DYN3_RAT - dbPTM
DYN3_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DYN3_RAT
UniProt AC Q08877
Protein Name Dynamin-3
Gene Name Dnm3
Organism Rattus norvegicus (Rat).
Sequence Length 869
Subcellular Localization Cytoplasm . Cytoplasm, cytoskeleton . Microtubule-associated. Isoform-specific localization.
Isoform 2: Cytoplasmic vesicle .
Isoform 8: Cytoplasm. Golgi apparatus .
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..
Protein Sequence MGNREMEELIPLVNRLQDAFSALGQSCLLELPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLVLQLVTSKAEYAEFLHCKGKKFTDFDEVRHEIEAETDRVTGMNKGISSVPINLRVYSPHVLNLTLIDLPGITKVPVGDQPPDIEYQIRDMIMQFITRENCLILAVTPANTDLANSDALKLAKEVDPQGLRTIGVITKLDLMDEGTDARDVLENKLLPLRRGYVGVVNRSQKDIDGKKDIKAAMLAERKFFLSHPAYRHIADRMGTPHLQKVLNQQLTNHIRDTLPNFRNKLQGQLLSIEHEVEAFKNFKPEDPTRKTKALLQMVQQFAVDFEKRIEGSGDQVDTLELSGGAKINRIFHERFPFEIVKMEFNEKELRREISYAIKNIHGIRTGLFTPDMAFEAIVKKQIVKLKGPSLKSVDLVMQELINTVKKCTKRLANFPRLCEETERIVANHIREREGKTKDQVLLLIDIQVSYINTNHEDFIGFANAQQRSSQVHKKSTIGNQGTNLPPSRQIVIRKGWLTVSNIGIMKGGSKGYWFVLTAESLSWYKDDEEKEKKYMLPLDNLKVRDVEKGFMSSKHVFALFNTEQRNVYKDYRSLELACDSQEDVDSWKASLLRAGVYPDKSFTENDENGQAENFSMDPQLERQVETIRNLVDSYMSIINKCIRDLIPKTIMHLMINNVKDFINSELLAQLYSSEDQNTLMEESVEQAQRRDEMLRMYQALKEALAIIGDINTVTVSTPAPPPVDDSWLQHSRRSPPPSPTTQRRLTLSAPLPRPASSRGPAPAIPSPGPHSGAPPVPFRPGPLPPFPNSSDSYGAPPQVPSRPTRAPPSVPSRRPPPSPTRPTIIRPLESSLLD
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
25.4325403869
46PhosphorylationGQSAGKSSVLENFVG
CCCCCCHHHHHHHCC
33.9225403869
61PhosphorylationRDFLPRGSGIVTRRP
CCCCCCCCCCCCCCC
26.9925403869
80PhosphorylationLVTSKAEYAEFLHCK
HHHCHHHHHHHHCCC
19.11-
191AcetylationSDALKLAKEVDPQGL
CHHHHHHHHCCCCCC
69.57-
231PhosphorylationLLPLRRGYVGVVNRS
CCCCCCCCEEEECCC
7.69-
257AcetylationAAMLAERKFFLSHPA
HHHHHHHHHHHCCHH
31.7922902405
299AcetylationTLPNFRNKLQGQLLS
HHHHHHHHHHHHEEC
37.6222902405
568AcetylationDDEEKEKKYMLPLDN
CCHHHHHCEEEECCC
36.6622902405
603PhosphorylationNTEQRNVYKDYRSLE
EHHCCHHHHCHHHHH
11.16-
604AcetylationTEQRNVYKDYRSLEL
HHCCHHHHCHHHHHH
43.9622902405
769PhosphorylationWLQHSRRSPPPSPTT
HHHCCCCCCCCCCCC
40.4214762214
773PhosphorylationSRRSPPPSPTTQRRL
CCCCCCCCCCCCCEE
40.4230411139
775PhosphorylationRSPPPSPTTQRRLTL
CCCCCCCCCCCEEEE
39.6427097102
776PhosphorylationSPPPSPTTQRRLTLS
CCCCCCCCCCEEEEE
24.3822108457
853PhosphorylationPSRRPPPSPTRPTII
CCCCCCCCCCCCCCC
44.6817376771

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_RAT !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DYN3_RAT !!

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_RAT !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of DYN3_RAT !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DYN3_RAT

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"The in vivo phosphorylation sites of rat brain dynamin I.";
Graham M.E., Anggono V., Bache N., Larsen M.R., Craft G.E.,Robinson P.J.;
J. Biol. Chem. 282:14695-14707(2007).
Cited for: PROTEIN SEQUENCE OF 839-859 (ISOFORM 1/3/5/7/9/11), PHOSPHORYLATION ATSER-769; SER-773 AND SER-853, AND MASS SPECTROMETRY.

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