SEP10_HUMAN - dbPTM
SEP10_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SEP10_HUMAN
UniProt AC Q9P0V9
Protein Name Septin-10
Gene Name 10-Sep
Organism Homo sapiens (Human).
Sequence Length 454
Subcellular Localization Cytoplasm . Cytoplasm, cytoskeleton. Using a GFP-fusion protein, detected in the nucleus.
Protein Description Filament-forming cytoskeletal GTPase. May play a role in cytokinesis (Potential)..
Protein Sequence MASSEVARHLLFQSHMATKTTCMSSQGSDDEQIKRENIRSLTMSGHVGFESLPDQLVNRSIQQGFCFNILCVGETGIGKSTLIDTLFNTNFEDYESSHFCPNVKLKAQTYELQESNVQLKLTIVNTVGFGDQINKEESYQPIVDYIDAQFEAYLQEELKIKRSLFTYHDSRIHVCLYFISPTGHSLKTLDLLTMKNLDSKVNIIPVIAKADTVSKTELQKFKIKLMSELVSNGVQIYQFPTDDDTIAKVNAAMNGQLPFAVVGSMDEVKVGNKMVKARQYPWGVVQVENENHCDFVKLREMLICTNMEDLREQTHTRHYELYRRCKLEEMGFTDVGPENKPVSVQETYEAKRHEFHGERQRKEEEMKQMFVQRVKEKEAILKEAERELQAKFEHLKRLHQEERMKLEEKRRLLEEEIIAFSKKKATSEIFHSQSFLATGSNLRKDKDRKNSNFL
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
20PhosphorylationQSHMATKTTCMSSQG
HHHCCCHHHHHCCCC		22.3723403867
21PhosphorylationSHMATKTTCMSSQGS
HHCCCHHHHHCCCCC		14.0423403867
24PhosphorylationATKTTCMSSQGSDDE
CCHHHHHCCCCCCHH		22.9623403867
25PhosphorylationTKTTCMSSQGSDDEQ
CHHHHHCCCCCCHHH		16.2125159151
28PhosphorylationTCMSSQGSDDEQIKR
HHHCCCCCCHHHHHH		33.9623927012
44PhosphorylationNIRSLTMSGHVGFES
HHHHHHHCCCCCHHC		22.1026471730
51PhosphorylationSGHVGFESLPDQLVN
CCCCCHHCCCHHHHH		42.8325247763
75PhosphorylationNILCVGETGIGKSTL
EEEEECCCCCCHHHH		28.33-
80PhosphorylationGETGIGKSTLIDTLF
CCCCCCHHHHHHHHC		24.1927732954
81PhosphorylationETGIGKSTLIDTLFN
CCCCCHHHHHHHHCC		31.0827732954
85PhosphorylationGKSTLIDTLFNTNFE
CHHHHHHHHCCCCCC		26.6727732954
89PhosphorylationLIDTLFNTNFEDYES
HHHHHCCCCCCCCCC		33.6727732954
94PhosphorylationFNTNFEDYESSHFCP
CCCCCCCCCCCCCCC		15.5427732954
96PhosphorylationTNFEDYESSHFCPNV
CCCCCCCCCCCCCCC		23.9227732954
97PhosphorylationNFEDYESSHFCPNVK
CCCCCCCCCCCCCCE		14.5127732954
104AcetylationSHFCPNVKLKAQTYE
CCCCCCCEEEEEEEE		51.4123236377
106 (in isoform 2)Ubiquitination-32.5021906983
106UbiquitinationFCPNVKLKAQTYELQ
CCCCCEEEEEEEEEH		32.5021906983
106 (in isoform 1)Ubiquitination-32.5021906983
110PhosphorylationVKLKAQTYELQESNV
CEEEEEEEEEHHHCC		11.5429496907
177PhosphorylationSRIHVCLYFISPTGH
CCEEEEEEEECCCCC		8.17-
188PhosphorylationPTGHSLKTLDLLTMK
CCCCCHHHHHHHHHC		30.6921406692
193PhosphorylationLKTLDLLTMKNLDSK
HHHHHHHHHCCCCCC		33.1421406692
195 (in isoform 2)Ubiquitination-49.4721906983
195UbiquitinationTLDLLTMKNLDSKVN
HHHHHHHCCCCCCCC		49.4721906983
195 (in isoform 1)Ubiquitination-49.4721906983
199PhosphorylationLTMKNLDSKVNIIPV
HHHCCCCCCCCEEEE		41.4925693802
200UbiquitinationTMKNLDSKVNIIPVI
HHCCCCCCCCEEEEE		38.6821906983
200 (in isoform 1)Ubiquitination-38.6821906983
200 (in isoform 2)Ubiquitination-38.6821906983
209 (in isoform 1)Ubiquitination-35.3521906983
209UbiquitinationNIIPVIAKADTVSKT
CEEEEEEECCCCCHH		35.3521906983
209 (in isoform 2)Ubiquitination-35.3521906983
215 (in isoform 1)Ubiquitination-41.5021906983
215UbiquitinationAKADTVSKTELQKFK
EECCCCCHHHHHHHH		41.5021906983
215 (in isoform 2)Ubiquitination-41.5021906983
216PhosphorylationKADTVSKTELQKFKI
ECCCCCHHHHHHHHH		34.13-
220 (in isoform 1)Ubiquitination-62.3421906983
220UbiquitinationVSKTELQKFKIKLMS
CCHHHHHHHHHHHHH		62.3421906983
220 (in isoform 2)Ubiquitination-62.3421906983
220AcetylationVSKTELQKFKIKLMS
CCHHHHHHHHHHHHH		62.3426051181
269UbiquitinationVGSMDEVKVGNKMVK
EECCCEEEECCEEEE		42.2321906983
269 (in isoform 2)Ubiquitination-42.2321906983
269 (in isoform 1)Ubiquitination-42.2321906983
319PhosphorylationEQTHTRHYELYRRCK
HHHHHHHHHHHHHHC		12.35-
322PhosphorylationHTRHYELYRRCKLEE
HHHHHHHHHHHCHHH		5.53-
333PhosphorylationKLEEMGFTDVGPENK
CHHHCCCCCCCCCCC		24.8521945579
340 (in isoform 1)Ubiquitination-45.1721906983
340 (in isoform 2)Ubiquitination-45.1721906983
340UbiquitinationTDVGPENKPVSVQET
CCCCCCCCCCCHHHH		45.17-
343PhosphorylationGPENKPVSVQETYEA
CCCCCCCCHHHHHHH		26.9821945579
347PhosphorylationKPVSVQETYEAKRHE
CCCCHHHHHHHHCHH		15.0121945579
348PhosphorylationPVSVQETYEAKRHEF
CCCHHHHHHHHCHHH		17.0921945579
351 (in isoform 2)Ubiquitination-42.2021906983
351 (in isoform 1)Ubiquitination-42.2021906983
351UbiquitinationVQETYEAKRHEFHGE
HHHHHHHHCHHHCCH		42.20-
382AcetylationKEKEAILKEAERELQ
HHHHHHHHHHHHHHH		49.0926051181
391UbiquitinationAERELQAKFEHLKRL
HHHHHHHHHHHHHHH		38.02-
422UbiquitinationEEIIAFSKKKATSEI
HHHHHHHCCCCCHHH		52.41-
422 (in isoform 1)Ubiquitination-52.4121906983
422 (in isoform 2)Ubiquitination-52.4121906983
426PhosphorylationAFSKKKATSEIFHSQ
HHHCCCCCHHHHHCC		35.4529255136
427PhosphorylationFSKKKATSEIFHSQS
HHCCCCCHHHHHCCC		33.2929255136
432PhosphorylationATSEIFHSQSFLATG
CCHHHHHCCCHHHCC		19.4429255136
434PhosphorylationSEIFHSQSFLATGSN
HHHHHCCCHHHCCCC		25.8329255136
438PhosphorylationHSQSFLATGSNLRKD
HCCCHHHCCCCCCCC		43.2029255136
440PhosphorylationQSFLATGSNLRKDKD
CCHHHCCCCCCCCCC		28.4729255136
449MethylationLRKDKDRKNSNFL--
CCCCCCCCCCCCC--		74.90-
451PhosphorylationKDKDRKNSNFL----
CCCCCCCCCCC----		31.8125394399
492 (in isoform 2)Phosphorylation-29083192
493 (in isoform 2)Phosphorylation-29083192
494 (in isoform 2)Phosphorylation-29083192
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 SEP10_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SEP10_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 SEP10_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SEPT5_HUMANSEPT5physical
22939629
YTDC1_HUMANYTHDC1physical
21988832
PSME4_HUMANPSME4physical
22863883
COR1C_HUMANCORO1Cphysical
26344197
SEP14_HUMANSEPT14physical
28514442
SEPT8_HUMANSEPT8physical
28514442
SEPT5_HUMANSEPT5physical
28514442
SEPT9_HUMANSEPT9physical
28514442
SEP11_HUMANSEPT11physical
28514442
SEPT4_HUMANSEPT4physical
28514442
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 SEP10_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-451, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory