitinationNPRDAMLKQAPASRN
CHHHHHHHHCCCCCC		31.1822790023
269UbiquitinationAPASRNEKAPMEFGY
CCCCCCCCCCCCCCC		62.4322790023
276PhosphorylationKAPMEFGYVGIDSIL
CCCCCCCCCCHHHHH		10.7922817900
318AcetylationTLINTLFKSKISRKS
HHHHHHHHHCCCCCC		54.6922826441
318UbiquitinationTLINTLFKSKISRKS
HHHHHHHHHCCCCCC		54.6922790023
322PhosphorylationTLFKSKISRKSVQPT
HHHHHCCCCCCCCCC		37.0725338131
325PhosphorylationKSKISRKSVQPTSEE
HHCCCCCCCCCCCCC		25.5225521595
329PhosphorylationSRKSVQPTSEERIPK
CCCCCCCCCCCCCCC		31.5123737553
330PhosphorylationRKSVQPTSEERIPKT
CCCCCCCCCCCCCCE		44.1125521595
336MalonylationTSEERIPKTIEIKSI
CCCCCCCCEEEEEEE		60.8226320211
336UbiquitinationTSEERIPKTIEIKSI
CCCCCCCCEEEEEEE		60.82-
350AcetylationITHDIEEKGVRMKLT
EECCHHHHCCEEEEE		50.3323236377
350UbiquitinationITHDIEEKGVRMKLT
EECCHHHHCCEEEEE		50.3322790023
404PhosphorylationRKKRIPDTRVHCCLY
CCCCCCCCCEEEEEE		29.2730387612
429AcetylationPLDIEFMKRLSKVVN
CCCHHHHHHHHHHHC		56.3523954790
433UbiquitinationEFMKRLSKVVNIVPV
HHHHHHHHHHCHHHE		55.5922790023
433AcetylationEFMKRLSKVVNIVPV
HHHHHHHHHHCHHHE		55.5922826441
446PhosphorylationPVIAKADTLTLEERV
HEEEECCCCCHHHHH		26.8826643407
471PhosphorylationLSNGIDVYPQKEFDE
HHCCCEECCCHHCCC		9.0121454597
474UbiquitinationGIDVYPQKEFDEDAE
CCEECCCHHCCCCHH		56.7122790023
488UbiquitinationEDRLVNEKFREMIPF
HHHHHCHHHHHHCCE		44.5122790023
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 SEPT9_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SEPT9_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 SEPT9_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ANX11_HUMANANXA11physical
26496610
SEPT7_HUMANSEPT7physical
26496610
FLNA_HUMANFLNAphysical
26496610
LEG1_HUMANLGALS1physical
26496610
ABLM1_HUMANABLIM1physical
26496610
MYPT1_HUMANPPP1R12Aphysical
26496610
SEPT2_HUMANSEPT2physical
26496610
P3C2A_HUMANPIK3C2Aphysical
26496610
SEPT5_HUMANSEPT5physical
26496610
DPOG1_HUMANPOLGphysical
26496610
SDF2_HUMANSDF2physical
26496610
SPTB2_HUMANSPTBN1physical
26496610
SVIL_HUMANSVILphysical
26496610
LUZP1_HUMANLUZP1physical
26496610
RMP_HUMANURI1physical
26496610
ARHGB_HUMANARHGEF11physical
26496610
BASP1_HUMANBASP1physical
26496610
AKAP2_HUMANAKAP2physical
26496610
SYNPO_HUMANSYNPOphysical
26496610
SEPT6_HUMANSEPT6physical
26496610
SEPT8_HUMANSEPT8physical
26496610
COBL_HUMANCOBLphysical
26496610
BORG4_HUMANCDC42EP4physical
26496610
SDF2L_HUMANSDF2L1physical
26496610
CSN7A_HUMANCOPS7Aphysical
26496610
HSP7E_HUMANHSPA14physical
26496610
DJB11_HUMANDNAJB11physical
26496610
SEP11_HUMANSEPT11physical
26496610
COR1B_HUMANCORO1Bphysical
26496610
AFAP1_HUMANAFAP1physical
26496610
INF2_HUMANINF2physical
26496610
CYTSB_HUMANSPECC1physical
26496610
HELB_HUMANHELBphysical
26496610
CAVN3_HUMANPRKCDBPphysical
26496610
MISP_HUMANMISPphysical
26496610
SEP10_HUMANSEPT10physical
26496610
CAVN1_HUMANPTRFphysical
26496610
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SEPT9_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-30 AND SER-161, AND MASSSPECTROMETRY.
"Specific phosphopeptide enrichment with immobilized titanium ionaffinity chromatography adsorbent for phosphoproteome analysis.";
Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
J. Proteome Res. 7:3957-3967(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85, 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 SER-30, AND MASSSPECTROMETRY.

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