DYN3_MOUSE - dbPTM
DYN3_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DYN3_MOUSE
UniProt AC Q8BZ98
Protein Name Dynamin-3
Gene Name Dnm3
Organism Mus musculus (Mouse).
Sequence Length 863
Subcellular Localization Cytoplasm. Cytoplasm, cytoskeleton. Microtubule-associated..
Protein Description Microtubule-associated force-producing protein involved in producing microtubule bundles and able to bind and hydrolyze GTP. Most probably involved in vesicular trafficking processes, in particular endocytosis (By similarity)..
Protein Sequence MGNREMEELIPLVNRLQDAFSALGQSCLLELPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLVLQLVTSKAEYAEFLHCKGKKFTDFDEVRHEIEAETDRVTGMNKGISSIPINLRVYSPHVLNLTLIDLPGITKVPVGDQPPDIEYQIRDMIMQFITRENCLILAVTPANTDLANSDALKLAKEVDPQGLRTIGVITKLDLMDEGTDARDVLENKLLPLRRGYVGVVNRSQKDIDGKKDIKAAMLAERKFFLSHPAYRHIADRMGTPHLQKVLNQQLTNHIRDTLPNFRNKLQGQLLSIEHEVEAFKNFKPEDPTRKTKALLQMVQQFAVDFEKRIEGSGDQVDTLELSGGAKINRIFHERFPFEIVKMEFNEKELRREISYAIKNIHGIRTGLFTPDMAFEAIVKKQIVKLKGPSLKSVDLVMQELINTVKKCTKRLANFPRLCEETERIVANHIREREGKTKDQVLLLIDIQVSYINTNHEDFIGFANAQQRSSQVHKKSTIGNQVIRKGWLTVSNIGIMKGGSKGYWFVLTAESLSWYKDDEEKEKKYMLPLDNLKVRDVEKGFMSSKHVFALFNTEQRNVYKDYRFLELACDSQEDVDSWKASLLRAGVYPDKSVGSNKTENDENGQAENFSMDPQLERQVETIRNLVDSYMSIINKCIRDLIPKTIMHLMINNVKDFINSELLAQLYSSEDQNTLMEESAEQAQRRDEMLRMYQALKEALAIIGDINTATVSTPAPPPVDDSWLQHSRRSPPPSPTTQRRLTISAPLPRPTSGRGPAPAIPSPGPHSGAPPVPFRPGPLPPFPNSSDSFGAPPQVPSRPTRAPPSVPSRRPPPSPTRPTIIRPLESSLLD
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
45PhosphorylationGGQSAGKSSVLENFV
CCCCCCCHHHHHHHC		25.4325521595
46PhosphorylationGQSAGKSSVLENFVG
CCCCCCHHHHHHHCC		33.9225521595
61PhosphorylationRDFLPRGSGIVTRRP
CCCCCCCCCCCCCCC		26.9929899451
75PhosphorylationPLVLQLVTSKAEYAE
CEEHHHHHCHHHHHH		32.8528507225
76PhosphorylationLVLQLVTSKAEYAEF
EEHHHHHCHHHHHHH		23.5328507225
113UbiquitinationDRVTGMNKGISSIPI
CCCCCCCCCCCCCCE		49.0527667366
200PhosphorylationVDPQGLRTIGVITKL
CCCCCHHEEEEEEEH		27.4220531401
206UbiquitinationRTIGVITKLDLMDEG
HEEEEEEEHHHCCCC		28.95-
223UbiquitinationARDVLENKLLPLRRG
HHHHHHHCCCCCCCC		41.8627667366
231PhosphorylationLLPLRRGYVGVVNRS
CCCCCCCCEEEECCC		7.69-
240UbiquitinationGVVNRSQKDIDGKKD
EEECCCHHCCCCCHH		58.8827667366
249UbiquitinationIDGKKDIKAAMLAER
CCCCHHHHHHHHHHH		39.9822790023
257UbiquitinationAAMLAERKFFLSHPA
HHHHHHHHHHHCCHH		31.79-
299AcetylationTLPNFRNKLQGQLLS
HHHHHHHHHHHHEEC		37.62-
306PhosphorylationKLQGQLLSIEHEVEA
HHHHHEECHHHHHHH		34.2329899451
342UbiquitinationQFAVDFEKRIEGSGD
HHHHCHHHHCCCCCC		59.68-
347PhosphorylationFEKRIEGSGDQVDTL
HHHHCCCCCCCCEEE		26.8029899451
353PhosphorylationGSGDQVDTLELSGGA
CCCCCCEEEEECCCC		24.2329899451
357PhosphorylationQVDTLELSGGAKINR
CCEEEEECCCCEECH		26.3021183079
393UbiquitinationREISYAIKNIHGIRT
HHHHHHHHHHHCCCC		41.50-
559PhosphorylationDEEKEKKYMLPLDNL
CHHHHHCEEEECCCC		18.23-
579AcetylationEKGFMSSKHVFALFN
HHCCCCCCCEEEEEE		36.1615608143
593PhosphorylationNTEQRNVYKDYRFLE
ECCCCHHHCCHHHHH		11.16-
594AcetylationTEQRNVYKDYRFLEL
CCCCHHHCCHHHHHH		43.96-
596PhosphorylationQRNVYKDYRFLELAC
CCHHHCCHHHHHHHC		10.1025521595
603S-palmitoylationYRFLELACDSQEDVD
HHHHHHHCCCHHHHH		8.9328680068
678PhosphorylationIRDLIPKTIMHLMIN
HHHHCCHHHHHHHHH		20.4122817900
755PhosphorylationAPPPVDDSWLQHSRR
CCCCCCCCHHHCCCC		25.8129899451
760PhosphorylationDDSWLQHSRRSPPPS
CCCHHHCCCCCCCCC		19.2129899451
763PhosphorylationWLQHSRRSPPPSPTT
HHHCCCCCCCCCCCC		40.4225521595
767PhosphorylationSRRSPPPSPTTQRRL
CCCCCCCCCCCCCEE		40.4225521595
769PhosphorylationRSPPPSPTTQRRLTI
CCCCCCCCCCCEEEE		39.6430372032
770PhosphorylationSPPPSPTTQRRLTIS
CCCCCCCCCCEEEEE		24.3830372032
775PhosphorylationPTTQRRLTISAPLPR
CCCCCEEEEECCCCC		15.8629899451
777PhosphorylationTQRRLTISAPLPRPT
CCCEEEEECCCCCCC		20.7122817900
784PhosphorylationSAPLPRPTSGRGPAP
ECCCCCCCCCCCCCC		45.13-
785PhosphorylationAPLPRPTSGRGPAPA
CCCCCCCCCCCCCCC		29.22-
847PhosphorylationPSRRPPPSPTRPTII
CCCCCCCCCCCCCCC		44.68-
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 DYN3_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DYN3_MOUSE !!
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 DYN3_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of DYN3_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DYN3_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations.";
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
Mol. Cell. Proteomics 6:283-293(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-763, AND MASSSPECTROMETRY.

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