P45880 · VDAC2_HUMAN
- ProteinVoltage-dependent anion-selective channel protein 2
- GeneVDAC2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids294 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
The channel adopts an open conformation at low or zero membrane potential and a closed conformation at potentials above 30-40 mV (By similarity).
The open state has a weak anion selectivity whereas the closed state is cation-selective (By similarity).
Binds various lipids, including the sphingolipid ceramide, the phospholipid phosphatidylcholine, and the sterols cholesterol and oxysterol (PubMed:31015432).
Binding of ceramide promotes the mitochondrial outer membrane permeabilization (MOMP) apoptotic pathway (PubMed:31015432).
Features
Showing features for binding site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 23 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 31 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Site | 84 | Involved in ceramide and phosphatidylcholine binding | ||||
Sequence: E | ||||||
Binding site | 253-255 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: LIG | ||||||
Binding site | 271-275 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: SALVD |
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameVoltage-dependent anion-selective channel protein 2
- Short namesVDAC-2; hVDAC2
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP45880
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 37-46 | Beta stranded | ||||
Sequence: LVKLDVKTKS | ||||||
Transmembrane | 50-58 | Beta stranded | ||||
Sequence: VEFSTSGSS | ||||||
Transmembrane | 65-75 | Beta stranded | ||||
Sequence: VTGTLETKYKW | ||||||
Transmembrane | 80-87 | Beta stranded | ||||
Sequence: LTFTEKWN | ||||||
Transmembrane | 91-100 | Beta stranded | ||||
Sequence: TLGTEIAIED | ||||||
Transmembrane | 106-115 | Beta stranded | ||||
Sequence: LKLTFDTTFS | ||||||
Transmembrane | 122-131 | Beta stranded | ||||
Sequence: SGKIKSSYKR | ||||||
Transmembrane | 134-141 | Beta stranded | ||||
Sequence: INLGCDVD | ||||||
Transmembrane | 148-156 | Beta stranded | ||||
Sequence: AIHGSAVFG | ||||||
Transmembrane | 161-169 | Beta stranded | ||||
Sequence: LAGYQMTFD | ||||||
Transmembrane | 174-186 | Beta stranded | ||||
Sequence: KLTRNNFAVGYRT | ||||||
Transmembrane | 189-196 | Beta stranded | ||||
Sequence: FQLHTNVN | ||||||
Transmembrane | 200-209 | Beta stranded | ||||
Sequence: EFGGSIYQKV | ||||||
Transmembrane | 213-222 | Beta stranded | ||||
Sequence: LDTSVNLAWT | ||||||
Transmembrane | 229-238 | Beta stranded | ||||
Sequence: RFGIAAKYQL | ||||||
Transmembrane | 242-249 | Beta stranded | ||||
Sequence: ASISAKVN | ||||||
Transmembrane | 253-262 | Beta stranded | ||||
Sequence: LIGVGYTQTL | ||||||
Transmembrane | 265-274 | Beta stranded | ||||
Sequence: GVKLTLSALV | ||||||
Transmembrane | 284-293 | Beta stranded | ||||
Sequence: HKVGLALELE |
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_006380 | 24 | ||||
Sequence: A → V | ||||||
Mutagenesis | 84 | Abolishes ceramide and phosphatidylcholine binding. Decreases apoptosis frequency following mitochondrial targeting of ceramide. | ||||
Sequence: E → Q |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 308 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain, cross-link, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Initiator methionine | 1 | UniProt | Removed | ||||
Sequence: M | |||||||
Modified residue | 2 | UniProt | N-acetylalanine | ||||
Sequence: A | |||||||
Chain | PRO_0000050505 | 2-294 | UniProt | Voltage-dependent anion-selective channel protein 2 | |||
Sequence: ATHGQTCARPMCIPPSYADLGKAARDIFNKGFGFGLVKLDVKTKSCSGVEFSTSGSSNTDTGKVTGTLETKYKWCEYGLTFTEKWNTDNTLGTEIAIEDQICQGLKLTFDTTFSPNTGKKSGKIKSSYKRECINLGCDVDFDFAGPAIHGSAVFGYEGWLAGYQMTFDSAKSKLTRNNFAVGYRTGDFQLHTNVNDGTEFGGSIYQKVCEDLDTSVNLAWTSGTNCTRFGIAAKYQLDPTASISAKVNNSSLIGVGYTQTLRPGVKLTLSALVDGKSINAGGHKVGLALELEA | |||||||
Modified residue | 31 | UniProt | N6-acetyllysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 31 | UniProt | N6-succinyllysine; alternate | ||||
Sequence: K | |||||||
Cross-link | 31 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 46 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 48 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 64 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 66 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 68 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Cross-link | 72 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | |||||||
Modified residue | 78 | UniProt | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 109 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 112 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 113 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 115 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 118 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 118 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 120 | UniProt | N6-acetyllysine; alternate | ||||
Sequence: K | |||||||
Cross-link | 120 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate | ||||
Sequence: K | |||||||
Cross-link | 121 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | |||||||
Cross-link | 124 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | |||||||
Cross-link | 172 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 243 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 251 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 251 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 252 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 261 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 277 | UniProt | N6-acetyllysine; alternate | ||||
Sequence: K | |||||||
Cross-link | 277 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate | ||||
Sequence: K | |||||||
Cross-link | 285 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K |
Post-translational modification
Keywords
- PTM
Proteomic databases
2D gel databases
PTM databases
Interaction
Subunit
Interacts with hexokinases (By similarity).
Interacts with ARMC12 in a TBC1D21-dependent manner (By similarity).
Interacts with KLC3 (By similarity).
Interacts with SPATA33 (By similarity).
Interacts with PPP3CC in a SPATA33-dependent manner (By similarity).
Binary interactions
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Domain
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
P45880-3
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name3
- Length294
- Mass (Da)31,567
- Last updated2007-09-11 v2
- ChecksumF4EAE732E653637E
P45880-1
- Name1
- Differences from canonical
- 1-11: MATHGQTCARP → MSWCNELRLPALKQHSIGRGLESHIT
P45880-2
- Name2
- Differences from canonical
- 1-11: Missing
Computationally mapped potential isoform sequences
There are 4 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
Q5JSD1 | Q5JSD1_HUMAN | VDAC2 | 204 | ||
Q5JSD2 | Q5JSD2_HUMAN | VDAC2 | 194 | ||
A0A0A0MR02 | A0A0A0MR02_HUMAN | VDAC2 | 282 | ||
A2A3S1 | A2A3S1_HUMAN | VDAC2 | 109 |
Sequence caution
Features
Showing features for alternative sequence.
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
L08666 EMBL· GenBank· DDBJ | AAA60144.1 EMBL· GenBank· DDBJ | mRNA | Frameshift | |
L08666 EMBL· GenBank· DDBJ | AAA60145.1 EMBL· GenBank· DDBJ | mRNA | Frameshift | |
L06328 EMBL· GenBank· DDBJ | AAB59457.1 EMBL· GenBank· DDBJ | mRNA | ||
AF152227 EMBL· GenBank· DDBJ | AAD40241.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF152220 EMBL· GenBank· DDBJ | AAD40241.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF152221 EMBL· GenBank· DDBJ | AAD40241.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF152222 EMBL· GenBank· DDBJ | AAD40241.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF152223 EMBL· GenBank· DDBJ | AAD40241.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF152224 EMBL· GenBank· DDBJ | AAD40241.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF152225 EMBL· GenBank· DDBJ | AAD40241.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF152226 EMBL· GenBank· DDBJ | AAD40241.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CR456964 EMBL· GenBank· DDBJ | CAG33245.1 EMBL· GenBank· DDBJ | mRNA | ||
AL390034 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL392111 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC000165 EMBL· GenBank· DDBJ | AAH00165.2 EMBL· GenBank· DDBJ | mRNA | ||
BC012883 EMBL· GenBank· DDBJ | AAH12883.2 EMBL· GenBank· DDBJ | mRNA | ||
BC072407 EMBL· GenBank· DDBJ | AAH72407.1 EMBL· GenBank· DDBJ | mRNA |