DYN1_MOUSE - dbPTM
DYN1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DYN1_MOUSE
UniProt AC P39053
Protein Name Dynamin-1
Gene Name Dnm1
Organism Mus musculus (Mouse).
Sequence Length 867
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. Involved in receptor-mediated endocytosis (By similarity)..
Protein Sequence MGNRGMEDLIPLVNRLQDAFSAIGQNADLDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLVLQLVNSTTEYAEFLHCKGKKFTDFEEVRLEIEAETDRVTGTNKGISPVPINLRVYSPHVLNLTLVDLPGMTKVPVGDQPPDIEFQIRDMLMQFVTKENCLILAVSPANSDLANSDALKIAKEVDPQGQRTIGVITKLDLMDEGTDARDVLENKLLPLRRGYIGVVNRSQKDIDGKKDITAALAAERKFFLSHPSYRHLADRMGTPYLQKVLNQQLTNHIRDTLPGLRNKLQSQLLSIEKEVDEYKNFRPDDPARKTKALLQMVQQFAVDFEKRIEGSGDQIDTYELSGGARINRIFHERFPFELVKMEFDEKELRREISYAIKNIHGIRTGLFTPDMAFETIVKKQVKKIREPCLKCVDMVISELISTVRQCTKKLQQYPRLREEMERIVTTHIREREGRTKEQVMLLIDIELAYMNTNHEDFIGFANAQQRSNQMNKKKTSGNQDEILVIRKGWLTINNIGIMKGGSKEYWFVLTAENLSWYKDDEEKEKKYMLSVDNLKLRDVEKGFMSSKHIFALFNTEQRNVYKDYRQLELACETQEEVDSWKASFLRAGVYPERVGDKEKASETEENGSDSFMHSMDPQLERQVETIRNLVDSYMAIVNKTVRDLMPKTIMHLMINNTKEFIFSELLANLYSCGDQNTLMEESAEQAQRRDEMLRMYHALKEALSIIGDINTTTVSTPMPPPVDDSWLQVQSVPAGRRSPTSSPTPQRRAPAVPPARPGSRGPAPGPPPAGSALGGAPPVPSRPGASPDPFGPPPQVPSRPNRAPPGVPSLGAWRLNSPQGKHENRAGKARL
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
76PhosphorylationLVLQLVNSTTEYAEF
CHHHHHCCCHHHHHH		29.2629899451
77PhosphorylationVLQLVNSTTEYAEFL
HHHHHCCCHHHHHHH		20.6029899451
80PhosphorylationLVNSTTEYAEFLHCK
HHCCCHHHHHHHCCC		14.8929899451
86S-nitrosocysteineEYAEFLHCKGKKFTD
HHHHHHCCCCCCCCC		7.27-
86S-nitrosylationEYAEFLHCKGKKFTD
HHHHHHCCCCCCCCC		7.2719101475
86S-palmitoylationEYAEFLHCKGKKFTD
HHHHHHCCCCCCCCC		7.2728680068
92PhosphorylationHCKGKKFTDFEEVRL
CCCCCCCCCHHHEEE		48.97-
111PhosphorylationETDRVTGTNKGISPV
ECCCCCCCCCCCCCC		25.1318779572
125Nitrated tyrosineVPINLRVYSPHVLNL
CCEEEEEECCEEEEE		15.28-
125PhosphorylationVPINLRVYSPHVLNL
CCEEEEEECCEEEEE		15.2820415495
125NitrationVPINLRVYSPHVLNL
CCEEEEEECCEEEEE		15.2816800626
125NitrationVPINLRVYSPHVLNL
CCEEEEEECCEEEEE		15.2816800626
126PhosphorylationPINLRVYSPHVLNLT
CEEEEEECCEEEEEE		12.9829899451
175PhosphorylationNCLILAVSPANSDLA
CEEEEEECCCCCCCC		16.8225521595
200PhosphorylationVDPQGQRTIGVITKL
CCCCCCEEEEEEEEH		17.7528059163
206 (in isoform 4)Ubiquitination-28.9522790023
206UbiquitinationRTIGVITKLDLMDEG
EEEEEEEEHHHCCCC		28.9522790023
223UbiquitinationARDVLENKLLPLRRG
HHHHHHHCCCCCCCC		41.8622790023
223 (in isoform 4)Ubiquitination-41.8622790023
231PhosphorylationLLPLRRGYIGVVNRS
CCCCCCCCEEEEECC		7.8418779572
238PhosphorylationYIGVVNRSQKDIDGK
CEEEEECCHHCCCCC		36.0618779572
257UbiquitinationAALAAERKFFLSHPS
HHHHHHHHHHHCCHH		31.7922790023
257 (in isoform 4)Ubiquitination-31.7922790023
261PhosphorylationAERKFFLSHPSYRHL
HHHHHHHCCHHHHHH		28.35-
264PhosphorylationKFFLSHPSYRHLADR
HHHHCCHHHHHHHHH		29.40-
265NitrationFFLSHPSYRHLADRM
HHHCCHHHHHHHHHC		13.40-
299 (in isoform 4)Ubiquitination-41.2822790023
299UbiquitinationTLPGLRNKLQSQLLS
HCHHHHHHHHHHHHH		41.2822790023
302PhosphorylationGLRNKLQSQLLSIEK
HHHHHHHHHHHHHHH		32.9820415495
306PhosphorylationKLQSQLLSIEKEVDE
HHHHHHHHHHHHHHH		36.9819060867
309 (in isoform 4)Ubiquitination-62.4622790023
309UbiquitinationSQLLSIEKEVDEYKN
HHHHHHHHHHHHHHC		62.4622790023
315UbiquitinationEKEVDEYKNFRPDDP
HHHHHHHHCCCCCCH		47.7822790023
315 (in isoform 4)Ubiquitination-47.7822790023
342UbiquitinationQFAVDFEKRIEGSGD
HHHHCHHHHCCCCCC		59.68-
347PhosphorylationFEKRIEGSGDQIDTY
HHHHCCCCCCCCEEE		26.8025521595
353PhosphorylationGSGDQIDTYELSGGA
CCCCCCEEEEECCCC		22.1129899451
354PhosphorylationSGDQIDTYELSGGAR
CCCCCEEEEECCCCC		15.8915592455
354NitrationSGDQIDTYELSGGAR
CCCCCEEEEECCCCC		15.89-
376 (in isoform 4)Ubiquitination-45.3922790023
376UbiquitinationRFPFELVKMEFDEKE
CCCHHHEECCCCHHH		45.3922790023
382 (in isoform 4)Ubiquitination-64.9922790023
382UbiquitinationVKMEFDEKELRREIS
EECCCCHHHHHHHHH		64.9922790023
393 (in isoform 4)Ubiquitination-41.5022790023
393UbiquitinationREISYAIKNIHGIRT
HHHHHHHHHHHCCCC		41.5022790023
400 (in isoform 3)Phosphorylation-35.9922324799
404 (in isoform 3)Phosphorylation-24.3420415495
412 (in isoform 3)Phosphorylation-3.1722324799
414 (in isoform 3)Ubiquitination-33.37-
449PhosphorylationCTKKLQQYPRLREEM
HHHHHHHCHHHHHHH		4.20-
511PhosphorylationNQMNKKKTSGNQDEI
HHHCCCCCCCCCCCE		51.2325521595
512PhosphorylationQMNKKKTSGNQDEIL
HHCCCCCCCCCCCEE		44.6325521595
535 (in isoform 4)Ubiquitination-59.1922790023
535UbiquitinationINNIGIMKGGSKEYW
EECEEEECCCCEEEE		59.1922790023
538PhosphorylationIGIMKGGSKEYWFVL
EEEECCCCEEEEEEE		30.86-
563PhosphorylationDEEKEKKYMLSVDNL
HHHHHHHEEEEEECC		17.8525521595
566PhosphorylationKEKKYMLSVDNLKLR
HHHHEEEEEECCCCH		15.7625521595
571 (in isoform 4)Ubiquitination-47.9722790023
571UbiquitinationMLSVDNLKLRDVEKG
EEEEECCCCHHHHHH		47.9722790023
619PhosphorylationEVDSWKASFLRAGVY
HHHHHHHHHHHHCCC		22.5324704852
635 (in isoform 4)Ubiquitination-64.0522790023
635UbiquitinationERVGDKEKASETEEN
HHCCCHHHCCCCCCC		64.0522790023
639PhosphorylationDKEKASETEENGSDS
CHHHCCCCCCCCCCC		46.2129899451
644PhosphorylationSETEENGSDSFMHSM
CCCCCCCCCCCHHHC		41.4829899451
650PhosphorylationGSDSFMHSMDPQLER
CCCCCHHHCCHHHHH		17.06-
676PhosphorylationYMAIVNKTVRDLMPK
HHHHHCHHHHHHCCH		18.6418779572
761PhosphorylationMPPPVDDSWLQVQSV
CCCCCCCCCEEEECC		25.8129899451
767PhosphorylationDSWLQVQSVPAGRRS
CCCEEEECCCCCCCC		31.0829899451
774PhosphorylationSVPAGRRSPTSSPTP
CCCCCCCCCCCCCCC		31.0425521595
776PhosphorylationPAGRRSPTSSPTPQR
CCCCCCCCCCCCCCC		42.9825521595
777PhosphorylationAGRRSPTSSPTPQRR
CCCCCCCCCCCCCCC		37.3925521595
778PhosphorylationGRRSPTSSPTPQRRA
CCCCCCCCCCCCCCC		34.9625521595
780PhosphorylationRSPTSSPTPQRRAPA
CCCCCCCCCCCCCCC		33.7227742792
795PhosphorylationVPPARPGSRGPAPGP
CCCCCCCCCCCCCCC		36.4328418008
796MethylationPPARPGSRGPAPGPP
CCCCCCCCCCCCCCC		62.1124129315
807PhosphorylationPGPPPAGSALGGAPP
CCCCCCCCCCCCCCC		23.5625777480
817 (in isoform 5)Phosphorylation-51.8729899451
817PhosphorylationGGAPPVPSRPGASPD
CCCCCCCCCCCCCCC		51.8721659605
817 (in isoform 3)Phosphorylation-51.8729899451
822 (in isoform 3)Phosphorylation-35.4324453211
822 (in isoform 5)Phosphorylation-35.4324453211
822PhosphorylationVPSRPGASPDPFGPP
CCCCCCCCCCCCCCC		35.4326160508
830 (in isoform 6)Phosphorylation-51.4329899451
834 (in isoform 4)Phosphorylation-62.6129899451
834PhosphorylationGPPPQVPSRPNRAPP
CCCCCCCCCCCCCCC		62.6126160508
845 (in isoform 4)Phosphorylation-36.7129899451
847 (in isoform 6)Phosphorylation-27.6826824392
847 (in isoform 4)Phosphorylation-27.6830372032
849 (in isoform 6)Phosphorylation-11.9624453211
851 (in isoform 4)Phosphorylation-5.3322324799
853 (in isoform 4)Phosphorylation-24.1622324799
857 (in isoform 4)Phosphorylation-42.3622324799
857 (in isoform 6)Phosphorylation-42.3626239621
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 DYN1_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DYN1_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 DYN1_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KIF2A_MOUSEKif2aphysical
20037577
KIF5A_MOUSEKif5aphysical
20037577
TBA1A_MOUSETuba1aphysical
20037577
DYN1_MOUSEDnm1physical
9463375
SH3G2_MOUSESh3gl2physical
22167186
SH3G1_MOUSESh3gl1physical
22167186
KCMA1_MOUSEKcnma1physical
20114047
CLH1_MOUSECltcphysical
20114047
SH3K1_MOUSESh3kbp1physical
20551902
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DYN1_MOUSE

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Related Literatures of Post-Translational Modification
Nitration
ReferencePubMed
"Endogenously nitrated proteins in mouse brain: links toneurodegenerative disease.";
Sacksteder C.A., Qian W.-J., Knyushko T.V., Wang H., Chin M.H.,Lacan G., Melega W.P., Camp D.G. II, Smith R.D., Smith D.J.,Squier T.C., Bigelow D.J.;
Biochemistry 45:8009-8022(2006).
Cited for: NITRATION [LARGE SCALE ANALYSIS] AT TYR-125, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-778, AND MASSSPECTROMETRY.
"Large-scale identification and evolution indexing of tyrosinephosphorylation sites from murine brain.";
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
J. Proteome Res. 7:311-318(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-80; TYR-125 AND TYR-354,AND MASS SPECTROMETRY.

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