Tag Content
UniProt Accession
Theoretical PI
Molecular Weight
31733 Da  
Genbank Nucleotide ID
Genbank Protein ID
Gene Name
Gene Synonyms/Alias
Protein Name
Voltage-dependent anion-selective channel protein 2 
Protein Synonyms/Alias
VDAC-2mVDAC2 Outer mitochondrial membrane protein porin 2; Voltage-dependent anion-selective channel protein 6;VDAC-6mVDAC6 
Mus musculus (Mouse) 
NCBI Taxonomy ID
Chromosome Location
View in Ensembl genome browser  
Function in Stage
Function in Cell Type
Probability (GAS) of Function in Spermatogenesis
The probability was calculated by GAS algorithm, ranging from 0 to 1. The closer it is to 1, the more possibly it functions in spermatogenesis.
Temporarily unavailable 
Abstract of related literatures
1. Voltage-dependent anion channels (VDACs) are small pore-forming channels found in the mitochondrial outer membrane of all eukaryotes. VDACs conduct adenine nucleotides and are the binding sites for several cytosolic enzymes, including the isoforms of hexokinase and glycerol kinase. VDAC binding is developmentally and metabolically regulated and allows the kinases preferential access to mitochondrial ATP. Two human VDAC cDNAs have recently been identified, and a total of four VDAC loci have been mapped. Here, the isolation of two mouse VDAC cDNAs (VDAC5 and VDAC6) is described. By Northern analysis the two mouse VDAC isoforms show nearly identical expression patterns, with high levels of expression detected in heart, kidney, brain, and skeletal muscle and lesser levels of expression in all other tissues examined. The only exception is the lack of expression of VDAC5 in testes, whereas VDAC6 expression is highest in this tissue. VDAC6 appears to be encoded by more than one transcript. The mouse VDAC5 gene was mapped using an interspecies DNA mapping panel to the proximal region of chromosome 11, and the mouse VDAC6 gene was mapped using a panel to the proximal region of chromosome 14. PMID: [8660977] 

2. This study describes comprehensive polling of transcription start and termination sites and analysis of previously unidentified full-length complementary DNAs derived from the mouse genome. We identify the 5' and 3' boundaries of 181,047 transcripts with extensive variation in transcripts arising from alternative promoter usage, splicing, and polyadenylation. There are 16,247 new mouse protein-coding transcripts, including 5154 encoding previously unidentified proteins. Genomic mapping of the transcriptome reveals transcriptional forests, with overlapping transcription on both strands, separated by deserts in which few transcripts are observed. The data provide a comprehensive platform for the comparative analysis of mammalian transcriptional regulation in differentiation and development. PMID: [16141072] 

3. The National Institutes of Health's Mammalian Gene Collection (MGC) project was designed to generate and sequence a publicly accessible cDNA resource containing a complete open reading frame (ORF) for every human and mouse gene. The project initially used a random strategy to select clones from a large number of cDNA libraries from diverse tissues. Candidate clones were chosen based on 5'-EST sequences, and then fully sequenced to high accuracy and analyzed by algorithms developed for this project. Currently, more than 11,000 human and 10,000 mouse genes are represented in MGC by at least one clone with a full ORF. The random selection approach is now reaching a saturation point, and a transition to protocols targeted at the missing transcripts is now required to complete the mouse and human collections. Comparison of the sequence of the MGC clones to reference genome sequences reveals that most cDNA clones are of very high sequence quality, although it is likely that some cDNAs may carry missense variants as a consequence of experimental artifact, such as PCR, cloning, or reverse transcriptase errors. Recently, a rat cDNA component was added to the project, and ongoing frog (Xenopus) and zebrafish (Danio) cDNA projects were expanded to take advantage of the high-throughput MGC pipeline. PMID: [15489334] 

4. Acetylation of proteins on lysine residues is a dynamic posttranslational modification that is known to play a key role in regulating transcription and other DNA-dependent nuclear processes. However, the extent of this modification in diverse cellular proteins remains largely unknown, presenting a major bottleneck for lysine-acetylation biology. Here we report the first proteomic survey of this modification, identifying 388 acetylation sites in 195 proteins among proteins derived from HeLa cells and mouse liver mitochondria. In addition to regulators of chromatin-based cellular processes, nonnuclear localized proteins with diverse functions were identified. Most strikingly, acetyllysine was found in more than 20% of mitochondrial proteins, including many longevity regulators and metabolism enzymes. Our study reveals previously unappreciated roles for lysine acetylation in the regulation of diverse cellular pathways outside of the nucleus. The combined data sets offer a rich source for further characterization of the contribution of this modification to cellular physiology and human diseases. PMID: [16916647] 

5. Metazoans employ reversible tyrosine phosphorylation to regulate innumerable biological processes. Thus, the large-scale identification of tyrosine phosphorylation sites from primary tissues is an essential step toward a molecular systems understanding of dynamic regulation in vivo. The relative paucity of phosphotyrosine has greatly limited its identification in large-scale phosphoproteomic experiments. However, using antiphosphotyrosine peptide immunoprecipitations, we report the largest study to date of tyrosine phosphorylation sites from primary tissue, identifying 414 unique tyrosine phosphorylation sites from murine brain. To measure the conservation of phosphorylated tyrosines and their surrounding residues, we constructed a computational pipeline and identified patterns of conservation within the signature of phosphotyrosine. PMID: [18034455] 

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Forms a channel through the mitochondrial outer membranethat allows diffusion of small hydrophilic molecules. The channeladopts an open conformation at low or zero membrane potential anda closed conformation at potentials above 30-40 mV. The open statehas a weak anion selectivity whereas the closed state is cation-selective (By similarity). 
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Subcellular Location
Mitochondrion outer membrane. 
Tissue Specificity
Highest levels of expression detected intestis, less but still abundant expression in heart, kidney,brain, and skeletal muscle. 
Gene Ontology
GO IDGO termEvidence
GO:0005743 C:mitochondrial inner membrane IDA:MGI.
GO:0042645 C:mitochondrial nucleoid IEA:Compara.
GO:0005741 C:mitochondrial outer 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 IEA:InterPro.
GO:2001243 P:negative regulation of intrinsic apoptotic signaling pathway IMP:UniProtKB.
GO:0032272 P:negative regulation of protein polymerization IMP:UniProtKB.
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IPR001925;    Porin_Euk.
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PF01459;    Porin_3;    1.
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PS00558;    EUKARYOTIC_PORIN;    1.
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PR00185;    EUKARYTPORIN.;   
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Created Date
Record Type
GAS predicted 
Sequence Annotation
CHAIN         1    295       Voltage-dependent anion-selective channel
                             protein 2.
TRANSMEM     38     47       Beta stranded; (By similarity).
TRANSMEM     51     59       Beta stranded; (By similarity).
TRANSMEM     66     76       Beta stranded; (By similarity).
TRANSMEM     81     88       Beta stranded; (By similarity).
TRANSMEM     92    101       Beta stranded; (By similarity).
TRANSMEM    107    116       Beta stranded; (By similarity).
TRANSMEM    123    132       Beta stranded; (By similarity).
TRANSMEM    135    142       Beta stranded; (By similarity).
TRANSMEM    149    157       Beta stranded; (By similarity).
TRANSMEM    162    170       Beta stranded; (By similarity).
TRANSMEM    175    187       Beta stranded; (By similarity).
TRANSMEM    190    197       Beta stranded; (By similarity).
TRANSMEM    201    210       Beta stranded; (By similarity).
TRANSMEM    214    223       Beta stranded; (By similarity).
TRANSMEM    230    239       Beta stranded; (By similarity).
TRANSMEM    243    250       Beta stranded; (By similarity).
TRANSMEM    254    263       Beta stranded; (By similarity).
TRANSMEM    266    275       Beta stranded; (By similarity).
TRANSMEM    285    294       Beta stranded; (By similarity).
NP_BIND     254    256       NAD (By similarity).
NP_BIND     272    276       NAD (By similarity).
SITE         85     85       Involved in hexokinase binding (By
MOD_RES      32     32       N6-acetyllysine.
MOD_RES      40     40       N6-acetyllysine (By similarity).
MOD_RES      73     73       N6-acetyllysine (By similarity).
MOD_RES      75     75       N6-acetyllysine.
MOD_RES     116    116       Phosphoserine (By similarity).
MOD_RES     207    207       Phosphotyrosine.
MOD_RES     237    237       Phosphotyrosine (By similarity).
CONFLICT    260    260       T -> A (in Ref. 4; AAH03731).
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Nucleotide Sequence
Length: 1662 bp   Go to nucleotide: FASTA
Protein Sequence
Length: 295 bp   Go to amino acid: FASTA
The verified Protein-Protein interaction information
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