SEPT6_HUMAN - dbPTM
SEPT6_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SEPT6_HUMAN
UniProt AC Q14141
Protein Name Septin-6
Gene Name 6-Sep
Organism Homo sapiens (Human).
Sequence Length 434
Subcellular Localization Cytoplasm . Cytoplasm, cytoskeleton, spindle . Chromosome, centromere, kinetochore . Cleavage furrow . Midbody . Cell projection, cilium, flagellum . In metaphase cells, localized within the microtubule spindle. At the metaphase plate, in close appos
Protein Description Filament-forming cytoskeletal GTPase. Required for normal organization of the actin cytoskeleton. Involved in cytokinesis. May play a role in HCV RNA replication. Forms a filamentous structure with SEPT12, SEPT6, SEPT2 and probably SEPT4 at the sperm annulus which is required for the structural integrity and motility of the sperm tail during postmeiotic differentiation. [PubMed: 25588830]
Protein Sequence MAATDIARQVGEGCRTVPLAGHVGFDSLPDQLVNKSVSQGFCFNILCVGETGLGKSTLMDTLFNTKFEGEPATHTQPGVQLQSNTYDLQESNVRLKLTIVSTVGFGDQINKEDSYKPIVEFIDAQFEAYLQEELKIRRVLHTYHDSRIHVCLYFIAPTGHSLKSLDLVTMKKLDSKVNIIPIIAKADAISKSELTKFKIKITSELVSNGVQIYQFPTDDESVAEINGTMNAHLPFAVIGSTEELKIGNKMMRARQYPWGTVQVENEAHCDFVKLREMLIRVNMEDLREQTHTRHYELYRRCKLEEMGFKDTDPDSKPFSLQETYEAKRNEFLGELQKKEEEMRQMFVQRVKEKEAELKEAEKELHEKFDRLKKLHQDEKKKLEDKKKSLDDEVNAFKQRKTAAELLQSQGSQAGGSQTLKRDKEKKNNPWLCTE
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
2Acetylation------MAATDIARQ
------CCHHHHHHH		21.0419413330
27PhosphorylationAGHVGFDSLPDQLVN
CCCCCCCCCCHHHCC		39.2730576142
47GlutathionylationGFCFNILCVGETGLG
CCCEEEEEECCCCCC		3.0622555962
56PhosphorylationGETGLGKSTLMDTLF
CCCCCCHHHHHHHHC		25.6021712546
57PhosphorylationETGLGKSTLMDTLFN
CCCCCHHHHHHHHCC		29.5921712546
65PhosphorylationLMDTLFNTKFEGEPA
HHHHHCCCCCCCCCC		29.7621712546
66 (in isoform 2)Ubiquitination-42.39-
66UbiquitinationMDTLFNTKFEGEPAT
HHHHCCCCCCCCCCC		42.39-
83PhosphorylationQPGVQLQSNTYDLQE
CCCEEEECCCCCCCC		39.4728796482
85PhosphorylationGVQLQSNTYDLQESN
CEEEECCCCCCCCCC		24.5328796482
86PhosphorylationVQLQSNTYDLQESNV
EEEECCCCCCCCCCE		20.9328796482
91PhosphorylationNTYDLQESNVRLKLT
CCCCCCCCCEEEEEE		27.8828796482
146PhosphorylationVLHTYHDSRIHVCLY
HHHHHHHCCEEEEEE		21.59-
164PhosphorylationPTGHSLKSLDLVTMK
CCCCCCCCCCEEEHH		32.2021964256
169PhosphorylationLKSLDLVTMKKLDSK
CCCCCEEEHHHCCCC		30.4820068231
170SulfoxidationKSLDLVTMKKLDSKV
CCCCEEEHHHCCCCC		2.5521406390
171UbiquitinationSLDLVTMKKLDSKVN
CCCEEEHHHCCCCCC		40.60-
171AcetylationSLDLVTMKKLDSKVN
CCCEEEHHHCCCCCC		40.6025953088
176UbiquitinationTMKKLDSKVNIIPII
EHHHCCCCCCCEEEE		38.68-
185UbiquitinationNIIPIIAKADAISKS
CCEEEEEECCCCCHH		36.07-
185 (in isoform 2)Ubiquitination-36.07-
190PhosphorylationIAKADAISKSELTKF
EEECCCCCHHHHHCC		31.6728122231
191AcetylationAKADAISKSELTKFK
EECCCCCHHHHHCCE		41.6626822725
191 (in isoform 2)Ubiquitination-41.66-
191UbiquitinationAKADAISKSELTKFK
EECCCCCHHHHHCCE		41.66-
192PhosphorylationKADAISKSELTKFKI
ECCCCCHHHHHCCEE		30.9223684312
195PhosphorylationAISKSELTKFKIKIT
CCCHHHHHCCEEEEE		30.3128122231
196UbiquitinationISKSELTKFKIKITS
CCHHHHHCCEEEEEH		58.2319608861
196AcetylationISKSELTKFKIKITS
CCHHHHHCCEEEEEH		58.2319608861
249UbiquitinationEELKIGNKMMRARQY
CEEECCCCHHHCCCC		28.94-
273AcetylationEAHCDFVKLREMLIR
CCCCCHHHHHHHHHH		41.6525953088
273UbiquitinationEAHCDFVKLREMLIR
CCCCCHHHHHHHHHH		41.65-
295PhosphorylationEQTHTRHYELYRRCK
HHHHHHHHHHHHHHC		12.35-
298PhosphorylationHTRHYELYRRCKLEE
HHHHHHHHHHHCHHH		5.53-
302UbiquitinationYELYRRCKLEEMGFK
HHHHHHHCHHHCCCC		58.06-
302AcetylationYELYRRCKLEEMGFK
HHHHHHHCHHHCCCC		58.0625953088
302 (in isoform 2)Ubiquitination-58.06-
309AcetylationKLEEMGFKDTDPDSK
CHHHCCCCCCCCCCC		54.7326051181
309UbiquitinationKLEEMGFKDTDPDSK
CHHHCCCCCCCCCCC		54.73-
311PhosphorylationEEMGFKDTDPDSKPF
HHCCCCCCCCCCCCC		50.45-
315PhosphorylationFKDTDPDSKPFSLQE
CCCCCCCCCCCCHHH		47.84-
316AcetylationKDTDPDSKPFSLQET
CCCCCCCCCCCHHHH		58.4226051181
316UbiquitinationKDTDPDSKPFSLQET
CCCCCCCCCCCHHHH		58.42-
316 (in isoform 2)Ubiquitination-58.4221890473
316 (in isoform 4)Ubiquitination-58.4221890473
319PhosphorylationDPDSKPFSLQETYEA
CCCCCCCCHHHHHHH		37.3626657352
323PhosphorylationKPFSLQETYEAKRNE
CCCCHHHHHHHHHHH		17.4425627689
324PhosphorylationPFSLQETYEAKRNEF
CCCHHHHHHHHHHHH		17.0925159151
327 (in isoform 2)Ubiquitination-43.7621890473
327UbiquitinationLQETYEAKRNEFLGE
HHHHHHHHHHHHHHH		43.76-
327 (in isoform 4)Ubiquitination-43.7621890473
337 (in isoform 2)Ubiquitination-74.83-
337UbiquitinationEFLGELQKKEEEMRQ
HHHHHHHHHHHHHHH		74.83-
337AcetylationEFLGELQKKEEEMRQ
HHHHHHHHHHHHHHH		74.8326051181
338AcetylationFLGELQKKEEEMRQM
HHHHHHHHHHHHHHH		58.3526051181
338UbiquitinationFLGELQKKEEEMRQM
HHHHHHHHHHHHHHH		58.35-
346 (in isoform 1)Ubiquitination-2.9921890473
351UbiquitinationQMFVQRVKEKEAELK
HHHHHHHHHHHHHHH		66.32-
358AcetylationKEKEAELKEAEKELH
HHHHHHHHHHHHHHH		46.5125953088
358UbiquitinationKEKEAELKEAEKELH
HHHHHHHHHHHHHHH		46.51-
358MalonylationKEKEAELKEAEKELH
HHHHHHHHHHHHHHH		46.5126320211
362UbiquitinationAELKEAEKELHEKFD
HHHHHHHHHHHHHHH		73.04-
362AcetylationAELKEAEKELHEKFD
HHHHHHHHHHHHHHH		73.0423749302
367UbiquitinationAEKELHEKFDRLKKL
HHHHHHHHHHHHHHH		41.6419608861
367AcetylationAEKELHEKFDRLKKL
HHHHHHHHHHHHHHH		41.6419608861
379AcetylationKKLHQDEKKKLEDKK
HHHCHHHHHHHHHHH		64.5922361509
380AcetylationKLHQDEKKKLEDKKK
HHCHHHHHHHHHHHH		61.627910671
386UbiquitinationKKKLEDKKKSLDDEV
HHHHHHHHHHHHHHH		60.97-
387UbiquitinationKKLEDKKKSLDDEVN
HHHHHHHHHHHHHHH		63.09-
388PhosphorylationKLEDKKKSLDDEVNA
HHHHHHHHHHHHHHH		46.0023401153
397UbiquitinationDDEVNAFKQRKTAAE
HHHHHHHHHHHHHHH		46.94-
397AcetylationDDEVNAFKQRKTAAE
HHHHHHHHHHHHHHH		46.9425953088
400UbiquitinationVNAFKQRKTAAELLQ
HHHHHHHHHHHHHHH		39.77-
401PhosphorylationNAFKQRKTAAELLQS
HHHHHHHHHHHHHHH		33.0323684312
408PhosphorylationTAAELLQSQGSQAGG
HHHHHHHHCCCCCCC		36.1617525332
411PhosphorylationELLQSQGSQAGGSQT
HHHHHCCCCCCCCHH		14.8223401153
416 (in isoform 2)Phosphorylation-21.0529507054
416PhosphorylationQGSQAGGSQTLKRDK
CCCCCCCCHHHCCCH		21.0523401153
418 (in isoform 2)Phosphorylation-35.6217525332
418PhosphorylationSQAGGSQTLKRDKEK
CCCCCCHHHCCCHHH		35.6217525332
420AcetylationAGGSQTLKRDKEKKN
CCCCHHHCCCHHHCC		63.0425953088
420UbiquitinationAGGSQTLKRDKEKKN
CCCCHHHCCCHHHCC		63.04-
420 (in isoform 2)Ubiquitination-63.04-
426UbiquitinationLKRDKEKKNNPWLCT
HCCCHHHCCCCCCCC		64.15-
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 SEPT6_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SEPT6_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 SEPT6_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SOCS7_HUMANSOCS7physical
17803907
SEPT2_HUMANSEPT2physical
17803907
KDM1A_HUMANKDM1Aphysical
23455924
NSD3_HUMANWHSC1L1physical
23455924
SEPT3_HUMANSEPT3physical
25416956
PKHF2_HUMANPLEKHF2physical
25416956
MORN4_HUMANMORN4physical
25416956
SEPT4_HUMANSEPT4physical
26186194
SEPT2_HUMANSEPT2physical
26186194
SEPT7_HUMANSEPT7physical
26186194
SEP14_HUMANSEPT14physical
26186194
SEPT5_HUMANSEPT5physical
26186194
SEPT8_HUMANSEPT8physical
26186194
SEP11_HUMANSEPT11physical
26186194
SEP10_HUMANSEPT10physical
26186194
SEPT9_HUMANSEPT9physical
26186194
TRI32_HUMANTRIM32physical
26186194
GDS1_HUMANRAP1GDS1physical
26186194
CEP72_HUMANCEP72physical
26186194
FLNB_HUMANFLNBphysical
26344197
SEPT5_HUMANSEPT5physical
26344197
UBA1_HUMANUBA1physical
26344197
SEP10_HUMANSEPT10physical
28514442
SEPT5_HUMANSEPT5physical
28514442
SEPT4_HUMANSEPT4physical
28514442
SEP14_HUMANSEPT14physical
28514442
SEPT9_HUMANSEPT9physical
28514442
SEPT8_HUMANSEPT8physical
28514442
TRI32_HUMANTRIM32physical
28514442
SEP11_HUMANSEPT11physical
28514442
GDS1_HUMANRAP1GDS1physical
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 SEPT6_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-416, AND MASS SPECTROMETRY.
"Exploring proteomes and analyzing protein processing by massspectrometric identification of sorted N-terminal peptides.";
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,Thomas G.R., Vandekerckhove J.;
Nat. Biotechnol. 21:566-569(2003).
Cited for: PROTEIN SEQUENCE OF 2-8, AND ACETYLATION AT ALA-2.
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-196 AND LYS-367, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-416, AND MASS SPECTROMETRY.
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-408; SER-411; SER-416AND THR-418, AND MASS SPECTROMETRY.
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-418, AND MASSSPECTROMETRY.

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