SEPT5_HUMAN - dbPTM
SEPT5_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SEPT5_HUMAN
UniProt AC Q99719
Protein Name Septin-5
Gene Name 5-Sep
Organism Homo sapiens (Human).
Sequence Length 369
Subcellular Localization Cytoplasm. Cytoplasm, cytoskeleton. In platelets, found in areas surrounding alpha-granules.
Protein Description Filament-forming cytoskeletal GTPase (By similarity). May play a role in cytokinesis (Potential). May play a role in platelet secretion (By similarity)..
Protein Sequence MSTGLRYKSKLATPEDKQDIDKQYVGFATLPNQVHRKSVKKGFDFTLMVAGESGLGKSTLVHSLFLTDLYKDRKLLSAEERISQTVEILKHTVDIEEKGVKLKLTIVDTPGFGDAVNNTECWKPITDYVDQQFEQYFRDESGLNRKNIQDNRVHCCLYFISPFGHGLRPVDVGFMKALHEKVNIVPLIAKADCLVPSEIRKLKERIREEIDKFGIHVYQFPECDSDEDEDFKQQDRELKESAPFAVIGSNTVVEAKGQRVRGRLYPWGIVEVENQAHCDFVKLRNMLIRTHMHDLKDVTCDVHYENYRAHCIQQMTSKLTQDSRMESPIPILPLPTPDAETEKLIRMKDEELRRMQEMLQRMKQQMQDQ
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
6Methylation--MSTGLRYKSKLAT
--CCCCCHHHCCCCC
37.87115916453
13PhosphorylationRYKSKLATPEDKQDI
HHHCCCCCHHHHHCC
37.3323312004
17 (in isoform 2)Phosphorylation-48.4828450419
24PhosphorylationKQDIDKQYVGFATLP
HHCCCHHHCEEEECC
14.3128060719
29PhosphorylationKQYVGFATLPNQVHR
HHHCEEEECCCHHHH
40.2528060719
33 (in isoform 2)Phosphorylation-30.38-
41UbiquitinationVHRKSVKKGFDFTLM
HHHHHHHCCCCEEEE
63.76-
77PhosphorylationYKDRKLLSAEERISQ
HHCHHHHCHHHHHHH
44.0321815630
83PhosphorylationLSAEERISQTVEILK
HCHHHHHHHHHHHHH
26.4830266825
85PhosphorylationAEERISQTVEILKHT
HHHHHHHHHHHHHHH
17.2030266825
168MethylationSPFGHGLRPVDVGFM
CCCCCCCCCCCHHHH
33.51-
218PhosphorylationDKFGIHVYQFPECDS
HHHCEEEEECCCCCC
7.1220873877
225PhosphorylationYQFPECDSDEDEDFK
EECCCCCCCCCCHHH
55.3422617229
241PhosphorylationQDRELKESAPFAVIG
HHHHHHHHCCEEEEC
39.3925693802
249PhosphorylationAPFAVIGSNTVVEAK
CCEEEECCCCEEEEC
20.4325693802
251PhosphorylationFAVIGSNTVVEAKGQ
EEEECCCCEEEECCE
27.8525693802
318UbiquitinationCIQQMTSKLTQDSRM
HHHHHHHHCCCCCCC
46.52-
320PhosphorylationQQMTSKLTQDSRMES
HHHHHHCCCCCCCCC
33.7826074081
323PhosphorylationTSKLTQDSRMESPIP
HHHCCCCCCCCCCCC
24.5726074081
327PhosphorylationTQDSRMESPIPILPL
CCCCCCCCCCCCCCC
20.8430278072
336PhosphorylationIPILPLPTPDAETEK
CCCCCCCCCCHHHHH
41.2921082442
341PhosphorylationLPTPDAETEKLIRMK
CCCCCHHHHHHHHHC
39.8926074081
343UbiquitinationTPDAETEKLIRMKDE
CCCHHHHHHHHHCHH
57.54-
363MethylationQEMLQRMKQQMQDQ-
HHHHHHHHHHHHCC-
39.30-

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
17SPhosphorylationKinaseCDK5Q00535
PSP
-KUbiquitinationE3 ubiquitin ligasePRKNO60260
PMID:14559152

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SEPT5_HUMAN !!

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_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SEPT8_HUMANSEPT8physical
12909369
KAT7_HUMANKAT7physical
16169070
PROF2_HUMANPFN2physical
16169070
SEPT8_HUMANSEPT8physical
12023038
STX4_HUMANSTX4physical
11880646
PRKN_HUMANPARK2physical
18845538
A4_HUMANAPPphysical
21832049
SEPT2_HUMANSEPT2physical
24722188
SEPT5_HUMANSEPT5physical
24722188
MYOG_HUMANMYOGphysical
24722188
SEPT1_HUMANSEPT1physical
24722188
SEPT6_HUMANSEPT6physical
24722188
SEPT2_HUMANSEPT2physical
18330356
SEPT6_HUMANSEPT6physical
18330356
SEPT7_HUMANSEPT7physical
18330356
SEP11_HUMANSEPT11physical
18330356
SEPT5_HUMANSEPT5physical
25416956
SEPT6_HUMANSEPT6physical
25416956
SEP10_HUMANSEPT10physical
25416956
SEP10_HUMANSEPT10physical
26344197
PKHF2_HUMANPLEKHF2physical
21516116

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SEPT5_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-225 AND SER-327, ANDMASS SPECTROMETRY.
"Phosphoproteome of resting human platelets.";
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.;
J. Proteome Res. 7:526-534(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-225, AND MASSSPECTROMETRY.

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