O76083 · PDE9A_HUMAN
- ProteinHigh affinity cGMP-specific 3',5'-cyclic phosphodiesterase 9A
- GenePDE9A
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids593 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Specifically hydrolyzes the second messenger cGMP, which is a key regulator of many important physiological processes. Highly specific: compared to other members of the cyclic nucleotide phosphodiesterase family, has the highest affinity and selectivity for cGMP (PubMed:18757755, PubMed:21483814, PubMed:9624146).
Specifically regulates natriuretic-peptide-dependent cGMP signaling in heart, acting as a regulator of cardiac hypertrophy in myocytes and muscle. Does not regulate nitric oxide-dependent cGMP in heart (PubMed:25799991).
Additional experiments are required to confirm whether its ability to hydrolyze natriuretic-peptide-dependent cGMP is specific to heart or is a general feature of the protein (Probable). In brain, involved in cognitive function, such as learning and long-term memory (By similarity).
Specifically regulates natriuretic-peptide-dependent cGMP signaling in heart, acting as a regulator of cardiac hypertrophy in myocytes and muscle. Does not regulate nitric oxide-dependent cGMP in heart (PubMed:25799991).
Additional experiments are required to confirm whether its ability to hydrolyze natriuretic-peptide-dependent cGMP is specific to heart or is a general feature of the protein (Probable). In brain, involved in cognitive function, such as learning and long-term memory (By similarity).
Miscellaneous
PDE9A is a potential target for treatment of diseases such as stress-induced heart disease or long-term memory defects. Specific inhibitors, such as BAY-73-6691 or PF-4449613 are promising candidates for clinical tests.
N-(4-methoxyphenyl)-N~2~-[1-(2-methylphenyl)-4-oxo-4,5-dihydro-1H-pyrazolo[3,4-d]pyrimidin-6-yl]-L-alaninamide correspond to compound 28.
Catalytic activity
- 3',5'-cyclic GMP + H2O = GMP + H+
Cofactor
Protein has several cofactor binding sites:
Note: Binds 1 Zn2+ ion per subunit. Binds 2 divalent metal cations per subunit: site 1 preferentially binds zinc, while site 2 has a preference for magnesium. Tightly binds zinc.
Note: Binds 1 Mg2+ ions per subunit. Binds 2 divalent metal cations per subunit: site 1 preferentially binds zinc, while site 2 has a preference for magnesium. Binds magnesium less tightly than zinc.
Activity regulation
Inhibited by zaprinast; inhibitor is however not specific to PDE9A (PubMed:9624146).
Specifically inhibited by BAY-73-6691 (1-(2-chlorophenyl)-6-((2R)-3,3,3- trifluoro-2-methylpropyl)-1,5-dihydro-4H-pyrazolo(3,4-d)pyrimidine-4-one) (PubMed:16150925).
BAY-73-9961 has two enantiomers, (R) and (S), due to the presence of a chiral center, and both forms vary in their pattern of interaction (PubMed:20121115, PubMed:21483814).
Specifically inhibited by PF-4181366 (4H-Pyrazolo[3,4-d]pyrimidin-4-one, 1- cyclopentyl-1,5-dihydro-6-[(3S,4S)-4-methyl- 1-(6-quinoxalinylmethyl)-3-pyrrolidinyl]-one) (PubMed:19919087).
Specifically inhibited by PF-4449613 ((R)-6-(1-(3-phenoxyazetidin-1-yl)ethyl)-1-(tetrahydro-2H-pyran-4-yl)-1H-pyrazolo[3,4-d]pyrimidin- 4(5H)-one) (PubMed:25799991).
Specifically inhibited by inhibitor 28 (2-((1-(2-Chlorophenyl)-4-hydroxy-1Hpyrazolo[ 3,4-d]pyrimidin-6-yl)amino)-N-(4- methoxyphenyl)propanamide): inhibitor forms a hydrogen bond with Tyr-484 and Gln-513 (PubMed:22985069).
Specifically inhibited by 1-Cyclopentyl-6-[(1r)-1-(3-phenoxyazetidin- 1-Yl)ethyl]-1,5-dihydro-4h-pyrazolo[3,4-D] pyrimidin-4-one: inhibitor forms a hydrogen bond with Tyr-484 and Gln-513 (PubMed:23025719).
Specifically inhibited by BAY-73-6691 (1-(2-chlorophenyl)-6-((2R)-3,3,3- trifluoro-2-methylpropyl)-1,5-dihydro-4H-pyrazolo(3,4-d)pyrimidine-4-one) (PubMed:16150925).
BAY-73-9961 has two enantiomers, (R) and (S), due to the presence of a chiral center, and both forms vary in their pattern of interaction (PubMed:20121115, PubMed:21483814).
Specifically inhibited by PF-4181366 (4H-Pyrazolo[3,4-d]pyrimidin-4-one, 1- cyclopentyl-1,5-dihydro-6-[(3S,4S)-4-methyl- 1-(6-quinoxalinylmethyl)-3-pyrrolidinyl]-one) (PubMed:19919087).
Specifically inhibited by PF-4449613 ((R)-6-(1-(3-phenoxyazetidin-1-yl)ethyl)-1-(tetrahydro-2H-pyran-4-yl)-1H-pyrazolo[3,4-d]pyrimidin- 4(5H)-one) (PubMed:25799991).
Specifically inhibited by inhibitor 28 (2-((1-(2-Chlorophenyl)-4-hydroxy-1Hpyrazolo[ 3,4-d]pyrimidin-6-yl)amino)-N-(4- methoxyphenyl)propanamide): inhibitor forms a hydrogen bond with Tyr-484 and Gln-513 (PubMed:22985069).
Specifically inhibited by 1-Cyclopentyl-6-[(1r)-1-(3-phenoxyazetidin- 1-Yl)ethyl]-1,5-dihydro-4h-pyrazolo[3,4-D] pyrimidin-4-one: inhibitor forms a hydrogen bond with Tyr-484 and Gln-513 (PubMed:23025719).
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
0.113 μM | cGMP | |||||
501 μM | cAMP |
Vmax | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|
0.285 μmol/min/mg | with cGMP as substrate | ||||
3.7 μmol/min/mg | with cAMP as substrate |
kcat is 0.18 sec-1 for cGMP. kcat is 2.37 sec-1 for cAMP.
Pathway
Purine metabolism; 3',5'-cyclic GMP degradation; GMP from 3',5'-cyclic GMP: step 1/1.
Features
Showing features for active site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 312 | Proton donor | ||||
Sequence: H | ||||||
Binding site | 312-316 | 3',5'-cyclic GMP (UniProtKB | ChEBI) | ||||
Sequence: HNFRH | ||||||
Binding site | 316 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 352 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 353 | 3',5'-cyclic GMP (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 353 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 353 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 462 | 3',5'-cyclic GMP (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 462 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 484 | 3',5'-cyclic GMP (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 512-513 | 3',5'-cyclic GMP (UniProtKB | ChEBI) | ||||
Sequence: AQ |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | endoplasmic reticulum | |
Cellular Component | Golgi apparatus | |
Cellular Component | nucleoplasm | |
Cellular Component | perikaryon | |
Cellular Component | perinuclear region of cytoplasm | |
Cellular Component | plasma membrane | |
Cellular Component | ruffle membrane | |
Cellular Component | sarcolemma | |
Molecular Function | 3',5'-cyclic-AMP phosphodiesterase activity | |
Molecular Function | 3',5'-cyclic-GMP phosphodiesterase activity | |
Molecular Function | 3',5'-cyclic-nucleotide phosphodiesterase activity | |
Molecular Function | identical protein binding | |
Molecular Function | metal ion binding | |
Biological Process | cAMP-mediated signaling | |
Biological Process | cGMP catabolic process | |
Biological Process | cGMP metabolic process | |
Biological Process | negative regulation of neural precursor cell proliferation | |
Biological Process | positive regulation of cardiac muscle hypertrophy | |
Biological Process | positive regulation of long-term synaptic potentiation | |
Biological Process | signal transduction |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameHigh affinity cGMP-specific 3',5'-cyclic phosphodiesterase 9A
- EC number
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionO76083
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Isoform PDE9A1
Isoform PDE9A2
Isoform PDE9A3
Isoform PDE9A17
Keywords
- Cellular component
Disease & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 312 | Completely abolishes catalytic activity. | ||||
Sequence: H → A | ||||||
Mutagenesis | 356 | Reduces catalytic activity, but has no effect on substrate affinity. | ||||
Sequence: H → A | ||||||
Mutagenesis | 425 | Induces a 2 fold change in inhibitory sensitivity by BAY-73-9961. | ||||
Sequence: M → A | ||||||
Mutagenesis | 463 | Induces a 6-9 fold change in inhibitory sensitivity by BAY-73-9961. | ||||
Sequence: I → A | ||||||
Mutagenesis | 466 | Decreased affinity and catalytic activity for cGMP and cAMP. | ||||
Sequence: E → A | ||||||
Mutagenesis | 480 | Induces a 6-9 fold change in inhibitory sensitivity by BAY-73-9961. | ||||
Sequence: L → A | ||||||
Mutagenesis | 484 | Induces a 6-9 fold change in inhibitory sensitivity by BAY-73-9961. | ||||
Sequence: Y → A | ||||||
Mutagenesis | 501 | Induces a 2 fold change in inhibitory sensitivity by BAY-73-9961. | ||||
Sequence: F → A | ||||||
Mutagenesis | 513 | Induces a dramatic change in inhibitory sensitivity by BAY-73-9961. | ||||
Sequence: Q → A | ||||||
Mutagenesis | 513 | 2 fold decreased affinity and catalytic activity for cGMP. 8 fold decreased catalytic activity for cAMP without affecting the affinity for cAMP. | ||||
Sequence: Q → E | ||||||
Mutagenesis | 516 | Induces a dramatic change in inhibitory sensitivity by BAY-73-9961. | ||||
Sequence: F → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 647 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 chain, modified residue, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000198841 | 1-593 | UniProt | High affinity cGMP-specific 3',5'-cyclic phosphodiesterase 9A | |||
Sequence: MGSGSSSYRPKAIYLDIDGRIQKVIFSKYCNSSDIMDLFCIATGLPRNTTISLLTTDDAMVSIDPTMPANSERTPYKVRPVAIKQLSAGVEDKRTTSRGQSAERPLRDRRVVGLEQPRREGAFESGQVEPRPREPQGCYQEGQRIPPEREELIQSVLAQVAEQFSRAFKINELKAEVANHLAVLEKRVELEGLKVVEIEKCKSDIKKMREELAARSSRTNCPCKYSFLDNHKKLTPRRDVPTYPKYLLSPETIEALRKPTFDVWLWEPNEMLSCLEHMYHDLGLVRDFSINPVTLRRWLFCVHDNYRNNPFHNFRHCFCVAQMMYSMVWLCSLQEKFSQTDILILMTAAICHDLDHPGYNNTYQINARTELAVRYNDISPLENHHCAVAFQILAEPECNIFSNIPPDGFKQIRQGMITLILATDMARHAEIMDSFKEKMENFDYSNEEHMTLLKMILIKCCDISNEVRPMEVAEPWVDCLLEEYFMQSDREKSEGLPVAPFMDRDKVTKATAQIGFIKFVLIPMFETVTKLFPMVEEIMLQPLWESRDRYEELKRIDDAMKELQKKTDSLTSGATEKSRERSRDVKNSEGDCA | |||||||
Modified residue | 379 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 569 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in all tissues examined (testis, brain, small intestine, skeletal muscle, heart, lung, thymus, spleen, placenta, kidney, liver, pancreas, ovary and prostate) except blood (PubMed:9624146).
Highest levels in brain, heart, kidney, spleen, prostate and colon. Isoform PDE9A12 is found in prostate (PubMed:12565835).
In brain, present in the cortex, cerebellum, and subiculum (at protein level) (PubMed:22328573).
In heart, primarily localizes to myocytes (PubMed:25799991).
Highest levels in brain, heart, kidney, spleen, prostate and colon. Isoform PDE9A12 is found in prostate (PubMed:12565835).
In brain, present in the cortex, cerebellum, and subiculum (at protein level) (PubMed:22328573).
In heart, primarily localizes to myocytes (PubMed:25799991).
Induction
Up-regulated in left ventricular hypertrophy from aortic stenosis and following heart failure with preserved ejection fraction (at protein level).
Gene expression databases
Organism-specific databases
Interaction
Subunit
Homodimer.
Binary interactions
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 87-141 | Disordered | ||||
Sequence: SAGVEDKRTTSRGQSAERPLRDRRVVGLEQPRREGAFESGQVEPRPREPQGCYQE | ||||||
Compositional bias | 96-127 | Basic and acidic residues | ||||
Sequence: TSRGQSAERPLRDRRVVGLEQPRREGAFESGQ | ||||||
Domain | 236-557 | PDEase | ||||
Sequence: PRRDVPTYPKYLLSPETIEALRKPTFDVWLWEPNEMLSCLEHMYHDLGLVRDFSINPVTLRRWLFCVHDNYRNNPFHNFRHCFCVAQMMYSMVWLCSLQEKFSQTDILILMTAAICHDLDHPGYNNTYQINARTELAVRYNDISPLENHHCAVAFQILAEPECNIFSNIPPDGFKQIRQGMITLILATDMARHAEIMDSFKEKMENFDYSNEEHMTLLKMILIKCCDISNEVRPMEVAEPWVDCLLEEYFMQSDREKSEGLPVAPFMDRDKVTKATAQIGFIKFVLIPMFETVTKLFPMVEEIMLQPLWESRDRYEELKRID | ||||||
Region | 564-593 | Disordered | ||||
Sequence: QKKTDSLTSGATEKSRERSRDVKNSEGDCA | ||||||
Compositional bias | 572-593 | Basic and acidic residues | ||||
Sequence: SGATEKSRERSRDVKNSEGDCA |
Sequence similarities
Belongs to the cyclic nucleotide phosphodiesterase family. PDE9 subfamily.
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 16 isoforms produced by Alternative splicing.
O76083-1
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.
- NamePDE9A1
- Length593
- Mass (Da)68,493
- Last updated1998-11-01 v1
- ChecksumE2731C7C828C0994
O76083-2
- NamePDE9A2
- Differences from canonical
- 88-147: Missing
O76083-3
- NamePDE9A3
O76083-4
- NamePDE9A4
- Differences from canonical
- 24-165: VIFSKYCNSSDIMDLFCIATGLPRNTTISLLTTDDAMVSIDPTMPANSERTPYKVRPVAIKQLSAGVEDKRTTSRGQSAERPLRDRRVVGLEQPRREGAFESGQVEPRPREPQGCYQEGQRIPPEREELIQSVLAQVAEQFS → HSVQSETCGHQATL
O76083-5
- NamePDE9A5
- Differences from canonical
- 74-165: TPYKVRPVAIKQLSAGVEDKRTTSRGQSAERPLRDRRVVGLEQPRREGAFESGQVEPRPREPQGCYQEGQRIPPEREELIQSVLAQVAEQFS → NELILYTSLRNLLFLPSKESWASHQHSVQSETCGHQATL
O76083-6
- NamePDE9A6
- SynonymsPDE9A5
O76083-7
- NamePDE9A7
- SynonymsPDE9A8, PDE9A14, PDE9A19, PDE9A20
- Differences from canonical
- 1-207: Missing
O76083-8
- NamePDE9A9
O76083-9
- NamePDE9A10
O76083-10
- NamePDE9A11
- SynonymsPDE9A15
O76083-11
- NamePDE9A12
O76083-12
- NamePDE9A13
- Differences from canonical
- 24-165: VIFSKYCNSSDIMDLFCIATGLPRNTTISLLTTDDAMVSIDPTMPANSERTPYKVRPVAIKQLSAGVEDKRTTSRGQSAERPLRDRRVVGLEQPRREGAFESGQVEPRPREPQGCYQEGQRIPPEREELIQSVLAQVAEQFS → EHDHLPADHRRRHGLHRPHHAREFRTHSVQSETCGHQATL
O76083-13
- NamePDE9A16
- Differences from canonical
- 1-73: MGSGSSSYRPKAIYLDIDGRIQKVIFSKYCNSSDIMDLFCIATGLPRNTTISLLTTDDAMVSIDPTMPANSER → MDAFRS
O76083-14
- NamePDE9A17
- Differences from canonical
- 1-46: MGSGSSSYRPKAIYLDIDGRIQKVIFSKYCNSSDIMDLFCIATGLP → MDAFR
O76083-15
- NamePDE9A18
- Differences from canonical
- 48-73: Missing
O76083-16
- NamePDE9A21
Features
Showing features for alternative sequence, sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_017305 | 1-46 | in isoform PDE9A6, isoform PDE9A12 and isoform PDE9A17 | |||
Sequence: MGSGSSSYRPKAIYLDIDGRIQKVIFSKYCNSSDIMDLFCIATGLP → MDAFR | ||||||
Alternative sequence | VSP_038647 | 1-73 | in isoform PDE9A21 | |||
Sequence: MGSGSSSYRPKAIYLDIDGRIQKVIFSKYCNSSDIMDLFCIATGLPRNTTISLLTTDDAMVSIDPTMPANSER → MSSFSIHHSVTCCFYLVRSHGRPTS | ||||||
Alternative sequence | VSP_004598 | 1-73 | in isoform PDE9A3 and isoform PDE9A16 | |||
Sequence: MGSGSSSYRPKAIYLDIDGRIQKVIFSKYCNSSDIMDLFCIATGLPRNTTISLLTTDDAMVSIDPTMPANSER → MDAFRS | ||||||
Alternative sequence | VSP_017304 | 1-160 | in isoform PDE9A10 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_017303 | 1-207 | in isoform PDE9A7 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_017302 | 1-217 | in isoform PDE9A11 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_017306 | 24-165 | in isoform PDE9A13 | |||
Sequence: VIFSKYCNSSDIMDLFCIATGLPRNTTISLLTTDDAMVSIDPTMPANSERTPYKVRPVAIKQLSAGVEDKRTTSRGQSAERPLRDRRVVGLEQPRREGAFESGQVEPRPREPQGCYQEGQRIPPEREELIQSVLAQVAEQFS → EHDHLPADHRRRHGLHRPHHAREFRTHSVQSETCGHQATL | ||||||
Alternative sequence | VSP_004600 | 24-165 | in isoform PDE9A4 | |||
Sequence: VIFSKYCNSSDIMDLFCIATGLPRNTTISLLTTDDAMVSIDPTMPANSERTPYKVRPVAIKQLSAGVEDKRTTSRGQSAERPLRDRRVVGLEQPRREGAFESGQVEPRPREPQGCYQEGQRIPPEREELIQSVLAQVAEQFS → HSVQSETCGHQATL | ||||||
Alternative sequence | VSP_017307 | 48-73 | in isoform PDE9A9 and isoform PDE9A18 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_017308 | 73-165 | in isoform PDE9A12 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_017309 | 74-165 | in isoform PDE9A5 | |||
Sequence: TPYKVRPVAIKQLSAGVEDKRTTSRGQSAERPLRDRRVVGLEQPRREGAFESGQVEPRPREPQGCYQEGQRIPPEREELIQSVLAQVAEQFS → NELILYTSLRNLLFLPSKESWASHQHSVQSETCGHQATL | ||||||
Sequence conflict | 79 | in Ref. 6; BAG57446 | ||||
Sequence: R → G | ||||||
Alternative sequence | VSP_004599 | 88-147 | in isoform PDE9A2, isoform PDE9A3, isoform PDE9A6, isoform PDE9A9 and isoform PDE9A21 | |||
Sequence: Missing | ||||||
Compositional bias | 96-127 | Basic and acidic residues | ||||
Sequence: TSRGQSAERPLRDRRVVGLEQPRREGAFESGQ | ||||||
Alternative sequence | VSP_017310 | 161-165 | in isoform PDE9A10 | |||
Sequence: AEQFS → MDAFR | ||||||
Alternative sequence | VSP_017311 | 218 | in isoform PDE9A11 | |||
Sequence: R → M | ||||||
Compositional bias | 572-593 | Basic and acidic residues | ||||
Sequence: SGATEKSRERSRDVKNSEGDCA |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF048837 EMBL· GenBank· DDBJ | AAC39778.1 EMBL· GenBank· DDBJ | mRNA | ||
AB017602 EMBL· GenBank· DDBJ | BAA88847.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF067223 EMBL· GenBank· DDBJ | AAC26723.1 EMBL· GenBank· DDBJ | mRNA | ||
AF067224 EMBL· GenBank· DDBJ | AAC26724.1 EMBL· GenBank· DDBJ | mRNA | ||
AF067225 EMBL· GenBank· DDBJ | AAC26725.1 EMBL· GenBank· DDBJ | mRNA | ||
AF067226 EMBL· GenBank· DDBJ | AAC26726.1 EMBL· GenBank· DDBJ | mRNA | ||
AY196299 EMBL· GenBank· DDBJ | AAO34685.1 EMBL· GenBank· DDBJ | mRNA | ||
AY196300 EMBL· GenBank· DDBJ | AAO34686.1 EMBL· GenBank· DDBJ | mRNA | ||
AY196301 EMBL· GenBank· DDBJ | AAO34687.1 EMBL· GenBank· DDBJ | mRNA | ||
AY196302 EMBL· GenBank· DDBJ | AAO34688.1 EMBL· GenBank· DDBJ | mRNA | ||
AY196303 EMBL· GenBank· DDBJ | AAO34689.1 EMBL· GenBank· DDBJ | mRNA | ||
AY196304 EMBL· GenBank· DDBJ | AAO34690.1 EMBL· GenBank· DDBJ | mRNA | ||
AY196305 EMBL· GenBank· DDBJ | AAO34691.1 EMBL· GenBank· DDBJ | mRNA | ||
AY196306 EMBL· GenBank· DDBJ | AAO34692.1 EMBL· GenBank· DDBJ | mRNA | ||
AY196307 EMBL· GenBank· DDBJ | AAO34693.1 EMBL· GenBank· DDBJ | mRNA | ||
AY196308 EMBL· GenBank· DDBJ | AAO34694.1 EMBL· GenBank· DDBJ | mRNA | ||
AY196309 EMBL· GenBank· DDBJ | AAO34695.1 EMBL· GenBank· DDBJ | mRNA | ||
AY196310 EMBL· GenBank· DDBJ | AAO34696.1 EMBL· GenBank· DDBJ | mRNA | ||
AY196311 EMBL· GenBank· DDBJ | AAO34697.1 EMBL· GenBank· DDBJ | mRNA | ||
AY196312 EMBL· GenBank· DDBJ | AAO34698.1 EMBL· GenBank· DDBJ | mRNA | ||
AY196313 EMBL· GenBank· DDBJ | AAO34699.1 EMBL· GenBank· DDBJ | mRNA | ||
AY196314 EMBL· GenBank· DDBJ | AAO34700.1 EMBL· GenBank· DDBJ | mRNA | ||
AY242121 EMBL· GenBank· DDBJ | AAO88210.1 EMBL· GenBank· DDBJ | mRNA | ||
AY701187 EMBL· GenBank· DDBJ | AAV84271.1 EMBL· GenBank· DDBJ | mRNA | ||
AK294112 EMBL· GenBank· DDBJ | BAG57446.1 EMBL· GenBank· DDBJ | mRNA | ||
AK314679 EMBL· GenBank· DDBJ | BAG37232.1 EMBL· GenBank· DDBJ | mRNA | ||
BT007016 EMBL· GenBank· DDBJ | AAP35662.1 EMBL· GenBank· DDBJ | mRNA | ||
AP001747 EMBL· GenBank· DDBJ | BAA95552.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471079 EMBL· GenBank· DDBJ | EAX09544.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471079 EMBL· GenBank· DDBJ | EAX09536.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471079 EMBL· GenBank· DDBJ | EAX09537.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471079 EMBL· GenBank· DDBJ | EAX09541.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471079 EMBL· GenBank· DDBJ | EAX09542.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471079 EMBL· GenBank· DDBJ | EAX09546.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471079 EMBL· GenBank· DDBJ | EAX09540.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471079 EMBL· GenBank· DDBJ | EAX09548.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471079 EMBL· GenBank· DDBJ | EAX09549.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC009047 EMBL· GenBank· DDBJ | AAH09047.1 EMBL· GenBank· DDBJ | mRNA |