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Q9HCR9

- PDE11_HUMAN

UniProt

Q9HCR9 - PDE11_HUMAN

Protein

Dual 3',5'-cyclic-AMP and -GMP phosphodiesterase 11A

Gene

PDE11A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 104 (01 Oct 2014)
      Sequence version 2 (18 May 2010)
      Previous versions | rss
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    Functioni

    Plays a role in signal transduction by regulating the intracellular concentration of cyclic nucleotides cAMP and cGMP. Catalyzes the hydrolysis of both cAMP and cGMP to 5'-AMP and 5'-GMP, respectively.3 Publications

    Catalytic activityi

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

    Enzyme regulationi

    Inhibited by 3-isobutyl-1-methylxanthine (IBMX), zaprinast and dipyridamole. cGMP acts as an allosteric activator. Weakly inhibited by Sildenafil (Viagra) and Tadalafil (Cialis); however, the fact that the protein is probably absent from testis, suggests that it is not biologically relevant and is not related with erectile dysfunction.4 Publications

    Kineticsi

    1. KM=3.0 µM for cAMP (isoform 1)3 Publications
    2. KM=1.4 µM for cGMP (isoform 1)3 Publications
    3. KM=3.0 µM for cAMP (isoform 2)3 Publications
    4. KM=1.5 µM for cGMP (isoform 2)3 Publications
    5. KM=3.3 µM for cAMP (isoform 3)3 Publications
    6. KM=3.7 µM for cGMP (isoform 3)3 Publications
    7. KM=1.04 µM for cAMP (isoform 4)3 Publications
    8. KM=0.52 µM for cGMP (isoform 4)3 Publications

    Vmax=3.6 pmol/min/µg enzyme with cAMP as substrate (isoform 4)3 Publications

    Vmax=3.9 pmol/min/µg enzyme with cGMP as substrate (isoform 4)3 Publications

    Vmax=270 pmol/min/µg enzyme with cAMP as substrate (isoform 1)3 Publications

    Vmax=120 pmol/min/µg enzyme with cGMP as substrate (isoform 1)3 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei664 – 6641Proton donorBy similarity
    Metal bindingi668 – 6681Divalent metal cation 1By similarity
    Metal bindingi704 – 7041Divalent metal cation 1By similarity
    Metal bindingi705 – 7051Divalent metal cation 1By similarity
    Metal bindingi705 – 7051Divalent metal cation 2By similarity
    Metal bindingi708 – 7081Divalent metal cation 2By similarity
    Metal bindingi734 – 7341Divalent metal cation 2By similarity
    Metal bindingi816 – 8161Divalent metal cation 1By similarity
    Binding sitei869 – 8691cAMP or cGMPBy similarity

    GO - Molecular functioni

    1. 3',5'-cyclic-GMP phosphodiesterase activity Source: UniProtKB-EC
    2. 3',5'-cyclic-nucleotide phosphodiesterase activity Source: ProtInc
    3. cAMP binding Source: Ensembl
    4. cGMP binding Source: UniProtKB
    5. cGMP-stimulated cyclic-nucleotide phosphodiesterase activity Source: UniProtKB
    6. cyclic-nucleotide phosphodiesterase activity Source: UniProtKB
    7. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. blood coagulation Source: Reactome
    2. cAMP catabolic process Source: Ensembl
    3. cGMP catabolic process Source: Ensembl
    4. signal transduction Source: ProtInc

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    cAMP, cGMP, Metal-binding

    Enzyme and pathway databases

    BRENDAi3.1.4.17. 2681.
    ReactomeiREACT_19327. G alpha (s) signalling events.
    REACT_23767. cGMP effects.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dual 3',5'-cyclic-AMP and -GMP phosphodiesterase 11A (EC:3.1.4.17, EC:3.1.4.35)
    Alternative name(s):
    cAMP and cGMP phosphodiesterase 11A
    Gene namesi
    Name:PDE11A
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:8773. PDE11A.

    Subcellular locationi

    Cytoplasmcytosol 1 Publication

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. perikaryon Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Involvement in diseasei

    Primary pigmented nodular adrenocortical disease 2 (PPNAD2) [MIM:610475]: A rare bilateral adrenal defect causing ACTH-independent Cushing syndrome. Macroscopic appearance of the adrenals is characteristic with small pigmented micronodules observed in the cortex. Adrenal glands show overall normal size and weight, and multiple small yellow-to-dark brown nodules surrounded by a cortex with a uniform appearance. Microscopically, there are moderate diffuse cortical hyperplasia with mostly nonpigmented nodules, multiple capsular deficits and massive circumscribed and infiltrating extra-adrenal cortical excrescences with micronodules. Clinical manifestations of Cushing syndrome include facial and truncal obesity, abdominal striae, muscular weakness, osteoporosis, arterial hypertension, diabetes.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi355 – 3551D → A: Induces a decrease in enzyme activity due to the inability of cGMP to bind and stimulate enzyme activity. 1 Publication

    Keywords - Diseasei

    Cushing syndrome

    Organism-specific databases

    MIMi610475. phenotype.
    Orphaneti189439. Primary pigmented nodular adrenocortical disease.
    PharmGKBiPA33121.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 933933Dual 3',5'-cyclic-AMP and -GMP phosphodiesterase 11APRO_0000247040Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei239 – 2391Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiQ9HCR9.
    PRIDEiQ9HCR9.

    PTM databases

    PhosphoSiteiQ9HCR9.

    Expressioni

    Tissue specificityi

    Isoform 1 is present in prostate, pituitary, heart and liver. It is however not present in testis nor in penis, suggesting that weak inhibition by Tadalafil (Cialis) is not relevant (at protein level). Isoform 2 may be expressed in testis. Isoform 4 is expressed in adrenal cortex.5 Publications

    Gene expression databases

    ArrayExpressiQ9HCR9.
    BgeeiQ9HCR9.
    CleanExiHS_PDE11A.
    GenevestigatoriQ9HCR9.

    Organism-specific databases

    HPAiHPA034560.

    Interactioni

    Protein-protein interaction databases

    STRINGi9606.ENSP00000286063.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9HCR9.
    SMRiQ9HCR9. Positions 205-911.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini217 – 370154GAF 1Add
    BLAST
    Domaini402 – 558157GAF 2Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni640 – 905266CatalyticBy similarityAdd
    BLAST

    Domaini

    The tandem GAF domains bind cGMP, and regulate enzyme activity. The binding of cGMP stimulates enzyme activity.1 Publication

    Sequence similaritiesi

    Contains 2 GAF domains.Curated

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG270709.
    HOVERGENiHBG101207.
    InParanoidiQ9HCR9.
    KOiK13298.
    OMAiDYSDLMQ.
    OrthoDBiEOG7RRF69.
    PhylomeDBiQ9HCR9.
    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 (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9HCR9-1) [UniParc]FASTAAdd to Basket

    Also known as: PDE11A4

    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

    MAASRLDFGE VETFLDRHPE LFEDYLMRKG KQEMVEKWLQ RHSQGQGALG    50
    PRPSLAGTSS LAHSTCRGGS SVGGGTGPNG SAHSQPLPGG GDCGGVPLSP 100
    SWAGGSRGDG NLQRRASQKE LRKSFARSKA IHVNRTYDEQ VTSRAQEPLS 150
    SVRRRALLRK ASSLPPTTAH ILSALLESRV NLPRYPPTAI DYKCHLKKHN 200
    ERQFFLELVK DISNDLDLTS LSYKILIFVC LMVDADRCSL FLVEGAAAGK 250
    KTLVSKFFDV HAGTPLLPCS STENSNEVQV PWGKGIIGYV GEHGETVNIP 300
    DAYQDRRFND EIDKLTGYKT KSLLCMPIRS SDGEIIGVAQ AINKIPEGAP 350
    FTEDDEKVMQ MYLPFCGIAI SNAQLFAASR KEYERSRALL EVVNDLFEEQ 400
    TDLEKIVKKI MHRAQTLLKC ERCSVLLLED IESPVVKFTK SFELMSPKCS 450
    ADAENSFKES MEKSSYSDWL INNSIAELVA STGLPVNISD AYQDPRFDAE 500
    ADQISGFHIR SVLCVPIWNS NHQIIGVAQV LNRLDGKPFD DADQRLFEAF 550
    VIFCGLGINN TIMYDQVKKS WAKQSVALDV LSYHATCSKA EVDKFKAANI 600
    PLVSELAIDD IHFDDFSLDV DAMITAALRM FMELGMVQKF KIDYETLCRW 650
    LLTVRKNYRM VLYHNWRHAF NVCQLMFAML TTAGFQDILT EVEILAVIVG 700
    CLCHDLDHRG TNNAFQAKSG SALAQLYGTS ATLEHHHFNH AVMILQSEGH 750
    NIFANLSSKE YSDLMQLLKQ SILATDLTLY FERRTEFFEL VSKGEYDWNI 800
    KNHRDIFRSM LMTACDLGAV TKPWEISRQV AELVTSEFFE QGDRERLELK 850
    LTPSAIFDRN RKDELPRLQL EWIDSICMPL YQALVKVNVK LKPMLDSVAT 900
    NRSKWEELHQ KRLLASTASS SPASVMVAKE DRN 933
    Length:933
    Mass (Da):104,752
    Last modified:May 18, 2010 - v2
    Checksum:iB725AE6963D6E799
    GO
    Isoform 2 (identifier: Q9HCR9-2) [UniParc]FASTAAdd to Basket

    Also known as: PDE11A3

    The sequence of this isoform differs from the canonical sequence as follows:
         1-250: Missing.
         251-304: KTLVSKFFDV...ETVNIPDAYQ → MLKQARRPLF...FLIQRQTKTK

    Show »
    Length:683
    Mass (Da):78,047
    Checksum:i82DD9BB77C941A1C
    GO
    Isoform 3 (identifier: Q9HCR9-3) [UniParc]FASTAAdd to Basket

    Also known as: PDE11A2

    The sequence of this isoform differs from the canonical sequence as follows:
         1-358: Missing.

    Show »
    Length:575
    Mass (Da):65,679
    Checksum:iA1DDA7F4BAF43221
    GO
    Isoform 4 (identifier: Q9HCR9-4) [UniParc]FASTAAdd to Basket

    Also known as: PDE11A1

    The sequence of this isoform differs from the canonical sequence as follows:
         1-444: Missing.

    Show »
    Length:489
    Mass (Da):55,700
    Checksum:i3E6ED2AAE9CBF03C
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti184 – 1841R → Q in BAB16371. (PubMed:10906126)Curated
    Sequence conflicti184 – 1841R → Q in BAB62712. (PubMed:11121118)Curated
    Sequence conflicti184 – 1841R → Q in AAI12394. (PubMed:15489334)Curated
    Sequence conflicti184 – 1841R → Q in AAI14432. (PubMed:15489334)Curated
    Sequence conflicti921 – 9211S → SS in BAB16371. (PubMed:10906126)Curated
    Sequence conflicti921 – 9211S → SS in BAB16372. (PubMed:10906126)Curated
    Sequence conflicti921 – 9211S → SS in CAB82573. (PubMed:10725373)Curated
    Sequence conflicti921 – 9211S → SS in AAG32023. (PubMed:11050148)Curated
    Sequence conflicti921 – 9211S → SS in CAC15567. (PubMed:11050148)Curated
    Sequence conflicti921 – 9211S → SS in BAB62712. (PubMed:11121118)Curated
    Sequence conflicti921 – 9211S → SS in BAB62713. (PubMed:11121118)Curated
    Sequence conflicti921 – 9211S → SS in BAB62714. (PubMed:11121118)Curated
    Sequence conflicti921 – 9211S → SS in AAI12394. (PubMed:15489334)Curated
    Sequence conflicti921 – 9211S → SS in AAI14432. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti804 – 8041R → H.1 Publication
    Corresponds to variant rs75127279 [ dbSNP | Ensembl ].
    VAR_027056
    Natural varianti867 – 8671R → G.1 Publication
    Corresponds to variant rs61306957 [ dbSNP | Ensembl ].
    VAR_027057

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 444444Missing in isoform 4. 1 PublicationVSP_019898Add
    BLAST
    Alternative sequencei1 – 358358Missing in isoform 3. 1 PublicationVSP_019899Add
    BLAST
    Alternative sequencei1 – 250250Missing in isoform 2. 2 PublicationsVSP_019900Add
    BLAST
    Alternative sequencei251 – 30454KTLVS…PDAYQ → MLKQARRPLFRNVLSATQWK KVKITRLVQISGASLAEKQE KHQDFLIQRQTKTK in isoform 2. 2 PublicationsVSP_019901Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB036704 mRNA. Translation: BAB16371.1.
    AB038041 mRNA. Translation: BAB16372.1.
    AJ251509 mRNA. Translation: CAB82573.1.
    AF281865 mRNA. Translation: AAG32023.1.
    AJ278682 mRNA. Translation: CAC15567.1.
    AB048423 Genomic DNA. Translation: BAB62712.1.
    AB048423 Genomic DNA. Translation: BAB62713.2.
    AB048423 Genomic DNA. Translation: BAB62714.1.
    AC073834 Genomic DNA. No translation available.
    AC073892 Genomic DNA. No translation available.
    AC083824 Genomic DNA. No translation available.
    AC011998 Genomic DNA. No translation available.
    AC012499 Genomic DNA. Translation: AAY14803.1.
    BC112393 mRNA. Translation: AAI12394.1.
    BC114431 mRNA. Translation: AAI14432.1.
    CCDSiCCDS33334.1. [Q9HCR9-1]
    CCDS42785.1. [Q9HCR9-2]
    CCDS42786.1. [Q9HCR9-4]
    CCDS46459.1. [Q9HCR9-3]
    RefSeqiNP_001070664.1. NM_001077196.1. [Q9HCR9-4]
    NP_001070665.1. NM_001077197.1. [Q9HCR9-2]
    NP_001070826.1. NM_001077358.1. [Q9HCR9-3]
    NP_058649.3. NM_016953.3. [Q9HCR9-1]
    UniGeneiHs.570273.

    Genome annotation databases

    EnsembliENST00000286063; ENSP00000286063; ENSG00000128655. [Q9HCR9-1]
    ENST00000358450; ENSP00000351232; ENSG00000128655. [Q9HCR9-2]
    ENST00000389683; ENSP00000374333; ENSG00000128655. [Q9HCR9-4]
    ENST00000409504; ENSP00000386539; ENSG00000128655. [Q9HCR9-3]
    GeneIDi50940.
    KEGGihsa:50940.
    UCSCiuc002ulp.3. human. [Q9HCR9-1]
    uc002ulr.3. human. [Q9HCR9-2]

    Polymorphism databases

    DMDMi296439264.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB036704 mRNA. Translation: BAB16371.1 .
    AB038041 mRNA. Translation: BAB16372.1 .
    AJ251509 mRNA. Translation: CAB82573.1 .
    AF281865 mRNA. Translation: AAG32023.1 .
    AJ278682 mRNA. Translation: CAC15567.1 .
    AB048423 Genomic DNA. Translation: BAB62712.1 .
    AB048423 Genomic DNA. Translation: BAB62713.2 .
    AB048423 Genomic DNA. Translation: BAB62714.1 .
    AC073834 Genomic DNA. No translation available.
    AC073892 Genomic DNA. No translation available.
    AC083824 Genomic DNA. No translation available.
    AC011998 Genomic DNA. No translation available.
    AC012499 Genomic DNA. Translation: AAY14803.1 .
    BC112393 mRNA. Translation: AAI12394.1 .
    BC114431 mRNA. Translation: AAI14432.1 .
    CCDSi CCDS33334.1. [Q9HCR9-1 ]
    CCDS42785.1. [Q9HCR9-2 ]
    CCDS42786.1. [Q9HCR9-4 ]
    CCDS46459.1. [Q9HCR9-3 ]
    RefSeqi NP_001070664.1. NM_001077196.1. [Q9HCR9-4 ]
    NP_001070665.1. NM_001077197.1. [Q9HCR9-2 ]
    NP_001070826.1. NM_001077358.1. [Q9HCR9-3 ]
    NP_058649.3. NM_016953.3. [Q9HCR9-1 ]
    UniGenei Hs.570273.

    3D structure databases

    ProteinModelPortali Q9HCR9.
    SMRi Q9HCR9. Positions 205-911.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9606.ENSP00000286063.

    Chemistry

    ChEMBLi CHEMBL2717.
    GuidetoPHARMACOLOGYi 1311.

    PTM databases

    PhosphoSitei Q9HCR9.

    Polymorphism databases

    DMDMi 296439264.

    Proteomic databases

    PaxDbi Q9HCR9.
    PRIDEi Q9HCR9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000286063 ; ENSP00000286063 ; ENSG00000128655 . [Q9HCR9-1 ]
    ENST00000358450 ; ENSP00000351232 ; ENSG00000128655 . [Q9HCR9-2 ]
    ENST00000389683 ; ENSP00000374333 ; ENSG00000128655 . [Q9HCR9-4 ]
    ENST00000409504 ; ENSP00000386539 ; ENSG00000128655 . [Q9HCR9-3 ]
    GeneIDi 50940.
    KEGGi hsa:50940.
    UCSCi uc002ulp.3. human. [Q9HCR9-1 ]
    uc002ulr.3. human. [Q9HCR9-2 ]

    Organism-specific databases

    CTDi 50940.
    GeneCardsi GC02M178487.
    HGNCi HGNC:8773. PDE11A.
    HPAi HPA034560.
    MIMi 604961. gene.
    610475. phenotype.
    neXtProti NX_Q9HCR9.
    Orphaneti 189439. Primary pigmented nodular adrenocortical disease.
    PharmGKBi PA33121.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG270709.
    HOVERGENi HBG101207.
    InParanoidi Q9HCR9.
    KOi K13298.
    OMAi DYSDLMQ.
    OrthoDBi EOG7RRF69.
    PhylomeDBi Q9HCR9.
    TreeFami TF316499.

    Enzyme and pathway databases

    BRENDAi 3.1.4.17. 2681.
    Reactomei REACT_19327. G alpha (s) signalling events.
    REACT_23767. cGMP effects.

    Miscellaneous databases

    GeneWikii PDE11A.
    GenomeRNAii 50940.
    NextBioi 53391.
    PROi Q9HCR9.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9HCR9.
    Bgeei Q9HCR9.
    CleanExi HS_PDE11A.
    Genevestigatori Q9HCR9.

    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 two novel phosphodiesterase PDE11A variants showing unique structure and tissue-specific expression."
      Yuasa K., Kotera J., Fujishige K., Michibata H., Sasaki T., Omori K.
      J. Biol. Chem. 275:31469-31479(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES.
      Tissue: Prostate.
    2. "Molecular cloning and characterization of a distinct human phosphodiesterase gene family: PDE11A."
      Fawcett L., Baxendale R., Stacey P., McGrouther C., Harrow I., Soderling S., Hetman J., Beavo J.A., Phillips S.C.
      Proc. Natl. Acad. Sci. U.S.A. 97:3702-3707(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, TISSUE SPECIFICITY.
      Tissue: Skeletal muscle.
    3. "Cloning and characterisation of two splice variants of human phosphodiesterase 11A."
      Hetman J.M., Robas N.M., Baxendale R., Fidock M., Phillips S.C., Soderling S.H., Beavo J.A.
      Proc. Natl. Acad. Sci. U.S.A. 97:12891-12895(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
    4. "Genomic organization of the human phosphodiesterase PDE11A gene: evolutionary relatedness with other PDEs containing GAF domains."
      Yuasa K., Kanoh Y., Okumura K., Omori K.
      Eur. J. Biochem. 268:168-178(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORMS 1; 2 AND 4), TISSUE SPECIFICITY.
    5. "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].
    6. "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 1).
    7. "3',5'-cyclic nucleotide phosphodiesterase 11A: localization in human tissues."
      Loughney K., Taylor J., Florio V.A.
      Int. J. Impot. Res. 17:320-325(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    8. "Phosphodiesterase 11 (PDE11): is it a player in human testicular function?"
      Francis S.H.
      Int. J. Impot. Res. 17:467-468(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION, TISSUE SPECIFICITY.
    9. "cAMP is a ligand for the tandem GAF domain of human phosphodiesterase 10 and cGMP for the tandem GAF domain of phosphodiesterase 11."
      Gross-Langenhoff M., Hofbauer K., Weber J., Schultz A., Schultz J.E.
      J. Biol. Chem. 281:2841-2846(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: DOMAIN, ENZYME REGULATION, MUTAGENESIS OF ASP-355.
    10. Cited for: INVOLVEMENT IN PPNAD2, TISSUE SPECIFICITY, VARIANTS HIS-804 AND GLY-867.
    11. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-239, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.

    Entry informationi

    Entry nameiPDE11_HUMAN
    AccessioniPrimary (citable) accession number: Q9HCR9
    Secondary accession number(s): Q14CD1
    , Q53T16, Q96S76, Q9GZY7, Q9HB46, Q9NY45
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 25, 2006
    Last sequence update: May 18, 2010
    Last modified: October 1, 2014
    This is version 104 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

    Allosteric enzyme, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 2
      Human chromosome 2: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3