SEPT9_RAT - dbPTM
SEPT9_RAT - PTM Information in dbPTM
Basic Information of Protein
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
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
1Acetylation-------MERDRITA
-------CCHHHHHH
9.58-
12PhosphorylationRITALKRSFEVEEIE
HHHHHHHCEEEEECC
24.9524259510
23PhosphorylationEEIEPPNSTPPRRVQ
EECCCCCCCCCCCCC
48.3327097102
24PhosphorylationEIEPPNSTPPRRVQT
ECCCCCCCCCCCCCC
43.9127097102
31PhosphorylationTPPRRVQTPLLRATV
CCCCCCCCHHHHHHH
17.0429779826
37PhosphorylationQTPLLRATVASSSQK
CCHHHHHHHCCCCHH
15.3525575281
40PhosphorylationLLRATVASSSQKFQD
HHHHHHCCCCHHHHH
26.6223984901
41PhosphorylationLRATVASSSQKFQDL
HHHHHCCCCHHHHHH
27.3523984901
42PhosphorylationRATVASSSQKFQDLG
HHHHCCCCHHHHHHC
34.5925403869
44AcetylationTVASSSQKFQDLGVK
HHCCCCHHHHHHCCC
47.1122902405
62PhosphorylationPAARLVDTLSQRSPK
HHHHHHHHHHHCCCC
22.3425403869
64PhosphorylationARLVDTLSQRSPKPS
HHHHHHHHHCCCCCC
26.1627097102
67PhosphorylationVDTLSQRSPKPSLRR
HHHHHHCCCCCCCCC
29.6428689409
71PhosphorylationSQRSPKPSLRRVDLA
HHCCCCCCCCCHHCC
40.4025403869
90PhosphorylationPEPMSRRTELSIDIS
CCCCCCCEEEEEECC
39.9227097102
93PhosphorylationMSRRTELSIDISSKQ
CCCCEEEEEECCCCC
16.3927097102
97PhosphorylationTELSIDISSKQVEST
EEEEEECCCCCCCCC
27.9530181290
98PhosphorylationELSIDISSKQVESTA
EEEEECCCCCCCCCC
27.6930181290
103PhosphorylationISSKQVESTASTPGP
CCCCCCCCCCCCCCC
30.3423984901
104PhosphorylationSSKQVESTASTPGPS
CCCCCCCCCCCCCCC
15.8923984901
106PhosphorylationKQVESTASTPGPSRF
CCCCCCCCCCCCCHH
34.9123984901
107PhosphorylationQVESTASTPGPSRFG
CCCCCCCCCCCCHHC
29.7822108457
111PhosphorylationTASTPGPSRFGLKRA
CCCCCCCCHHCCCHH
46.2723984901
125PhosphorylationAEVLGHKTPEPVPRR
HHHCCCCCCCCCCCC
27.4923298284
139AcetylationRTEITIVKPQESGLR
CCEEEEECCCCCCCC
36.8122902405
150PhosphorylationSGLRRVETPASKAPE
CCCCCCCCCHHHCCC
22.6929779826
153PhosphorylationRRVETPASKAPEGSA
CCCCCCHHHCCCCCC
30.4716641100
258PhosphorylationKAPVDFGYVGIDSIL
CCCCCCCCCCHHHHH
8.76-
307PhosphorylationKSKISRKSVQPISEE
HCCCCCCCCCCCCHH
25.5229779826
312PhosphorylationRKSVQPISEERIPKT
CCCCCCCCHHHCCCE
39.8425403869
332AcetylationITHDIEEKGVRMKLT
EECCHHHHCCEEEEE
50.3322902405
332UbiquitinationITHDIEEKGVRMKLT
EECCHHHHCCEEEEE
50.33-
428PhosphorylationPVIAKADTLTLEERV
HEEEECCCCCHHHHH
26.8823984901
430PhosphorylationIAKADTLTLEERVYF
EEECCCCCHHHHHHH
33.9323984901

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_RAT !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SEPT9_RAT !!

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_RAT !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of SEPT9_RAT !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SEPT9_RAT

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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.

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