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Protein

High affinity cGMP-specific 3',5'-cyclic phosphodiesterase 9A

Gene

PDE9A

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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:9624146, PubMed:18757755, PubMed:21483814). 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).By similarityCurated4 Publications

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.1 Publication1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Protein has several cofactor binding sites:

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

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).1 Publication8 Publications

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

kcat is 0.18 sec(-1) for cGMP. kcat is 2.37 sec(-1) for cAMP.1 Publication
  1. KM=0.113 µM for cGMP1 Publication
  2. KM=501 µM for cAMP1 Publication
  1. Vmax=0.285 µmol/min/mg enzyme with cGMP as substrate1 Publication
  2. Vmax=3.7 µmol/min/mg enzyme with cAMP as substrate1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: 3',5'-cyclic GMP degradation

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:
  1. cAMP and cAMP-inhibited cGMP 3',5'-cyclic phosphodiesterase 10A (PDE10A), High affinity cGMP-specific 3',5'-cyclic phosphodiesterase 9A (PDE9A), cGMP-specific 3',5'-cyclic phosphodiesterase (PDE5A)
This subpathway is part of the pathway 3',5'-cyclic GMP degradation, which is itself part of Purine metabolism.
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 keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei312Proton donor1 Publication1
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi316Zinc; via tele nitrogenCombined sources6 Publications1
Metal bindingi352Zinc; via tele nitrogenCombined sources6 Publications1
Metal bindingi353MagnesiumCombined sources6 Publications1
Metal bindingi353ZincCombined sources6 Publications1
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei353cGMP1 Publication1
Metal bindingi462ZincCombined sources6 Publications1
Binding sitei462cGMP1 Publication1
Binding sitei484cGMP1 Publication1
Binding sitei484Inhibitor specific to PDE9A3 Publications1
Binding sitei513Inhibitor5 Publications1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi312 – 316cGMP1 Publication5
Nucleotide bindingi512 – 513cGMP1 Publication2

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

  • 3',5'-cyclic-GMP phosphodiesterase activity Source: UniProtKB
  • 3',5'-cyclic-nucleotide phosphodiesterase activity Source: ProtInc
  • identical protein binding Source: IntAct
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionHydrolase
LigandcGMP, Magnesium, Metal-binding, Zinc

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.1.4.35 2681

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-418457 cGMP effects

SABIO-RK: Biochemical Reaction Kinetics Database

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SABIO-RKi
O76083

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00763;UER00748

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
High affinity cGMP-specific 3',5'-cyclic phosphodiesterase 9ACurated (EC:3.1.4.353 Publications)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:PDE9AImported
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 21

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000160191.17

Human Gene Nomenclature Database

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HGNCi
HGNC:8795 PDE9A

Online Mendelian Inheritance in Man (OMIM)

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MIMi
602973 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_O76083

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Cell projection, Cytoplasm, Endoplasmic reticulum, Golgi apparatus, Membrane

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi312H → A: Completely abolishes catalytic activity. 1 Publication1
Mutagenesisi356H → A: Reduces catalytic activity, but has no effect on substrate affinity. 1 Publication1
Mutagenesisi425M → A: Induces a 2 fold change in inhibitory sensitivity by BAY-73-9961. 1 Publication1
Mutagenesisi463I → A: Induces a 6-9 fold change in inhibitory sensitivity by BAY-73-9961. 1 Publication1
Mutagenesisi466E → A: Decreased affinity and catalytic activity for cGMP and cAMP. 1 Publication1
Mutagenesisi480L → A: Induces a 6-9 fold change in inhibitory sensitivity by BAY-73-9961. 1 Publication1
Mutagenesisi484Y → A: Induces a 6-9 fold change in inhibitory sensitivity by BAY-73-9961. 1 Publication1
Mutagenesisi501F → A: Induces a 2 fold change in inhibitory sensitivity by BAY-73-9961. 1 Publication1
Mutagenesisi513Q → A: Induces a dramatic change in inhibitory sensitivity by BAY-73-9961. 1 Publication1
Mutagenesisi513Q → E: 2 fold decreased affinity and catalytic activity for cGMP. 8 fold decreased catalytic activity for cAMP without affecting the affinity for cAMP. 1 Publication1
Mutagenesisi516F → A: Induces a dramatic change in inhibitory sensitivity by BAY-73-9961. 1 Publication1

Organism-specific databases

DisGeNET

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DisGeNETi
5152

Open Targets

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OpenTargetsi
ENSG00000160191

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA33143

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL3535

Drug and drug target database

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DrugBanki
DB07954 3-isobutyl-1-methyl-7H-xanthine
DB00201 Caffeine
DB03597 Gamma-Glutamyl[S-(2-Iodobenzyl)Cysteinyl]Glycine

IUPHAR/BPS Guide to PHARMACOLOGY

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GuidetoPHARMACOLOGYi
1309

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
PDE9A

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001988411 – 593High affinity cGMP-specific 3',5'-cyclic phosphodiesterase 9AAdd BLAST593

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei379PhosphoserineBy similarity1

Keywords - PTMi

Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
O76083

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
O76083

PeptideAtlas

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PeptideAtlasi
O76083

PRoteomics IDEntifications database

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PRIDEi
O76083

ProteomicsDB human proteome resource

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ProteomicsDBi
50391
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

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
O76083

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
O76083

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

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).4 Publications

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Up-regulated in left ventricular hypertrophy from aortic stenosis and following heart failure with preserved ejection fraction (at protein level).1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000160191 Expressed in 179 organ(s), highest expression level in mucosa of transverse colon

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
O76083 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
O76083 HS

Organism-specific databases

Human Protein Atlas

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HPAi
HPA011380

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer.2 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
111178, 33 interactors

Protein interaction database and analysis system

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IntActi
O76083, 34 interactors

STRING: functional protein association networks

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STRINGi
9606.ENSP00000291539

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
O76083

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1593
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
O76083

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
O76083

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
O76083

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini236 – 557PDEasePROSITE-ProRule annotationAdd BLAST322

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG3689 Eukaryota
ENOG410XRI7 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000155587

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG053545

KEGG Orthology (KO)

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KOi
K13761

Identification of Orthologs from Complete Genome Data

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OMAi
PSYPKYM

Database of Orthologous Groups

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OrthoDBi
EOG091G082I

Database for complete collections of gene phylogenies

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PhylomeDBi
O76083

TreeFam database of animal gene trees

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TreeFami
TF314638

Family and domain databases

Conserved Domains Database

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CDDi
cd00077 HDc, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
1.10.1300.10, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR003607 HD/PDEase_dom
IPR023088 PDEase
IPR002073 PDEase_catalytic_dom
IPR036971 PDEase_catalytic_dom_sf
IPR023174 PDEase_CS

Pfam protein domain database

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Pfami
View protein in Pfam
PF00233 PDEase_I, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00387 PDIESTERASE1

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00471 HDc, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS00126 PDEASE_I_1, 1 hit
PS51845 PDEASE_I_2, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (16)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry describes 16 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket
Isoform PDE9A1 (identifier: O76083-1) [UniParc]FASTAAdd to basket

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.

« Hide
        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
Length:593
Mass (Da):68,493
Last modified:November 1, 1998 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iE2731C7C828C0994
GO
Isoform PDE9A2 (identifier: O76083-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     88-147: Missing.

Show »
Length:533
Mass (Da):61,709
Checksum:i728ADAAACE0E4D29
GO
Isoform PDE9A3 (identifier: O76083-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-73: MGSGSSSYRP...DPTMPANSER → MDAFRS
     88-147: Missing.

Show »
Length:466
Mass (Da):54,440
Checksum:iDE087DD09AAF4794
GO
Isoform PDE9A4 (identifier: O76083-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     24-165: VIFSKYCNSS...VLAQVAEQFS → HSVQSETCGHQATL

Show »
Length:465
Mass (Da):54,096
Checksum:iBDD6A8F85E591A67
GO
Isoform PDE9A5 (identifier: O76083-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     74-165: TPYKVRPVAI...VLAQVAEQFS → NELILYTSLR...SETCGHQATL

Show »
Length:540
Mass (Da):62,491
Checksum:i612A2ECEE7F656B4
GO
Isoform PDE9A6 (identifier: O76083-6) [UniParc]FASTAAdd to basket
Also known as: PDE9A5

The sequence of this isoform differs from the canonical sequence as follows:
     1-46: MGSGSSSYRPKAIYLDIDGRIQKVIFSKYCNSSDIMDLFCIATGLP → MDAFR
     88-147: Missing.

Show »
Length:492
Mass (Da):57,285
Checksum:i1FE4F709AD50C0E6
GO
Isoform PDE9A7 (identifier: O76083-7) [UniParc]FASTAAdd to basket
Also known as: PDE9A8, PDE9A14, PDE9A19, PDE9A20

The sequence of this isoform differs from the canonical sequence as follows:
     1-207: Missing.

Show »
Length:386
Mass (Da):45,290
Checksum:i4120AB778B9746B9
GO
Isoform PDE9A9 (identifier: O76083-8) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     48-73: Missing.
     88-147: Missing.

Show »
Length:507
Mass (Da):58,933
Checksum:iE211E0EB8B67F284
GO
Isoform PDE9A10 (identifier: O76083-9) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-160: Missing.
     161-165: AEQFS → MDAFR

Show »
Length:433
Mass (Da):50,713
Checksum:iD6036BB3CA9FB7B2
GO
Isoform PDE9A11 (identifier: O76083-10) [UniParc]FASTAAdd to basket
Also known as: PDE9A15

The sequence of this isoform differs from the canonical sequence as follows:
     1-217: Missing.
     218-218: R → M

Show »
Length:376
Mass (Da):44,134
Checksum:iBF896546AED87831
GO
Isoform PDE9A12 (identifier: O76083-11) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-46: MGSGSSSYRPKAIYLDIDGRIQKVIFSKYCNSSDIMDLFCIATGLP → MDAFR
     73-165: Missing.

Show »
Length:459
Mass (Da):53,489
Checksum:iE7DA06012931A850
GO
Isoform PDE9A13 (identifier: O76083-12) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     24-165: VIFSKYCNSS...VLAQVAEQFS → EHDHLPADHR...SETCGHQATL

Show »
Length:491
Mass (Da):57,350
Checksum:iCA53A1793F405CDB
GO
Isoform PDE9A16 (identifier: O76083-13) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-73: MGSGSSSYRP...DPTMPANSER → MDAFRS

Show »
Length:526
Mass (Da):61,223
Checksum:i02A36AE5185CEDF3
GO
Isoform PDE9A17 (identifier: O76083-14) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-46: MGSGSSSYRPKAIYLDIDGRIQKVIFSKYCNSSDIMDLFCIATGLP → MDAFR

Show »
Length:552
Mass (Da):64,068
Checksum:iF10D41FE319A6D28
GO
Isoform PDE9A18 (identifier: O76083-15) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     48-73: Missing.

Show »
Length:567
Mass (Da):65,717
Checksum:i2DFEB16AFCA94F0D
GO
Isoform PDE9A21 (identifier: O76083-16) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-73: MGSGSSSYRP...DPTMPANSER → MSSFSIHHSVTCCFYLVRSHGRPTS
     88-147: Missing.

Show »
Length:485
Mass (Da):56,554
Checksum:i82275A46E46C4D83
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti79R → G in BAG57446 (PubMed:14702039).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0173021 – 217Missing in isoform PDE9A11. 1 PublicationAdd BLAST217
Alternative sequenceiVSP_0173031 – 207Missing in isoform PDE9A7. 1 PublicationAdd BLAST207
Alternative sequenceiVSP_0173041 – 160Missing in isoform PDE9A10. 1 PublicationAdd BLAST160
Alternative sequenceiVSP_0386471 – 73MGSGS…ANSER → MSSFSIHHSVTCCFYLVRSH GRPTS in isoform PDE9A21. 1 PublicationAdd BLAST73
Alternative sequenceiVSP_0045981 – 73MGSGS…ANSER → MDAFRS in isoform PDE9A3 and isoform PDE9A16. 3 PublicationsAdd BLAST73
Alternative sequenceiVSP_0173051 – 46MGSGS…ATGLP → MDAFR in isoform PDE9A6, isoform PDE9A12 and isoform PDE9A17. 2 PublicationsAdd BLAST46
Alternative sequenceiVSP_01730624 – 165VIFSK…AEQFS → EHDHLPADHRRRHGLHRPHH AREFRTHSVQSETCGHQATL in isoform PDE9A13. 1 PublicationAdd BLAST142
Alternative sequenceiVSP_00460024 – 165VIFSK…AEQFS → HSVQSETCGHQATL in isoform PDE9A4. 1 PublicationAdd BLAST142
Alternative sequenceiVSP_01730748 – 73Missing in isoform PDE9A9 and isoform PDE9A18. 1 PublicationAdd BLAST26
Alternative sequenceiVSP_01730873 – 165Missing in isoform PDE9A12. 1 PublicationAdd BLAST93
Alternative sequenceiVSP_01730974 – 165TPYKV…AEQFS → NELILYTSLRNLLFLPSKES WASHQHSVQSETCGHQATL in isoform PDE9A5. 1 PublicationAdd BLAST92
Alternative sequenceiVSP_00459988 – 147Missing in isoform PDE9A2, isoform PDE9A3, isoform PDE9A6, isoform PDE9A9 and isoform PDE9A21. 7 PublicationsAdd BLAST60
Alternative sequenceiVSP_017310161 – 165AEQFS → MDAFR in isoform PDE9A10. 1 Publication5
Alternative sequenceiVSP_017311218R → M in isoform PDE9A11. 1 Publication1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AF048837 mRNA Translation: AAC39778.1
AB017602 Genomic DNA Translation: BAA88847.1
AF067223 mRNA Translation: AAC26723.1
AF067224 mRNA Translation: AAC26724.1
AF067225 mRNA Translation: AAC26725.1
AF067226 mRNA Translation: AAC26726.1
AY196299 mRNA Translation: AAO34685.1
AY196300 mRNA Translation: AAO34686.1
AY196301 mRNA Translation: AAO34687.1
AY196302 mRNA Translation: AAO34688.1
AY196303 mRNA Translation: AAO34689.1
AY196304 mRNA Translation: AAO34690.1
AY196305 mRNA Translation: AAO34691.1
AY196306 mRNA Translation: AAO34692.1
AY196307 mRNA Translation: AAO34693.1
AY196308 mRNA Translation: AAO34694.1
AY196309 mRNA Translation: AAO34695.1
AY196310 mRNA Translation: AAO34696.1
AY196311 mRNA Translation: AAO34697.1
AY196312 mRNA Translation: AAO34698.1
AY196313 mRNA Translation: AAO34699.1
AY196314 mRNA Translation: AAO34700.1
AY242121 mRNA Translation: AAO88210.1
AY701187 mRNA Translation: AAV84271.1
AK294112 mRNA Translation: BAG57446.1
AK314679 mRNA Translation: BAG37232.1
BT007016 mRNA Translation: AAP35662.1
AP001747 Genomic DNA Translation: BAA95552.1
CH471079 Genomic DNA Translation: EAX09544.1
CH471079 Genomic DNA Translation: EAX09536.1
CH471079 Genomic DNA Translation: EAX09537.1
CH471079 Genomic DNA Translation: EAX09541.1
CH471079 Genomic DNA Translation: EAX09542.1
CH471079 Genomic DNA Translation: EAX09546.1
CH471079 Genomic DNA Translation: EAX09540.1
CH471079 Genomic DNA Translation: EAX09548.1
CH471079 Genomic DNA Translation: EAX09549.1
BC009047 mRNA Translation: AAH09047.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS13690.1 [O76083-1]
CCDS33567.1 [O76083-5]
CCDS33568.1 [O76083-2]
CCDS33569.1 [O76083-15]
CCDS33570.1 [O76083-12]
CCDS33571.1 [O76083-4]
CCDS42941.1 [O76083-8]
CCDS42942.1 [O76083-14]
CCDS42943.1 [O76083-6]
CCDS42944.1 [O76083-11]
CCDS42945.1 [O76083-13]
CCDS42946.1 [O76083-3]
CCDS42947.1 [O76083-9]

NCBI Reference Sequences

More...
RefSeqi
NP_001001567.1, NM_001001567.1 [O76083-2]
NP_001001568.1, NM_001001568.1 [O76083-3]
NP_001001569.1, NM_001001569.1 [O76083-4]
NP_001001570.1, NM_001001570.1 [O76083-5]
NP_001001571.1, NM_001001571.1 [O76083-6]
NP_001001572.1, NM_001001572.1 [O76083-7]
NP_001001573.1, NM_001001573.1 [O76083-7]
NP_001001574.1, NM_001001574.1 [O76083-8]
NP_001001575.1, NM_001001575.1 [O76083-9]
NP_001001576.1, NM_001001576.1 [O76083-10]
NP_001001577.1, NM_001001577.1 [O76083-11]
NP_001001578.1, NM_001001578.1 [O76083-12]
NP_001001579.1, NM_001001579.1 [O76083-7]
NP_001001580.1, NM_001001580.1 [O76083-10]
NP_001001581.1, NM_001001581.1 [O76083-13]
NP_001001582.1, NM_001001582.1 [O76083-14]
NP_001001583.1, NM_001001583.1 [O76083-15]
NP_001001584.1, NM_001001584.2 [O76083-7]
NP_001001585.1, NM_001001585.1 [O76083-7]
NP_001302462.1, NM_001315533.1 [O76083-16]
NP_002597.1, NM_002606.2 [O76083-1]
XP_016883855.1, XM_017028366.1 [O76083-7]

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Hs.473927

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000291539; ENSP00000291539; ENSG00000160191 [O76083-1]
ENST00000328862; ENSP00000328699; ENSG00000160191 [O76083-15]
ENST00000335440; ENSP00000335365; ENSG00000160191 [O76083-12]
ENST00000335512; ENSP00000335242; ENSG00000160191 [O76083-2]
ENST00000349112; ENSP00000344730; ENSG00000160191 [O76083-4]
ENST00000380328; ENSP00000369685; ENSG00000160191 [O76083-5]
ENST00000398224; ENSP00000381280; ENSG00000160191 [O76083-3]
ENST00000398225; ENSP00000381281; ENSG00000160191 [O76083-14]
ENST00000398227; ENSP00000381283; ENSG00000160191 [O76083-9]
ENST00000398229; ENSP00000381285; ENSG00000160191 [O76083-11]
ENST00000398232; ENSP00000381287; ENSG00000160191 [O76083-13]
ENST00000398234; ENSP00000381289; ENSG00000160191 [O76083-6]
ENST00000398236; ENSP00000381291; ENSG00000160191 [O76083-8]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
5152

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:5152

UCSC genome browser

More...
UCSCi
uc002zbm.4 human [O76083-1]

Keywords - Coding sequence diversityi

Alternative splicing

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF048837 mRNA Translation: AAC39778.1
AB017602 Genomic DNA Translation: BAA88847.1
AF067223 mRNA Translation: AAC26723.1
AF067224 mRNA Translation: AAC26724.1
AF067225 mRNA Translation: AAC26725.1
AF067226 mRNA Translation: AAC26726.1
AY196299 mRNA Translation: AAO34685.1
AY196300 mRNA Translation: AAO34686.1
AY196301 mRNA Translation: AAO34687.1
AY196302 mRNA Translation: AAO34688.1
AY196303 mRNA Translation: AAO34689.1
AY196304 mRNA Translation: AAO34690.1
AY196305 mRNA Translation: AAO34691.1
AY196306 mRNA Translation: AAO34692.1
AY196307 mRNA Translation: AAO34693.1
AY196308 mRNA Translation: AAO34694.1
AY196309 mRNA Translation: AAO34695.1
AY196310 mRNA Translation: AAO34696.1
AY196311 mRNA Translation: AAO34697.1
AY196312 mRNA Translation: AAO34698.1
AY196313 mRNA Translation: AAO34699.1
AY196314 mRNA Translation: AAO34700.1
AY242121 mRNA Translation: AAO88210.1
AY701187 mRNA Translation: AAV84271.1
AK294112 mRNA Translation: BAG57446.1
AK314679 mRNA Translation: BAG37232.1
BT007016 mRNA Translation: AAP35662.1
AP001747 Genomic DNA Translation: BAA95552.1
CH471079 Genomic DNA Translation: EAX09544.1
CH471079 Genomic DNA Translation: EAX09536.1
CH471079 Genomic DNA Translation: EAX09537.1
CH471079 Genomic DNA Translation: EAX09541.1
CH471079 Genomic DNA Translation: EAX09542.1
CH471079 Genomic DNA Translation: EAX09546.1
CH471079 Genomic DNA Translation: EAX09540.1
CH471079 Genomic DNA Translation: EAX09548.1
CH471079 Genomic DNA Translation: EAX09549.1
BC009047 mRNA Translation: AAH09047.1
CCDSiCCDS13690.1 [O76083-1]
CCDS33567.1 [O76083-5]
CCDS33568.1 [O76083-2]
CCDS33569.1 [O76083-15]
CCDS33570.1 [O76083-12]
CCDS33571.1 [O76083-4]
CCDS42941.1 [O76083-8]
CCDS42942.1 [O76083-14]
CCDS42943.1 [O76083-6]
CCDS42944.1 [O76083-11]
CCDS42945.1 [O76083-13]
CCDS42946.1 [O76083-3]
CCDS42947.1 [O76083-9]
RefSeqiNP_001001567.1, NM_001001567.1 [O76083-2]
NP_001001568.1, NM_001001568.1 [O76083-3]
NP_001001569.1, NM_001001569.1 [O76083-4]
NP_001001570.1, NM_001001570.1 [O76083-5]
NP_001001571.1, NM_001001571.1 [O76083-6]
NP_001001572.1, NM_001001572.1 [O76083-7]
NP_001001573.1, NM_001001573.1 [O76083-7]
NP_001001574.1, NM_001001574.1 [O76083-8]
NP_001001575.1, NM_001001575.1 [O76083-9]
NP_001001576.1, NM_001001576.1 [O76083-10]
NP_001001577.1, NM_001001577.1 [O76083-11]
NP_001001578.1, NM_001001578.1 [O76083-12]
NP_001001579.1, NM_001001579.1 [O76083-7]
NP_001001580.1, NM_001001580.1 [O76083-10]
NP_001001581.1, NM_001001581.1 [O76083-13]
NP_001001582.1, NM_001001582.1 [O76083-14]
NP_001001583.1, NM_001001583.1 [O76083-15]
NP_001001584.1, NM_001001584.2 [O76083-7]
NP_001001585.1, NM_001001585.1 [O76083-7]
NP_001302462.1, NM_001315533.1 [O76083-16]
NP_002597.1, NM_002606.2 [O76083-1]
XP_016883855.1, XM_017028366.1 [O76083-7]
UniGeneiHs.473927

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2HD1X-ray2.23A/B241-566[»]
2YY2X-ray2.80A/B241-566[»]
3DY8X-ray2.15A/B242-566[»]
3DYLX-ray2.70A/B242-566[»]
3DYNX-ray2.10A/B242-566[»]
3DYQX-ray2.50A/B242-566[»]
3DYSX-ray2.30A/B242-566[»]
3JSIX-ray2.72A/B242-566[»]
3JSWX-ray2.30A/B242-566[»]
3K3EX-ray2.70A/B241-566[»]
3K3HX-ray2.50A/B241-566[»]
3N3ZX-ray2.75A/B241-566[»]
3QI3X-ray2.30A/B1-593[»]
3QI4X-ray2.50A/B1-593[»]
4E90X-ray2.50A/B242-566[»]
4G2JX-ray2.40A/B242-566[»]
4G2LX-ray3.00A/B242-566[»]
4GH6X-ray2.70A/B241-566[»]
4Y86X-ray2.01A/B1-593[»]
4Y87X-ray3.10A/B1-593[»]
4Y8CX-ray2.70A/B1-593[»]
ProteinModelPortaliO76083
SMRiO76083
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111178, 33 interactors
IntActiO76083, 34 interactors
STRINGi9606.ENSP00000291539

Chemistry databases

BindingDBiO76083
ChEMBLiCHEMBL3535
DrugBankiDB07954 3-isobutyl-1-methyl-7H-xanthine
DB00201 Caffeine
DB03597 Gamma-Glutamyl[S-(2-Iodobenzyl)Cysteinyl]Glycine
GuidetoPHARMACOLOGYi1309

PTM databases

iPTMnetiO76083
PhosphoSitePlusiO76083

Polymorphism and mutation databases

BioMutaiPDE9A

Proteomic databases

EPDiO76083
PaxDbiO76083
PeptideAtlasiO76083
PRIDEiO76083
ProteomicsDBi50391
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

The DNASU plasmid repository

More...
DNASUi
5152
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000291539; ENSP00000291539; ENSG00000160191 [O76083-1]
ENST00000328862; ENSP00000328699; ENSG00000160191 [O76083-15]
ENST00000335440; ENSP00000335365; ENSG00000160191 [O76083-12]
ENST00000335512; ENSP00000335242; ENSG00000160191 [O76083-2]
ENST00000349112; ENSP00000344730; ENSG00000160191 [O76083-4]
ENST00000380328; ENSP00000369685; ENSG00000160191 [O76083-5]
ENST00000398224; ENSP00000381280; ENSG00000160191 [O76083-3]
ENST00000398225; ENSP00000381281; ENSG00000160191 [O76083-14]
ENST00000398227; ENSP00000381283; ENSG00000160191 [O76083-9]
ENST00000398229; ENSP00000381285; ENSG00000160191 [O76083-11]
ENST00000398232; ENSP00000381287; ENSG00000160191 [O76083-13]
ENST00000398234; ENSP00000381289; ENSG00000160191 [O76083-6]
ENST00000398236; ENSP00000381291; ENSG00000160191 [O76083-8]
GeneIDi5152
KEGGihsa:5152
UCSCiuc002zbm.4 human [O76083-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
5152
DisGeNETi5152
EuPathDBiHostDB:ENSG00000160191.17

GeneCards: human genes, protein and diseases

More...
GeneCardsi
PDE9A
HGNCiHGNC:8795 PDE9A
HPAiHPA011380
MIMi602973 gene
neXtProtiNX_O76083
OpenTargetsiENSG00000160191
PharmGKBiPA33143

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG3689 Eukaryota
ENOG410XRI7 LUCA
GeneTreeiENSGT00940000155587
HOVERGENiHBG053545
KOiK13761
OMAiPSYPKYM
OrthoDBiEOG091G082I
PhylomeDBiO76083
TreeFamiTF314638

Enzyme and pathway databases

UniPathwayi
UPA00763;UER00748

BRENDAi3.1.4.35 2681
ReactomeiR-HSA-418457 cGMP effects
SABIO-RKiO76083

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

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ChiTaRSi
PDE9A human
EvolutionaryTraceiO76083

The Gene Wiki collection of pages on human genes and proteins

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GeneWikii
PDE9A

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

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GenomeRNAii
5152

Protein Ontology

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PROi
PR:O76083

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
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Gene expression databases

BgeeiENSG00000160191 Expressed in 179 organ(s), highest expression level in mucosa of transverse colon
ExpressionAtlasiO76083 baseline and differential
GenevisibleiO76083 HS

Family and domain databases

CDDicd00077 HDc, 1 hit
Gene3Di1.10.1300.10, 1 hit
InterProiView protein in InterPro
IPR003607 HD/PDEase_dom
IPR023088 PDEase
IPR002073 PDEase_catalytic_dom
IPR036971 PDEase_catalytic_dom_sf
IPR023174 PDEase_CS
PfamiView protein in Pfam
PF00233 PDEase_I, 1 hit
PRINTSiPR00387 PDIESTERASE1
SMARTiView protein in SMART
SM00471 HDc, 1 hit
PROSITEiView protein in PROSITE
PS00126 PDEASE_I_1, 1 hit
PS51845 PDEASE_I_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiPDE9A_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: O76083
Secondary accession number(s): B2RBI5
, B4DFI5, D3DSJ8, D3DSJ9, O75490, O75491, O95225, Q53Y40, Q5QD39, Q86SF7, Q86SI6, Q86SJ3, Q86WN3, Q86WN4, Q86WN5, Q86WN6, Q86WN7, Q86WN8, Q86WN9, Q86WP0
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: November 1, 1998
Last modified: December 5, 2018
This is version 178 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Human chromosome 21
    Human chromosome 21: entries, gene names and cross-references to MIM
  4. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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