DYN1_RAT - dbPTM
DYN1_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DYN1_RAT
UniProt AC P21575
Protein Name Dynamin-1
Gene Name Dnm1
Organism Rattus norvegicus (Rat).
Sequence Length 864
Subcellular Localization Cytoplasm . Cytoplasm, cytoskeleton . Microtubule-associated (PubMed:9725914). Isoform-specific localization (PubMed:9725914).
Isoform 2: Cytoplasm .
Isoform 6: 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. Involved in receptor-mediated endocytosis (By similarity)..
Protein Sequence MGNRGMEDLIPLVNRLQDAFSAIGQNADLDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLVLQLVNSTTEYAEFLHCKGKKFTDFEEVRLEIEAETDRVTGTNKGISPVPINLRVYSPHVLNLTLVDLPGMTKVPVGDQPPDIEFQIRDMLMQFVTKENCLILAVSPANSDLANSDALKIAKEVDPQGQRTIGVITKLDLMDEGTDARDVLENKLLPLRRGYIGVVNRSQKDIDGKKDITAALAAERKFFLSHPSYRHLADRMGTPYLQKVLNQQLTNHIRDTLPGLRNKLQSQLLSIEKEVDEYKNFRPDDPARKTKALLQMVQQFAVDFEKRIEGSGDQIDTYELSGGARINRIFHERFPFELVKMEFDEKELRREISYAIKNIHGIRTGLFTPDLAFEATVKKQVQKLKEPSIKCVDMVVSELTSTIRKCSEKLQQYPRLREEMERIVTTHIREREGRTKEQVMLLIDIELAYMNTNHEDFIGFANAQQRSNQMNKKKTSGNQDEILVIRKGWLTINNIGIMKGGSKEYWFVLTAENLSWYKDDEEKEKKYMLSVDNLKLRDVEKGFMSSKHIFALFNTEQRNVYKDYRQLELACETQEEVDSWKASFLRAGVYPERVGDKEKASETEENGSDSFMHSMDPQLERQVETIRNLVDSYMAIVNKTVRDLMPKTIMHLMINNTKEFIFSELLANLYSCGDQNTLMEESAEQAQRRDEMLRMYHALKEALSIIGDINTTTVSTPMPPPVDDSWLQVQSVPAGRRSPTSSPTPQRRAPAVPPARPGSRGPAPGPPPAGSALGGAPPVPSRPGASPDPFGPPPQVPSRPNRAPPGVPSRSGQASPSRPESPRPPFDL
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
76PhosphorylationLVLQLVNSTTEYAEF
CHHHHHCCCHHHHHH		29.2625403869
77PhosphorylationVLQLVNSTTEYAEFL
HHHHHCCCHHHHHHH		20.6025403869
80PhosphorylationLVNSTTEYAEFLHCK
HHCCCHHHHHHHCCC		14.8925403869
90AcetylationFLHCKGKKFTDFEEV
HHCCCCCCCCCHHHE		63.2622902405
111PhosphorylationETDRVTGTNKGISPV
ECCCCCCCCCCCCCC		25.1318779572
113UbiquitinationDRVTGTNKGISPVPI
CCCCCCCCCCCCCCE		58.41-
116PhosphorylationTGTNKGISPVPINLR
CCCCCCCCCCCEEEE		28.6323984901
125NitrationVPINLRVYSPHVLNL
CCEEEEEECCEEEEE		15.28-
125PhosphorylationVPINLRVYSPHVLNL
CCEEEEEECCEEEEE		15.28-
125Nitrated tyrosineVPINLRVYSPHVLNL
CCEEEEEECCEEEEE		15.28-
191AcetylationSDALKIAKEVDPQGQ
CCHHHHHHHCCCCCC		62.8422902405
231PhosphorylationLLPLRRGYIGVVNRS
CCCCCCCCEEEEECC		7.8418779572
238PhosphorylationYIGVVNRSQKDIDGK
CEEEEECCHHCCCCC		36.0618779572
245AcetylationSQKDIDGKKDITAAL
CHHCCCCCHHHHHHH		43.4522902405
257AcetylationAALAAERKFFLSHPS
HHHHHHHHHHHCCHH		31.7922902405
306PhosphorylationKLQSQLLSIEKEVDE
HHHHHHHHHHHHHHH		36.9825403869
315AcetylationEKEVDEYKNFRPDDP
HHHHHHHHCCCCCCH		47.7822902405
347PhosphorylationFEKRIEGSGDQIDTY
HHHHCCCCCCCCEEE		26.8017376771
353PhosphorylationGSGDQIDTYELSGGA
CCCCCCEEEEECCCC		22.11-
354PhosphorylationSGDQIDTYELSGGAR
CCCCCEEEEECCCCC		15.8922276854
382AcetylationVKMEFDEKELRREIS
EECCCCHHHHHHHHH		64.9922902405
393UbiquitinationREISYAIKNIHGIRT
HHHHHHHHHHHCCCC		41.50-
421AcetylationKKQVQKLKEPSIKCV
HHHHHHHCCCCCHHH		74.7022902405
445UbiquitinationTIRKCSEKLQQYPRL
HHHHHHHHHHHCHHH		34.99-
511PhosphorylationNQMNKKKTSGNQDEI
HHHCCCCCCCCCCCE		51.2327115346
512PhosphorylationQMNKKKTSGNQDEIL
HHCCCCCCCCCCCEE		44.6317376771
562AcetylationDDEEKEKKYMLSVDN
CHHHHHHHEEEEEEC		36.6622902405
566PhosphorylationKEKKYMLSVDNLKLR
HHHHEEEEEECCCCH		15.7622673903
577AcetylationLKLRDVEKGFMSSKH
CCCHHHHHHCCCCHH		58.2422902405
597PhosphorylationNTEQRNVYKDYRQLE
CHHHCHHHHHHHHHH		11.1620231454
598AcetylationTEQRNVYKDYRQLEL
HHHCHHHHHHHHHHH		43.9622643393
619PhosphorylationEVDSWKASFLRAGVY
HHHHHHHHHHHHCCC		22.5322673903
676PhosphorylationYMAIVNKTVRDLMPK
HHHHHCHHHHHHCCH		18.6418779572
774PhosphorylationSVPAGRRSPTSSPTP
CCCCCCCCCCCCCCC		31.0420526333
776PhosphorylationPAGRRSPTSSPTPQR
CCCCCCCCCCCCCCC		42.9830411139
777PhosphorylationAGRRSPTSSPTPQRR
CCCCCCCCCCCCCCC		37.3927097102
778PhosphorylationGRRSPTSSPTPQRRA
CCCCCCCCCCCCCCC		34.9620526333
780PhosphorylationRSPTSSPTPQRRAPA
CCCCCCCCCCCCCCC		33.7227097102
795PhosphorylationVPPARPGSRGPAPGP
CCCCCCCCCCCCCCC		36.4325403869
796MethylationPPARPGSRGPAPGPP
CCCCCCCCCCCCCCC		62.11-
817PhosphorylationGGAPPVPSRPGASPD
CCCCCCCCCCCCCCC		51.8728432305
822PhosphorylationVPSRPGASPDPFGPP
CCCCCCCCCCCCCCC		35.4317376771
834PhosphorylationGPPPQVPSRPNRAPP
CCCCCCCCCCCCCCC		62.6128432305
847PhosphorylationPPGVPSRSGQASPSR
CCCCCCCCCCCCCCC		39.3328551015
851PhosphorylationPSRSGQASPSRPESP
CCCCCCCCCCCCCCC		18.6030411139
853PhosphorylationRSGQASPSRPESPRP
CCCCCCCCCCCCCCC		58.9527097102
857PhosphorylationASPSRPESPRPPFDL
CCCCCCCCCCCCCCC		28.9730411139
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
231YPhosphorylationKinaseSRCP12931
PSP
231YPhosphorylationKinaseSRCQ9WUD9
PSP
597YPhosphorylationKinaseSRCP12931
PSP
597YPhosphorylationKinaseSRCQ9WUD9
PSP
774SPhosphorylationKinaseCDK5Q03114
PSP
774SPhosphorylationKinaseGSK3BP49841
PSP
778SPhosphorylationKinaseCDK5Q00535
PSP
778SPhosphorylationKinaseCDK5Q03114
PSP
778SPhosphorylationKinaseDYRK1AQ63470
GPS
795SPhosphorylationKinaseDYRK1AQ63470
PSP
795SPhosphorylationKinasePRKCAP05696
GPS
857SPhosphorylationKinaseDYRK1AQ63470
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DYN1_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 DYN1_RAT !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CLIC4_HUMANCLIC4physical
11563969
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DYN1_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 343-364; 511-522 AND 797-838 (ISOFORM1/2/4/5/6/8), PROTEIN SEQUENCE OF 847-864 (ISOFORM 1/5),PHOSPHORYLATION AT SER-347; SER-512; SER-774; SER-778; SER-822;SER-851 AND SER-857, AND MASS SPECTROMETRY.

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