P08559 · ODPA_HUMAN
- ProteinPyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial
- GenePDHA1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids390 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2, and thereby links the glycolytic pathway to the tricarboxylic cycle.
Catalytic activity
- H+ + N6-[(R)-lipoyl]-L-lysyl-[dihydrolipoyllysine-residue acetyltransferase] + pyruvate = CO2 + N6-[(R)-S8-acetyldihydrolipoyl]-L-lysyl-[dihydrolipoyllysine-residue acetyltransferase]
Cofactor
Mg2+ (UniProtKB | Rhea| CHEBI:18420 )
Activity regulation
Pyruvate dehydrogenase activity is inhibited by phosphorylation of PDHA1; it is reactivated by dephosphorylation.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
41 μM | pyruvate |
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 92 | pyruvate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 118 | pyruvate (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 118 | thiamine diphosphate (UniProtKB | ChEBI); ligand shared with beta subunit | ||||
Sequence: Y | ||||||
Binding site | 119 | pyruvate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 119 | thiamine diphosphate (UniProtKB | ChEBI); ligand shared with beta subunit | ||||
Sequence: R | ||||||
Binding site | 157 | pyruvate (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 165 | pyruvate (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 165 | thiamine diphosphate (UniProtKB | ChEBI); ligand shared with beta subunit | ||||
Sequence: G | ||||||
Binding site | 167 | pyruvate (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Binding site | 167 | thiamine diphosphate (UniProtKB | ChEBI); ligand shared with beta subunit | ||||
Sequence: V | ||||||
Binding site | 196 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 196 | pyruvate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 196 | thiamine diphosphate (UniProtKB | ChEBI); ligand shared with beta subunit | ||||
Sequence: D | ||||||
Binding site | 197 | pyruvate (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 197 | thiamine diphosphate (UniProtKB | ChEBI); ligand shared with beta subunit | ||||
Sequence: G | ||||||
Binding site | 198 | pyruvate (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 198 | thiamine diphosphate (UniProtKB | ChEBI); ligand shared with beta subunit | ||||
Sequence: A | ||||||
Binding site | 225 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 225 | pyruvate (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 225 | thiamine diphosphate (UniProtKB | ChEBI); ligand shared with beta subunit | ||||
Sequence: N | ||||||
Binding site | 227 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 227 | pyruvate (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 292 | thiamine diphosphate (UniProtKB | ChEBI); ligand shared with beta subunit | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | mitochondrial matrix | |
Cellular Component | mitochondrion | |
Cellular Component | nucleolus | |
Cellular Component | nucleus | |
Cellular Component | pyruvate dehydrogenase complex | |
Molecular Function | pyruvate dehydrogenase (acetyl-transferring) activity | |
Molecular Function | pyruvate dehydrogenase (NAD+) activity | |
Biological Process | acetyl-CoA biosynthetic process from pyruvate | |
Biological Process | glucose metabolic process | |
Biological Process | tricarboxylic acid cycle |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP08559
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Involvement in disease
Pyruvate dehydrogenase E1-alpha deficiency (PDHAD)
- Note
- DescriptionAn enzymatic defect causing primary lactic acidosis in children. It is associated with a broad clinical spectrum ranging from fatal lactic acidosis in the newborn to chronic neurologic dysfunction with structural abnormalities in the central nervous system without systemic acidosis.
- See alsoMIM:312170
Natural variants in PDHAD
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_010238 | 10 | R>P | in PDHAD; affects mitochondrial import of precursor protein; dbSNP:rs137853257 | |
VAR_004949 | 72 | R>C | in PDHAD; dbSNP:rs863224148 | |
VAR_004950 | 113 | H>D | in PDHAD | |
VAR_004951 | 162 | G>R | in PDHAD; dbSNP:rs866868610 | |
VAR_004952 | 167 | V>M | in PDHAD; disrupts magnesium binding and results in deficient activity of the pyruvate dehydrogenase complex; dbSNP:rs2063174067 | |
VAR_004953 | 199 | A>T | in PDHAD | |
VAR_004954 | 205 | F>L | in PDHAD; dbSNP:rs137853254 | |
VAR_004955 | 210 | M>V | in PDHAD; dbSNP:rs794727843 | |
VAR_004956 | 217 | P>L | in PDHAD; dbSNP:rs1131691792 | |
VAR_004957 | 231 | T>A | in PDHAD | |
VAR_021053 | 243 | Y>N | in PDHAD; dbSNP:rs137853255 | |
VAR_004958 | 258 | D>A | in PDHAD; dbSNP:rs137853253 | |
VAR_004959 | 263 | R>G | in PDHAD; dbSNP:rs137853259 | |
VAR_004960 | 263 | R>Q | in PDHAD | |
VAR_021055 | 288 | R>H | in PDHAD; dbSNP:rs137853258 | |
VAR_004961 | 292 | H>L | in PDHAD | |
VAR_004962 | 302 | R>C | in PDHAD; loss of activity; common mutation; dbSNP:rs137853252 | |
VAR_004963 | 302 | R>H | in PDHAD; dbSNP:rs1064794149 | |
VAR_020908 | 305 | E>EDSYRTRE | in PDHAD | |
VAR_020909 | 307 | I>IPPHSYRTREEI | in PDHAD | |
VAR_004964 | 311 | missing | in PDHAD | |
VAR_004965 | 313 | missing | in PDHAD; dbSNP:rs137853251 | |
VAR_021056 | 315 | D>N | in PDHAD; dbSNP:rs137853256 | |
VAR_004966 | 378 | R>H | in PDHAD; dbSNP:rs137853250 |
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_010238 | 10 | in PDHAD; affects mitochondrial import of precursor protein; dbSNP:rs137853257 | |||
Sequence: R → P | ||||||
Natural variant | VAR_004949 | 72 | in PDHAD; dbSNP:rs863224148 | |||
Sequence: R → C | ||||||
Natural variant | VAR_004950 | 113 | in PDHAD | |||
Sequence: H → D | ||||||
Natural variant | VAR_069381 | 136 | found in a patient with moderate developmental delay, mild dysmorphism and mildly elevated serum lactate; uncertain significance; dbSNP:rs138727886 | |||
Sequence: A → T | ||||||
Natural variant | VAR_004951 | 162 | in PDHAD; dbSNP:rs866868610 | |||
Sequence: G → R | ||||||
Natural variant | VAR_004952 | 167 | in PDHAD; disrupts magnesium binding and results in deficient activity of the pyruvate dehydrogenase complex; dbSNP:rs2063174067 | |||
Sequence: V → M | ||||||
Natural variant | VAR_004953 | 199 | in PDHAD | |||
Sequence: A → T | ||||||
Natural variant | VAR_004954 | 205 | in PDHAD; dbSNP:rs137853254 | |||
Sequence: F → L | ||||||
Natural variant | VAR_004955 | 210 | in PDHAD; dbSNP:rs794727843 | |||
Sequence: M → V | ||||||
Natural variant | VAR_004956 | 217 | in PDHAD; dbSNP:rs1131691792 | |||
Sequence: P → L | ||||||
Natural variant | VAR_004957 | 231 | in PDHAD | |||
Sequence: T → A | ||||||
Mutagenesis | 232 | Abolishes inactivation by phosphorylation; when associated with A-293 and A-300. | ||||
Sequence: S → A | ||||||
Natural variant | VAR_021053 | 243 | in PDHAD; dbSNP:rs137853255 | |||
Sequence: Y → N | ||||||
Natural variant | VAR_004958 | 258 | in PDHAD; dbSNP:rs137853253 | |||
Sequence: D → A | ||||||
Natural variant | VAR_004959 | 263 | in PDHAD; dbSNP:rs137853259 | |||
Sequence: R → G | ||||||
Natural variant | VAR_004960 | 263 | in PDHAD | |||
Sequence: R → Q | ||||||
Natural variant | VAR_021054 | 282 | in dbSNP:rs2229137 | |||
Sequence: M → L | ||||||
Natural variant | VAR_021055 | 288 | in PDHAD; dbSNP:rs137853258 | |||
Sequence: R → H | ||||||
Natural variant | VAR_004961 | 292 | in PDHAD | |||
Sequence: H → L | ||||||
Mutagenesis | 293 | Reduces enzyme activity. Abolishes inactivation by phosphorylation; when associated with A-232 and A-300. | ||||
Sequence: S → A | ||||||
Mutagenesis | 293 | Interferes with substrate binding. | ||||
Sequence: S → E | ||||||
Mutagenesis | 300 | Abolishes inactivation by phosphorylation; when associated with A-232 and A-293. | ||||
Sequence: S → A | ||||||
Natural variant | VAR_004962 | 302 | in PDHAD; loss of activity; common mutation; dbSNP:rs137853252 | |||
Sequence: R → C | ||||||
Natural variant | VAR_004963 | 302 | in PDHAD; dbSNP:rs1064794149 | |||
Sequence: R → H | ||||||
Natural variant | VAR_020908 | 305 | in PDHAD | |||
Sequence: E → EDSYRTRE | ||||||
Natural variant | VAR_020909 | 307 | in PDHAD | |||
Sequence: I → IPPHSYRTREEI | ||||||
Natural variant | VAR_004964 | 311 | in PDHAD | |||
Sequence: Missing | ||||||
Natural variant | VAR_004965 | 313 | in PDHAD; dbSNP:rs137853251 | |||
Sequence: Missing | ||||||
Natural variant | VAR_021056 | 315 | in PDHAD; dbSNP:rs137853256 | |||
Sequence: D → N | ||||||
Natural variant | VAR_050436 | 333 | in dbSNP:rs2228067 | |||
Sequence: E → D | ||||||
Natural variant | VAR_004966 | 378 | in PDHAD; dbSNP:rs137853250 | |||
Sequence: R → H |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 404 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for transit peptide, chain, modified residue, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Transit peptide | 1-29 | UniProt | Mitochondrion | ||||
Sequence: MRKMLAAVSRVLSGASQKPASRVLVASRN | |||||||
Chain | PRO_0000020440 | 30-390 | UniProt | Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial | |||
Sequence: FANDATFEIKKCDLHRLEEGPPVTTVLTREDGLKYYRMMQTVRRMELKADQLYKQKIIRGFCHLCDGQEACCVGLEAGINPTDHLITAYRAHGFTFTRGLSVREILAELTGRKGGCAKGKGGSMHMYAKNFYGGNGIVGAQVPLGAGIALACKYNGKDEVCLTLYGDGAANQGQIFEAYNMAALWKLPCIFICENNRYGMGTSVERAAASTDYYKRGDFIPGLRVDGMDILCVREATRFAAAYCRSGKGPILMELQTYRYHGHSMSDPGVSYRTREEIQEVRSKSDPIMLLKDRMVNSNLASVEELKEIDVEVRKEIEDAAQFATADPEPPLEELGYHIYSSDPPFEVRGANQWIKFKSVS | |||||||
Modified residue | 63 | UniProt | N6-acetyllysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 63 | UniProt | N6-succinyllysine; alternate | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 231 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 232 | UniProt | Phosphoserine; by PDK1 | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 232 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 244 | UniProt | N6-acetyllysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 244 | UniProt | N6-succinyllysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 277 | UniProt | N6-succinyllysine | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 289 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 293 | UniProt | Phosphoserine; by PDK1, PDK2, PDK3 and PDK4 | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 293 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 295 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 295 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 300 | UniProt | Phosphoserine; by PDK1, PDK2, PDK3 and PDK4 | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 300 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 301 | UniProt | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 301 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 303 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 312 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 313 | UniProt | N6-acetyllysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 313 | UniProt | N6-succinyllysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 321 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue | 336 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 366 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 385 | UniProt | N6-succinyllysine | ||||
Sequence: K |
Post-translational modification
Phosphorylation at Ser-232, Ser-293 and Ser-300 by PDK family kinases inactivates the enzyme; for this phosphorylation at a single site is sufficient. Dephosphorylation at all three sites, i.e. at Ser-232, Ser-293 and Ser-300, is required for reactivation.
Acetylation alters the phosphorylation pattern. Deacetylated by SIRT3 (By similarity).
Keywords
- PTM
Proteomic databases
2D gel databases
PTM databases
Expression
Tissue specificity
Ubiquitous.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Heterotetramer of two PDHA1 and two PDHB subunits. The heterotetramer interacts with DLAT, and is part of the multimeric pyruvate dehydrogenase complex that contains multiple copies of pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (DLAT, E2) and lipoamide dehydrogenase (DLD, E3). These subunits are bound to an inner core composed of about 48 DLAT and 12 PDHX molecules.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P08559 | CFTR P13569 | 5 | EBI-715747, EBI-349854 | |
BINARY | P08559 | IMMT Q16891 | 4 | EBI-715747, EBI-473801 | |
BINARY | P08559 | PDHB P11177 | 5 | EBI-715747, EBI-1035872 | |
BINARY | P08559 | PDK1 Q15118 | 2 | EBI-715747, EBI-7016221 | |
BINARY | P08559-1 | PDHB P11177-1 | 4 | EBI-25766512, EBI-25766519 |
Protein-protein interaction databases
Miscellaneous
Structure
Sequence & Isoforms
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
This entry describes 4 isoforms produced by Alternative splicing.
P08559-1
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.
- Name1
- Length390
- Mass (Da)43,296
- Last updated1992-05-01 v3
- Checksum4D685BBE44A92D4B
P08559-2
- Name2
- Differences from canonical
- 96-96: G → GQFLLPLT
P08559-3
- Name3
- Differences from canonical
- 170-200: Missing
P08559-4
- Name4
- Differences from canonical
- 19-19: P → PRHGLATLPSLVSISRLKQSSHLGLPKCWDYSHSLKTRQ
Computationally mapped potential isoform sequences
There are 6 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
Q5JPU0 | Q5JPU0_HUMAN | PDHA1 | 180 | ||
Q5JPU1 | Q5JPU1_HUMAN | PDHA1 | 205 | ||
Q5JPU2 | Q5JPU2_HUMAN | PDHA1 | 418 | ||
Q5JPT9 | Q5JPT9_HUMAN | PDHA1 | 203 | ||
A0A8Q3WLI8 | A0A8Q3WLI8_HUMAN | PDHA1 | 150 | ||
A0A8Q3WLK5 | A0A8Q3WLK5_HUMAN | PDHA1 | 160 |
Sequence caution
Features
Showing features for alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_043363 | 19 | in isoform 4 | |||
Sequence: P → PRHGLATLPSLVSISRLKQSSHLGLPKCWDYSHSLKTRQ | ||||||
Alternative sequence | VSP_042569 | 96 | in isoform 2 | |||
Sequence: G → GQFLLPLT | ||||||
Alternative sequence | VSP_042570 | 170-200 | in isoform 3 | |||
Sequence: Missing | ||||||
Sequence conflict | 278 | in Ref. 9; BAG35194 | ||||
Sequence: G → E | ||||||
Sequence conflict | 301 | in Ref. 15; AAD23857 | ||||
Sequence: Y → S | ||||||
Sequence conflict | 306 | in Ref. 15; AAD23857 | ||||
Sequence: E → D | ||||||
Sequence conflict | 349 | in Ref. 6; AAA60055 | ||||
Sequence: A → P | ||||||
Sequence conflict | 354 | in Ref. 6; AAA60055 | ||||
Sequence: T → A |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
D90084 EMBL· GenBank· DDBJ | BAA14121.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M24848 EMBL· GenBank· DDBJ | AAA36533.1 EMBL· GenBank· DDBJ | mRNA | ||
X52709 EMBL· GenBank· DDBJ | CAA36933.1 EMBL· GenBank· DDBJ | mRNA | ||
X52710 EMBL· GenBank· DDBJ | CAA36934.1 EMBL· GenBank· DDBJ | mRNA | ||
M27257 EMBL· GenBank· DDBJ | AAA60051.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M29155 EMBL· GenBank· DDBJ | AAA60051.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M29156 EMBL· GenBank· DDBJ | AAA60051.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M29157 EMBL· GenBank· DDBJ | AAA60051.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M29158 EMBL· GenBank· DDBJ | AAA60051.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M29159 EMBL· GenBank· DDBJ | AAA60051.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M29160 EMBL· GenBank· DDBJ | AAA60051.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M29161 EMBL· GenBank· DDBJ | AAA60051.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M29162 EMBL· GenBank· DDBJ | AAA60051.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M29163 EMBL· GenBank· DDBJ | AAA60051.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M29164 EMBL· GenBank· DDBJ | AAA60051.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
L13318 EMBL· GenBank· DDBJ | AAA60227.1 EMBL· GenBank· DDBJ | mRNA | ||
J03503 EMBL· GenBank· DDBJ | AAA60055.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
J03575 EMBL· GenBank· DDBJ | AAA60050.1 EMBL· GenBank· DDBJ | mRNA | ||
L48690 EMBL· GenBank· DDBJ | AAB59581.1 EMBL· GenBank· DDBJ | mRNA | Frameshift | |
EF590117 EMBL· GenBank· DDBJ | ABQ59099.1 EMBL· GenBank· DDBJ | mRNA | ||
AK293250 EMBL· GenBank· DDBJ | BAH11476.1 EMBL· GenBank· DDBJ | mRNA | ||
AK296457 EMBL· GenBank· DDBJ | BAH12361.1 EMBL· GenBank· DDBJ | mRNA | ||
AK312263 EMBL· GenBank· DDBJ | BAG35194.1 EMBL· GenBank· DDBJ | mRNA | ||
AK296341 EMBL· GenBank· DDBJ | BAH12323.1 EMBL· GenBank· DDBJ | mRNA | ||
AK222740 EMBL· GenBank· DDBJ | BAD96460.1 EMBL· GenBank· DDBJ | mRNA | ||
AL732326 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471074 EMBL· GenBank· DDBJ | EAW98960.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC002406 EMBL· GenBank· DDBJ | AAH02406.1 EMBL· GenBank· DDBJ | mRNA | ||
AF125053 EMBL· GenBank· DDBJ | AAD23841.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF125054 EMBL· GenBank· DDBJ | AAD23842.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF125055 EMBL· GenBank· DDBJ | AAD23843.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF125056 EMBL· GenBank· DDBJ | AAD23844.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF125057 EMBL· GenBank· DDBJ | AAD23845.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF125058 EMBL· GenBank· DDBJ | AAD23846.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF125059 EMBL· GenBank· DDBJ | AAD23847.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF125060 EMBL· GenBank· DDBJ | AAD23848.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF125061 EMBL· GenBank· DDBJ | AAD23849.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF125062 EMBL· GenBank· DDBJ | AAD23850.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF125063 EMBL· GenBank· DDBJ | AAD23851.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF125064 EMBL· GenBank· DDBJ | AAD23852.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF125065 EMBL· GenBank· DDBJ | AAD23853.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF125066 EMBL· GenBank· DDBJ | AAD23854.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF125067 EMBL· GenBank· DDBJ | AAD23855.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF125068 EMBL· GenBank· DDBJ | AAD23856.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF125069 EMBL· GenBank· DDBJ | AAD23857.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF125070 EMBL· GenBank· DDBJ | AAD23858.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF125071 EMBL· GenBank· DDBJ | AAD23859.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF125072 EMBL· GenBank· DDBJ | AAD23860.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF125073 EMBL· GenBank· DDBJ | AAD23861.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF125074 EMBL· GenBank· DDBJ | AAD23862.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF125075 EMBL· GenBank· DDBJ | AAD23863.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF125076 EMBL· GenBank· DDBJ | AAD23864.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF125078 EMBL· GenBank· DDBJ | AAD23866.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF125079 EMBL· GenBank· DDBJ | AAD23867.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF125080 EMBL· GenBank· DDBJ | AAD23868.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF125081 EMBL· GenBank· DDBJ | AAD23869.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF125082 EMBL· GenBank· DDBJ | AAD23870.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF125083 EMBL· GenBank· DDBJ | AAD23871.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF125084 EMBL· GenBank· DDBJ | AAD23872.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF125085 EMBL· GenBank· DDBJ | AAD23873.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF125086 EMBL· GenBank· DDBJ | AAD23874.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF125087 EMBL· GenBank· DDBJ | AAD23875.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF125088 EMBL· GenBank· DDBJ | AAD23876.1 EMBL· GenBank· DDBJ | Genomic DNA |