Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

O76074

- PDE5A_HUMAN

UniProt

O76074 - PDE5A_HUMAN

Protein

cGMP-specific 3',5'-cyclic phosphodiesterase

Gene

PDE5A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 145 (01 Oct 2014)
      Sequence version 2 (11 Jan 2011)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Plays a role in signal transduction by regulating the intracellular concentration of cyclic nucleotides. This phosphodiesterase catalyzes the specific hydrolysis of cGMP to 5'-GMP.

    Catalytic activityi

    Guanosine 3',5'-cyclic phosphate + H2O = guanosine 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.

    Enzyme regulationi

    Sildenafil (Viagra) is a highly selective and potent inhibitor of PDE5A and is effective in the treatment of penile erectile dysfunction. Also inhibited by zaprinast.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei613 – 6131Proton donorBy similarity
    Metal bindingi617 – 6171Divalent metal cation 1
    Metal bindingi653 – 6531Divalent metal cation 1
    Metal bindingi654 – 6541Divalent metal cation 1
    Metal bindingi654 – 6541Divalent metal cation 2
    Metal bindingi764 – 7641Divalent metal cation 1
    Binding sitei817 – 8171cGMP

    GO - Molecular functioni

    1. 3',5'-cyclic-GMP phosphodiesterase activity Source: UniProtKB-EC
    2. 3',5'-cyclic-nucleotide phosphodiesterase activity Source: UniProtKB
    3. cGMP binding Source: UniProtKB
    4. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. blood coagulation Source: Reactome
    2. cGMP catabolic process Source: UniProtKB
    3. negative regulation of cardiac muscle contraction Source: Ensembl
    4. negative regulation of T cell proliferation Source: Ensembl
    5. positive regulation of cardiac muscle hypertrophy Source: Ensembl
    6. positive regulation of MAP kinase activity Source: Ensembl
    7. positive regulation of oocyte development Source: Ensembl
    8. relaxation of cardiac muscle Source: Ensembl
    9. signal transduction Source: InterPro

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

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

    Enzyme and pathway databases

    BRENDAi3.1.4.35. 2681.
    ReactomeiREACT_23767. cGMP effects.
    UniPathwayiUPA00763; UER00748.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    cGMP-specific 3',5'-cyclic phosphodiesterase (EC:3.1.4.35)
    Alternative name(s):
    cGMP-binding cGMP-specific phosphodiesterase
    Short name:
    CGB-PDE
    Gene namesi
    Name:PDE5A
    Synonyms:PDE5
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 4

    Organism-specific databases

    HGNCiHGNC:8784. PDE5A.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA33132.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 875875cGMP-specific 3',5'-cyclic phosphodiesterasePRO_0000198823Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei102 – 1021PhosphoserineSequence Analysis

    Post-translational modificationi

    Phosphorylation is regulated by binding of cGMP to the two allosteric sites By similarity. Phosphorylation by PRKG1 leads to its activation.By similarity1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiO76074.
    PaxDbiO76074.
    PRIDEiO76074.

    PTM databases

    PhosphoSiteiO76074.

    Expressioni

    Tissue specificityi

    Expressed in aortic smooth muscle cells, heart, placenta, skeletal muscle and pancreas and, to a much lesser extent, in brain, liver and lung.

    Gene expression databases

    ArrayExpressiO76074.
    BgeeiO76074.
    CleanExiHS_PDE5A.
    GenevestigatoriO76074.

    Organism-specific databases

    HPAiHPA004729.
    HPA012873.

    Interactioni

    Protein-protein interaction databases

    BioGridi114205. 1 interaction.
    DIPiDIP-46287N.
    STRINGi9606.ENSP00000347046.

    Structurei

    Secondary structure

    1
    875
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi103 – 1064
    Beta strandi115 – 1173
    Turni118 – 1203
    Beta strandi121 – 1244
    Helixi148 – 16013
    Helixi165 – 17713
    Beta strandi182 – 19211
    Beta strandi198 – 2058
    Beta strandi208 – 2103
    Beta strandi213 – 2186
    Beta strandi221 – 2244
    Helixi228 – 2369
    Beta strandi240 – 2434
    Helixi245 – 2473
    Helixi254 – 2596
    Beta strandi266 – 2727
    Beta strandi278 – 28710
    Helixi299 – 34042
    Turni342 – 3454
    Helixi346 – 36217
    Beta strandi365 – 3728
    Beta strandi374 – 3763
    Beta strandi379 – 3879
    Turni388 – 3903
    Beta strandi391 – 3933
    Helixi400 – 4034
    Helixi407 – 4093
    Helixi410 – 4189
    Beta strandi422 – 4254
    Turni427 – 4293
    Beta strandi431 – 4333
    Beta strandi451 – 4577
    Beta strandi461 – 47111
    Turni476 – 4783
    Helixi486 – 50621
    Helixi535 – 54511
    Helixi551 – 5544
    Turni555 – 5573
    Helixi568 – 58114
    Helixi584 – 5874
    Helixi592 – 60413
    Turni606 – 6083
    Beta strandi610 – 6145
    Helixi615 – 63016
    Turni631 – 6333
    Helixi635 – 6373
    Helixi640 – 65213
    Turni653 – 6564
    Helixi662 – 6676
    Helixi671 – 6755
    Beta strandi677 – 6793
    Helixi680 – 69415
    Turni700 – 7034
    Helixi706 – 72217
    Helixi725 – 74016
    Beta strandi746 – 7483
    Helixi749 – 76416
    Helixi766 – 7694
    Helixi772 – 79625
    Helixi803 – 8053
    Helixi807 – 8126
    Helixi813 – 82311
    Helixi825 – 83511
    Helixi837 – 8393
    Helixi840 – 85718

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1RKPX-ray2.05A535-860[»]
    1T9RX-ray2.10A531-875[»]
    1T9SX-ray2.00A/B534-858[»]
    1TBFX-ray1.30A534-858[»]
    1UDTX-ray2.30A537-860[»]
    1UDUX-ray2.83A/B537-860[»]
    1UHOX-ray2.50A537-860[»]
    1XOZX-ray1.37A534-875[»]
    1XP0X-ray1.79A534-875[»]
    2CHMX-ray1.60A534-656[»]
    A682-858[»]
    2H40X-ray1.85A535-860[»]
    2H42X-ray2.30A/B/C535-860[»]
    2H44X-ray1.80A535-860[»]
    2XSSX-ray2.50A/B346-509[»]
    3B2RX-ray2.07A/B535-860[»]
    3BJCX-ray2.00A1-875[»]
    3HC8X-ray1.79A536-858[»]
    3HDZX-ray1.80A536-657[»]
    A682-858[»]
    3JWQX-ray2.87A/B/C/D535-786[»]
    A/B/C/D827-860[»]
    3JWRX-ray2.99A/B535-786[»]
    A/B706-860[»]
    3LFVX-ray2.80A/B98-518[»]
    3MF0X-ray3.10A/B89-518[»]
    3SHYX-ray2.65A535-860[»]
    3SHZX-ray2.45A535-860[»]
    3SIEX-ray1.93A/B535-860[»]
    3TGEX-ray1.96A534-656[»]
    A682-858[»]
    3TGGX-ray1.91A534-858[»]
    3TSEX-ray2.14A535-860[»]
    3TSFX-ray2.44A535-860[»]
    4G2WX-ray2.28A535-860[»]
    4G2YX-ray2.40A535-860[»]
    4I9ZX-ray2.08A535-860[»]
    4IA0X-ray2.17A535-860[»]
    ProteinModelPortaliO76074.
    SMRiO76074. Positions 98-860.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO76074.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini164 – 314151GAF 1Add
    BLAST
    Domaini346 – 503158GAF 2Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni588 – 853266CatalyticBy similarityAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi10 – 2415Poly-GlnAdd
    BLAST

    Domaini

    Composed of a C-terminal catalytic domain containing two putative divalent metal sites and an N-terminal regulatory domain which contains two homologous allosteric cGMP-binding regions, A and B.

    Sequence similaritiesi

    Contains 2 GAF domains.Curated

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG270709.
    HOVERGENiHBG101207.
    InParanoidiO76074.
    KOiK13762.
    OMAiREHDANK.
    OrthoDBiEOG7RRF69.
    PhylomeDBiO76074.
    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. 2 hits.
    PROSITEiPS00126. PDEASE_I. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform PDE5A1 (identifier: O76074-1) [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

    MERAGPSFGQ QRQQQQPQQQ KQQQRDQDSV EAWLDDHWDF TFSYFVRKAT    50
    REMVNAWFAE RVHTIPVCKE GIRGHTESCS CPLQQSPRAD NSAPGTPTRK 100
    ISASEFDRPL RPIVVKDSEG TVSFLSDSEK KEQMPLTPPR FDHDEGDQCS 150
    RLLELVKDIS SHLDVTALCH KIFLHIHGLI SADRYSLFLV CEDSSNDKFL 200
    ISRLFDVAEG STLEEVSNNC IRLEWNKGIV GHVAALGEPL NIKDAYEDPR 250
    FNAEVDQITG YKTQSILCMP IKNHREEVVG VAQAINKKSG NGGTFTEKDE 300
    KDFAAYLAFC GIVLHNAQLY ETSLLENKRN QVLLDLASLI FEEQQSLEVI 350
    LKKIAATIIS FMQVQKCTIF IVDEDCSDSF SSVFHMECEE LEKSSDTLTR 400
    EHDANKINYM YAQYVKNTME PLNIPDVSKD KRFPWTTENT GNVNQQCIRS 450
    LLCTPIKNGK KNKVIGVCQL VNKMEENTGK VKPFNRNDEQ FLEAFVIFCG 500
    LGIQNTQMYE AVERAMAKQM VTLEVLSYHA SAAEEETREL QSLAAAVVPS 550
    AQTLKITDFS FSDFELSDLE TALCTIRMFT DLNLVQNFQM KHEVLCRWIL 600
    SVKKNYRKNV AYHNWRHAFN TAQCMFAALK AGKIQNKLTD LEILALLIAA 650
    LSHDLDHRGV NNSYIQRSEH PLAQLYCHSI MEHHHFDQCL MILNSPGNQI 700
    LSGLSIEEYK TTLKIIKQAI LATDLALYIK RRGEFFELIR KNQFNLEDPH 750
    QKELFLAMLM TACDLSAITK PWPIQQRIAE LVATEFFDQG DRERKELNIE 800
    PTDLMNREKK NKIPSMQVGF IDAICLQLYE ALTHVSEDCF PLLDGCRKNR 850
    QKWQALAEQQ EKMLINGESG QAKRN 875
    Length:875
    Mass (Da):99,985
    Last modified:January 11, 2011 - v2
    Checksum:i9E30C6C182F13388
    GO
    Isoform PDE5A2 (identifier: O76074-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-49: MERAGPSFGQQRQQQQPQQQKQQQRDQDSVEAWLDDHWDFTFSYFVRKA → MLPFGDK

    Show »
    Length:833
    Mass (Da):94,805
    Checksum:i41D0B4B1BAB57D6D
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti159 – 1591I → V in AAP31235. (PubMed:10393044)Curated
    Sequence conflicti310 – 3101C → G in AAP31235. (PubMed:10393044)Curated
    Sequence conflicti381 – 3811S → F in AAP31235. (PubMed:10393044)Curated
    Sequence conflicti406 – 4061K → R in AAP31235. (PubMed:10393044)Curated
    Sequence conflicti642 – 6421E → G in BAA81667. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti93 – 931A → V.5 Publications
    Corresponds to variant rs3733526 [ dbSNP | Ensembl ].
    VAR_027775
    Natural varianti181 – 1811S → A.
    Corresponds to variant rs17051276 [ dbSNP | Ensembl ].
    VAR_027776

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 4949MERAG…FVRKA → MLPFGDK in isoform PDE5A2. 3 PublicationsVSP_004591Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF043731 mRNA. Translation: AAC63967.1.
    AF043732 mRNA. Translation: AAC63968.1.
    AB001635 Genomic DNA. Translation: BAA33372.2.
    D89094 mRNA. Translation: BAA28945.1.
    AJ004865 mRNA. Translation: CAA06170.1.
    AB015656 mRNA. Translation: BAA81667.1.
    AY264918 mRNA. Translation: AAP21809.1.
    AK290189 mRNA. Translation: BAF82878.1.
    AC093752 Genomic DNA. No translation available.
    AC080089 Genomic DNA. No translation available.
    BC126233 mRNA. Translation: AAI26234.1.
    AY266363 mRNA. Translation: AAP31235.1.
    CCDSiCCDS34055.1. [O76074-2]
    CCDS3713.1. [O76074-1]
    PIRiJW0106.
    RefSeqiNP_001074.2. NM_001083.3. [O76074-1]
    NP_236914.2. NM_033430.2. [O76074-2]
    NP_246273.2. NM_033437.3.
    UniGeneiHs.647971.

    Genome annotation databases

    EnsembliENST00000264805; ENSP00000264805; ENSG00000138735. [O76074-2]
    ENST00000354960; ENSP00000347046; ENSG00000138735. [O76074-1]
    GeneIDi8654.
    KEGGihsa:8654.
    UCSCiuc003idf.3. human. [O76074-2]
    uc003idg.3. human. [O76074-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF043731 mRNA. Translation: AAC63967.1 .
    AF043732 mRNA. Translation: AAC63968.1 .
    AB001635 Genomic DNA. Translation: BAA33372.2 .
    D89094 mRNA. Translation: BAA28945.1 .
    AJ004865 mRNA. Translation: CAA06170.1 .
    AB015656 mRNA. Translation: BAA81667.1 .
    AY264918 mRNA. Translation: AAP21809.1 .
    AK290189 mRNA. Translation: BAF82878.1 .
    AC093752 Genomic DNA. No translation available.
    AC080089 Genomic DNA. No translation available.
    BC126233 mRNA. Translation: AAI26234.1 .
    AY266363 mRNA. Translation: AAP31235.1 .
    CCDSi CCDS34055.1. [O76074-2 ]
    CCDS3713.1. [O76074-1 ]
    PIRi JW0106.
    RefSeqi NP_001074.2. NM_001083.3. [O76074-1 ]
    NP_236914.2. NM_033430.2. [O76074-2 ]
    NP_246273.2. NM_033437.3.
    UniGenei Hs.647971.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1RKP X-ray 2.05 A 535-860 [» ]
    1T9R X-ray 2.10 A 531-875 [» ]
    1T9S X-ray 2.00 A/B 534-858 [» ]
    1TBF X-ray 1.30 A 534-858 [» ]
    1UDT X-ray 2.30 A 537-860 [» ]
    1UDU X-ray 2.83 A/B 537-860 [» ]
    1UHO X-ray 2.50 A 537-860 [» ]
    1XOZ X-ray 1.37 A 534-875 [» ]
    1XP0 X-ray 1.79 A 534-875 [» ]
    2CHM X-ray 1.60 A 534-656 [» ]
    A 682-858 [» ]
    2H40 X-ray 1.85 A 535-860 [» ]
    2H42 X-ray 2.30 A/B/C 535-860 [» ]
    2H44 X-ray 1.80 A 535-860 [» ]
    2XSS X-ray 2.50 A/B 346-509 [» ]
    3B2R X-ray 2.07 A/B 535-860 [» ]
    3BJC X-ray 2.00 A 1-875 [» ]
    3HC8 X-ray 1.79 A 536-858 [» ]
    3HDZ X-ray 1.80 A 536-657 [» ]
    A 682-858 [» ]
    3JWQ X-ray 2.87 A/B/C/D 535-786 [» ]
    A/B/C/D 827-860 [» ]
    3JWR X-ray 2.99 A/B 535-786 [» ]
    A/B 706-860 [» ]
    3LFV X-ray 2.80 A/B 98-518 [» ]
    3MF0 X-ray 3.10 A/B 89-518 [» ]
    3SHY X-ray 2.65 A 535-860 [» ]
    3SHZ X-ray 2.45 A 535-860 [» ]
    3SIE X-ray 1.93 A/B 535-860 [» ]
    3TGE X-ray 1.96 A 534-656 [» ]
    A 682-858 [» ]
    3TGG X-ray 1.91 A 534-858 [» ]
    3TSE X-ray 2.14 A 535-860 [» ]
    3TSF X-ray 2.44 A 535-860 [» ]
    4G2W X-ray 2.28 A 535-860 [» ]
    4G2Y X-ray 2.40 A 535-860 [» ]
    4I9Z X-ray 2.08 A 535-860 [» ]
    4IA0 X-ray 2.17 A 535-860 [» ]
    ProteinModelPortali O76074.
    SMRi O76074. Positions 98-860.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114205. 1 interaction.
    DIPi DIP-46287N.
    STRINGi 9606.ENSP00000347046.

    Chemistry

    BindingDBi O76074.
    ChEMBLi CHEMBL2111340.
    DrugBanki DB00975. Dipyridamole.
    DB00806. Pentoxifylline.
    DB00203. Sildenafil.
    DB00820. Tadalafil.
    DB00277. Theophylline.
    DB00862. Vardenafil.
    GuidetoPHARMACOLOGYi 1304.

    PTM databases

    PhosphoSitei O76074.

    Proteomic databases

    MaxQBi O76074.
    PaxDbi O76074.
    PRIDEi O76074.

    Protocols and materials databases

    DNASUi 8654.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000264805 ; ENSP00000264805 ; ENSG00000138735 . [O76074-2 ]
    ENST00000354960 ; ENSP00000347046 ; ENSG00000138735 . [O76074-1 ]
    GeneIDi 8654.
    KEGGi hsa:8654.
    UCSCi uc003idf.3. human. [O76074-2 ]
    uc003idg.3. human. [O76074-1 ]

    Organism-specific databases

    CTDi 8654.
    GeneCardsi GC04M120415.
    HGNCi HGNC:8784. PDE5A.
    HPAi HPA004729.
    HPA012873.
    MIMi 603310. gene.
    neXtProti NX_O76074.
    PharmGKBi PA33132.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG270709.
    HOVERGENi HBG101207.
    InParanoidi O76074.
    KOi K13762.
    OMAi REHDANK.
    OrthoDBi EOG7RRF69.
    PhylomeDBi O76074.
    TreeFami TF316499.

    Enzyme and pathway databases

    UniPathwayi UPA00763 ; UER00748 .
    BRENDAi 3.1.4.35. 2681.
    Reactomei REACT_23767. cGMP effects.

    Miscellaneous databases

    ChiTaRSi PDE5A. human.
    EvolutionaryTracei O76074.
    GeneWikii CGMP-specific_phosphodiesterase_type_5.
    GenomeRNAii 8654.
    NextBioi 32453.
    PROi O76074.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O76074.
    Bgeei O76074.
    CleanExi HS_PDE5A.
    Genevestigatori O76074.

    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. 2 hits.
    PROSITEi PS00126. PDEASE_I. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Isolation and characterization of cDNAs encoding PDE5A, a human cGMP-binding, cGMP-specific 3',5'-cyclic nucleotide phosphodiesterase."
      Loughney K., Hill T.R., Florio V.A., Uher L., Rosman G.J., Wolda S.L., Jones B.A., Howard M.L., McAllister-Lucas L.M., Sonnenburg W.K., Francis S.H., Corbin J.D., Beavo J.A., Ferguson K.
      Gene 216:139-147(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS PDE5A1 AND PDE5A2), VARIANT VAL-93.
    2. "Expression, structure and chromosomal localization of the human cGMP-binding cGMP-specific phosphodiesterase PDE5A gene."
      Yanaka N., Kotera J., Ohtsuka A., Akatsuka H., Imai Y., Michibata H., Fujishige K., Kawai E., Takebayashi S., Okumura K., Omori K.
      Eur. J. Biochem. 255:391-399(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM PDE5A1), VARIANT VAL-93.
      Tissue: Lung and Placenta.
    3. "Molecular cloning and expression of human cGMP-binding cGMP-specific phosphodiesterase."
      Stacey P., Rulten S., Dapling A., Phillips S.C.
      Biochem. Biophys. Res. Commun. 247:249-254(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PDE5A1), VARIANT VAL-93.
      Tissue: Prostate and Skeletal muscle.
    4. "Molecular cloning and characterization of human cGMP-specific phosphodiesterase 5A2 cDNA."
      Kotera J., Imai Y., Omori K.
      Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PDE5A2), VARIANT VAL-93.
      Tissue: Lung.
    5. "PDE5A splice variants in T84 cells."
      Sopory S., Visweswariah S.S.
      Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PDE5A2).
      Tissue: Colon carcinoma.
    6. "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] (ISOFORM PDE5A1), VARIANT VAL-93.
      Tissue: Thalamus.
    7. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM PDE5A1).
    9. "Multiple cyclic nucleotide phosphodiesterases in human trabecular meshwork cells."
      Zhou L., Thompson W.J., Potter D.E.
      Invest. Ophthalmol. Vis. Sci. 40:1745-1752(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 157-411.
      Tissue: Trabecular meshwork.
    10. "Regulation of cGMP-specific phosphodiesterase (PDE5) phosphorylation in smooth muscle cells."
      Rybalkin S.D., Rybalkina I.G., Feil R., Hofmann F., Beavo J.A.
      J. Biol. Chem. 277:3310-3317(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION BY PRKG1.
    11. "Structure of the catalytic domain of human phosphodiesterase 5 with bound drug molecules."
      Sung B.-J., Hwang K.Y., Jeon Y.H., Lee J.I., Heo Y.-S., Kim J.H., Moon J., Yoon J.M., Hyun Y.-L., Kim E., Eum S.J., Park S.-Y., Lee J.-O., Lee T.G., Ro S., Cho J.M.
      Nature 425:98-102(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 537-860 IN COMPLEX WITH THE INHIBITORS SILDENAFIL; TADALAFIL AND VARDENAFIL, METAL-BINDING.

    Entry informationi

    Entry nameiPDE5A_HUMAN
    AccessioniPrimary (citable) accession number: O76074
    Secondary accession number(s): A0AV69
    , A8K2C4, O75026, O75887, Q86UI0, Q86V66, Q9Y6Z6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1999
    Last sequence update: January 11, 2011
    Last modified: October 1, 2014
    This is version 145 of the entry and version 2 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

    Keywords - Technical termi

    3D-structure, Allosteric enzyme, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 4
      Human chromosome 4: 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3