DYN3_HUMAN - dbPTM
DYN3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DYN3_HUMAN
UniProt AC Q9UQ16
Protein Name Dynamin-3
Gene Name DNM3
Organism Homo sapiens (Human).
Sequence Length 869
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 MGNREMEELIPLVNRLQDAFSALGQSCLLELPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLVLQLVTSKAEYAEFLHCKGKKFTDFDEVRLEIEAETDRVTGMNKGISSIPINLRVYSPHVLNLTLIDLPGITKVPVGDQPPDIEYQIREMIMQFITRENCLILAVTPANTDLANSDALKLAKEVDPQGLRTIGVITKLDLMDEGTDARDVLENKLLPLRRGYVGVVNRSQKDIDGKKDIKAAMLAERKFFLSHPAYRHIADRMGTPHLQKVLNQQLTNHIRDTLPNFRNKLQGQLLSIEHEVEAYKNFKPEDPTRKTKALLQMVQQFAVDFEKRIEGSGDQVDTLELSGGAKINRIFHERFPFEIVKMEFNEKELRREISYAIKNIHGIRTGLFTPDMAFEAIVKKQIVKLKGPSLKSVDLVIQELINTVKKCTKKLANFPRLCEETERIVANHIREREGKTKDQVLLLIDIQVSYINTNHEDFIGFANAQQRSSQVHKKTTVGNQGTNLPPSRQIVIRKGWLTISNIGIMKGGSKGYWFVLTAESLSWYKDDEEKEKKYMLPLDNLKVRDVEKSFMSSKHIFALFNTEQRNVYKDYRFLELACDSQEDVDSWKASLLRAGVYPDKSVAENDENGQAENFSMDPQLERQVETIRNLVDSYMSIINKCIRDLIPKTIMHLMINNVKDFINSELLAQLYSSEDQNTLMEESAEQAQRRDEMLRMYQALKEALGIIGDISTATVSTPAPPPVDDSWIQHSRRSPPPSPTTQRRPTLSAPLARPTSGRGPAPAIPSPGPHSGAPPVPFRPGPLPPFPSSSDSFGAPPQVPSRPTRAPPSVPSRRPPPSPTRPTIIRPLESSLLD
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		25.4325332170
46PhosphorylationGQSAGKSSVLENFVG
CCCCCCHHHHHHHCC		33.9221712546
61PhosphorylationRDFLPRGSGIVTRRP
CCCCCCCCCCCCCCC		26.9924719451
75PhosphorylationPLVLQLVTSKAEYAE
CEEHHHHHCHHHHHH		32.85-
90UbiquitinationFLHCKGKKFTDFDEV
HHCCCCCCCCCHHHE		63.2629967540
109PhosphorylationEAETDRVTGMNKGIS
EEECCCCCCCCCCCC		31.4429523821
113UbiquitinationDRVTGMNKGISSIPI
CCCCCCCCCCCCCCE		49.0521890473
116PhosphorylationTGMNKGISSIPINLR
CCCCCCCCCCCEEEE		30.7720860994
117PhosphorylationGMNKGISSIPINLRV
CCCCCCCCCCEEEEE		30.3920860994
125PhosphorylationIPINLRVYSPHVLNL
CCEEEEEECCCEEEE		15.28-
126PhosphorylationPINLRVYSPHVLNLT
CEEEEEECCCEEEEE		12.9824076635
147UbiquitinationITKVPVGDQPPDIEY
CCEECCCCCCCCHHH		59.0321890473
180UbiquitinationAVTPANTDLANSDAL
EECCCCCCCCCCHHH		43.5221890473
200PhosphorylationVDPQGLRTIGVITKL
CCCCCCEEEEEEEEH		27.4218452278
206 (in isoform 1)Ubiquitination-28.9521906983
206 (in isoform 2)Ubiquitination-28.9521906983
206UbiquitinationRTIGVITKLDLMDEG
EEEEEEEEHHHCCCC		28.9521906983
206 (in isoform 3)Ubiquitination-28.9521906983
206 (in isoform 4)Ubiquitination-28.9521906983
214PhosphorylationLDLMDEGTDARDVLE
HHHCCCCCCHHHHHH		25.16-
214UbiquitinationLDLMDEGTDARDVLE
HHHCCCCCCHHHHHH		25.1621890473
217MethylationMDEGTDARDVLENKL
CCCCCCHHHHHHHCC		37.06-
223UbiquitinationARDVLENKLLPLRRG
HHHHHHHCCCCCCCC		41.8632015554
231PhosphorylationLLPLRRGYVGVVNRS
CCCCCCCCEEEECCC		7.69-
238PhosphorylationYVGVVNRSQKDIDGK
CEEEECCCHHCCCCC		36.06-
257UbiquitinationAAMLAERKFFLSHPA
HHHHHHHHHHHCCHH		31.7921890473
274PhosphorylationHIADRMGTPHLQKVL
HHHHHCCCHHHHHHH		9.74-
286PhosphorylationKVLNQQLTNHIRDTL
HHHHHHHHHHHHHHH		22.03-
299AcetylationTLPNFRNKLQGQLLS
HHHHHHHHHHHHEEC		37.62-
342UbiquitinationQFAVDFEKRIEGSGD
HHHHCHHHHCCCCCC		59.6830230243
347PhosphorylationFEKRIEGSGDQVDTL
HHHHCCCCCCCCEEE		26.8020068231
353PhosphorylationGSGDQVDTLELSGGA
CCCCCCEEEEECCCC		24.23-
389PhosphorylationKELRREISYAIKNIH
HHHHHHHHHHHHHHH		12.0828102081
390PhosphorylationELRREISYAIKNIHG
HHHHHHHHHHHHHHC		20.2928102081
393UbiquitinationREISYAIKNIHGIRT
HHHHHHHHHHHCCCC		41.5030230243
445UbiquitinationTVKKCTKKLANFPRL
HHHHHHHHHHCCHHH		34.3829967540
510 (in isoform 2)Phosphorylation-31.3621406692
510 (in isoform 3)Phosphorylation-31.3621406692
510 (in isoform 5)Phosphorylation-31.3621406692
511 (in isoform 2)Phosphorylation-34.9821406692
511 (in isoform 3)Phosphorylation-34.9821406692
511 (in isoform 5)Phosphorylation-34.9821406692
541AcetylationISNIGIMKGGSKGYW
EEEEEEECCCCCCEE		59.1920167786
569PhosphorylationDEEKEKKYMLPLDNL
CHHHHHCEEEECCCC		18.2320068231
603PhosphorylationNTEQRNVYKDYRFLE
ECCCCHHHCCHHHHH		11.16-
604AcetylationTEQRNVYKDYRFLEL
CCCCHHHCCHHHHHH		43.9622643397
606PhosphorylationQRNVYKDYRFLELAC
CCHHHCCHHHHHHHC		10.1029083192
615PhosphorylationFLELACDSQEDVDSW
HHHHHCCCHHHHHHH		35.0429083192
621PhosphorylationDSQEDVDSWKASLLR
CCHHHHHHHHHHHHH		30.2629083192
622 (in isoform 3)Phosphorylation-8.8618452278
622PhosphorylationSQEDVDSWKASLLRA
CHHHHHHHHHHHHHC		8.8618452278
632PhosphorylationSLLRAGVYPDKSVAE
HHHHCCCCCCCCHHC		12.56-
632 (in isoform 4)Phosphorylation-12.5618452278
746PhosphorylationLGIIGDISTATVSTP
HCCCCCCCEEEECCC		19.4123403867
763PhosphorylationPPVDDSWIQHSRRSP
CCCCCCHHHCCCCCC		2.8214762214
767PhosphorylationDSWIQHSRRSPPPSP
CCHHHCCCCCCCCCC		40.7614762214
769PhosphorylationWIQHSRRSPPPSPTT
HHHCCCCCCCCCCCC		40.4222617229
773PhosphorylationSRRSPPPSPTTQRRP
CCCCCCCCCCCCCCC		40.4222617229
775PhosphorylationRSPPPSPTTQRRPTL
CCCCCCCCCCCCCCC		39.6426033855
776PhosphorylationSPPPSPTTQRRPTLS
CCCCCCCCCCCCCCC		24.3829691806
783PhosphorylationTQRRPTLSAPLARPT
CCCCCCCCCCCCCCC		30.25-
790PhosphorylationSAPLARPTSGRGPAP
CCCCCCCCCCCCCCC		37.9628555341
791PhosphorylationAPLARPTSGRGPAPA
CCCCCCCCCCCCCCC		29.22-
801PhosphorylationGPAPAIPSPGPHSGA
CCCCCCCCCCCCCCC		36.0523312004
806PhosphorylationIPSPGPHSGAPPVPF
CCCCCCCCCCCCCCC		39.5223312004
853PhosphorylationPSRRPPPSPTRPTII
CCCCCCCCCCCCCCC		44.6830576142
855PhosphorylationRRPPPSPTRPTIIRP
CCCCCCCCCCCCCCC		54.3323312004
858PhosphorylationPPSPTRPTIIRPLES
CCCCCCCCCCCCCHH		26.2523312004
865PhosphorylationTIIRPLESSLLD---
CCCCCCHHHHCC---		33.6923312004
866PhosphorylationIIRPLESSLLD----
CCCCCHHHHCC----		24.4723312004
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_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DYN3_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 DYN3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DYN1_HUMANDNM1physical
26186194
DYN2_HUMANDNM2physical
26186194
ALMS1_HUMANALMS1physical
26186194
SNX5_HUMANSNX5physical
26186194
CO1A1_HUMANCOL1A1physical
26186194
KIF2C_HUMANKIF2Cphysical
26186194
SNX6_HUMANSNX6physical
26186194
HECD1_HUMANHECTD1physical
26186194
KIF11_HUMANKIF11physical
26186194
SNX1_HUMANSNX1physical
26186194
SNX2_HUMANSNX2physical
26186194
HAUS8_HUMANHAUS8physical
26186194
HERC1_HUMANHERC1physical
26186194
P73_HUMANTP73physical
26186194
RAPH1_HUMANRAPH1physical
26186194
DNMBP_HUMANDNMBPphysical
26186194
GLGB_HUMANGBE1physical
26344197
RPE_HUMANRPEphysical
26344197
DYN1_HUMANDNM1physical
28514442
DNMBP_HUMANDNMBPphysical
28514442
DYN2_HUMANDNM2physical
28514442
SNX2_HUMANSNX2physical
28514442
SNX1_HUMANSNX1physical
28514442
RAPH1_HUMANRAPH1physical
28514442
KIF2C_HUMANKIF2Cphysical
28514442
SNX6_HUMANSNX6physical
28514442
SNX5_HUMANSNX5physical
28514442
ALMS1_HUMANALMS1physical
28514442
HAUS8_HUMANHAUS8physical
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 DYN3_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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-604, AND MASS SPECTROMETRY.

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