CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-014275
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Voltage-dependent anion-selective channel protein 1 
Protein Synonyms/Alias
 VDAC-1; mVDAC1; Outer mitochondrial membrane protein porin 1; Plasmalemmal porin; Voltage-dependent anion-selective channel protein 5; VDAC-5; mVDAC5 
Gene Name
 Vdac1 
Gene Synonyms/Alias
 Vdac5 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
33SARDVFTKGYGFGLIacetylation[1, 2, 3]
33SARDVFTKGYGFGLIubiquitination[4]
41GYGFGLIKLDLKTKSacetylation[1, 2, 3]
41GYGFGLIKLDLKTKSubiquitination[4]
45GLIKLDLKTKSENGLacetylation[3]
47IKLDLKTKSENGLEFacetylation[3]
47IKLDLKTKSENGLEFubiquitination[4]
66SANTETTKVNGSLETubiquitination[4]
74VNGSLETKYRWTEYGacetylation[1, 2, 3]
74VNGSLETKYRWTEYGubiquitination[4]
109DQLARGLKLTFDSSFacetylation[3]
122SFSPNTGKKNAKIKTubiquitination[4]
210FGGSIYQKVNKKLETacetylation[3]
210FGGSIYQKVNKKLETubiquitination[4]
237TRFGIAAKYQVDPDAacetylation[1, 2, 3, 5, 6, 7, 8, 9, 10]
249PDACFSAKVNNSSLIacetylation[7, 8, 9, 10]
249PDACFSAKVNNSSLIsuccinylation[9]
265LGYTQTLKPGIKLTLacetylation[3, 6, 8, 10, 11]
265LGYTQTLKPGIKLTLubiquitination[4]
279LSALLDGKNVNAGGHacetylation[3, 5, 8, 10, 11]
279LSALLDGKNVNAGGHubiquitination[4]
287NVNAGGHKLGLGLEFacetylation[11]
287NVNAGGHKLGLGLEFubiquitination[4]
Reference
 [1] Substrate and functional diversity of lysine acetylation revealed by a proteomics survey.
 Kim SC, Sprung R, Chen Y, Xu Y, Ball H, Pei J, Cheng T, Kho Y, Xiao H, Xiao L, Grishin NV, White M, Yang XJ, Zhao Y.
 Mol Cell. 2006 Aug;23(4):607-18. [PMID: 16916647]
 [2] Proteomics of mitochondrial inner and outer membranes.
 Distler AM, Kerner J, Hoppel CL.
 Proteomics. 2008 Oct;8(19):4066-82. [PMID: 18763707]
 [3] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
 Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
 Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123]
 [4] 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]
 [5] The fasted/fed mouse metabolic acetylome: N6-acetylation differences suggest acetylation coordinates organ-specific fuel switching.
 Yang L, Vaitheesvaran B, Hartil K, Robinson AJ, Hoopmann MR, Eng JK, Kurland IJ, Bruce JE.
 J Proteome Res. 2011 Sep 2;10(9):4134-49. [PMID: 21728379]
 [6] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [7] 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]
 [8] Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways.
 Rardin MJ, Newman JC, Held JM, Cusack MP, Sorensen DJ, Li B, Schilling B, Mooney SD, Kahn CR, Verdin E, Gibson BW.
 Proc Natl Acad Sci U S A. 2013 Apr 16;110(16):6601-6. [PMID: 23576753]
 [9] 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]
 [10] Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation.
 Still AJ, Floyd BJ, Hebert AS, Bingman CA, Carson JJ, Gunderson DR, Dolan BK, Grimsrud PA, Dittenhafer-Reed KE, Stapleton DS, Keller MP, Westphall MS, Denu JM, Attie AD, Coon JJ, Pagliarini DJ.
 J Biol Chem. 2013 Jul 17;. [PMID: 23864654]
 [11] Quantitative assessment of the impact of the gut microbiota on lysine epsilon-acetylation of host proteins using gnotobiotic mice.
 Simon GM, Cheng J, Gordon JI.
 Proc Natl Acad Sci U S A. 2012 Jul 10;109(28):11133-8. [PMID: 22733758
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 255 257 NAD (By similarity).
 NP_BIND 273 277 NAD (By similarity).
 MOD_RES 14 14 N-acetylmethionine; in isoform Mt-VDAC1
 MOD_RES 26 26 Phosphoserine (By similarity).
 MOD_RES 33 33 N6-acetyllysine.
 MOD_RES 41 41 N6-acetyllysine.
 MOD_RES 74 74 N6-acetyllysine.
 MOD_RES 80 80 Phosphotyrosine.
 MOD_RES 117 117 Phosphoserine.
 MOD_RES 208 208 Phosphotyrosine.
 MOD_RES 237 237 N6-acetyllysine.
 MOD_RES 279 279 N6-acetyllysine (By similarity).  
Keyword
 3D-structure; Acetylation; Alternative splicing; Apoptosis; Cell membrane; Complete proteome; Direct protein sequencing; Ion transport; Membrane; Mitochondrion; Mitochondrion outer membrane; NAD; Nucleotide-binding; Phosphoprotein; Porin; Reference proteome; Transmembrane; Transmembrane beta strand; Transport. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 296 AA 
Protein Sequence
MCSFFLVLLL WQNMAVPPTY ADLGKSARDV FTKGYGFGLI KLDLKTKSEN GLEFTSSGSA 60
NTETTKVNGS LETKYRWTEY GLTFTEKWNT DNTLGTEITV EDQLARGLKL TFDSSFSPNT 120
GKKNAKIKTG YKREHINLGC DVDFDIAGPS IRGALVLGYE GWLAGYQMNF ETSKSRVTQS 180
NFAVGYKTDE FQLHTNVNDG TEFGGSIYQK VNKKLETAVN LAWTAGNSNT RFGIAAKYQV 240
DPDACFSAKV NNSSLIGLGY TQTLKPGIKL TLSALLDGKN VNAGGHKLGL GLEFQA 296 
Gene Ontology
 GO:0005743; C:mitochondrial inner membrane; IDA:MGI.
 GO:0042645; C:mitochondrial nucleoid; IEA:Compara.
 GO:0005741; C:mitochondrial outer membrane; ISO:MGI.
 GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
 GO:0046930; C:pore complex; IEA:UniProtKB-KW.
 GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
 GO:0015288; F:porin activity; IEA:UniProtKB-KW.
 GO:0008308; F:voltage-gated anion channel activity; IDA:UniProtKB.
 GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
 GO:0001662; P:behavioral fear response; IMP:MGI.
 GO:0007612; P:learning; IMP:MGI.
 GO:0007270; P:neuron-neuron synaptic transmission; IMP:MGI. 
Interpro
 IPR023614; Porin_dom.
 IPR001925; Porin_Euk.
 IPR027246; Porin_Euk/Tom40. 
Pfam
 PF01459; Porin_3 
SMART
  
PROSITE
 PS00558; EUKARYOTIC_PORIN 
PRINTS
 PR00185; EUKARYTPORIN.