SEPT1_HUMAN - dbPTM
SEPT1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SEPT1_HUMAN
UniProt AC Q8WYJ6
Protein Name Septin-1
Gene Name 1-Sep
Organism Homo sapiens (Human).
Sequence Length 367
Subcellular Localization Cytoplasm. Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Midbody. Remains at the centrosomes and the nearby microtubules throughout mitosis. Localizes to the midbody during cytokinesis.
Protein Description Filament-forming cytoskeletal GTPase (By similarity). May play a role in cytokinesis (Potential)..
Protein Sequence MDKEYVGFAALPNQLHRKSVKKGFDFTLMVAGESGLGKSTLINSLFLTNLYEDRQVPEASARLTQTLAIERRGVEIEEGGVKVKLTLVDTPGFGDSVDCSDCWLPVVKFIEEQFEQYLRDESGLNRKNIQDSRVHCCLYFISPFGRGLRPLDVAFLRAVHEKVNIIPVIGKADALMPQETQALKQKIRDQLKEEEIHIYQFPECDSDEDEDFKRQDAEMKESIPFAVVGSCEVVRDGGNRPVRGRRYSWGTVEVENPHHCDFLNLRRMLVQTHLQDLKEVTHDLLYEGYRARCLQSLARPGARDRASRSKLSRQSATEIPLPMLPLADTEKLIREKDEELRRMQEMLEKMQAQMQQSQAQGEQSDAL
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
3Ubiquitination-----MDKEYVGFAA
-----CCHHHCCEEC		50.04-
5Phosphorylation---MDKEYVGFAALP
---CCHHHCCEECCC		16.1830576142
19PhosphorylationPNQLHRKSVKKGFDF
CCHHHHHHHHCCCCE		38.84-
22UbiquitinationLHRKSVKKGFDFTLM
HHHHHHHCCCCEEEE		63.76-
44PhosphorylationGKSTLINSLFLTNLY
CHHHHHHHHHHCCCC		17.3230631047
48PhosphorylationLINSLFLTNLYEDRQ
HHHHHHHCCCCCCCC		18.82-
51PhosphorylationSLFLTNLYEDRQVPE
HHHHCCCCCCCCCCH		20.1828674151
60PhosphorylationDRQVPEASARLTQTL
CCCCCHHHHHHHHHH		16.56-
65UbiquitinationEASARLTQTLAIERR
HHHHHHHHHHHHHHC		38.82-
69UbiquitinationRLTQTLAIERRGVEI
HHHHHHHHHHCCEEE		4.81-
82UbiquitinationEIEEGGVKVKLTLVD
EEEECCEEEEEEEEC		36.61-
84UbiquitinationEEGGVKVKLTLVDTP
EECCEEEEEEEECCC		30.00-
129UbiquitinationSGLNRKNIQDSRVHC
CCCCCCCCCCCCHHH		5.59-
131UbiquitinationLNRKNIQDSRVHCCL
CCCCCCCCCCHHHHH		34.31-
132PhosphorylationNRKNIQDSRVHCCLY
CCCCCCCCCHHHHHH		21.59-
162AcetylationFLRAVHEKVNIIPVI
HHHHHHHHCCEEEEE		26.2125953088
162UbiquitinationFLRAVHEKVNIIPVI
HHHHHHHHCCEEEEE		26.21-
171UbiquitinationNIIPVIGKADALMPQ
CEEEEECCHHHCCHH		31.78-
174UbiquitinationPVIGKADALMPQETQ
EEECCHHHCCHHHHH		15.60-
176SulfoxidationIGKADALMPQETQAL
ECCHHHCCHHHHHHH		3.2721406390
184UbiquitinationPQETQALKQKIRDQL
HHHHHHHHHHHHHHH		53.19-
186UbiquitinationETQALKQKIRDQLKE
HHHHHHHHHHHHHHH		37.81-
199PhosphorylationKEEEIHIYQFPECDS
HHCCEEEEECCCCCC		7.0230576142
206PhosphorylationYQFPECDSDEDEDFK
EECCCCCCCCCCCHH		55.3420058876
209UbiquitinationPECDSDEDEDFKRQD
CCCCCCCCCCHHHHC		66.80-
211PhosphorylationCDSDEDEDFKRQDAE
CCCCCCCCHHHHCHH		67.6924275569
218UbiquitinationDFKRQDAEMKESIPF
CHHHHCHHHHHHCCE		60.11-
220UbiquitinationKRQDAEMKESIPFAV
HHHCHHHHHHCCEEE		39.55-
222PhosphorylationQDAEMKESIPFAVVG
HCHHHHHHCCEEEEE		30.0026074081
231UbiquitinationPFAVVGSCEVVRDGG
CEEEEECEEEEECCC		3.65-
233UbiquitinationAVVGSCEVVRDGGNR
EEEECEEEEECCCCC		5.12-
240MethylationVVRDGGNRPVRGRRY
EEECCCCCCCCCCEE		34.07115387871
246PhosphorylationNRPVRGRRYSWGTVE
CCCCCCCEEECEEEE		32.44-
247PhosphorylationRPVRGRRYSWGTVEV
CCCCCCEEECEEEEE		13.8626657352
248PhosphorylationPVRGRRYSWGTVEVE
CCCCCEEECEEEEEC		19.7423401153
251PhosphorylationGRRYSWGTVEVENPH
CCEEECEEEEECCCC		13.7728122231
253PhosphorylationRYSWGTVEVENPHHC
EEECEEEEECCCCCC		43.9119690332
256PhosphorylationWGTVEVENPHHCDFL
CEEEEECCCCCCCHH		46.51-
260UbiquitinationEVENPHHCDFLNLRR
EECCCCCCCHHHHHH		3.44-
267UbiquitinationCDFLNLRRMLVQTHL
CCHHHHHHHHHHHHH		26.42-
278UbiquitinationQTHLQDLKEVTHDLL
HHHHHHHHHHHHHHH		59.43-
286PhosphorylationEVTHDLLYEGYRARC
HHHHHHHHHHHHHHH		18.0128796482
287MethylationVTHDLLYEGYRARCL
HHHHHHHHHHHHHHH		50.12-
289PhosphorylationHDLLYEGYRARCLQS
HHHHHHHHHHHHHHH		6.8029978859
294PhosphorylationEGYRARCLQSLARPG
HHHHHHHHHHHCCCC		3.0227251275
295PhosphorylationGYRARCLQSLARPGA
HHHHHHHHHHCCCCC		39.7720058876
298PhosphorylationARCLQSLARPGARDR
HHHHHHHCCCCCHHH		22.37-
307PhosphorylationPGARDRASRSKLSRQ
CCCHHHHHHHHHCCC		37.6726074081
309PhosphorylationARDRASRSKLSRQSA
CHHHHHHHHHCCCCC		35.1429978859
312PhosphorylationRASRSKLSRQSATEI
HHHHHHHCCCCCCCC		31.8223401153
315PhosphorylationRSKLSRQSATEIPLP
HHHHCCCCCCCCCCC		35.7320164059
317PhosphorylationKLSRQSATEIPLPML
HHCCCCCCCCCCCCC		39.4328787133
320PhosphorylationRQSATEIPLPMLPLA
CCCCCCCCCCCCCCC		24.9516179162
325UbiquitinationEIPLPMLPLADTEKL
CCCCCCCCCCCHHHH		21.17-
329PhosphorylationPMLPLADTEKLIREK
CCCCCCCHHHHHHHH		29.4326074081
331UbiquitinationLPLADTEKLIREKDE
CCCCCHHHHHHHHHH		51.84-
349UbiquitinationRMQEMLEKMQAQMQQ
HHHHHHHHHHHHHHH		32.14-
354PhosphorylationLEKMQAQMQQSQAQG
HHHHHHHHHHHHHHH		4.3716179162
357PhosphorylationMQAQMQQSQAQGEQS
HHHHHHHHHHHHHHC		15.5928111955
362PhosphorylationQQSQAQGEQSDAL--
HHHHHHHHHCCCC--		34.5316179162
364PhosphorylationSQAQGEQSDAL----
HHHHHHHCCCC----		22.1330576142
378Ubiquitination------------------
------------------		-
383Ubiquitination-----------------------
-----------------------		-
396Ubiquitination------------------------------------
------------------------------------		-
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
248SPhosphorylationKinaseAURBQ96GD4
PSP
307SPhosphorylationKinaseAURBQ96GD4
PSP
315SPhosphorylationKinaseAURBQ96GD4
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SEPT1_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 SEPT1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SEPT6_HUMANSEPT6physical
16189514
TOLIP_HUMANTOLLIPphysical
16189514
SEPT1_HUMANSEPT1physical
16189514
A4_HUMANAPPphysical
21832049
AURKB_HUMANAURKBphysical
16179162
SEPT1_HUMANSEPT1physical
25416956
SEPT5_HUMANSEPT5physical
25416956
SEPT6_HUMANSEPT6physical
25416956
TEX11_HUMANTEX11physical
25416956
SEP12_HUMANSEPT12physical
25416956
AMOT_HUMANAMOTphysical
25416956
SEPT4_HUMANSEPT4physical
26186194
SEPT5_HUMANSEPT5physical
26186194
SEPT2_HUMANSEPT2physical
26186194
SEPT7_HUMANSEPT7physical
26186194
SEPT6_HUMANSEPT6physical
26186194
SEPT8_HUMANSEPT8physical
26186194
SEP11_HUMANSEPT11physical
26186194
SEP10_HUMANSEPT10physical
26186194
SEPT9_HUMANSEPT9physical
26186194
SEPT3_HUMANSEPT3physical
26186194
MY18A_HUMANMYO18Aphysical
26186194
NRDC_HUMANNRD1physical
26186194
ASB7_HUMANASB7physical
26186194
SEPT5_HUMANSEPT5physical
28514442
SEPT4_HUMANSEPT4physical
28514442
SEPT3_HUMANSEPT3physical
28514442
SEPT8_HUMANSEPT8physical
28514442
SEP10_HUMANSEPT10physical
28514442
SEPT9_HUMANSEPT9physical
28514442
SEP11_HUMANSEPT11physical
28514442
ASB7_HUMANASB7physical
28514442
SEPT2_HUMANSEPT2physical
28514442
SEPT7_HUMANSEPT7physical
28514442
SEPT6_HUMANSEPT6physical
28514442
NRDC_HUMANNRD1physical
28514442
MY18A_HUMANMYO18Aphysical
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 SEPT1_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-248 AND SER-315, ANDMASS SPECTROMETRY.
"Septin1, a new interaction partner for human serine/threonine kinaseaurora-B.";
Qi M., Yu W., Liu S., Jia H., Tang L., Shen M., Yan X., Saiyin H.,Lang Q., Wan B., Zhao S., Yu L.;
Biochem. Biophys. Res. Commun. 336:994-1000(2005).
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH AURKB, PHOSPHORYLATION ATSER-248; SER-307 AND SER-315, AND MUTAGENESIS OF SER-19; SER-206;SER-248; SER-307; SER-312 AND SER-315.

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