P21796 · VDAC1_HUMAN
- ProteinNon-selective voltage-gated ion channel VDAC1
- GeneVDAC1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids283 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Non-selective voltage-gated ion channel that mediates the transport of anions and cations through the mitochondrion outer membrane and plasma membrane (PubMed:10661876, PubMed:11845315, PubMed:18755977, PubMed:30061676, PubMed:8420959).
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 (PubMed:10661876, PubMed:11845315, PubMed:18755977, PubMed:8420959).
It adopts an open conformation at low or zero membrane potential and a closed conformation at potentials above 30-40 mV (PubMed:10661876, PubMed:18755977, PubMed:8420959).
The open state has a weak anion selectivity whereas the closed state is cation-selective (PubMed:18755977, PubMed:8420959).
Binds various signaling molecules, including the sphingolipid ceramide, the phospholipid phosphatidylcholine, and the sterols cholesterol and oxysterol (PubMed:18755977, PubMed:31015432).
In depolarized mitochondria, acts downstream of PRKN and PINK1 to promote mitophagy or prevent apoptosis; polyubiquitination by PRKN promotes mitophagy, while monoubiquitination by PRKN decreases mitochondrial calcium influx which ultimately inhibits apoptosis (PubMed:32047033).
May participate in the formation of the permeability transition pore complex (PTPC) responsible for the release of mitochondrial products that triggers apoptosis (PubMed:15033708, PubMed:25296756).
May mediate ATP export from cells (PubMed:30061676).
Part of a complex composed of HSPA9, ITPR1 and VDAC1 that regulates mitochondrial calcium-dependent apoptosis by facilitating calcium transport from the ER lumen to the mitochondria intermembrane space thus providing calcium for the downstream calcium channel MCU that directly releases it into mitochondria matrix (By similarity).
Mediates cytochrome c efflux (PubMed:20230784).
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 (PubMed:10661876, PubMed:11845315, PubMed:18755977, PubMed:8420959).
It adopts an open conformation at low or zero membrane potential and a closed conformation at potentials above 30-40 mV (PubMed:10661876, PubMed:18755977, PubMed:8420959).
The open state has a weak anion selectivity whereas the closed state is cation-selective (PubMed:18755977, PubMed:8420959).
Binds various signaling molecules, including the sphingolipid ceramide, the phospholipid phosphatidylcholine, and the sterols cholesterol and oxysterol (PubMed:18755977, PubMed:31015432).
In depolarized mitochondria, acts downstream of PRKN and PINK1 to promote mitophagy or prevent apoptosis; polyubiquitination by PRKN promotes mitophagy, while monoubiquitination by PRKN decreases mitochondrial calcium influx which ultimately inhibits apoptosis (PubMed:32047033).
May participate in the formation of the permeability transition pore complex (PTPC) responsible for the release of mitochondrial products that triggers apoptosis (PubMed:15033708, PubMed:25296756).
May mediate ATP export from cells (PubMed:30061676).
Part of a complex composed of HSPA9, ITPR1 and VDAC1 that regulates mitochondrial calcium-dependent apoptosis by facilitating calcium transport from the ER lumen to the mitochondria intermembrane space thus providing calcium for the downstream calcium channel MCU that directly releases it into mitochondria matrix (By similarity).
Mediates cytochrome c efflux (PubMed:20230784).
Catalyzes the scrambling of phospholipids across the outer mitochondrial membrane; the mechanism is unrelated to channel activity and is capable of translocating both anionic and zwitterionic phospholipids.
Catalytic activity
- chloride(in) = chloride(out)
- K+(in) = K+(out)
- ATP(in) = ATP(out)
- Ca2+(in) = Ca2+(out)
- Na+(in) = Na+(out)
- Mg2+(in) = Mg2+(out)
- L-glutamate(out) = L-glutamate(in)
- dopamine(out) = dopamine(in)
- acetylcholine(in) = acetylcholine(out)
- Fe(III)-[cytochrome c](out) = Fe(III)-[cytochrome c](in)
Activity regulation
Inhibited by nitric oxide.
Features
Showing features for binding site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 12 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 20 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Site | 73 | Involved in ceramide and phosphatidylcholine binding. Critical for channel structural stability and gating | ||||
Sequence: E | ||||||
Binding site | 242-244 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: LIG | ||||||
Binding site | 260-264 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: SALLD |
GO annotations
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameNon-selective voltage-gated ion channel VDAC1
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP21796
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Mitochondrion outer membrane ; Multi-pass membrane protein
Cell membrane ; Multi-pass membrane protein
Membrane raft ; Multi-pass membrane protein
Note: Found in a complex with HSPA9 and VDAC1 at the endoplasmic reticulum-mitochondria contact sites.
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 26-35 | Beta stranded | ||||
Sequence: LIKLDLKTKS | ||||||
Transmembrane | 39-47 | Beta stranded | ||||
Sequence: LEFTSSGSA | ||||||
Transmembrane | 54-64 | Beta stranded | ||||
Sequence: VTGSLETKYRW | ||||||
Transmembrane | 69-76 | Beta stranded | ||||
Sequence: LTFTEKWN | ||||||
Transmembrane | 80-89 | Beta stranded | ||||
Sequence: TLGTEITVED | ||||||
Transmembrane | 95-104 | Beta stranded | ||||
Sequence: LKLTFDSSFS | ||||||
Transmembrane | 111-120 | Beta stranded | ||||
Sequence: NAKIKTGYKR | ||||||
Transmembrane | 123-130 | Beta stranded | ||||
Sequence: INLGCDMD | ||||||
Transmembrane | 137-145 | Beta stranded | ||||
Sequence: SIRGALVLG | ||||||
Transmembrane | 150-158 | Beta stranded | ||||
Sequence: LAGYQMNFE | ||||||
Transmembrane | 163-175 | Beta stranded | ||||
Sequence: RVTQSNFAVGYKT | ||||||
Transmembrane | 178-185 | Beta stranded | ||||
Sequence: FQLHTNVN | ||||||
Transmembrane | 189-198 | Beta stranded | ||||
Sequence: EFGGSIYQKV | ||||||
Transmembrane | 202-211 | Beta stranded | ||||
Sequence: LETAVNLAWT | ||||||
Transmembrane | 218-227 | Beta stranded | ||||
Sequence: RFGIAAKYQI | ||||||
Transmembrane | 231-238 | Beta stranded | ||||
Sequence: ACFSAKVN | ||||||
Transmembrane | 242-251 | Beta stranded | ||||
Sequence: LIGLGYTQTL | ||||||
Transmembrane | 254-263 | Beta stranded | ||||
Sequence: GIKLTLSALL | ||||||
Transmembrane | 273-282 | Beta stranded | ||||
Sequence: HKLGLGLEFQ |
Keywords
- Cellular component
Disease & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 12 | PRKN-dependent polybiquitination is decreased, whereas PRKN-dependent monoubiquitination, mitochondrial calcium uptake and apoptosis are unaffected; when associated with R-20; R-53 and 109-R-R-110. | ||||
Sequence: K → R | ||||||
Mutagenesis | 20 | PRKN-dependent polybiquitination is decreased, whereas PRKN-dependent monoubiquitination, mitochondrial calcium uptake and apoptosis are unaffected; when associated with R-12; R-53 and 109-R-R-110. | ||||
Sequence: K → R | ||||||
Mutagenesis | 53 | PRKN-dependent polybiquitination is decreased, whereas PRKN-dependent monoubiquitination, mitochondrial calcium uptake and apoptosis are unaffected; when associated with R-12; R-20 and 109-R-R-110. | ||||
Sequence: K → R | ||||||
Mutagenesis | 73 | Abolishes ceramide and phosphatidylcholine binding. | ||||
Sequence: E → Q | ||||||
Mutagenesis | 109-110 | PRKN-dependent polybiquitination is decreased, whereas PRKN-dependent monoubiquitination, mitochondrial calcium uptake and apoptosis are unaffected; when associated with R-12; R-20 and R-53. | ||||
Sequence: KK → RR | ||||||
Mutagenesis | 193 | Conformation remains open and constitutively allows cytochrome c efflux. | ||||
Sequence: S → A | ||||||
Mutagenesis | 193 | Conformation remains closed and prevents cytochrome c leakage. | ||||
Sequence: S → E | ||||||
Mutagenesis | 274 | Loss of PRKN-dependent monoubiquitination increases mitochondria calcium uptake, and ultimately increased apoptosis. Consequently, mitochondria are swelled with defective cristae structures. PRKN-dependent polyubiquitination is unaffected. | ||||
Sequence: K → R |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 283 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_0000050499 | 2-283 | UniProt | Non-selective voltage-gated ion channel VDAC1 | |||
Sequence: AVPPTYADLGKSARDVFTKGYGFGLIKLDLKTKSENGLEFTSSGSANTETTKVTGSLETKYRWTEYGLTFTEKWNTDNTLGTEITVEDQLARGLKLTFDSSFSPNTGKKNAKIKTGYKREHINLGCDMDFDIAGPSIRGALVLGYEGWLAGYQMNFETAKSRVTQSNFAVGYKTDEFQLHTNVNDGTEFGGSIYQKVNKKLETAVNLAWTAGNSNTRFGIAAKYQIDPDACFSAKVNNSSLIGLGYTQTLKPGIKLTLSALLDGKNVNAGGHKLGLGLEFQA | |||||||
Cross-link | 12 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | |||||||
Modified residue | 13 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 19 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 20 | UniProt | N6-acetyllysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 20 | UniProt | N6-succinyllysine; alternate | ||||
Sequence: K | |||||||
Cross-link | 20 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 35 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 44 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 46 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 53 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 55 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 57 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 61 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | |||||||
Modified residue | 67 | UniProt | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 67 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 98 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 101 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 102 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 104 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 107 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 107 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 109 | UniProt | N6-acetyllysine; alternate | ||||
Sequence: K | |||||||
Cross-link | 109 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate | ||||
Sequence: K | |||||||
Cross-link | 110 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | |||||||
Cross-link | 161 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 165 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 193 | UniProt | Phosphoserine; by NEK1 | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 211 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 215 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 225 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 240 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 240 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 241 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 250 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 252 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue | 266 | UniProt | N6-acetyllysine; alternate | ||||
Sequence: K | |||||||
Cross-link | 266 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate | ||||
Sequence: K | |||||||
Cross-link | 274 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K |
Post-translational modification
Phosphorylation at Ser-193 by NEK1 promotes the closed conformational state preventing excessive mitochondrial membrane permeability and subsequent apoptotic cell death after injury (PubMed:20230784).
Phosphorylation by the AKT-GSK3B axis stabilizes the protein probably by preventing ubiquitin-mediated proteasomal degradation
Phosphorylation by the AKT-GSK3B axis stabilizes the protein probably by preventing ubiquitin-mediated proteasomal degradation
Ubiquitinated (PubMed:25621951, PubMed:32047033).
Undergoes monoubiquitination and polyubiquitination by PRKN; monoubiquitination at Lys-274 inhibits apoptosis, whereas polyubiquitination leads to its degradation and promotes mitophagy (PubMed:25621951, PubMed:32047033).
Deubiquitinated by USP30 (PubMed:25621951).
Undergoes monoubiquitination and polyubiquitination by PRKN; monoubiquitination at Lys-274 inhibits apoptosis, whereas polyubiquitination leads to its degradation and promotes mitophagy (PubMed:25621951, PubMed:32047033).
Deubiquitinated by USP30 (PubMed:25621951).
Keywords
- PTM
Proteomic databases
2D gel databases
PTM databases
Interaction
Subunit
Homodimer and homotrimer; in response to cyclic AMP or calcium; oligomerization is required for scramblase activity (PubMed:30061676, PubMed:38065946).
Component of the mitochondrial permeability transition pore complex (mPTPC), at least composed of SPG7, VDAC1 and PPIF (PubMed:26387735).
Interacts with SPG7, NIPSNAP2 and SLC25A30 (PubMed:26387735).
Interacts with hexokinases including HK1 (PubMed:22304920, PubMed:8420959).
The HK1-VDAC1 complex interacts with ATF2 (PubMed:22304920).
Interacts with BCL2L1 (PubMed:18755977, PubMed:25296756).
Interacts with BAK1 (PubMed:25296756).
Interacts with RTL10/BOP (via BH3 domain) (PubMed:23055042).
Interacts with amyloid-beta and APP; induces VDAC1 dephosphorylation (PubMed:25168729).
Interacts with TMEM41B (PubMed:30352685).
Interacts with BCAP31 (PubMed:31206022).
Interacts with HSPA9; this interaction couples ITPR1 to VDAC1 (By similarity).
Component of the mitochondrial permeability transition pore complex (mPTPC), at least composed of SPG7, VDAC1 and PPIF (PubMed:26387735).
Interacts with SPG7, NIPSNAP2 and SLC25A30 (PubMed:26387735).
Interacts with hexokinases including HK1 (PubMed:22304920, PubMed:8420959).
The HK1-VDAC1 complex interacts with ATF2 (PubMed:22304920).
Interacts with BCL2L1 (PubMed:18755977, PubMed:25296756).
Interacts with BAK1 (PubMed:25296756).
Interacts with RTL10/BOP (via BH3 domain) (PubMed:23055042).
Interacts with amyloid-beta and APP; induces VDAC1 dephosphorylation (PubMed:25168729).
Interacts with TMEM41B (PubMed:30352685).
Interacts with BCAP31 (PubMed:31206022).
Interacts with HSPA9; this interaction couples ITPR1 to VDAC1 (By similarity).
(Microbial infection) Interacts with influenza A virus PB1-F2 protein.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P21796 | APOE P02649 | 2 | EBI-354158, EBI-1222467 | |
BINARY | P21796 | CDK1 P06493 | 3 | EBI-354158, EBI-444308 | |
BINARY | P21796 | HK1 P19367 | 3 | EBI-354158, EBI-713162 | |
BINARY | P21796 | LRRK2 Q5S007 | 3 | EBI-354158, EBI-5323863 | |
XENO | P21796 | PB1 P0C0U1 | 4 | EBI-354158, EBI-12579807 | |
BINARY | P21796 | PRDX6 P30041 | 3 | EBI-354158, EBI-2255129 | |
BINARY | P21796 | RTL10 Q7L3V2 | 2 | EBI-354158, EBI-10697720 | |
BINARY | P21796 | SLC25A6 P12236 | 4 | EBI-354158, EBI-356254 | |
BINARY | P21796 | VDAC1 P21796 | 4 | EBI-354158, EBI-354158 | |
BINARY | P21796 | VDAC2 P45880 | 6 | EBI-354158, EBI-354022 | |
BINARY | P21796 | VDAC3 Q9Y277 | 4 | EBI-354158, EBI-354196 | |
BINARY | P21796 | YWHAE P62258 | 5 | EBI-354158, EBI-356498 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Domain
Consists mainly of a membrane-spanning beta-barrel formed by 19 beta-strands (PubMed:18755977, PubMed:18832158).
The helical N-terminus folds back into the pore opening and plays a role in voltage-gated channel activity (PubMed:18755977, PubMed:18832158).
The helical N-terminus folds back into the pore opening and plays a role in voltage-gated channel activity (PubMed:18755977, PubMed:18832158).
Sequence similarities
Belongs to the eukaryotic mitochondrial porin family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length283
- Mass (Da)30,773
- Last updated2007-01-23 v2
- Checksum89BA3378B04020D5
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
C9JI87 | C9JI87_HUMAN | VDAC1 | 183 |
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 225 | in Ref. 4; CAB58127 | ||||
Sequence: Y → L |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
L06132 EMBL· GenBank· DDBJ | AAA61272.1 EMBL· GenBank· DDBJ | mRNA | ||
AJ250032 EMBL· GenBank· DDBJ | CAB58127.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ250033 EMBL· GenBank· DDBJ | CAB58127.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ250034 EMBL· GenBank· DDBJ | CAB58127.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ250035 EMBL· GenBank· DDBJ | CAB58127.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ250036 EMBL· GenBank· DDBJ | CAB58127.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ250037 EMBL· GenBank· DDBJ | CAB58127.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ250038 EMBL· GenBank· DDBJ | CAB58127.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ250039 EMBL· GenBank· DDBJ | CAB58127.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF151097 EMBL· GenBank· DDBJ | AAD54939.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF151093 EMBL· GenBank· DDBJ | AAD54939.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF151094 EMBL· GenBank· DDBJ | AAD54939.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF151095 EMBL· GenBank· DDBJ | AAD54939.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF151096 EMBL· GenBank· DDBJ | AAD54939.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AC005200 EMBL· GenBank· DDBJ | AAC24723.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AK122953 EMBL· GenBank· DDBJ | BAG53816.1 EMBL· GenBank· DDBJ | mRNA | ||
AC008608 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471062 EMBL· GenBank· DDBJ | EAW62281.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471062 EMBL· GenBank· DDBJ | EAW62282.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471062 EMBL· GenBank· DDBJ | EAW62283.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471062 EMBL· GenBank· DDBJ | EAW62285.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471062 EMBL· GenBank· DDBJ | EAW62286.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC008482 EMBL· GenBank· DDBJ | AAH08482.1 EMBL· GenBank· DDBJ | mRNA | ||
BC071168 EMBL· GenBank· DDBJ | AAH71168.1 EMBL· GenBank· DDBJ | mRNA | ||
BC090042 EMBL· GenBank· DDBJ | AAH90042.1 EMBL· GenBank· DDBJ | mRNA |