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O95263

- PDE8B_HUMAN

UniProt

O95263 - PDE8B_HUMAN

Protein

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

Gene

PDE8B

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 145 (01 Oct 2014)
      Sequence version 2 (22 Aug 2003)
      Previous versions | rss
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    Functioni

    Hydrolyzes the second messenger cAMP, which is a key regulator of many important physiological processes. May be involved in specific signaling in the thyroid gland.

    Catalytic activityi

    Adenosine 3',5'-cyclic phosphate + H2O = adenosine 5'-phosphate.1 Publication

    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 dipyridimole. Insensitive to selective PDE inhibitors including rolipram and milrinone as well as to the non-selective inhibitor, IBMX. Unaffected by cGMP.1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei615 – 6151Proton donorBy similarity
    Metal bindingi619 – 6191Divalent metal cation 1By similarity
    Metal bindingi655 – 6551Divalent metal cation 1By similarity
    Metal bindingi656 – 6561Divalent metal cation 1By similarity
    Metal bindingi656 – 6561Divalent metal cation 2By similarity
    Metal bindingi781 – 7811Divalent metal cation 1By similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. cAMP catabolic process Source: UniProtKB-UniPathway
    2. cyclic nucleotide metabolic process Source: UniProtKB
    3. negative regulation of insulin secretion Source: Ensembl

    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 8B (EC:3.1.4.53)
    Short name:
    HsPDE8B
    Alternative name(s):
    Cell proliferation-inducing gene 22 protein
    Gene namesi
    Name:PDE8B
    ORF Names:PIG22
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:8794. PDE8B.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome

    Pathology & Biotechi

    Involvement in diseasei

    Striatal degeneration autosomal dominant (ADSD) [MIM:609161]: A movement disorder affecting the striatal part of the basal ganglia and characterized by bradykinesia, dysarthria and muscle rigidity. These symptoms resemble idiopathic Parkinson disease, but tremor is not present.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Primary pigmented nodular adrenocortical disease 3 (PPNAD3) [MIM:614190]: 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.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti305 – 3051H → P in PPNAD3; shows significantly higher cyclic AMP levels after transfection with the mutant protein than after transfection with the wild-type, indicating an impaired ability of the mutant protein to degrade cAMP. 1 Publication
    VAR_066503

    Keywords - Diseasei

    Cushing syndrome, Disease mutation

    Organism-specific databases

    MIMi609161. phenotype.
    614190. phenotype.
    Orphaneti228169. Autosomal dominant striatal neurodegeneration.
    189439. Primary pigmented nodular adrenocortical disease.
    PharmGKBiPA33142.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 885885High affinity cAMP-specific and IBMX-insensitive 3',5'-cyclic phosphodiesterase 8BPRO_0000198840Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei517 – 5171Phosphoserine2 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiO95263.
    PaxDbiO95263.
    PRIDEiO95263.

    2D gel databases

    UCD-2DPAGEO95263.

    PTM databases

    PhosphoSiteiO95263.

    Expressioni

    Tissue specificityi

    Abundantly expressed in the thyroid. Also very weakly expressed in brain, spinal cord and placenta. In the thyroid isoform 1 predominates, and isoforms 2 and 6 are also highly expressed. In the placenta isoforms 1 and 2 are expressed equally. In the brain isoform 2 predominates.2 Publications

    Gene expression databases

    ArrayExpressiO95263.
    BgeeiO95263.
    CleanExiHS_PDE8B.
    GenevestigatoriO95263.

    Organism-specific databases

    HPAiHPA036912.

    Interactioni

    Protein-protein interaction databases

    BioGridi114177. 1 interaction.
    STRINGi9606.ENSP00000264917.

    Structurei

    3D structure databases

    ProteinModelPortaliO95263.
    SMRiO95263. Positions 541-874.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini267 – 33872PASPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni590 – 868279CatalyticBy 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.
    InParanoidiO95263.
    KOiK01120.
    OMAiDHRQTQN.
    OrthoDBiEOG7X3QQM.
    PhylomeDBiO95263.
    TreeFamiTF314638.

    Family and domain databases

    Gene3Di1.10.1300.10. 1 hit.
    InterProiIPR003607. HD/PDEase_dom.
    IPR000014. PAS.
    IPR023088. PDEase.
    IPR002073. PDEase_catalytic_dom.
    IPR023174. PDEase_CS.
    IPR013938. PDEase_PDE8.
    IPR001789. Sig_transdc_resp-reg_receiver.
    [Graphical view]
    PfamiPF13426. PAS_9. 1 hit.
    PF08629. PDE8. 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: O95263-1) [UniParc]FASTAAdd to Basket

    Also known as: PDE8B1

    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

    MGCAPSIHVS QSGVIYCRDS DESSSPRQTT SVSQGPAAPL PGLFVQTDAA    50
    DAIPPSRASG PPSVARVRRA RTELGSGSSA GSAAPAATTS RGRRRHCCSS 100
    AEAETQTCYT SVKQVSSAEV RIGPMRLTQD PIQVLLIFAK EDSQSDGFWW 150
    ACDRAGYRCN IARTPESALE CFLDKHHEII VIDHRQTQNF DAEAVCRSIR 200
    ATNPSEHTVI LAVVSRVSDD HEEASVLPLL HAGFNRRFME NSSIIACYNE 250
    LIQIEHGEVR SQFKLRACNS VFTALDHCHE AIEITSDDHV IQYVNPAFER 300
    MMGYHKGELL GKELADLPKS DKNRADLLDT INTCIKKGKE WQGVYYARRK 350
    SGDSIQQHVK ITPVIGQGGK IRHFVSLKKL CCTTDNNKQI HKIHRDSGDN 400
    SQTEPHSFRY KNRRKESIDV KSISSRGSDA PSLQNRRYPS MARIHSMTIE 450
    APITKVINII NAAQENSPVT VAEALDRVLE ILRTTELYSP QLGTKDEDPH 500
    TSDLVGGLMT DGLRRLSGNE YVFTKNVHQS HSHLAMPITI NDVPPCISQL 550
    LDNEESWDFN IFELEAITHK RPLVYLGLKV FSRFGVCEFL NCSETTLRAW 600
    FQVIEANYHS SNAYHNSTHA ADVLHATAFF LGKERVKGSL DQLDEVAALI 650
    AATVHDVDHP GRTNSFLCNA GSELAVLYND TAVLESHHTA LAFQLTVKDT 700
    KCNIFKNIDR NHYRTLRQAI IDMVLATEMT KHFEHVNKFV NSINKPMAAE 750
    IEGSDCECNP AGKNFPENQI LIKRMMIKCA DVANPCRPLD LCIEWAGRIS 800
    EEYFAQTDEE KRQGLPVVMP VFDRNTCSIP KSQISFIDYF ITDMFDAWDA 850
    FAHLPALMQH LADNYKHWKT LDDLKCKSLR LPSDS 885

    Note: Major isoform.

    Length:885
    Mass (Da):98,979
    Last modified:August 22, 2003 - v2
    Checksum:iDB4F763E51F745A3
    GO
    Isoform 2 (identifier: O95263-2) [UniParc]FASTAAdd to Basket

    Also known as: PDE8B2, PDE8B3

    The sequence of this isoform differs from the canonical sequence as follows:
         293-389: Missing.

    Show »
    Length:788
    Mass (Da):87,974
    Checksum:i816AECACCAE45447
    GO
    Isoform 3 (identifier: O95263-3) [UniParc]FASTAAdd to Basket

    Also known as: PDE8B3

    The sequence of this isoform differs from the canonical sequence as follows:
         456-510: Missing.

    Show »
    Length:830
    Mass (Da):93,047
    Checksum:i5A39ED08E2A877E4
    GO
    Isoform 4 (identifier: O95263-4) [UniParc]FASTAAdd to Basket

    Also known as: PDE8B4

    The sequence of this isoform differs from the canonical sequence as follows:
         114-133: Missing.

    Show »
    Length:865
    Mass (Da):96,771
    Checksum:iDDC83E5525C7E7B7
    GO
    Isoform 5 (identifier: O95263-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-535: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:350
    Mass (Da):39,791
    Checksum:iA6D4F19BE26C045F
    GO
    Isoform 6 (identifier: O95263-6) [UniParc]FASTAAdd to Basket

    Also known as: PDE8B2

    The sequence of this isoform differs from the canonical sequence as follows:
         293-339: Missing.

    Show »
    Length:838
    Mass (Da):93,674
    Checksum:i013C790AC0F24F92
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti147 – 1471G → R in CAD38584. (PubMed:17974005)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti305 – 3051H → P in PPNAD3; shows significantly higher cyclic AMP levels after transfection with the mutant protein than after transfection with the wild-type, indicating an impaired ability of the mutant protein to degrade cAMP. 1 Publication
    VAR_066503

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 535535Missing in isoform 5. 2 PublicationsVSP_008081Add
    BLAST
    Alternative sequencei114 – 13320Missing in isoform 4. 1 PublicationVSP_008082Add
    BLAST
    Alternative sequencei293 – 38997Missing in isoform 2. 2 PublicationsVSP_008084Add
    BLAST
    Alternative sequencei293 – 33947Missing in isoform 6. 1 PublicationVSP_008083Add
    BLAST
    Alternative sequencei456 – 51055Missing in isoform 3. 1 PublicationVSP_008085Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY129948 mRNA. Translation: AAN71723.1.
    AY129949 mRNA. Translation: AAN71724.1.
    AY129950 Genomic DNA. Translation: AAN71725.1.
    AY129950 Genomic DNA. Translation: AAN71726.1.
    AY129950 Genomic DNA. Translation: AAN71727.1.
    AB085824 mRNA. Translation: BAC53762.1.
    AB085825 mRNA. Translation: BAC53763.1.
    AB085826 mRNA. Translation: BAC53764.1.
    AB085827 mRNA. Translation: BAC53765.1.
    AY423729 mRNA. Translation: AAS00492.1.
    CH471084 Genomic DNA. Translation: EAW95803.1.
    BC043209 mRNA. No translation available.
    AF079529 mRNA. Translation: AAC69564.2.
    AL831924 mRNA. Translation: CAD38584.1.
    CCDSiCCDS34190.1. [O95263-3]
    CCDS34191.1. [O95263-6]
    CCDS34192.1. [O95263-2]
    CCDS34193.1. [O95263-4]
    CCDS4037.1. [O95263-1]
    PIRiJE0293.
    RefSeqiNP_001025022.1. NM_001029851.2. [O95263-2]
    NP_001025023.1. NM_001029852.2. [O95263-3]
    NP_001025024.1. NM_001029853.2. [O95263-4]
    NP_001025025.1. NM_001029854.2. [O95263-6]
    NP_003710.1. NM_003719.3. [O95263-1]
    UniGeneiHs.584830.

    Genome annotation databases

    EnsembliENST00000264917; ENSP00000264917; ENSG00000113231. [O95263-1]
    ENST00000333194; ENSP00000331336; ENSG00000113231. [O95263-3]
    ENST00000340978; ENSP00000345446; ENSG00000113231. [O95263-6]
    ENST00000342343; ENSP00000345646; ENSG00000113231. [O95263-4]
    ENST00000346042; ENSP00000330428; ENSG00000113231. [O95263-2]
    ENST00000505283; ENSP00000423461; ENSG00000113231. [O95263-5]
    GeneIDi8622.
    KEGGihsa:8622.
    UCSCiuc003kfa.3. human. [O95263-1]
    uc003kfb.3. human. [O95263-4]
    uc003kfc.3. human. [O95263-3]
    uc003kfd.3. human. [O95263-6]
    uc003kfe.3. human. [O95263-2]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY129948 mRNA. Translation: AAN71723.1 .
    AY129949 mRNA. Translation: AAN71724.1 .
    AY129950 Genomic DNA. Translation: AAN71725.1 .
    AY129950 Genomic DNA. Translation: AAN71726.1 .
    AY129950 Genomic DNA. Translation: AAN71727.1 .
    AB085824 mRNA. Translation: BAC53762.1 .
    AB085825 mRNA. Translation: BAC53763.1 .
    AB085826 mRNA. Translation: BAC53764.1 .
    AB085827 mRNA. Translation: BAC53765.1 .
    AY423729 mRNA. Translation: AAS00492.1 .
    CH471084 Genomic DNA. Translation: EAW95803.1 .
    BC043209 mRNA. No translation available.
    AF079529 mRNA. Translation: AAC69564.2 .
    AL831924 mRNA. Translation: CAD38584.1 .
    CCDSi CCDS34190.1. [O95263-3 ]
    CCDS34191.1. [O95263-6 ]
    CCDS34192.1. [O95263-2 ]
    CCDS34193.1. [O95263-4 ]
    CCDS4037.1. [O95263-1 ]
    PIRi JE0293.
    RefSeqi NP_001025022.1. NM_001029851.2. [O95263-2 ]
    NP_001025023.1. NM_001029852.2. [O95263-3 ]
    NP_001025024.1. NM_001029853.2. [O95263-4 ]
    NP_001025025.1. NM_001029854.2. [O95263-6 ]
    NP_003710.1. NM_003719.3. [O95263-1 ]
    UniGenei Hs.584830.

    3D structure databases

    ProteinModelPortali O95263.
    SMRi O95263. Positions 541-874.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114177. 1 interaction.
    STRINGi 9606.ENSP00000264917.

    Chemistry

    BindingDBi O95263.
    ChEMBLi CHEMBL2363067.
    GuidetoPHARMACOLOGYi 1308.

    PTM databases

    PhosphoSitei O95263.

    2D gel databases

    UCD-2DPAGE O95263.

    Proteomic databases

    MaxQBi O95263.
    PaxDbi O95263.
    PRIDEi O95263.

    Protocols and materials databases

    DNASUi 8622.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000264917 ; ENSP00000264917 ; ENSG00000113231 . [O95263-1 ]
    ENST00000333194 ; ENSP00000331336 ; ENSG00000113231 . [O95263-3 ]
    ENST00000340978 ; ENSP00000345446 ; ENSG00000113231 . [O95263-6 ]
    ENST00000342343 ; ENSP00000345646 ; ENSG00000113231 . [O95263-4 ]
    ENST00000346042 ; ENSP00000330428 ; ENSG00000113231 . [O95263-2 ]
    ENST00000505283 ; ENSP00000423461 ; ENSG00000113231 . [O95263-5 ]
    GeneIDi 8622.
    KEGGi hsa:8622.
    UCSCi uc003kfa.3. human. [O95263-1 ]
    uc003kfb.3. human. [O95263-4 ]
    uc003kfc.3. human. [O95263-3 ]
    uc003kfd.3. human. [O95263-6 ]
    uc003kfe.3. human. [O95263-2 ]

    Organism-specific databases

    CTDi 8622.
    GeneCardsi GC05P076542.
    H-InvDB HIX0004971.
    HGNCi HGNC:8794. PDE8B.
    HPAi HPA036912.
    MIMi 603390. gene.
    609161. phenotype.
    614190. phenotype.
    neXtProti NX_O95263.
    Orphaneti 228169. Autosomal dominant striatal neurodegeneration.
    189439. Primary pigmented nodular adrenocortical disease.
    PharmGKBi PA33142.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG282089.
    HOVERGENi HBG053544.
    InParanoidi O95263.
    KOi K01120.
    OMAi DHRQTQN.
    OrthoDBi EOG7X3QQM.
    PhylomeDBi O95263.
    TreeFami TF314638.

    Enzyme and pathway databases

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

    Miscellaneous databases

    GeneWikii PDE8B.
    GenomeRNAii 8622.
    NextBioi 32309.
    PROi O95263.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O95263.
    Bgeei O95263.
    CleanExi HS_PDE8B.
    Genevestigatori O95263.

    Family and domain databases

    Gene3Di 1.10.1300.10. 1 hit.
    InterProi IPR003607. HD/PDEase_dom.
    IPR000014. PAS.
    IPR023088. PDEase.
    IPR002073. PDEase_catalytic_dom.
    IPR023174. PDEase_CS.
    IPR013938. PDEase_PDE8.
    IPR001789. Sig_transdc_resp-reg_receiver.
    [Graphical view ]
    Pfami PF13426. PAS_9. 1 hit.
    PF08629. PDE8. 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. "Genomic organization, chromosomal localization, and alternative splicing of the human phosphodiesterase 8B gene."
      Hayashi M., Shimada Y., Nishimura Y., Hama T., Tanaka T.
      Biochem. Biophys. Res. Commun. 297:1253-1258(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1; 2 AND 6), TISSUE SPECIFICITY.
    2. "Comparison of enzymatic characterization and gene organization of cyclic nucleotide phosphodiesterase 8 family in humans."
      Gamanuma M., Yuasa K., Sasaki T., Sakurai N., Kotera J., Omori K.
      Cell. Signal. 15:565-574(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), CATALYTIC ACTIVITY, ENZYME REGULATION, TISSUE SPECIFICITY.
      Tissue: Thyroid.
    3. "Identification of a human proliferation-inducing gene."
      Kim J.W.
      Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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 5).
      Tissue: Testis.
    6. "Molecular cloning and characterization of human PDE8B, a novel thyroid-specific isozyme of 3',5'-cyclic nucleotide phosphodiesterase."
      Hayashi M., Matsushima K., Ohashi H., Tsunoda H., Murase S., Kawarada Y., Tanaka T.
      Biochem. Biophys. Res. Commun. 250:751-756(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 227-885 (ISOFORM 1).
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 43-885 (ISOFORM 1).
      Tissue: Amygdala.
    8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-517, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. Cited for: INVOLVEMENT IN ADSD.
    10. "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-517, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "A cAMP-specific phosphodiesterase (PDE8B) that is mutated in adrenal hyperplasia is expressed widely in human and mouse tissues: a novel PDE8B isoform in human adrenal cortex."
      Horvath A., Giatzakis C., Tsang K., Greene E., Osorio P., Boikos S., Libe R., Patronas Y., Robinson-White A., Remmers E., Bertherat J., Nesterova M., Stratakis C.A.
      Eur. J. Hum. Genet. 16:1245-1253(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT PPNAD3 PRO-305, CHARACTERIZATION OF VARIANT PPNAD3 PRO-305.

    Entry informationi

    Entry nameiPDE8B_HUMAN
    AccessioniPrimary (citable) accession number: O95263
    Secondary accession number(s): Q5J7V7
    , Q86XK8, Q8IUJ7, Q8IUJ8, Q8IUJ9, Q8IUK0, Q8N3T2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: August 22, 2003
    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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 5
      Human chromosome 5: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3