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)

O60658

- PDE8A_HUMAN

UniProt

O60658 - PDE8A_HUMAN

Protein

High affinity cAMP-specific and IBMX-insensitive 3',5'-cyclic phosphodiesterase 8A

Gene

PDE8A

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 154 (01 Oct 2014)
      Sequence version 2 (19 Sep 2002)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Hydrolyzes the second messenger cAMP, which is a key regulator of many important physiological processes. May be involved in maintaining basal levels of the cyclic nucleotide and/or in the cAMP regulation of germ cell development.1 Publication

    Catalytic activityi

    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.1 Publication

    Enzyme regulationi

    Inhibited by dipyridimole. Insensitive to selective PDE inhibitors including rolipram and zaprinast as well as to the non-selective inhibitor, IBMX. Unaffected by cGMP.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei556 – 5561Proton donorBy similarity
    Metal bindingi560 – 5601Divalent metal cation 1
    Metal bindingi596 – 5961Divalent metal cation 1
    Metal bindingi597 – 5971Divalent metal cation 1
    Metal bindingi597 – 5971Divalent metal cation 2
    Metal bindingi726 – 7261Divalent metal cation 1

    GO - Molecular functioni

    1. 3',5'-cyclic-AMP phosphodiesterase activity Source: Ensembl
    2. 3',5'-cyclic-nucleotide phosphodiesterase activity Source: UniProtKB
    3. metal ion binding Source: UniProtKB-KW
    4. phosphorelay response regulator activity Source: InterPro

    GO - Biological processi

    1. cAMP catabolic process Source: UniProtKB-UniPathway
    2. cyclic nucleotide metabolic process Source: UniProtKB
    3. regulation of transcription, DNA-templated Source: InterPro

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    cAMP, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_19327. G alpha (s) signalling events.
    UniPathwayiUPA00762; UER00747.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    High affinity cAMP-specific and IBMX-insensitive 3',5'-cyclic phosphodiesterase 8A (EC:3.1.4.53)
    Gene namesi
    Name:PDE8A
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 15

    Organism-specific databases

    HGNCiHGNC:8793. PDE8A.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. extracellular vesicular exosome Source: UniProt

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi748 – 7481Y → F: Increases sensitivity to several nonselective or family selective PDE inhibitors. 1 Publication

    Organism-specific databases

    PharmGKBiPA33141.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 829829High affinity cAMP-specific and IBMX-insensitive 3',5'-cyclic phosphodiesterase 8APRO_0000198838Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei20 – 201Phosphoserine1 Publication
    Modified residuei359 – 3591Phosphoserine; by PKA1 Publication
    Modified residuei457 – 4571Phosphoserine3 Publications
    Modified residuei461 – 4611PhosphotyrosineBy similarity

    Post-translational modificationi

    Phosphorylated at Ser-359 by PKA under elevated cAMP conditions, this enhances catalytic activity.4 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiO60658.
    PaxDbiO60658.
    PRIDEiO60658.

    PTM databases

    PhosphoSiteiO60658.

    Expressioni

    Tissue specificityi

    Expressed in most tissues except thymus and peripheral blood leukocytes. Highest levels in testis, ovary, small intestine and colon.

    Gene expression databases

    ArrayExpressiO60658.
    BgeeiO60658.
    CleanExiHS_PDE8A.
    GenevestigatoriO60658.

    Organism-specific databases

    HPAiHPA007722.

    Interactioni

    Protein-protein interaction databases

    BioGridi111177. 3 interactions.
    IntActiO60658. 2 interactions.
    STRINGi9606.ENSP00000311453.

    Structurei

    Secondary structure

    1
    829
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi486 – 4916
    Turni492 – 4965
    Beta strandi497 – 4993
    Helixi502 – 5087
    Helixi513 – 52412
    Helixi528 – 5314
    Helixi535 – 54713
    Beta strandi553 – 5575
    Helixi558 – 57215
    Helixi575 – 5784
    Helixi583 – 59513
    Turni596 – 5994
    Helixi605 – 6106
    Helixi614 – 6185
    Turni619 – 6213
    Helixi624 – 63815
    Turni641 – 6433
    Turni645 – 6484
    Helixi651 – 66616
    Helixi670 – 6723
    Helixi673 – 68311
    Helixi685 – 6917
    Helixi692 – 6943
    Helixi698 – 70811
    Helixi711 – 72616
    Helixi729 – 7313
    Helixi734 – 75825
    Turni769 – 7713
    Helixi774 – 78411
    Helixi786 – 79712
    Helixi800 – 81415

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1LHQmodel-A482-821[»]
    1LXXmodel-A488-821[»]
    3ECMX-ray1.90A482-819[»]
    3ECNX-ray2.10A/B482-819[»]
    ProteinModelPortaliO60658.
    SMRiO60658. Positions 482-819.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO60658.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini213 – 28371PASPROSITE-ProRule annotationAdd
    BLAST
    Domaini287 – 32943PACAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni531 – 813283CatalyticBy similarityAdd
    BLAST

    Domaini

    Composed of a C-terminal catalytic domain containing two putative divalent metal sites and an N-terminal regulatory domain.

    Sequence similaritiesi

    Contains 1 PAS (PER-ARNT-SIM) domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG282089.
    HOVERGENiHBG053544.
    InParanoidiO60658.
    KOiK01120.
    OMAiQTGKHKD.
    OrthoDBiEOG7X3QQM.
    PhylomeDBiO60658.
    TreeFamiTF314638.

    Family and domain databases

    Gene3Di1.10.1300.10. 1 hit.
    InterProiIPR003607. HD/PDEase_dom.
    IPR000014. PAS.
    IPR013767. PAS_fold.
    IPR023088. PDEase.
    IPR002073. PDEase_catalytic_dom.
    IPR023174. PDEase_CS.
    IPR001789. Sig_transdc_resp-reg_receiver.
    [Graphical view]
    PfamiPF00989. PAS. 1 hit.
    PF00233. PDEase_I. 1 hit.
    PF00072. Response_reg. 1 hit.
    [Graphical view]
    PRINTSiPR00387. PDIESTERASE1.
    SMARTiSM00471. HDc. 1 hit.
    SM00091. PAS. 1 hit.
    [Graphical view]
    SUPFAMiSSF55785. SSF55785. 1 hit.
    TIGRFAMsiTIGR00229. sensory_box. 1 hit.
    PROSITEiPS50112. PAS. 1 hit.
    PS00126. PDEASE_I. 1 hit.
    [Graphical view]

    Sequences (6)i

    Sequence statusi: Complete.

    This entry describes 6 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O60658-1) [UniParc]FASTAAdd to Basket

    Also known as: PDE8A1

    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

    MGCAPSIHIS ERLVAEDAPS PAAPPLSSGG PRLPQGQKTA ALPRTRGAGL    50
    LESELRDGSG KKVAVADVQF GPMRFHQDQL QVLLVFTKED NQCNGFCRAC 100
    EKAGFKCTVT KEAQAVLACF LDKHHDIIII DHRNPRQLDA EALCRSIRSS 150
    KLSENTVIVG VVRRVDREEL SVMPFISAGF TRRYVENPNI MACYNELLQL 200
    EFGEVRSQLK LRACNSVFTA LENSEDAIEI TSEDRFIQYA NPAFETTMGY 250
    QSGELIGKEL GEVPINEKKA DLLDTINSCI RIGKEWQGIY YAKKKNGDNI 300
    QQNVKIIPVI GQGGKIRHYV SIIRVCNGNN KAEKISECVQ SDTHTDNQTG 350
    KHKDRRKGSL DVKAVASRAT EVSSQRRHSS MARIHSMTIE APITKVINII 400
    NAAQESSPMP VTEALDRVLE ILRTTELYSP QFGAKDDDPH ANDLVGGLMS 450
    DGLRRLSGNE YVLSTKNTQM VSSNIITPIS LDDVPPRIAR AMENEEYWDF 500
    DIFELEAATH NRPLIYLGLK MFARFGICEF LHCSESTLRS WLQIIEANYH 550
    SSNPYHNSTH SADVLHATAY FLSKERIKET LDPIDEVAAL IAATIHDVDH 600
    PGRTNSFLCN AGSELAILYN DTAVLESHHA ALAFQLTTGD DKCNIFKNME 650
    RNDYRTLRQG IIDMVLATEM TKHFEHVNKF VNSINKPLAT LEENGETDKN 700
    QEVINTMLRT PENRTLIKRM LIKCADVSNP CRPLQYCIEW AARISEEYFS 750
    QTDEEKQQGL PVVMPVFDRN TCSIPKSQIS FIDYFITDMF DAWDAFVDLP 800
    DLMQHLDNNF KYWKGLDEMK LRNLRPPPE 829
    Length:829
    Mass (Da):93,304
    Last modified:September 19, 2002 - v2
    Checksum:i99BD05EA185A42CD
    GO
    Isoform 2 (identifier: O60658-2) [UniParc]FASTAAdd to Basket

    Also known as: PDE8A2

    The sequence of this isoform differs from the canonical sequence as follows:
         239-284: Missing.

    Show »
    Length:783
    Mass (Da):88,293
    Checksum:i67BB1FBE670D7EFE
    GO
    Isoform 3 (identifier: O60658-3) [UniParc]FASTAAdd to Basket

    Also known as: PDE8A3

    The sequence of this isoform differs from the canonical sequence as follows:
         213-231: ACNSVFTALENSEDAIEIT → SGKEFTMQKRKTEIIYNKM
         232-829: Missing.

    Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay. No experimental confirmation available.

    Show »
    Length:231
    Mass (Da):25,744
    Checksum:iD7E21A8D19D661A6
    GO
    Isoform 4 (identifier: O60658-4) [UniParc]FASTAAdd to Basket

    Also known as: PDE8A4

    The sequence of this isoform differs from the canonical sequence as follows:
         212-228: RACNSVFTALENSEDAI → SMQILHLKQQWAISQVN
         229-829: Missing.

    Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay. No experimental confirmation available.

    Show »
    Length:228
    Mass (Da):25,279
    Checksum:i4667A08AAA57F17F
    GO
    Isoform 5 (identifier: O60658-5) [UniParc]FASTAAdd to Basket

    Also known as: PDE8A5

    The sequence of this isoform differs from the canonical sequence as follows:
         239-272: YANPAFETTMGYQSGELIGKELGEVPINEKKADL → PCCSSSWFGAAHIPSSAPVEVGVGLLPSWSLRRT
         273-829: Missing.

    Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay. No experimental confirmation available.

    Show »
    Length:272
    Mass (Da):29,852
    Checksum:iFEECE2A0C9115E13
    GO
    Isoform 6 (identifier: O60658-6) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-72: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:757
    Mass (Da):86,049
    Checksum:i66EB20F0822E42AC
    GO

    Sequence cautioni

    The sequence BAG54458.1 differs from that shown. Reason: Intron retention.
    The sequence EAX01967.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti55 – 551L → V in AAK57641. (PubMed:11371644)Curated
    Sequence conflicti344 – 3441H → R in AAK57641. (PubMed:11371644)Curated
    Sequence conflicti344 – 3441H → R in AAC39763. (PubMed:9618252)Curated
    Sequence conflicti399 – 3991I → V in AAK57641. (PubMed:11371644)Curated
    Sequence conflicti399 – 3991I → V in AAC39763. (PubMed:9618252)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti112 – 1121E → G.2 Publications
    Corresponds to variant rs17855018 [ dbSNP | Ensembl ].
    VAR_069109

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 7272Missing in isoform 6. 1 PublicationVSP_046017Add
    BLAST
    Alternative sequencei212 – 22817RACNS…SEDAI → SMQILHLKQQWAISQVN in isoform 4. 1 PublicationVSP_041674Add
    BLAST
    Alternative sequencei213 – 23119ACNSV…AIEIT → SGKEFTMQKRKTEIIYNKM in isoform 3. 1 PublicationVSP_041675Add
    BLAST
    Alternative sequencei229 – 829601Missing in isoform 4. 1 PublicationVSP_041676Add
    BLAST
    Alternative sequencei232 – 829598Missing in isoform 3. 1 PublicationVSP_041677Add
    BLAST
    Alternative sequencei239 – 28446Missing in isoform 2. 2 PublicationsVSP_004597Add
    BLAST
    Alternative sequencei239 – 27234YANPA…KKADL → PCCSSSWFGAAHIPSSAPVE VGVGLLPSWSLRRT in isoform 5. 1 PublicationVSP_041678Add
    BLAST
    Alternative sequencei273 – 829557Missing in isoform 5. 1 PublicationVSP_041679Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF388183 mRNA. Translation: AAL18610.1.
    AF388184 mRNA. Translation: AAL18611.1.
    AF388185 mRNA. Translation: AAL18612.1. Sequence problems.
    AF388186 mRNA. Translation: AAL18613.1. Sequence problems.
    AF388187 mRNA. Translation: AAL18614.1. Sequence problems.
    AF332653 mRNA. Translation: AAK57641.1.
    AK074280 mRNA. No translation available.
    AK127232 mRNA. Translation: BAG54458.1. Sequence problems.
    AC027078 Genomic DNA. No translation available.
    AC087468 Genomic DNA. No translation available.
    CH471101 Genomic DNA. Translation: EAX01967.1. Sequence problems.
    BC060762 mRNA. Translation: AAH60762.1.
    BC075822 mRNA. Translation: AAH75822.1.
    AF056490 mRNA. Translation: AAC39763.1.
    AL109687 mRNA. Translation: CAB52020.1.
    AL109778 mRNA. Translation: CAB52432.1.
    CCDSiCCDS10336.1. [O60658-1]
    CCDS10337.1. [O60658-2]
    CCDS58397.1. [O60658-6]
    PIRiJW0088.
    RefSeqiNP_001230066.1. NM_001243137.1. [O60658-6]
    NP_002596.1. NM_002605.2. [O60658-1]
    NP_775656.1. NM_173454.1. [O60658-2]
    XP_006720630.1. XM_006720567.1.
    UniGeneiHs.9333.

    Genome annotation databases

    EnsembliENST00000310298; ENSP00000311453; ENSG00000073417. [O60658-1]
    ENST00000339708; ENSP00000340679; ENSG00000073417. [O60658-2]
    ENST00000394553; ENSP00000378056; ENSG00000073417. [O60658-1]
    ENST00000478717; ENSP00000432309; ENSG00000073417. [O60658-4]
    ENST00000557957; ENSP00000453808; ENSG00000073417. [O60658-6]
    GeneIDi5151.
    KEGGihsa:5151.
    UCSCiuc002blh.3. human. [O60658-1]
    uc002bli.3. human. [O60658-2]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF388183 mRNA. Translation: AAL18610.1 .
    AF388184 mRNA. Translation: AAL18611.1 .
    AF388185 mRNA. Translation: AAL18612.1 . Sequence problems.
    AF388186 mRNA. Translation: AAL18613.1 . Sequence problems.
    AF388187 mRNA. Translation: AAL18614.1 . Sequence problems.
    AF332653 mRNA. Translation: AAK57641.1 .
    AK074280 mRNA. No translation available.
    AK127232 mRNA. Translation: BAG54458.1 . Sequence problems.
    AC027078 Genomic DNA. No translation available.
    AC087468 Genomic DNA. No translation available.
    CH471101 Genomic DNA. Translation: EAX01967.1 . Sequence problems.
    BC060762 mRNA. Translation: AAH60762.1 .
    BC075822 mRNA. Translation: AAH75822.1 .
    AF056490 mRNA. Translation: AAC39763.1 .
    AL109687 mRNA. Translation: CAB52020.1 .
    AL109778 mRNA. Translation: CAB52432.1 .
    CCDSi CCDS10336.1. [O60658-1 ]
    CCDS10337.1. [O60658-2 ]
    CCDS58397.1. [O60658-6 ]
    PIRi JW0088.
    RefSeqi NP_001230066.1. NM_001243137.1. [O60658-6 ]
    NP_002596.1. NM_002605.2. [O60658-1 ]
    NP_775656.1. NM_173454.1. [O60658-2 ]
    XP_006720630.1. XM_006720567.1.
    UniGenei Hs.9333.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1LHQ model - A 482-821 [» ]
    1LXX model - A 488-821 [» ]
    3ECM X-ray 1.90 A 482-819 [» ]
    3ECN X-ray 2.10 A/B 482-819 [» ]
    ProteinModelPortali O60658.
    SMRi O60658. Positions 482-819.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111177. 3 interactions.
    IntActi O60658. 2 interactions.
    STRINGi 9606.ENSP00000311453.

    Chemistry

    BindingDBi O60658.
    ChEMBLi CHEMBL4640.
    GuidetoPHARMACOLOGYi 1307.

    PTM databases

    PhosphoSitei O60658.

    Proteomic databases

    MaxQBi O60658.
    PaxDbi O60658.
    PRIDEi O60658.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000310298 ; ENSP00000311453 ; ENSG00000073417 . [O60658-1 ]
    ENST00000339708 ; ENSP00000340679 ; ENSG00000073417 . [O60658-2 ]
    ENST00000394553 ; ENSP00000378056 ; ENSG00000073417 . [O60658-1 ]
    ENST00000478717 ; ENSP00000432309 ; ENSG00000073417 . [O60658-4 ]
    ENST00000557957 ; ENSP00000453808 ; ENSG00000073417 . [O60658-6 ]
    GeneIDi 5151.
    KEGGi hsa:5151.
    UCSCi uc002blh.3. human. [O60658-1 ]
    uc002bli.3. human. [O60658-2 ]

    Organism-specific databases

    CTDi 5151.
    GeneCardsi GC15P085523.
    H-InvDB HIX0012539.
    HGNCi HGNC:8793. PDE8A.
    HPAi HPA007722.
    MIMi 602972. gene.
    neXtProti NX_O60658.
    PharmGKBi PA33141.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG282089.
    HOVERGENi HBG053544.
    InParanoidi O60658.
    KOi K01120.
    OMAi QTGKHKD.
    OrthoDBi EOG7X3QQM.
    PhylomeDBi O60658.
    TreeFami TF314638.

    Enzyme and pathway databases

    UniPathwayi UPA00762 ; UER00747 .
    Reactomei REACT_19327. G alpha (s) signalling events.

    Miscellaneous databases

    ChiTaRSi PDE8A. human.
    EvolutionaryTracei O60658.
    GeneWikii PDE8A.
    GenomeRNAii 5151.
    NextBioi 19878.
    PROi O60658.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O60658.
    Bgeei O60658.
    CleanExi HS_PDE8A.
    Genevestigatori O60658.

    Family and domain databases

    Gene3Di 1.10.1300.10. 1 hit.
    InterProi IPR003607. HD/PDEase_dom.
    IPR000014. PAS.
    IPR013767. PAS_fold.
    IPR023088. PDEase.
    IPR002073. PDEase_catalytic_dom.
    IPR023174. PDEase_CS.
    IPR001789. Sig_transdc_resp-reg_receiver.
    [Graphical view ]
    Pfami PF00989. PAS. 1 hit.
    PF00233. PDEase_I. 1 hit.
    PF00072. Response_reg. 1 hit.
    [Graphical view ]
    PRINTSi PR00387. PDIESTERASE1.
    SMARTi SM00471. HDc. 1 hit.
    SM00091. PAS. 1 hit.
    [Graphical view ]
    SUPFAMi SSF55785. SSF55785. 1 hit.
    TIGRFAMsi TIGR00229. sensory_box. 1 hit.
    PROSITEi PS50112. PAS. 1 hit.
    PS00126. PDEASE_I. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Human phosphodiesterase 8A splice variants: cloning, gene organization, and tissue distribution."
      Wang P., Wu P., Egan R.W., Billah M.M.
      Gene 280:183-194(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4 AND 5).
      Tissue: Testis.
    2. "T cell activation up-regulates cyclic nucleotide phosphodiesterases 8A1 and 7A3."
      Glavas N.A., Ostenson C., Schaefer J.B., Vasta V., Beavo J.A.
      Proc. Natl. Acad. Sci. U.S.A. 98:6319-6324(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    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] (ISOFORM 6), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 381-829 (ISOFORM 1), VARIANT GLY-112.
      Tissue: Hippocampus.
    4. "Analysis of the DNA sequence and duplication history of human chromosome 15."
      Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A.
      , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
      Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. 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), VARIANT GLY-112.
      Tissue: Liver and Placenta.
    7. "Isolation and characterization of PDE8A, a novel human cAMP-specific phosphodiesterase."
      Fisher D.A., Smith J.F., Pillar J.S., St Denis S.H., Cheng J.B.
      Biochem. Biophys. Res. Commun. 246:570-577(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 117-829 (ISOFORMS 1 AND 2).
    8. The European IMAGE consortium
      Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 554-829.
    9. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20 AND SER-457, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-457, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-457, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "Cyclic AMP-specific phosphodiesterase, PDE8A1, is activated by protein kinase A-mediated phosphorylation."
      Brown K.M., Lee L.C., Findlay J.E., Day J.P., Baillie G.S.
      FEBS Lett. 586:1631-1637(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-359.
    13. "Kinetic and structural studies of phosphodiesterase-8A and implication on the inhibitor selectivity."
      Wang H., Yan Z., Yang S., Cai J., Robinson H., Ke H.
      Biochemistry 47:12760-12768(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 482-819 IN COMPLEX WITH METAL IONS AND THE INHIBITOR IBMX, FUNCTION, COFACTOR, MUTAGENESIS OF TYR-748.

    Entry informationi

    Entry nameiPDE8A_HUMAN
    AccessioniPrimary (citable) accession number: O60658
    Secondary accession number(s): B3KXE6
    , H0YMZ7, Q6P9H3, Q969I1, Q96PC9, Q96PD0, Q96PD1, Q96T71, Q9UMB7, Q9UMC3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1999
    Last sequence update: September 19, 2002
    Last modified: October 1, 2014
    This is version 154 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, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 15
      Human chromosome 15: 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