CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-041072
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 Dynamin-2 
Protein Synonyms/Alias
  
Gene Name
 Dnm2 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
299SLPTLRSKLQSQLLSacetylation[1, 2]
376RFPFELVKMEFDEKDubiquitination[3]
393REISYAIKNIHGVRTubiquitination[3]
669SYVAIINKSIRDLMPubiquitination[3]
Reference
 [1] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [2] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
 [3] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023] 
Functional Description
  
Sequence Annotation
  
Keyword
 Complete proteome; GTP-binding; Nucleotide-binding; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 870 AA 
Protein Sequence
MGNRGMEELI PLVNKLQDAF SSIGQSCHLD LPQIAVVGGQ SAGKSSVLEN FVGRDFLPRG 60
SGIVTRRPLI LQLIFSKTEY AEFLHCKSKK FTDFDEVRQE IEAETDRVTG TNKGISPVPI 120
NLRVYSPHVL NLTLIDLPGI TKVPVGDQPP DIEYQIKDMI LQFISRESSL ILAVTPANMD 180
LANSDALKLA KEVDPQGLRT IGVITKLDLM DEGTDARDVL ENKLLPLRRG YIGVVNRSQK 240
DIEGKKDIRA ALAAERKFFL SHPAYRHMAD RMGTPHLQKT LNQQLTNHIR ESLPTLRSKL 300
QSQLLSLEKE VEEYKNFRPD DPTRKTKALL QMVQQFGVDF EKRIEGSGDQ VDTLELSGGA 360
RINRIFHERF PFELVKMEFD EKDLRREISY AIKNIHGVRT GLFTPDLAFE AIVKKQVVKL 420
KEPCLKCVDL VIQELISTVR QCTSKLSSYP RLREETERIV TTYIREREGR TKDQILLLID 480
IEQSYINTNH EDFIGFANAQ QRSTQLNKKR AIPNQGHVAV IRRGWLTINN ISLMKGGSKE 540
YWFVLTAESL SWYKDEEEKE KKYMLPLDNL KIRDVEKGFM SNKHVFAIFN TEQRNVYKDL 600
RQIELACDSQ EDVDSWKASF LRAGVYPEKD QAENEDGAQE NTFSMDPQLE RQVETIRNLV 660
DSYVAIINKS IRDLMPKTIM HLMINNTKAF IHHELLAYLY SSADQSSLME ESAEQAQRRD 720
DMLRMYHALK EALNIIGDIS TSTVSTPVPP PVDDTWLQNT SGHSPTPQRR PVSSVHPPGR 780
PPAVRGPTPG PPLIPMPVGA TSSFSAPPIP SRPGPQSVFA NNDPFSAPPQ IPSRPARIPP 840
GIPPGVPSRR APAAPSRPTI IRPAEPSLLD 870 
Gene Ontology
 GO:0005874; C:microtubule; IEA:InterPro.
 GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
 GO:0003924; F:GTPase activity; IEA:InterPro.
 GO:0005543; F:phospholipid binding; IEA:InterPro.
 GO:0006897; P:endocytosis; IEA:InterPro.
 GO:0006184; P:GTP catabolic process; IEA:GOC. 
Interpro
 IPR027188; DNM2.
 IPR022812; Dynamin.
 IPR000375; Dynamin_central.
 IPR001401; Dynamin_GTPase.
 IPR019762; Dynamin_GTPase_CS.
 IPR003130; GED.
 IPR020850; GTPase_effector_domain_GED.
 IPR027417; P-loop_NTPase.
 IPR011993; PH_like_dom.
 IPR001849; Pleckstrin_homology. 
Pfam
 PF01031; Dynamin_M
 PF00350; Dynamin_N
 PF02212; GED
 PF00169; PH 
SMART
 SM00053; DYNc
 SM00302; GED
 SM00233; PH 
PROSITE
 PS00410; DYNAMIN
 PS51388; GED
 PS50003; PH_DOMAIN 
PRINTS
 PR00195; DYNAMIN.