CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-036561
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Dynamin-like 120 kDa protein, mitochondrial 
Protein Synonyms/Alias
 Mitochondrial dynamin-like 120 kDa protein; Optic atrophy 1 (Autosomal dominant), isoform CRA_g 
Gene Name
 OPA1 
Gene Synonyms/Alias
 hCG_17270 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
154IDFEKIRKALPSSEDubiquitination[1]
261STSYAQQKRKVSDKEubiquitination[1, 2, 3]
283ELLHTQLKYQRILERubiquitination[1, 2, 4, 5, 6, 7]
356VGDQSAGKTSVLEMIubiquitination[1, 2]
544IQQIIEGKLFPMKALubiquitination[1]
585FQNSKLLKTSMLKAHubiquitination[1]
623EQQADSFKATRFNLEubiquitination[1, 2, 5]
653NELFEKAKNEILDEVubiquitination[1, 2]
768EESIKRHKWNDFAEDubiquitination[1]
847QCVHNETKNELEKMLubiquitination[6]
889EVDPSLIKDTWHQVYacetylation[8]
966RRLEKNVKEVLEDFAubiquitination[1]
Reference
 [1] 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]
 [2] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [3] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [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] 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]
 [6] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [7] 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]
 [8] 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
Functional Description
  
Sequence Annotation
  
Keyword
 Complete proteome; GTP-binding; Nucleotide-binding; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1015 AA 
Protein Sequence
MWRLRRAAVA CEVCQSLVKH SSGIKGSLPL QKLHLVSRSI YHSHHPTLKL QRPQLRTSFQ 60
QFSSLTNLPL RKLKFSPIKY GYQPRRNFWP ARLATRLLKL RYLILGSAVG GGYTAKKTFD 120
QWKDMIPDLS EYKWIVPDIV WEIDEYIDFE KIRKALPSSE DLVKLAPDFD KIVESLSLLK 180
DFFTSGHKLV SEVIGASDLL LLLGSPEETA FRATDRGSES DKHFRKGLLG ELILLQQQIQ 240
EHEEEARRAA GQYSTSYAQQ KRKVSDKEKI DQLQEELLHT QLKYQRILER LEKENKELRK 300
LVLQKDDKGI HHRKLKKSLI DMYSEVLDVL SDYDASYNTQ DHLPRVVVVG DQSAGKTSVL 360
EMIAQARIFP RGSGEMMTRS PVKVTLSEGP HHVALFKDSS REFDLTKEED LAALRHEIEL 420
RMRKNVKEGC TVSPETISLN VKGPGLQRMV LVDLPGVINT VTSGMAPDTK ETIFSISKAY 480
MQNPNAIILC IQDGSVDAER SIVTDLVSQM DPHGRRTIFV LTKVDLAEKN VASPSRIQQI 540
IEGKLFPMKA LGYFAVVTGK GNSSESIEAI REYEEEFFQN SKLLKTSMLK AHQVTTRNLS 600
LAVSDCFWKM VRESVEQQAD SFKATRFNLE TEWKNNYPRL RELDRNELFE KAKNEILDEV 660
ISLSQVTPKH WEEILQQSLW ERVSTHVIEN IYLPAAQTMN SGTFNTTVDI KLKQWTDKQL 720
PNKAVEVAWE TLQEEFSRFM TEPKGKEHDD IFDKLKEAVK EESIKRHKWN DFAEDSLRVI 780
QHNALEDRSI SDKQQWDAAI YFMEEALQAR LKDTENAIEN MVGPDWKKRW LYWKNRTQEQ 840
CVHNETKNEL EKMLKCNEEH PAYLASDEIT TVRKNLESRG VEVDPSLIKD TWHQVYRRHF 900
LKTALNHCNL CRRGFYYYQR HFVDSELECN DVVLFWRIQR MLAITANTLR QQLTNTEVRR 960
LEKNVKEVLE DFAEDGEKKI KLLTGKRVQL AEDLKKVREI QEKLDAFIEA LHQEK 1015 
Gene Ontology
 GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
 GO:0003924; F:GTPase activity; IEA:InterPro.
 GO:0006184; P:GTP catabolic process; IEA:GOC. 
Interpro
 IPR022812; Dynamin.
 IPR001401; Dynamin_GTPase.
 IPR027417; P-loop_NTPase. 
Pfam
 PF00350; Dynamin_N 
SMART
 SM00053; DYNc 
PROSITE
  
PRINTS
 PR00195; DYNAMIN.