CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-008315
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Dynamin-2 
Protein Synonyms/Alias
  
Gene Name
 DNM2 
Gene Synonyms/Alias
 DYN2 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
206RTIGVITKLDLMDEGubiquitination[1, 2]
223ARDVLENKLLPLRRGubiquitination[2, 3, 4]
257AALAAERKFFLSHPAubiquitination[2, 3, 4]
393REISYAIKNIHGVRTubiquitination[2, 3, 4]
414LAFEAIVKKQVVKLKubiquitination[1]
415AFEAIVKKQVVKLKEubiquitination[2]
562DEEEKEKKYMLPLDNubiquitination[1]
598TEQRNVYKDLRQIELacetylation[5]
598TEQRNVYKDLRQIELubiquitination[2]
669SYVAIINKSIRDLMPubiquitination[1, 3, 4]
Reference
 [1] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [2] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [3] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [4] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [5] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861] 
Functional 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. Involved in cytokinesis. 
Sequence Annotation
 DOMAIN 519 625 PH.
 DOMAIN 653 744 GED.
 NP_BIND 38 45 GTP (By similarity).
 NP_BIND 136 140 GTP (By similarity).
 NP_BIND 205 208 GTP (By similarity).
 MOD_RES 298 298 Phosphoserine (By similarity).
 MOD_RES 302 302 Phosphoserine (By similarity).
 MOD_RES 597 597 Phosphotyrosine (By similarity).
 MOD_RES 598 598 N6-acetyllysine.
 MOD_RES 764 764 Phosphoserine; by CDK1 (By similarity).  
Keyword
 3D-structure; Acetylation; Alternative splicing; Cell junction; Cell membrane; Charcot-Marie-Tooth disease; Complete proteome; Cytoplasm; Cytoskeleton; Disease mutation; Endocytosis; GTP-binding; Hydrolase; Membrane; Microtubule; Motor protein; Neuropathy; Nucleotide-binding; Phosphoprotein; Polymorphism; Postsynaptic cell membrane; Reference proteome; Synapse. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 870 AA 
Protein Sequence
MGNRGMEELI PLVNKLQDAF SSIGQSCHLD LPQIAVVGGQ SAGKSSVLEN FVGRDFLPRG 60
SGIVTRRPLI LQLIFSKTEH AEFLHCKSKK FTDFDEVRQE IEAETDRVTG TNKGISPVPI 120
NLRVYSPHVL NLTLIDLPGI TKVPVGDQPP DIEYQIKDMI LQFISRESSL ILAVTPANMD 180
LANSDALKLA KEVDPQGLRT IGVITKLDLM DEGTDARDVL ENKLLPLRRG YIGVVNRSQK 240
DIEGKKDIRA ALAAERKFFL SHPAYRHMAD RMGTPHLQKT LNQQLTNHIR ESLPALRSKL 300
QSQLLSLEKE VEEYKNFRPD DPTRKTKALL QMVQQFGVDF EKRIEGSGDQ VDTLELSGGA 360
RINRIFHERF PFELVKMEFD EKDLRREISY AIKNIHGVRT GLFTPDLAFE AIVKKQVVKL 420
KEPCLKCVDL VIQELINTVR QCTSKLSSYP RLREETERIV TTYIREREGR TKDQILLLID 480
IEQSYINTNH EDFIGFANAQ QRSTQLNKKR AIPNQGEILV IRRGWLTINN ISLMKGGSKE 540
YWFVLTAESL SWYKDEEEKE KKYMLPLDNL KIRDVEKGFM SNKHVFAIFN TEQRNVYKDL 600
RQIELACDSQ EDVDSWKASF LRAGVYPEKD QAENEDGAQE NTFSMDPQLE RQVETIRNLV 660
DSYVAIINKS IRDLMPKTIM HLMINNTKAF IHHELLAYLY SSADQSSLME ESADQAQRRD 720
DMLRMYHALK EALNIIGDIS TSTVSTPVPP PVDDTWLQSA SSHSPTPQRR PVSSIHPPGR 780
PPAVRGPTPG PPLIPVPVGA AASFSAPPIP SRPGPQSVFA NSDLFPAPPQ IPSRPVRIPP 840
GIPPGVPSRR PPAAPSRPTI IRPAEPSLLD 870 
Gene Ontology
 GO:0030054; C:cell junction; IEA:UniProtKB-KW.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0030666; C:endocytic vesicle membrane; TAS:Reactome.
 GO:0000139; C:Golgi membrane; TAS:Reactome.
 GO:0005874; C:microtubule; IDA:UniProtKB.
 GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
 GO:0005886; C:plasma membrane; TAS:Reactome.
 GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
 GO:0045211; C:postsynaptic membrane; IDA:UniProtKB.
 GO:0019899; F:enzyme binding; NAS:UniProtKB.
 GO:0005525; F:GTP binding; NAS:UniProtKB.
 GO:0003924; F:GTPase activity; NAS:UniProtKB.
 GO:0008017; F:microtubule binding; NAS:UniProtKB.
 GO:0005543; F:phospholipid binding; IEA:InterPro.
 GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; TAS:Reactome.
 GO:0016044; P:cellular membrane organization; TAS:Reactome.
 GO:0000086; P:G2/M transition of mitotic cell cycle; NAS:UniProtKB.
 GO:0046209; P:nitric oxide metabolic process; TAS:Reactome.
 GO:0043065; P:positive regulation of apoptotic process; NAS:UniProtKB.
 GO:0045893; P:positive regulation of transcription, DNA-dependent; NAS:UniProtKB.
 GO:0006892; P:post-Golgi vesicle-mediated transport; TAS:Reactome.
 GO:0031623; P:receptor internalization; IMP:BHF-UCL.
 GO:0050999; P:regulation of nitric-oxide synthase activity; TAS:Reactome.
 GO:0007165; P:signal transduction; NAS:UniProtKB.
 GO:0048489; P:synaptic vesicle transport; NAS:UniProtKB.
 GO:0033572; P:transferrin transport; IMP:BHF-UCL. 
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.