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O00408

- PDE2A_HUMAN

UniProt

O00408 - PDE2A_HUMAN

Protein

cGMP-dependent 3',5'-cyclic phosphodiesterase

Gene

PDE2A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 129 (01 Oct 2014)
      Sequence version 1 (01 Jul 1997)
      Previous versions | rss
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    Functioni

    Cyclic nucleotide phosphodiesterase with a dual-specificity for the second messengers cAMP and cGMP, which are key regulators of many important physiological processes.
    Isoform PDE2A2: Regulates Mitochondrial cAMP Levels and Respiration.

    Catalytic activityi

    Nucleoside 3',5'-cyclic phosphate + H2O = nucleoside 5'-phosphate.

    Cofactori

    Binds 2 divalent metal cations per subunit. Site 1 may preferentially bind zinc ions, while site 2 has a preference for magnesium and/or manganese ions By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei431 – 4311cGMPBy similarity
    Binding sitei446 – 4461cGMPBy similarity
    Binding sitei499 – 4991cGMPBy similarity
    Active sitei656 – 6561Proton donorBy similarity
    Metal bindingi660 – 6601Divalent metal cation 1
    Metal bindingi696 – 6961Divalent metal cation 1
    Metal bindingi697 – 6971Divalent metal cation 1
    Metal bindingi697 – 6971Divalent metal cation 2
    Binding sitei697 – 6971Substrate
    Metal bindingi808 – 8081Divalent metal cation 1
    Binding sitei808 – 8081Substrate

    GO - Molecular functioni

    1. calcium channel activity Source: UniProtKB
    2. cAMP binding Source: UniProtKB
    3. cGMP binding Source: UniProtKB
    4. cGMP-stimulated cyclic-nucleotide phosphodiesterase activity Source: UniProtKB
    5. cyclic-nucleotide phosphodiesterase activity Source: UniProtKB
    6. drug binding Source: UniProtKB
    7. metal ion binding Source: UniProtKB-KW
    8. protein binding Source: IntAct
    9. protein homodimerization activity Source: UniProtKB
    10. TPR domain binding Source: UniProtKB

    GO - Biological processi

    1. blood coagulation Source: Reactome
    2. calcium ion transmembrane transport Source: GOC
    3. cAMP catabolic process Source: UniProtKB
    4. cAMP-mediated signaling Source: UniProtKB
    5. cellular response to cGMP Source: UniProtKB
    6. cellular response to drug Source: UniProtKB
    7. cellular response to granulocyte macrophage colony-stimulating factor stimulus Source: UniProtKB
    8. cellular response to macrophage colony-stimulating factor stimulus Source: UniProtKB
    9. cellular response to mechanical stimulus Source: UniProtKB
    10. cellular response to transforming growth factor beta stimulus Source: UniProtKB
    11. cGMP catabolic process Source: UniProtKB
    12. cGMP-mediated signaling Source: UniProtKB
    13. establishment of endothelial barrier Source: UniProtKB
    14. metabolic process Source: UniProtKB
    15. monocyte differentiation Source: UniProtKB
    16. negative regulation of cAMP biosynthetic process Source: UniProtKB
    17. negative regulation of protein import into nucleus, translocation Source: UniProtKB
    18. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    19. negative regulation of vascular permeability Source: UniProtKB
    20. positive regulation of inflammatory response Source: UniProtKB
    21. positive regulation of vascular permeability Source: UniProtKB
    22. protein targeting to mitochondrion Source: UniProtKB

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    cAMP, cGMP, cGMP-binding, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_19327. G alpha (s) signalling events.
    REACT_23767. cGMP effects.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    cGMP-dependent 3',5'-cyclic phosphodiesterase (EC:3.1.4.17)
    Alternative name(s):
    Cyclic GMP-stimulated phosphodiesterase
    Short name:
    CGS-PDE
    Short name:
    cGSPDE
    Gene namesi
    Name:PDE2A
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:8777. PDE2A.

    Subcellular locationi

    Isoform PDE2A3 : Cell membrane 1 Publication; Lipid-anchor 1 Publication
    Isoform PDE2A2 : Mitochondrion matrix 1 Publication
    Isoform PDE2A1 : Cytoplasm 1 Publication

    GO - Cellular componenti

    1. axon Source: Ensembl
    2. cytoplasm Source: UniProtKB
    3. cytosol Source: UniProtKB
    4. dendrite Source: Ensembl
    5. endoplasmic reticulum Source: UniProtKB
    6. Golgi apparatus Source: UniProtKB
    7. mitochondrial matrix Source: UniProtKB
    8. nucleus Source: UniProtKB
    9. perinuclear region of cytoplasm Source: UniProtKB
    10. plasma membrane Source: UniProtKB
    11. presynaptic membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane, Mitochondrion

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA33125.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed
    Chaini2 – 941940cGMP-dependent 3',5'-cyclic phosphodiesterasePRO_0000198796Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi2 – 21N-myristoyl glycine2 Publications
    Lipidationi5 – 51S-palmitoyl cysteine; in isoform PDE2A31 Publication
    Lipidationi11 – 111S-palmitoyl cysteine; in isoform PDE2A31 Publication

    Keywords - PTMi

    Lipoprotein, Myristate, Palmitate

    Proteomic databases

    MaxQBiO00408.
    PaxDbiO00408.
    PRIDEiO00408.

    PTM databases

    PhosphoSiteiO00408.

    Expressioni

    Tissue specificityi

    Expressed in brain and to a lesser extent in heart, placenta, lung, skeletal muscle, kidney and pancreas.

    Gene expression databases

    ArrayExpressiO00408.
    BgeeiO00408.
    CleanExiHS_PDE2A.
    GenevestigatoriO00408.

    Organism-specific databases

    HPAiCAB009752.

    Interactioni

    Subunit structurei

    Homodimer.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    AIPO001706EBI-1785967,EBI-704197

    Protein-protein interaction databases

    BioGridi111164. 1 interaction.
    DIPiDIP-40269N.
    IntActiO00408. 3 interactions.
    STRINGi9606.ENSP00000334910.

    Structurei

    Secondary structure

    1
    941
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi226 – 23611
    Helixi242 – 25615
    Beta strandi262 – 2676
    Beta strandi271 – 2799
    Beta strandi282 – 29110
    Beta strandi294 – 2963
    Helixi297 – 3026
    Helixi308 – 3103
    Helixi313 – 32311
    Beta strandi330 – 3367
    Beta strandi338 – 3403
    Beta strandi342 – 35514
    Helixi362 – 40342
    Turni410 – 4123
    Helixi413 – 42513
    Beta strandi427 – 4359
    Beta strandi437 – 4437
    Beta strandi446 – 4483
    Beta strandi456 – 4605
    Helixi464 – 4729
    Beta strandi476 – 4794
    Beta strandi502 – 5065
    Beta strandi510 – 5123
    Beta strandi516 – 52813
    Turni531 – 5344
    Helixi535 – 57036
    Turni571 – 5733
    Helixi580 – 5878
    Helixi593 – 5953
    Turni598 – 6014
    Helixi607 – 6093
    Helixi612 – 6143
    Helixi615 – 62511
    Helixi628 – 6314
    Helixi636 – 64813
    Beta strandi654 – 6574
    Helixi658 – 67518
    Helixi677 – 6793
    Helixi683 – 69513
    Turni696 – 6994
    Helixi705 – 7106
    Helixi714 – 7196
    Turni720 – 7223
    Helixi725 – 73814
    Turni741 – 7433
    Turni745 – 7484
    Helixi751 – 76616
    Helixi770 – 78617
    Helixi793 – 80816
    Helixi810 – 8134
    Helixi816 – 83924
    Helixi846 – 8483
    Turni850 – 8523
    Helixi855 – 86511
    Helixi867 – 87711
    Helixi879 – 8813
    Helixi882 – 89817
    Helixi899 – 9024
    Beta strandi904 – 9063

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1Z1LX-ray1.70A578-919[»]
    3IBJX-ray3.02A/B215-900[»]
    3ITMX-ray2.49A/B/C/D579-919[»]
    3ITUX-ray1.58A/B/C/D579-919[»]
    4HTXX-ray1.90A/B/C/D578-919[»]
    4HTZX-ray2.00A/B/C/D578-919[»]
    4JIBX-ray1.72A/B/C/D579-919[»]
    ProteinModelPortaliO00408.
    SMRiO00408. Positions 223-916.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO00408.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini241 – 377137GAF 1Add
    BLAST
    Domaini409 – 548140GAF 2Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni633 – 891259CatalyticBy similarityAdd
    BLAST
    Regioni656 – 6605Substrate binding

    Domaini

    GAF 1 functions as a dimerization domain, whereas GAF 2 binds cGMP, which causes activation of the catalytic activity of the enzyme.By similarity

    Sequence similaritiesi

    Contains 2 GAF domains.Curated

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG270709.
    HOGENOMiHOG000007068.
    HOVERGENiHBG053540.
    InParanoidiO00408.
    KOiK18283.
    OMAiCFHYTGT.
    OrthoDBiEOG767393.
    PhylomeDBiO00408.
    TreeFamiTF316499.

    Family and domain databases

    Gene3Di1.10.1300.10. 1 hit.
    3.30.450.40. 2 hits.
    InterProiIPR003018. GAF.
    IPR029016. GAF_dom_like.
    IPR003607. HD/PDEase_dom.
    IPR023088. PDEase.
    IPR002073. PDEase_catalytic_dom.
    IPR023174. PDEase_CS.
    [Graphical view]
    PfamiPF01590. GAF. 2 hits.
    PF00233. PDEase_I. 1 hit.
    [Graphical view]
    PRINTSiPR00387. PDIESTERASE1.
    SMARTiSM00065. GAF. 2 hits.
    SM00471. HDc. 1 hit.
    [Graphical view]
    SUPFAMiSSF55781. SSF55781. 3 hits.
    PROSITEiPS00126. PDEASE_I. 1 hit.
    [Graphical view]

    Sequences (6)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 6 isoformsi produced by alternative splicing. Align

    Note: Additional isoforms seem to exist. Experimental confirmation may be lacking for some isoforms.

    Isoform PDE2A3 (identifier: O00408-1) [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

    MGQACGHSIL CRSQQYPAAR PAEPRGQQVF LKPDEPPPPP QPCADSLQDA    50
    LLSLGSVIDI SGLQRAVKEA LSAVLPRVET VYTYLLDGES QLVCEDPPHE 100
    LPQEGKVREA IISQKRLGCN GLGFSDLPGK PLARLVAPLA PDTQVLVMPL 150
    ADKEAGAVAA VILVHCGQLS DNEEWSLQAV EKHTLVALRR VQVLQQRGPR 200
    EAPRAVQNPP EGTAEDQKGG AAYTDRDRKI LQLCGELYDL DASSLQLKVL 250
    QYLQQETRAS RCCLLLVSED NLQLSCKVIG DKVLGEEVSF PLTGCLGQVV 300
    EDKKSIQLKD LTSEDVQQLQ SMLGCELQAM LCVPVISRAT DQVVALACAF 350
    NKLEGDLFTD EDEHVIQHCF HYTSTVLTST LAFQKEQKLK CECQALLQVA 400
    KNLFTHLDDV SVLLQEIITE ARNLSNAEIC SVFLLDQNEL VAKVFDGGVV 450
    DDESYEIRIP ADQGIAGHVA TTGQILNIPD AYAHPLFYRG VDDSTGFRTR 500
    NILCFPIKNE NQEVIGVAEL VNKINGPWFS KFDEDLATAF SIYCGISIAH 550
    SLLYKKVNEA QYRSHLANEM MMYHMKVSDD EYTKLLHDGI QPVAAIDSNF 600
    ASFTYTPRSL PEDDTSMAIL SMLQDMNFIN NYKIDCPTLA RFCLMVKKGY 650
    RDPPYHNWMH AFSVSHFCYL LYKNLELTNY LEDIEIFALF ISCMCHDLDH 700
    RGTNNSFQVA SKSVLAALYS SEGSVMERHH FAQAIAILNT HGCNIFDHFS 750
    RKDYQRMLDL MRDIILATDL AHHLRIFKDL QKMAEVGYDR NNKQHHRLLL 800
    CLLMTSCDLS DQTKGWKTTR KIAELIYKEF FSQGDLEKAM GNRPMEMMDR 850
    EKAYIPELQI SFMEHIAMPI YKLLQDLFPK AAELYERVAS NREHWTKVSH 900
    KFTIRGLPSN NSLDFLDEEY EVPDLDGTRA PINGCCSLDA E 941
    Length:941
    Mass (Da):105,717
    Last modified:July 1, 1997 - v1
    Checksum:i9797609B487FD64E
    GO
    Isoform PDE2A1 (identifier: O00408-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-48: MGQACGHSILCRSQQYPAARPAEPRGQQVFLKPDEPPPPPQPCADSLQ → MRRQPAASLDPLAKEPGPPGSRDDRLE

    Note: Soluble form.

    Show »
    Length:920
    Mass (Da):103,478
    Checksum:iCF77ED12741349C0
    GO
    Isoform PDE2A2 (identifier: O00408-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-24: MGQACGHSILCRSQQYPAARPAEP → MVLVLHHILIAVVQFLR

    Note: Contains a transit peptide at positions 1-17.

    Show »
    Length:934
    Mass (Da):105,147
    Checksum:i2C1E4885AD13F504
    GO
    Isoform PDE2A4 (identifier: O00408-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-24: MGQACGHSILCRSQQYPAARPAEP → MKKQRIQEGKSLAHR

    Show »
    Length:932
    Mass (Da):104,955
    Checksum:i9F5CE92BA3C2E2E5
    GO
    Isoform 5 (identifier: O00408-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-24: MGQACGHSILCRSQQYPAARPAEP → MVLVLHHILIAVVQFLR
         109-357: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:685
    Mass (Da):78,177
    Checksum:iA6087394B98221C3
    GO
    Isoform 6 (identifier: O00408-6) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-48: MGQACGHSILCRSQQYPAARPAEPRGQQVFLKPDEPPPPPQPCADSLQ → MRRQPAASLDPLAKEPGPPGSRDDRLE
         750-807: SRKDYQRMLD...LLLCLLMTSC → PLRTTTILMV...DPRTGRQAQV
         808-941: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:786
    Mass (Da):87,235
    Checksum:i33190E63C6351001
    GO

    Sequence cautioni

    The sequence AAS75515.1 differs from that shown. Reason: Frameshift at position 48.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti38 – 381P → L in AAS75513. 1 PublicationCurated
    Sequence conflicti99 – 991H → R in BAG35343. (PubMed:14702039)Curated
    Sequence conflicti213 – 2131T → A in AAS75513. 1 PublicationCurated
    Sequence conflicti664 – 6641V → A in AAS75513. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti224 – 2241T → I.
    Corresponds to variant rs341047 [ dbSNP | Ensembl ].
    VAR_024170

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 4848MGQAC…ADSLQ → MRRQPAASLDPLAKEPGPPG SRDDRLE in isoform PDE2A1 and isoform 6. 2 PublicationsVSP_055315Add
    BLAST
    Alternative sequencei1 – 2424MGQAC…RPAEP → MVLVLHHILIAVVQFLR in isoform PDE2A2 and isoform 5. 2 PublicationsVSP_055316Add
    BLAST
    Alternative sequencei1 – 2424MGQAC…RPAEP → MKKQRIQEGKSLAHR in isoform PDE2A4. 1 PublicationVSP_055317Add
    BLAST
    Alternative sequencei109 – 357249Missing in isoform 5. 1 PublicationVSP_055318Add
    BLAST
    Alternative sequencei750 – 80758SRKDY…LMTSC → PLRTTTILMVGLGPGGYRGP RKKLPEGQLSALQRGALGRS RMGLMGRRDPRTGRQAQV in isoform 6. 1 PublicationVSP_055319Add
    BLAST
    Alternative sequencei808 – 941134Missing in isoform 6. 1 PublicationVSP_055320Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U67733 mRNA. Translation: AAC51320.1.
    AY495087 mRNA. Translation: AAS75513.1.
    AY495088 mRNA. Translation: AAS75514.1.
    AY495089 mRNA. Translation: AAS75515.1. Frameshift.
    AK092278 mRNA. Translation: BAG52517.1.
    AK131525 mRNA. Translation: BAD18664.1.
    AK312434 mRNA. Translation: BAG35343.1.
    AP003065 Genomic DNA. No translation available.
    AP005019 Genomic DNA. No translation available.
    CCDSiCCDS44670.1. [O00408-3]
    CCDS53678.1. [O00408-4]
    CCDS8216.1. [O00408-1]
    RefSeqiNP_001137311.1. NM_001143839.3. [O00408-5]
    NP_001139681.1. NM_001146209.2. [O00408-4]
    NP_001230713.1. NM_001243784.1.
    NP_002590.1. NM_002599.4. [O00408-1]
    UniGeneiHs.503163.

    Genome annotation databases

    EnsembliENST00000334456; ENSP00000334910; ENSG00000186642. [O00408-1]
    ENST00000376450; ENSP00000365633; ENSG00000186642. [O00408-5]
    ENST00000444035; ENSP00000411657; ENSG00000186642. [O00408-4]
    ENST00000540345; ENSP00000446399; ENSG00000186642. [O00408-4]
    ENST00000544570; ENSP00000442256; ENSG00000186642. [O00408-3]
    GeneIDi5138.
    KEGGihsa:5138.
    UCSCiuc010rrb.2. human. [O00408-4]
    uc010rrc.2. human. [O00408-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U67733 mRNA. Translation: AAC51320.1 .
    AY495087 mRNA. Translation: AAS75513.1 .
    AY495088 mRNA. Translation: AAS75514.1 .
    AY495089 mRNA. Translation: AAS75515.1 . Frameshift.
    AK092278 mRNA. Translation: BAG52517.1 .
    AK131525 mRNA. Translation: BAD18664.1 .
    AK312434 mRNA. Translation: BAG35343.1 .
    AP003065 Genomic DNA. No translation available.
    AP005019 Genomic DNA. No translation available.
    CCDSi CCDS44670.1. [O00408-3 ]
    CCDS53678.1. [O00408-4 ]
    CCDS8216.1. [O00408-1 ]
    RefSeqi NP_001137311.1. NM_001143839.3. [O00408-5 ]
    NP_001139681.1. NM_001146209.2. [O00408-4 ]
    NP_001230713.1. NM_001243784.1.
    NP_002590.1. NM_002599.4. [O00408-1 ]
    UniGenei Hs.503163.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1Z1L X-ray 1.70 A 578-919 [» ]
    3IBJ X-ray 3.02 A/B 215-900 [» ]
    3ITM X-ray 2.49 A/B/C/D 579-919 [» ]
    3ITU X-ray 1.58 A/B/C/D 579-919 [» ]
    4HTX X-ray 1.90 A/B/C/D 578-919 [» ]
    4HTZ X-ray 2.00 A/B/C/D 578-919 [» ]
    4JIB X-ray 1.72 A/B/C/D 579-919 [» ]
    ProteinModelPortali O00408.
    SMRi O00408. Positions 223-916.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111164. 1 interaction.
    DIPi DIP-40269N.
    IntActi O00408. 3 interactions.
    STRINGi 9606.ENSP00000334910.

    Chemistry

    BindingDBi O00408.
    ChEMBLi CHEMBL2652.
    DrugBanki DB00203. Sildenafil.
    DB00605. Sulindac.
    GuidetoPHARMACOLOGYi 1297.

    PTM databases

    PhosphoSitei O00408.

    Proteomic databases

    MaxQBi O00408.
    PaxDbi O00408.
    PRIDEi O00408.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000334456 ; ENSP00000334910 ; ENSG00000186642 . [O00408-1 ]
    ENST00000376450 ; ENSP00000365633 ; ENSG00000186642 . [O00408-5 ]
    ENST00000444035 ; ENSP00000411657 ; ENSG00000186642 . [O00408-4 ]
    ENST00000540345 ; ENSP00000446399 ; ENSG00000186642 . [O00408-4 ]
    ENST00000544570 ; ENSP00000442256 ; ENSG00000186642 . [O00408-3 ]
    GeneIDi 5138.
    KEGGi hsa:5138.
    UCSCi uc010rrb.2. human. [O00408-4 ]
    uc010rrc.2. human. [O00408-1 ]

    Organism-specific databases

    CTDi 5138.
    GeneCardsi GC11M072287.
    HGNCi HGNC:8777. PDE2A.
    HPAi CAB009752.
    MIMi 602658. gene.
    neXtProti NX_O00408.
    PharmGKBi PA33125.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG270709.
    HOGENOMi HOG000007068.
    HOVERGENi HBG053540.
    InParanoidi O00408.
    KOi K18283.
    OMAi CFHYTGT.
    OrthoDBi EOG767393.
    PhylomeDBi O00408.
    TreeFami TF316499.

    Enzyme and pathway databases

    Reactomei REACT_19327. G alpha (s) signalling events.
    REACT_23767. cGMP effects.

    Miscellaneous databases

    ChiTaRSi PDE2A. human.
    EvolutionaryTracei O00408.
    GeneWikii PDE2A.
    GenomeRNAii 5138.
    NextBioi 19812.
    PROi O00408.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O00408.
    Bgeei O00408.
    CleanExi HS_PDE2A.
    Genevestigatori O00408.

    Family and domain databases

    Gene3Di 1.10.1300.10. 1 hit.
    3.30.450.40. 2 hits.
    InterProi IPR003018. GAF.
    IPR029016. GAF_dom_like.
    IPR003607. HD/PDEase_dom.
    IPR023088. PDEase.
    IPR002073. PDEase_catalytic_dom.
    IPR023174. PDEase_CS.
    [Graphical view ]
    Pfami PF01590. GAF. 2 hits.
    PF00233. PDEase_I. 1 hit.
    [Graphical view ]
    PRINTSi PR00387. PDIESTERASE1.
    SMARTi SM00065. GAF. 2 hits.
    SM00471. HDc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF55781. SSF55781. 3 hits.
    PROSITEi PS00126. PDEASE_I. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Isolation and characterization of human cDNAs encoding a cGMP-stimulated 3',5'-cyclic nucleotide phosphodiesterase."
      Rosman G.J., Martins T.J., Sonnenburg W.K., Beavo J.A., Ferguson K., Loughney K.
      Gene 191:89-95(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PDE2A3).
      Tissue: Fetal brain and Hippocampus.
    2. "Human PDE2A1, PDE2A2 and PDE2A4."
      Bugaj-Gaweda B., De Vivo M., Wang D.
      Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PDE2A4), NUCLEOTIDE SEQUENCE [MRNA] OF 1-27 (ISOFORM PDE2A1), NUCLEOTIDE SEQUENCE [MRNA] OF 1-55 (ISOFORM PDE2A2).
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS PDE2A3; 5 AND 6).
      Tissue: Adrenal gland, Brain and Tongue.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "Dual acylation of PDE2A splice variant 3: targeting to synaptic membranes."
      Russwurm C., Zoidl G., Koesling D., Russwurm M.
      J. Biol. Chem. 284:25782-25790(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: MYRISTOYLATION AT GLY-2, PALMITOYLATION AT CYS-5 AND CYS-11, SUBCELLULAR LOCATION (ISOFORMS PDE2A1 AND PDE2A3).
    6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    7. "Strategy for comprehensive identification of human N-myristoylated proteins using an insect cell-free protein synthesis system."
      Suzuki T., Moriya K., Nagatoshi K., Ota Y., Ezure T., Ando E., Tsunasawa S., Utsumi T.
      Proteomics 10:1780-1793(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: MYRISTOYLATION AT GLY-2.
    8. Cited for: FUNCTION (ISOFORM PDE2A2), SUBCELLULAR LOCATION (ISOFORM PDE2A2).
    9. "Structural determinants for inhibitor specificity and selectivity in PDE2A using the wheat germ in vitro translation system."
      Iffland A., Kohls D., Low S., Luan J., Zhang Y., Kothe M., Cao Q., Kamath A.V., Ding Y.H., Ellenberger T.
      Biochemistry 44:8312-8325(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 578-919 IN COMPLEX WITH METAL IONS AND PHOSPHATE, FUNCTION.
    10. "Mechanism for the allosteric regulation of phosphodiesterase 2A deduced from the X-ray structure of a near full-length construct."
      Pandit J., Forman M.D., Fennell K.F., Dillman K.S., Menniti F.S.
      Proc. Natl. Acad. Sci. U.S.A. 106:18225-18230(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.58 ANGSTROMS) OF 215-919 IN COMPLEX WITH METAL IONS AND THE INHIBITOR IBMX, SUBUNIT, FUNCTION.
    11. "X-ray crystal structure of phosphodiesterase 2 in complex with a highly selective, nanomolar inhibitor reveals a binding-induced pocket important for selectivity."
      Zhu J., Yang Q., Dai D., Huang Q.
      J. Am. Chem. Soc. 135:11708-11711(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 578-919 IN COMPLEX WITH INHIBITOR.

    Entry informationi

    Entry nameiPDE2A_HUMAN
    AccessioniPrimary (citable) accession number: O00408
    Secondary accession number(s): B2R646
    , B3KRV5, E9PGI1, F6W5Z0, Q5J791, Q5J792, Q5J793, Q6ZMR1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: July 1, 1997
    Last modified: October 1, 2014
    This is version 129 of the entry and version 1 of the sequence. [Complete history]
    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.

    Miscellaneousi

    Miscellaneous

    cGMP binds at an allosteric activator site.By similarity

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 11
      Human chromosome 11: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3