CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005004
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Voltage-dependent anion-selective channel protein 1 
Protein Synonyms/Alias
 VDAC-1; hVDAC1; Outer mitochondrial membrane protein porin 1; Plasmalemmal porin; Porin 31HL; Porin 31HM 
Gene Name
 VDAC1 
Gene Synonyms/Alias
 VDAC 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
12PTYADLGKSARDVFTubiquitination[1, 2]
20SARDVFTKGYGFGLIacetylation[3]
20SARDVFTKGYGFGLIubiquitination[1, 2, 4, 5, 6, 7, 8, 9]
28GYGFGLIKLDLKTKSacetylation[3, 10]
28GYGFGLIKLDLKTKSubiquitination[1]
34IKLDLKTKSENGLEFubiquitination[2, 6, 8]
53SANTETTKVTGSLETubiquitination[8]
61VTGSLETKYRWTEYGacetylation[3]
61VTGSLETKYRWTEYGubiquitination[1, 2, 5, 6, 8, 9]
109SFSPNTGKKNAKIKTubiquitination[2, 5, 6, 8, 9]
110FSPNTGKKNAKIKTGubiquitination[2]
161QMNFETAKSRVTQSNubiquitination[6, 7, 8]
197FGGSIYQKVNKKLETacetylation[11]
197FGGSIYQKVNKKLETubiquitination[2, 6, 8, 12]
224TRFGIAAKYQIDPDAacetylation[3, 11, 13, 14]
224TRFGIAAKYQIDPDAubiquitination[2]
252LGYTQTLKPGIKLTLubiquitination[1, 5, 6, 8, 9, 15]
266LSALLDGKNVNAGGHacetylation[3, 11, 13]
266LSALLDGKNVNAGGHubiquitination[5, 6, 8, 9]
274NVNAGGHKLGLGLEFubiquitination[1, 2, 4, 5, 6, 7, 8, 9]
Reference
 [1] 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]
 [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] 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]
 [4] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
 Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
 Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
 [5] 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]
 [6] 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]
 [7] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [8] 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]
 [9] 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]
 [10] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]
 [11] 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]
 [12] 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]
 [13] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
 [14] 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]
 [15] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724
Functional Description
 Forms a channel through the mitochondrial outer membrane and also the plasma membrane. The channel at the outer mitochondrial membrane allows diffusion of small hydrophilic molecules; in the plasma membrane it is involved in cell volume regulation and apoptosis. It adopts an open conformation at low or zero membrane potential and a closed conformation at potentials above 30-40 mV. The open state has a weak anion selectivity whereas the closed state is cation-selective. May participate in the formation of the permeability transition pore complex (PTPC) responsible for the release of mitochondrial products that triggers apoptosis. 
Sequence Annotation
 NP_BIND 242 244 NAD.
 NP_BIND 260 264 NAD.
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 13 13 Phosphoserine (By similarity).
 MOD_RES 20 20 N6-acetyllysine.
 MOD_RES 67 67 Phosphotyrosine (By similarity).
 MOD_RES 266 266 N6-acetyllysine.  
Keyword
 3D-structure; Acetylation; Apoptosis; Cell membrane; Complete proteome; Direct protein sequencing; Host-virus interaction; Ion transport; Membrane; Mitochondrion; Mitochondrion outer membrane; Phosphoprotein; Porin; Reference proteome; Transmembrane; Transmembrane beta strand; Transport. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 283 AA 
Protein Sequence
MAVPPTYADL GKSARDVFTK GYGFGLIKLD LKTKSENGLE FTSSGSANTE TTKVTGSLET 60
KYRWTEYGLT FTEKWNTDNT LGTEITVEDQ LARGLKLTFD SSFSPNTGKK NAKIKTGYKR 120
EHINLGCDMD FDIAGPSIRG ALVLGYEGWL AGYQMNFETA KSRVTQSNFA VGYKTDEFQL 180
HTNVNDGTEF GGSIYQKVNK KLETAVNLAW TAGNSNTRFG IAAKYQIDPD ACFSAKVNNS 240
SLIGLGYTQT LKPGIKLTLS ALLDGKNVNA GGHKLGLGLE FQA 283 
Gene Ontology
 GO:0005743; C:mitochondrial inner membrane; IEA:Compara.
 GO:0042645; C:mitochondrial nucleoid; IDA:BHF-UCL.
 GO:0005741; C:mitochondrial outer membrane; TAS:ProtInc.
 GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
 GO:0046930; C:pore complex; TAS:HGNC.
 GO:0015288; F:porin activity; IEA:UniProtKB-KW.
 GO:0008308; F:voltage-gated anion channel activity; ISS:UniProtKB.
 GO:0006915; P:apoptotic process; TAS:UniProtKB.
 GO:0001662; P:behavioral fear response; IEA:Compara.
 GO:0007612; P:learning; IEA:Compara.
 GO:0007270; P:neuron-neuron synaptic transmission; IEA:Compara.
 GO:0019048; P:virus-host interaction; IEA:UniProtKB-KW. 
Interpro
 IPR023614; Porin_dom.
 IPR001925; Porin_Euk.
 IPR027246; Porin_Euk/Tom40. 
Pfam
 PF01459; Porin_3 
SMART
  
PROSITE
 PS00558; EUKARYOTIC_PORIN 
PRINTS
 PR00185; EUKARYTPORIN.