SEP11_HUMAN - dbPTM
SEP11_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SEP11_HUMAN
UniProt AC Q9NVA2
Protein Name Septin-11
Gene Name 11-Sep
Organism Homo sapiens (Human).
Sequence Length 429
Subcellular Localization Cytoplasm, cytoskeleton. Cell junction, synapse. Cell projection, dendritic spine. Cell projection, axon. Partly colocalizes with stress fibers and microtubules. During bacterial infection, displays a collar shape structure next to actin at the pole
Protein Description Filament-forming cytoskeletal GTPase. May play a role in cytokinesis (Potential). May play a role in the cytoarchitecture of neurons, including dendritic arborization and dendritic spines, and in GABAergic synaptic connectivity (By similarity). During Listeria monocytogenes infection, not required for the bacterial entry process, but restricts its efficacy..
Protein Sequence MAVAVGRPSNEELRNLSLSGHVGFDSLPDQLVNKSTSQGFCFNILCVGETGIGKSTLMDTLFNTKFESDPATHNEPGVRLKARSYELQESNVRLKLTIVDTVGFGDQINKDDSYKPIVEYIDAQFEAYLQEELKIKRSLFNYHDTRIHACLYFIAPTGHSLKSLDLVTMKKLDSKVNIIPIIAKADTIAKNELHKFKSKIMSELVSNGVQIYQFPTDEETVAEINATMSVHLPFAVVGSTEEVKIGNKMAKARQYPWGVVQVENENHCDFVKLREMLIRVNMEDLREQTHTRHYELYRRCKLEEMGFKDTDPDSKPFSLQETYEAKRNEFLGELQKKEEEMRQMFVMRVKEKEAELKEAEKELHEKFDLLKRTHQEEKKKVEDKKKELEEEVNNFQKKKAAAQLLQSQAQQSGAQQTKKDKDKKNASFT
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------MAVAVGRPS
------CCEECCCCC		9.6612665801
9PhosphorylationAVAVGRPSNEELRNL
CEECCCCCHHHHHCC		56.3529255136
9O-linked_GlycosylationAVAVGRPSNEELRNL
CEECCCCCHHHHHCC		56.3523301498
17PhosphorylationNEELRNLSLSGHVGF
HHHHHCCCCCCCCCC		24.8428450419
19PhosphorylationELRNLSLSGHVGFDS
HHHCCCCCCCCCCCC		24.3928450419
26PhosphorylationSGHVGFDSLPDQLVN
CCCCCCCCCCHHHCC		39.2726699800
46GlutathionylationGFCFNILCVGETGIG
CCCEEEEEECCCCCC		3.0622555962
50PhosphorylationNILCVGETGIGKSTL
EEEEECCCCCCHHHH		28.33-
55PhosphorylationGETGIGKSTLMDTLF
CCCCCCHHHHHHHHH		22.8921712546
56PhosphorylationETGIGKSTLMDTLFN
CCCCCHHHHHHHHHC		29.5921712546
64PhosphorylationLMDTLFNTKFESDPA
HHHHHHCCCCCCCCC		29.7621712546
65UbiquitinationMDTLFNTKFESDPAT
HHHHHCCCCCCCCCC		48.52-
65AcetylationMDTLFNTKFESDPAT
HHHHHCCCCCCCCCC		48.5226051181
75 (in isoform 2)Ubiquitination-35.51-
84PhosphorylationGVRLKARSYELQESN
CCEEEEEEEECHHCC		28.0228152594
85PhosphorylationVRLKARSYELQESNV
CEEEEEEEECHHCCC		18.3328152594
90PhosphorylationRSYELQESNVRLKLT
EEEECHHCCCEEEEE		27.8824076635
145PhosphorylationSLFNYHDTRIHACLY
HHHCCHHHHHEEEEE		20.43-
163PhosphorylationPTGHSLKSLDLVTMK
CCCCCCCCCCEEEHH		32.2020068231
168PhosphorylationLKSLDLVTMKKLDSK
CCCCCEEEHHHCCCC		30.4820068231
170UbiquitinationSLDLVTMKKLDSKVN
CCCEEEHHHCCCCCC		40.60-
175UbiquitinationTMKKLDSKVNIIPII
EHHHCCCCCCEEEEE		38.68-
184UbiquitinationNIIPIIAKADTIAKN
CEEEEEECCCHHHHH		36.06-
190AcetylationAKADTIAKNELHKFK
ECCCHHHHHHHHHHH		47.2925953088
190MalonylationAKADTIAKNELHKFK
ECCCHHHHHHHHHHH		47.2926320211
194 (in isoform 2)Ubiquitination-27.59-
294PhosphorylationEQTHTRHYELYRRCK
HHHHHHHHHHHHHHC		12.35-
297PhosphorylationHTRHYELYRRCKLEE
HHHHHHHHHHHCHHH		5.53-
301UbiquitinationYELYRRCKLEEMGFK
HHHHHHHCHHHCCCC		58.06-
308UbiquitinationKLEEMGFKDTDPDSK
CHHHCCCCCCCCCCC		54.73-
310PhosphorylationEEMGFKDTDPDSKPF
HHCCCCCCCCCCCCC		50.45-
311 (in isoform 2)Ubiquitination-55.96-
314PhosphorylationFKDTDPDSKPFSLQE
CCCCCCCCCCCCHHH		47.84-
315UbiquitinationKDTDPDSKPFSLQET
CCCCCCCCCCCHHHH		58.42-
318 (in isoform 2)Ubiquitination-37.36-
318PhosphorylationDPDSKPFSLQETYEA
CCCCCCCCHHHHHHH		37.3626657352
322PhosphorylationKPFSLQETYEAKRNE
CCCCHHHHHHHHHHH		17.4425627689
323PhosphorylationPFSLQETYEAKRNEF
CCCHHHHHHHHHHHH		17.0925159151
325 (in isoform 2)Ubiquitination-12.99-
325UbiquitinationSLQETYEAKRNEFLG
CHHHHHHHHHHHHHH		12.9921906983
326 (in isoform 1)Ubiquitination-43.7621890473
326UbiquitinationLQETYEAKRNEFLGE
HHHHHHHHHHHHHHH		43.76-
336UbiquitinationEFLGELQKKEEEMRQ
HHHHHHHHHHHHHHH		74.83-
336 (in isoform 2)Ubiquitination-74.8321890473
337UbiquitinationFLGELQKKEEEMRQM
HHHHHHHHHHHHHHH		58.35-
346 (in isoform 2)Ubiquitination-1.69-
347 (in isoform 2)Ubiquitination-2.52-
357UbiquitinationKEKEAELKEAEKELH
HHHHHHHHHHHHHHH		46.51-
361AcetylationAELKEAEKELHEKFD
HHHHHHHHHHHHHHH		73.0428735889
366UbiquitinationAEKELHEKFDLLKRT
HHHHHHHHHHHHHHH		33.17-
367 (in isoform 2)Ubiquitination-7.93-
378AcetylationKRTHQEEKKKVEDKK
HHHHHHHHHHHHHHH		58.0830592309
381 (in isoform 2)Ubiquitination-18.47-
388 (in isoform 2)Ubiquitination-16.05-
397AcetylationEEVNNFQKKKAAAQL
HHHHHHHHHHHHHHH		52.7026051181
397SuccinylationEEVNNFQKKKAAAQL
HHHHHHHHHHHHHHH		52.7023954790
399UbiquitinationVNNFQKKKAAAQLLQ
HHHHHHHHHHHHHHH		50.74-
399MalonylationVNNFQKKKAAAQLLQ
HHHHHHHHHHHHHHH		50.7426320211
407PhosphorylationAAAQLLQSQAQQSGA
HHHHHHHHHHHHHCC		27.7025850435
412PhosphorylationLQSQAQQSGAQQTKK
HHHHHHHHCCHHCHH		24.8225850435
417PhosphorylationQQSGAQQTKKDKDKK
HHHCCHHCHHHHCCC		28.1630242111
418UbiquitinationQSGAQQTKKDKDKKN
HHCCHHCHHHHCCCC		55.42-
418AcetylationQSGAQQTKKDKDKKN
HHCCHHCHHHHCCCC		55.4226051181
418MalonylationQSGAQQTKKDKDKKN
HHCCHHCHHHHCCCC		55.4226320211
427PhosphorylationDKDKKNASFT-----
HHCCCCCCCC-----		38.5226853621
428UbiquitinationKDKKNASFT------
HCCCCCCCC------		9.7421906983
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 SEP11_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SEP11_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 SEP11_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SEPT9_HUMANSEPT9physical
22939629
SEPT7_HUMANSEPT7physical
22939629
SEPT5_HUMANSEPT5physical
22939629
TM189_HUMANTMEM189physical
22939629
STIM1_HUMANSTIM1physical
22939629
SUCA_HUMANSUCLG1physical
22939629
XRCC1_HUMANXRCC1physical
22939629
SIN3A_HUMANSIN3Aphysical
22939629
THTR_HUMANTSTphysical
22939629
TCOF_HUMANTCOF1physical
22939629
TOM40_HUMANTOMM40physical
22939629
SOSB1_HUMANNABP2physical
22939629
TM177_HUMANTMEM177physical
22939629
TMEM9_HUMANTMEM9physical
22939629
VDAC2_HUMANVDAC2physical
22939629
SMCA2_HUMANSMARCA2physical
22939629
THTM_HUMANMPSTphysical
22939629
SF01_HUMANSF1physical
22939629
SEPT5_HUMANSEPT5physical
26344197
SEPT9_HUMANSEPT9physical
26344197
PRCC_HUMANPRCCphysical
27173435
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 SEP11_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, 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 2-14 (ISOFORM 1), AND ACETYLATION AT ALA-2.

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