CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-000072
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Dynamin-1-like protein 
Protein Synonyms/Alias
 Dnm1p/Vps1p-like protein; DVLP; Dynamin family member proline-rich carboxyl-terminal domain less; Dymple; Dynamin-like protein; Dynamin-like protein 4; Dynamin-like protein IV; HdynIV; Dynamin-related protein 1 
Gene Name
 DNM1L 
Gene Synonyms/Alias
 DLP1; DRP1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
38VGTQSSGKSSVLESLsumoylation[1]
160VPVGDQPKDIELQIRubiquitination[2, 3]
238MGRVIPVKLGIIGVVubiquitination[3, 4, 5, 6]
283LANRNGTKYLARTLNacetylation[7]
532PSAVSRDKSSKVPSAsumoylation[8]
532PSAVSRDKSSKVPSAubiquitination[2]
535VSRDKSSKVPSALAPsumoylation[8]
558ASAEADGKLIQDSRRsumoylation[8]
568QDSRRETKNVASGGGsumoylation[8]
594GNWRGMLKTSKAEELsumoylation[8]
597RGMLKTSKAEELLAEsumoylation[8]
606EELLAEEKSKPIPIMsumoylation[8]
608LLAEEKSKPIPIMPAsumoylation[8]
Reference
 [1] Sumo1 conjugates mitochondrial substrates and participates in mitochondrial fission.
 Harder Z, Zunino R, McBride H.
 Curr Biol. 2004 Feb 17;14(4):340-5. [PMID: 14972687]
 [2] 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]
 [3] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [4] 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]
 [5] 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]
 [6] 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]
 [7] 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]
 [8] SUMOylation of the mitochondrial fission protein Drp1 occurs at multiple nonconsensus sites within the B domain and is linked to its activity cycle.
 Figueroa-Romero C, Iñiguez-Lluhí JA, Stadler J, Chang CR, Arnoult D, Keller PJ, Hong Y, Blackstone C, Feldman EL.
 FASEB J. 2009 Nov;23(11):3917-27. [PMID: 19638400] 
Functional Description
 Functions in mitochondrial and peroxisomal division. Mediates membrane fission through oligomerization into ring-like structures which wrap around the scission site to constict and sever the mitochondrial membrane through a GTP hydrolysis- dependent mechanism. Required for normal brain development. Facilitates developmentally-regulated apoptosis during neural tube development. Required for a normal rate of cytochrome c release and caspase activation during apoptosis. Also required for mitochondrial fission during mitosis. Required for programmed necrosis execution. May be involved in vesicle transport. 
Sequence Annotation
 DOMAIN 644 735 GED.
 NP_BIND 32 39 GTP (By similarity).
 NP_BIND 146 150 GTP (By similarity).
 NP_BIND 215 218 GTP (By similarity).
 REGION 1 343 GTPase domain.
 REGION 344 489 Middle domain.
 REGION 448 685 Interaction with GSK3B.
 REGION 502 569 B domain.
 MOD_RES 1 1 N-acetylmethionine.
 MOD_RES 529 529 Phosphoserine (By similarity).
 MOD_RES 548 548 Phosphoserine.
 MOD_RES 607 607 Phosphoserine.
 MOD_RES 616 616 Phosphoserine; by CDK1.
 MOD_RES 637 637 Phosphoserine; by CAMK1 and PKA.
 MOD_RES 644 644 S-nitrosocysteine.
 CARBOHYD 585 585 O-linked (GlcNAc...).
 CARBOHYD 586 586 O-linked (GlcNAc...).
 CROSSLNK 532 532 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 535 535 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 558 558 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 568 568 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 594 594 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 597 597 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 606 606 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 608 608 Glycyl lysine isopeptide (Lys-Gly)  
Keyword
 3D-structure; Acetylation; Alternative splicing; Complete proteome; Cytoplasm; Disease mutation; Glycoprotein; Golgi apparatus; GTP-binding; Hydrolase; Isopeptide bond; Membrane; Mitochondrion; Mitochondrion outer membrane; Necrosis; Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome; S-nitrosylation; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 736 AA 
Protein Sequence
MEALIPVINK LQDVFNTVGA DIIQLPQIVV VGTQSSGKSS VLESLVGRDL LPRGTGIVTR 60
RPLILQLVHV SQEDKRKTTG EENGVEAEEW GKFLHTKNKL YTDFDEIRQE IENETERISG 120
NNKGVSPEPI HLKIFSPNVV NLTLVDLPGM TKVPVGDQPK DIELQIRELI LRFISNPNSI 180
ILAVTAANTD MATSEALKIS REVDPDGRRT LAVITKLDLM DAGTDAMDVL MGRVIPVKLG 240
IIGVVNRSQL DINNKKSVTD SIRDEYAFLQ KKYPSLANRN GTKYLARTLN RLLMHHIRDC 300
LPELKTRINV LAAQYQSLLN SYGEPVDDKS ATLLQLITKF ATEYCNTIEG TAKYIETSEL 360
CGGARICYIF HETFGRTLES VDPLGGLNTI DILTAIRNAT GPRPALFVPE VSFELLVKRQ 420
IKRLEEPSLR CVELVHEEMQ RIIQHCSNYS TQELLRFPKL HDAIVEVVTC LLRKRLPVTN 480
EMVHNLVAIE LAYINTKHPD FADACGLMNN NIEEQRRNRL ARELPSAVSR DKSSKVPSAL 540
APASQEPSPA ASAEADGKLI QDSRRETKNV ASGGGGVGDG VQEPTTGNWR GMLKTSKAEE 600
LLAEEKSKPI PIMPASPQKG HAVNLLDVPV PVARKLSARE QRDCEVIERL IKSYFLIVRK 660
NIQDSVPKAV MHFLVNHVKD TLQSELVGQL YKSSLLDDLL TESEDMAQRR KEAADMLKAL 720
QGASQIIAEI RETHLW 736 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
 GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
 GO:0005874; C:microtubule; IDA:UniProtKB.
 GO:0005741; C:mitochondrial outer membrane; IDA:UniProtKB.
 GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
 GO:0005777; C:peroxisome; IDA:UniProtKB.
 GO:0043234; C:protein complex; IDA:UniProtKB.
 GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
 GO:0003924; F:GTPase activity; IEA:InterPro.
 GO:0006921; P:cellular component disassembly involved in execution phase of apoptosis; TAS:Reactome.
 GO:0003374; P:dynamin polymerization involved in mitochondrial fission; IDA:UniProtKB.
 GO:0006184; P:GTP catabolic process; IEA:GOC.
 GO:0090149; P:membrane fission involved in mitochondrial fission; IDA:UniProtKB.
 GO:0043653; P:mitochondrial fragmentation involved in apoptotic process; IMP:UniProtKB.
 GO:0070584; P:mitochondrion morphogenesis; IMP:MGI.
 GO:0016559; P:peroxisome fission; IDA:UniProtKB.
 GO:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; IMP:UniProtKB.
 GO:0090141; P:positive regulation of mitochondrial fission; TAS:BHF-UCL.
 GO:0050714; P:positive regulation of protein secretion; IDA:UniProtKB.
 GO:0090200; P:positive regulation of release of cytochrome c from mitochondria; IMP:UniProtKB.
 GO:0051289; P:protein homotetramerization; IDA:UniProtKB.
 GO:1900063; P:regulation of peroxisome organization; IMP:UniProtKB. 
Interpro
 IPR022812; Dynamin.
 IPR000375; Dynamin_central.
 IPR001401; Dynamin_GTPase.
 IPR019762; Dynamin_GTPase_CS.
 IPR003130; GED.
 IPR020850; GTPase_effector_domain_GED.
 IPR027417; P-loop_NTPase. 
Pfam
 PF01031; Dynamin_M
 PF00350; Dynamin_N
 PF02212; GED 
SMART
 SM00053; DYNc
 SM00302; GED 
PROSITE
 PS00410; DYNAMIN
 PS51388; GED 
PRINTS
 PR00195; DYNAMIN.