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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