UniProtKB - O76083 (PDE9A_HUMAN)
High affinity cGMP-specific 3',5'-cyclic phosphodiesterase 9A
PDE9A
Functioni
Miscellaneous
Catalytic activityi
- EC:3.1.4.353 Publications
Cofactori
Protein has several cofactor binding sites:- Zn2+1 Publication5 PublicationsNote: 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.1 Publication5 Publications
- Mg2+1 Publication5 PublicationsNote: 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.1 Publication5 Publications
Activity regulationi
Kineticsi
- KM=0.113 µM for cGMP1 Publication
- KM=501 µM for cAMP1 Publication
- Vmax=0.285 µmol/min/mg enzyme with cGMP as substrate1 Publication
- Vmax=3.7 µmol/min/mg enzyme with cAMP as substrate1 Publication
: 3',5'-cyclic GMP degradation Pathwayi
This protein is involved in step 1 of the subpathway that synthesizes GMP from 3',5'-cyclic GMP.Proteins known to be involved in this subpathway in this organism are:
- cGMP-specific 3',5'-cyclic phosphodiesterase (PDE5A), cAMP and cAMP-inhibited cGMP 3',5'-cyclic phosphodiesterase 10A (PDE10A), High affinity cGMP-specific 3',5'-cyclic phosphodiesterase 9A (PDE9A)
View all proteins of this organism that are known to be involved in the subpathway that synthesizes GMP from 3',5'-cyclic GMP, the pathway 3',5'-cyclic GMP degradation and in Purine metabolism.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Active sitei | 312 | Proton donor1 Publication | 1 | |
Metal bindingi | 316 | Zinc; via tele nitrogenCombined sources6 Publications | 1 | |
Metal bindingi | 352 | Zinc; via tele nitrogenCombined sources6 Publications | 1 | |
Metal bindingi | 353 | MagnesiumCombined sources6 Publications | 1 | |
Metal bindingi | 353 | ZincCombined sources6 Publications | 1 | |
Binding sitei | 353 | cGMP1 Publication | 1 | |
Metal bindingi | 462 | ZincCombined sources6 Publications | 1 | |
Binding sitei | 462 | cGMP1 Publication | 1 | |
Binding sitei | 484 | cGMP1 Publication | 1 | |
Binding sitei | 484 | Inhibitor specific to PDE9A3 Publications | 1 | |
Binding sitei | 513 | Inhibitor5 Publications | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 312 – 316 | cGMP1 Publication | 5 | |
Nucleotide bindingi | 512 – 513 | cGMP1 Publication | 2 |
GO - Molecular functioni
- 3',5'-cyclic-GMP phosphodiesterase activity Source: UniProtKB
- 3',5'-cyclic-nucleotide phosphodiesterase activity Source: GO_Central
- identical protein binding Source: IntAct
- metal ion binding Source: UniProtKB-KW
GO - Biological processi
- cGMP catabolic process Source: UniProtKB
- cGMP-mediated signaling Source: GO_Central
- cGMP metabolic process Source: UniProtKB
- positive regulation of cardiac muscle hypertrophy Source: UniProtKB
- signal transduction Source: GO_Central
Keywordsi
Molecular function | Hydrolase |
Ligand | cGMP, Magnesium, Metal-binding, Zinc |
Enzyme and pathway databases
BRENDAi | 3.1.4.35, 2681 |
PathwayCommonsi | O76083 |
Reactomei | R-HSA-418457, cGMP effects |
SABIO-RKi | O76083 |
UniPathwayi | UPA00763;UER00748 |
Names & Taxonomyi
Protein namesi | Recommended name: High affinity cGMP-specific 3',5'-cyclic phosphodiesterase 9ACurated (EC:3.1.4.353 Publications) |
Gene namesi | Name:PDE9AImported |
Organismi | Homo sapiens (Human) |
Taxonomic identifieri | 9606 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Proteomesi |
|
Organism-specific databases
HGNCi | HGNC:8795, PDE9A |
MIMi | 602973, gene |
neXtProti | NX_O76083 |
VEuPathDBi | HostDB:ENSG00000160191.17 |
Subcellular locationi
Plasma membrane
- ruffle membrane 1 Publication
- sarcolemma 1 Publication
Endoplasmic reticulum
- Endoplasmic reticulum 1 Publication
Golgi apparatus
- Golgi apparatus 1 Publication
Other locations
- perinuclear region 1 Publication
Plasma membrane
- ruffle membrane 1 Publication
Other locations
- perinuclear region 1 Publication
Endoplasmic reticulum
- Endoplasmic reticulum 1 Publication
Other locations
- Cytoplasm 1 Publication
Endoplasmic reticulum
- Endoplasmic reticulum 1 Publication
Other locations
- Cytoplasm 1 Publication
Cytosol
- cytosol Source: UniProtKB
Endoplasmic reticulum
- endoplasmic reticulum Source: UniProtKB-SubCell
Golgi apparatus
- Golgi apparatus Source: UniProtKB-SubCell
Plasma Membrane
- ruffle membrane Source: UniProtKB-SubCell
- sarcolemma Source: UniProtKB
Other locations
- perikaryon Source: Ensembl
- perinuclear region of cytoplasm Source: UniProtKB-SubCell
Keywords - Cellular componenti
Cell membrane, Cell projection, Cytoplasm, Endoplasmic reticulum, Golgi apparatus, MembranePathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 312 | H → A: Completely abolishes catalytic activity. 1 Publication | 1 | |
Mutagenesisi | 356 | H → A: Reduces catalytic activity, but has no effect on substrate affinity. 1 Publication | 1 | |
Mutagenesisi | 425 | M → A: Induces a 2 fold change in inhibitory sensitivity by BAY-73-9961. 1 Publication | 1 | |
Mutagenesisi | 463 | I → A: Induces a 6-9 fold change in inhibitory sensitivity by BAY-73-9961. 1 Publication | 1 | |
Mutagenesisi | 466 | E → A: Decreased affinity and catalytic activity for cGMP and cAMP. 1 Publication | 1 | |
Mutagenesisi | 480 | L → A: Induces a 6-9 fold change in inhibitory sensitivity by BAY-73-9961. 1 Publication | 1 | |
Mutagenesisi | 484 | Y → A: Induces a 6-9 fold change in inhibitory sensitivity by BAY-73-9961. 1 Publication | 1 | |
Mutagenesisi | 501 | F → A: Induces a 2 fold change in inhibitory sensitivity by BAY-73-9961. 1 Publication | 1 | |
Mutagenesisi | 513 | Q → A: Induces a dramatic change in inhibitory sensitivity by BAY-73-9961. 1 Publication | 1 | |
Mutagenesisi | 513 | Q → E: 2 fold decreased affinity and catalytic activity for cGMP. 8 fold decreased catalytic activity for cAMP without affecting the affinity for cAMP. 1 Publication | 1 | |
Mutagenesisi | 516 | F → A: Induces a dramatic change in inhibitory sensitivity by BAY-73-9961. 1 Publication | 1 |
Organism-specific databases
DisGeNETi | 5152 |
OpenTargetsi | ENSG00000160191 |
PharmGKBi | PA33143 |
Miscellaneous databases
Pharosi | O76083, Tchem |
Chemistry databases
ChEMBLi | CHEMBL3535 |
DrugBanki | DB07954, 3-isobutyl-1-methyl-7H-xanthine DB00201, Caffeine DB03597, gamma-Glutamyl[S-(2-iodobenzyl)cysteinyl]glycine DB09283, Trapidil |
DrugCentrali | O76083 |
GuidetoPHARMACOLOGYi | 1309 |
Genetic variation databases
BioMutai | PDE9A |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000198841 | 1 – 593 | High affinity cGMP-specific 3',5'-cyclic phosphodiesterase 9AAdd BLAST | 593 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 379 | PhosphoserineBy similarity | 1 |
Keywords - PTMi
PhosphoproteinProteomic databases
EPDi | O76083 |
jPOSTi | O76083 |
MassIVEi | O76083 |
PaxDbi | O76083 |
PeptideAtlasi | O76083 |
PRIDEi | O76083 |
ProteomicsDBi | 50391 [O76083-1] 50392 [O76083-10] 50393 [O76083-11] 50394 [O76083-12] 50395 [O76083-13] 50396 [O76083-14] 50397 [O76083-15] 50398 [O76083-16] 50399 [O76083-2] 50400 [O76083-3] 50401 [O76083-4] 50402 [O76083-5] 50403 [O76083-6] 50404 [O76083-7] 50405 [O76083-8] 50406 [O76083-9] |
PTM databases
iPTMneti | O76083 |
PhosphoSitePlusi | O76083 |
Expressioni
Tissue specificityi
Inductioni
Gene expression databases
Bgeei | ENSG00000160191, Expressed in mucosa of transverse colon and 190 other tissues |
ExpressionAtlasi | O76083, baseline and differential |
Genevisiblei | O76083, HS |
Organism-specific databases
HPAi | ENSG00000160191, Low tissue specificity |
Interactioni
Subunit structurei
Homodimer.
2 PublicationsBinary interactionsi
Hide detailsO76083
PDE9A - isoform PDE9A2 [O76083-2]
PDE9A - isoform PDE9A4 [O76083-4]
With | #Exp. | IntAct |
---|---|---|
TRIM32 [Q13049] | 3 | EBI-16433425,EBI-742790 |
GO - Molecular functioni
- identical protein binding Source: IntAct
Protein-protein interaction databases
BioGRIDi | 111178, 54 interactors |
IntActi | O76083, 34 interactors |
STRINGi | 9606.ENSP00000291539 |
Chemistry databases
BindingDBi | O76083 |
Miscellaneous databases
RNActi | O76083, protein |
Structurei
Secondary structure
3D structure databases
SMRi | O76083 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | O76083 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 236 – 557 | PDEasePROSITE-ProRule annotationAdd BLAST | 322 |
Sequence similaritiesi
Phylogenomic databases
eggNOGi | KOG3689, Eukaryota |
GeneTreei | ENSGT00940000155587 |
HOGENOMi | CLU_032104_1_0_1 |
OMAi | CNSRDIM |
OrthoDBi | 904682at2759 |
PhylomeDBi | O76083 |
TreeFami | TF314638 |
Family and domain databases
CDDi | cd00077, HDc, 1 hit |
Gene3Di | 1.10.1300.10, 1 hit |
InterProi | View protein in InterPro IPR003607, HD/PDEase_dom IPR023088, PDEase IPR002073, PDEase_catalytic_dom IPR036971, PDEase_catalytic_dom_sf IPR023174, PDEase_CS |
Pfami | View protein in Pfam PF00233, PDEase_I, 1 hit |
PRINTSi | PR00387, PDIESTERASE1 |
SMARTi | View protein in SMART SM00471, HDc, 1 hit |
PROSITEi | View protein in PROSITE PS00126, PDEASE_I_1, 1 hit PS51845, PDEASE_I_2, 1 hit |
s (16)i Sequence
Sequence statusi: Complete.
This entry describes 16 produced by isoformsialternative splicing. AlignAdd to basketThis isoform has been chosen as the sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. canonicali
10 20 30 40 50
MGSGSSSYRP KAIYLDIDGR IQKVIFSKYC NSSDIMDLFC IATGLPRNTT
60 70 80 90 100
ISLLTTDDAM VSIDPTMPAN SERTPYKVRP VAIKQLSAGV EDKRTTSRGQ
110 120 130 140 150
SAERPLRDRR VVGLEQPRRE GAFESGQVEP RPREPQGCYQ EGQRIPPERE
160 170 180 190 200
ELIQSVLAQV AEQFSRAFKI NELKAEVANH LAVLEKRVEL EGLKVVEIEK
210 220 230 240 250
CKSDIKKMRE ELAARSSRTN CPCKYSFLDN HKKLTPRRDV PTYPKYLLSP
260 270 280 290 300
ETIEALRKPT FDVWLWEPNE MLSCLEHMYH DLGLVRDFSI NPVTLRRWLF
310 320 330 340 350
CVHDNYRNNP FHNFRHCFCV AQMMYSMVWL CSLQEKFSQT DILILMTAAI
360 370 380 390 400
CHDLDHPGYN NTYQINARTE LAVRYNDISP LENHHCAVAF QILAEPECNI
410 420 430 440 450
FSNIPPDGFK QIRQGMITLI LATDMARHAE IMDSFKEKME NFDYSNEEHM
460 470 480 490 500
TLLKMILIKC CDISNEVRPM EVAEPWVDCL LEEYFMQSDR EKSEGLPVAP
510 520 530 540 550
FMDRDKVTKA TAQIGFIKFV LIPMFETVTK LFPMVEEIML QPLWESRDRY
560 570 580 590
EELKRIDDAM KELQKKTDSL TSGATEKSRE RSRDVKNSEG DCA
The sequence of this isoform differs from the canonical sequence as follows:
88-147: Missing.
The sequence of this isoform differs from the canonical sequence as follows:
1-73: MGSGSSSYRP...DPTMPANSER → MDAFRS
88-147: Missing.
The sequence of this isoform differs from the canonical sequence as follows:
24-165: VIFSKYCNSS...VLAQVAEQFS → HSVQSETCGHQATL
The sequence of this isoform differs from the canonical sequence as follows:
74-165: TPYKVRPVAI...VLAQVAEQFS → NELILYTSLR...SETCGHQATL
The sequence of this isoform differs from the canonical sequence as follows:
1-46: MGSGSSSYRPKAIYLDIDGRIQKVIFSKYCNSSDIMDLFCIATGLP → MDAFR
88-147: Missing.
The sequence of this isoform differs from the canonical sequence as follows:
1-207: Missing.
The sequence of this isoform differs from the canonical sequence as follows:
48-73: Missing.
88-147: Missing.
The sequence of this isoform differs from the canonical sequence as follows:
1-160: Missing.
161-165: AEQFS → MDAFR
The sequence of this isoform differs from the canonical sequence as follows:
1-217: Missing.
218-218: R → M
The sequence of this isoform differs from the canonical sequence as follows:
1-46: MGSGSSSYRPKAIYLDIDGRIQKVIFSKYCNSSDIMDLFCIATGLP → MDAFR
73-165: Missing.
The sequence of this isoform differs from the canonical sequence as follows:
24-165: VIFSKYCNSS...VLAQVAEQFS → EHDHLPADHR...SETCGHQATL
The sequence of this isoform differs from the canonical sequence as follows:
1-73: MGSGSSSYRP...DPTMPANSER → MDAFRS
The sequence of this isoform differs from the canonical sequence as follows:
1-46: MGSGSSSYRPKAIYLDIDGRIQKVIFSKYCNSSDIMDLFCIATGLP → MDAFR
The sequence of this isoform differs from the canonical sequence as follows:
48-73: Missing.
The sequence of this isoform differs from the canonical sequence as follows:
1-73: MGSGSSSYRP...DPTMPANSER → MSSFSIHHSVTCCFYLVRSHGRPTS
88-147: Missing.
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 79 | R → G in BAG57446 (PubMed:14702039).Curated | 1 |
Alternative sequence
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Alternative sequenceiVSP_017302 | 1 – 217 | Missing in isoform PDE9A11. 1 PublicationAdd BLAST | 217 | |
Alternative sequenceiVSP_017303 | 1 – 207 | Missing in isoform PDE9A7. 1 PublicationAdd BLAST | 207 | |
Alternative sequenceiVSP_017304 | 1 – 160 | Missing in isoform PDE9A10. 1 PublicationAdd BLAST | 160 | |
Alternative sequenceiVSP_038647 | 1 – 73 | MGSGS…ANSER → MSSFSIHHSVTCCFYLVRSH GRPTS in isoform PDE9A21. 1 PublicationAdd BLAST | 73 | |
Alternative sequenceiVSP_004598 | 1 – 73 | MGSGS…ANSER → MDAFRS in isoform PDE9A3 and isoform PDE9A16. 3 PublicationsAdd BLAST | 73 | |
Alternative sequenceiVSP_017305 | 1 – 46 | MGSGS…ATGLP → MDAFR in isoform PDE9A6, isoform PDE9A12 and isoform PDE9A17. 2 PublicationsAdd BLAST | 46 | |
Alternative sequenceiVSP_017306 | 24 – 165 | VIFSK…AEQFS → EHDHLPADHRRRHGLHRPHH AREFRTHSVQSETCGHQATL in isoform PDE9A13. 1 PublicationAdd BLAST | 142 | |
Alternative sequenceiVSP_004600 | 24 – 165 | VIFSK…AEQFS → HSVQSETCGHQATL in isoform PDE9A4. 1 PublicationAdd BLAST | 142 | |
Alternative sequenceiVSP_017307 | 48 – 73 | Missing in isoform PDE9A9 and isoform PDE9A18. 1 PublicationAdd BLAST | 26 | |
Alternative sequenceiVSP_017308 | 73 – 165 | Missing in isoform PDE9A12. 1 PublicationAdd BLAST | 93 | |
Alternative sequenceiVSP_017309 | 74 – 165 | TPYKV…AEQFS → NELILYTSLRNLLFLPSKES WASHQHSVQSETCGHQATL in isoform PDE9A5. 1 PublicationAdd BLAST | 92 | |
Alternative sequenceiVSP_004599 | 88 – 147 | Missing in isoform PDE9A2, isoform PDE9A3, isoform PDE9A6, isoform PDE9A9 and isoform PDE9A21. 7 PublicationsAdd BLAST | 60 | |
Alternative sequenceiVSP_017310 | 161 – 165 | AEQFS → MDAFR in isoform PDE9A10. 1 Publication | 5 | |
Alternative sequenceiVSP_017311 | 218 | R → M in isoform PDE9A11. 1 Publication | 1 |
Sequence databases
Genome annotation databases
Keywords - Coding sequence diversityi
Alternative splicingSimilar proteinsi
Cross-referencesi
Sequence databases
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
2HD1 | X-ray | 2.23 | A/B | 241-566 | [»] | |
2YY2 | X-ray | 2.80 | A/B | 241-566 | [»] | |
3DY8 | X-ray | 2.15 | A/B | 242-566 | [»] | |
3DYL | X-ray | 2.70 | A/B | 242-566 | [»] | |
3DYN | X-ray | 2.10 | A/B | 242-566 | [»] | |
3DYQ | X-ray | 2.50 | A/B | 242-566 | [»] | |
3DYS | X-ray | 2.30 | A/B | 242-566 | [»] | |
3JSI | X-ray | 2.72 | A/B | 242-566 | [»] | |
3JSW | X-ray | 2.30 | A/B | 242-566 | [»] | |
3K3E | X-ray | 2.70 | A/B | 241-566 | [»] | |
3K3H | X-ray | 2.50 | A/B | 241-566 | [»] | |
3N3Z | X-ray | 2.75 | A/B | 241-566 | [»] | |
3QI3 | X-ray | 2.30 | A/B | 1-593 | [»] | |
3QI4 | X-ray | 2.50 | A/B | 1-593 | [»] | |
4E90 | X-ray | 2.50 | A/B | 242-566 | [»] | |
4G2J | X-ray | 2.40 | A/B | 242-566 | [»] | |
4G2L | X-ray | 3.00 | A/B | 242-566 | [»] | |
4GH6 | X-ray | 2.70 | A/B | 241-566 | [»] | |
4Y86 | X-ray | 2.01 | A/B | 1-593 | [»] | |
4Y87 | X-ray | 3.10 | A/B | 1-593 | [»] | |
4Y8C | X-ray | 2.70 | A/B | 1-593 | [»] | |
6A3N | X-ray | 2.60 | A/B | 245-566 | [»] | |
SMRi | O76083 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 111178, 54 interactors |
IntActi | O76083, 34 interactors |
STRINGi | 9606.ENSP00000291539 |
Chemistry databases
BindingDBi | O76083 |
ChEMBLi | CHEMBL3535 |
DrugBanki | DB07954, 3-isobutyl-1-methyl-7H-xanthine DB00201, Caffeine DB03597, gamma-Glutamyl[S-(2-iodobenzyl)cysteinyl]glycine DB09283, Trapidil |
DrugCentrali | O76083 |
GuidetoPHARMACOLOGYi | 1309 |
PTM databases
iPTMneti | O76083 |
PhosphoSitePlusi | O76083 |
Genetic variation databases
BioMutai | PDE9A |
Proteomic databases
EPDi | O76083 |
jPOSTi | O76083 |
MassIVEi | O76083 |
PaxDbi | O76083 |
PeptideAtlasi | O76083 |
PRIDEi | O76083 |
ProteomicsDBi | 50391 [O76083-1] 50392 [O76083-10] 50393 [O76083-11] 50394 [O76083-12] 50395 [O76083-13] 50396 [O76083-14] 50397 [O76083-15] 50398 [O76083-16] 50399 [O76083-2] 50400 [O76083-3] 50401 [O76083-4] 50402 [O76083-5] 50403 [O76083-6] 50404 [O76083-7] 50405 [O76083-8] 50406 [O76083-9] |
Protocols and materials databases
Antibodypediai | 1648, 212 antibodies |
DNASUi | 5152 |
Genome annotation databases
Organism-specific databases
CTDi | 5152 |
DisGeNETi | 5152 |
GeneCardsi | PDE9A |
HGNCi | HGNC:8795, PDE9A |
HPAi | ENSG00000160191, Low tissue specificity |
MIMi | 602973, gene |
neXtProti | NX_O76083 |
OpenTargetsi | ENSG00000160191 |
PharmGKBi | PA33143 |
VEuPathDBi | HostDB:ENSG00000160191.17 |
GenAtlasi | Search... |
Phylogenomic databases
eggNOGi | KOG3689, Eukaryota |
GeneTreei | ENSGT00940000155587 |
HOGENOMi | CLU_032104_1_0_1 |
OMAi | CNSRDIM |
OrthoDBi | 904682at2759 |
PhylomeDBi | O76083 |
TreeFami | TF314638 |
Enzyme and pathway databases
UniPathwayi | UPA00763;UER00748 |
BRENDAi | 3.1.4.35, 2681 |
PathwayCommonsi | O76083 |
Reactomei | R-HSA-418457, cGMP effects |
SABIO-RKi | O76083 |
Miscellaneous databases
BioGRID-ORCSi | 5152, 5 hits in 874 CRISPR screens |
ChiTaRSi | PDE9A, human |
EvolutionaryTracei | O76083 |
GeneWikii | PDE9A |
GenomeRNAii | 5152 |
Pharosi | O76083, Tchem |
PROi | PR:O76083 |
RNActi | O76083, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSG00000160191, Expressed in mucosa of transverse colon and 190 other tissues |
ExpressionAtlasi | O76083, baseline and differential |
Genevisiblei | O76083, HS |
Family and domain databases
CDDi | cd00077, HDc, 1 hit |
Gene3Di | 1.10.1300.10, 1 hit |
InterProi | View protein in InterPro IPR003607, HD/PDEase_dom IPR023088, PDEase IPR002073, PDEase_catalytic_dom IPR036971, PDEase_catalytic_dom_sf IPR023174, PDEase_CS |
Pfami | View protein in Pfam PF00233, PDEase_I, 1 hit |
PRINTSi | PR00387, PDIESTERASE1 |
SMARTi | View protein in SMART SM00471, HDc, 1 hit |
PROSITEi | View protein in PROSITE PS00126, PDEASE_I_1, 1 hit PS51845, PDEASE_I_2, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | PDE9A_HUMAN | |
Accessioni | O76083Primary (citable) accession number: O76083 Secondary accession number(s): B2RBI5 Q86WP0 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 15, 1999 |
Last sequence update: | November 1, 1998 | |
Last modified: | February 10, 2021 | |
This is version 192 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program | |
Disclaimer | Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- Human chromosome 21
Human chromosome 21: entries, gene names and cross-references to MIM - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families