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Q13370

- PDE3B_HUMAN

UniProt

Q13370 - PDE3B_HUMAN

Protein

cGMP-inhibited 3',5'-cyclic phosphodiesterase B

Gene

PDE3B

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 140 (01 Oct 2014)
      Sequence version 2 (03 Apr 2007)
      Previous versions | rss
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    Functioni

    Cyclic nucleotide phosphodiesterase with a dual-specificity for the second messengers cAMP and cGMP, which are key regulators of many important physiological processes. May play a role in fat metabolism. Regulates cAMP binding of RAPGEF3. Through simultaneous binding to RAPGEF3 and PIK3R6 assembles a signaling complex in which the PI3K gamma complex is activated by RAPGEF3 and which is involved in angiogenesis.2 Publications

    Catalytic activityi

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

    Cofactori

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

    Enzyme regulationi

    Inhibited by cGMP.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei737 – 7371Proton donorBy similarity
    Metal bindingi741 – 7411Divalent metal cation 1
    Metal bindingi821 – 8211Divalent metal cation 1
    Metal bindingi822 – 8221Divalent metal cation 1
    Metal bindingi822 – 8221Divalent metal cation 2
    Metal bindingi937 – 9371Divalent metal cation 1

    GO - Molecular functioni

    1. 3',5'-cyclic-nucleotide phosphodiesterase activity Source: BHF-UCL
    2. cGMP-inhibited cyclic-nucleotide phosphodiesterase activity Source: ProtInc
    3. metal ion binding Source: UniProtKB-KW
    4. protein binding Source: IntAct
    5. protein kinase B binding Source: BHF-UCL

    GO - Biological processi

    1. angiogenesis Source: UniProtKB-KW
    2. blood coagulation Source: Reactome
    3. cAMP catabolic process Source: BHF-UCL
    4. cellular response to insulin stimulus Source: BHF-UCL
    5. endocrine pancreas development Source: Ensembl
    6. glucose homeostasis Source: Ensembl
    7. insulin receptor signaling pathway Source: Reactome
    8. negative regulation of angiogenesis Source: UniProtKB
    9. negative regulation of cAMP-mediated signaling Source: BHF-UCL
    10. negative regulation of cell adhesion Source: BHF-UCL
    11. negative regulation of cell adhesion mediated by integrin Source: BHF-UCL
    12. negative regulation of lipid catabolic process Source: BHF-UCL
    13. regulation of insulin secretion Source: Ensembl

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Angiogenesis

    Keywords - Ligandi

    cAMP, cGMP, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_1451. PDE3B signalling.
    REACT_19327. G alpha (s) signalling events.
    REACT_23767. cGMP effects.
    SignaLinkiQ13370.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    cGMP-inhibited 3',5'-cyclic phosphodiesterase B (EC:3.1.4.17)
    Alternative name(s):
    CGIPDE1
    Short name:
    CGIP1
    Cyclic GMP-inhibited phosphodiesterase B
    Short name:
    CGI-PDE B
    Gene namesi
    Name:PDE3B
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:8779. PDE3B.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. endoplasmic reticulum Source: BHF-UCL
    3. Golgi apparatus Source: BHF-UCL
    4. guanyl-nucleotide exchange factor complex Source: BHF-UCL
    5. integral component of membrane Source: UniProtKB-KW
    6. membrane Source: UniProtKB

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi2 – 21R → A: Abolishes interaction with RAPGEF3. 1 Publication
    Mutagenesisi3 – 31R → A: Abolishes interaction with RAPGEF3. 1 Publication
    Mutagenesisi6 – 61R → A: Abolishes interaction with RAPGEF3. 1 Publication
    Mutagenesisi8 – 81A → D: Impairs interaction with RAPGEF3. 1 Publication
    Mutagenesisi9 – 91K → A: Abolishes interaction with RAPGEF3. 1 Publication
    Mutagenesisi10 – 101A → D: Impairss interaction with RAPGEF3. 1 Publication
    Mutagenesisi12 – 121R → A: Abolishes interaction with RAPGEF3. 1 Publication
    Mutagenesisi439 – 4391R → A: Impairss interaction with PIK3R6. 1 Publication
    Mutagenesisi440 – 4401R → A: Impairss interaction with PIK3R6. 1 Publication
    Mutagenesisi445 – 4451S → A: Impairss interaction with PIK3R6. 1 Publication
    Mutagenesisi449 – 4491P → A: Impairss interaction with PIK3R6. 1 Publication

    Organism-specific databases

    PharmGKBiPA33127.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 11121112cGMP-inhibited 3',5'-cyclic phosphodiesterase BPRO_0000198802Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei295 – 2951Phosphoserine; by PKB/AKT1 or PKB/AKT2By similarity
    Modified residuei442 – 4421Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ13370.
    PaxDbiQ13370.
    PRIDEiQ13370.

    PTM databases

    PhosphoSiteiQ13370.

    Expressioni

    Tissue specificityi

    Abundant in adipose tissues.

    Gene expression databases

    ArrayExpressiQ13370.
    BgeeiQ13370.
    CleanExiHS_PDE3B.
    GenevestigatoriQ13370.

    Organism-specific databases

    HPAiCAB009497.
    HPA024342.

    Interactioni

    Subunit structurei

    Interacts with PIK3CG By similarity. Interacts with RAPGEF3 and PIK3R6.By similarity2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PIK3CGP487363EBI-6172856,EBI-1030384
    PIK3R6Q5UE933EBI-6172856,EBI-6172907
    RAPGEF3O953988EBI-6172856,EBI-6172806

    Protein-protein interaction databases

    BioGridi111166. 3 interactions.
    IntActiQ13370. 3 interactions.
    STRINGi9606.ENSP00000282096.

    Structurei

    Secondary structure

    1
    1112
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi662 – 67413
    Helixi681 – 6888
    Helixi689 – 6946
    Helixi695 – 70612
    Helixi709 – 7124
    Helixi717 – 72812
    Beta strandi735 – 7384
    Helixi739 – 75214
    Helixi802 – 8043
    Helixi808 – 82013
    Turni821 – 8244
    Helixi830 – 8356
    Helixi839 – 8435
    Turni844 – 8463
    Helixi849 – 86315
    Helixi866 – 8683
    Turni870 – 8734
    Helixi876 – 89116
    Helixi895 – 8973
    Helixi898 – 90912
    Beta strandi911 – 9133
    Helixi922 – 93716
    Helixi940 – 9423
    Helixi945 – 96824
    Helixi984 – 99411
    Helixi996 – 100510
    Beta strandi1012 – 10154
    Beta strandi1055 – 10584
    Helixi1060 – 107213

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1SO2X-ray2.40A/B/C/D654-1073[»]
    1SOJX-ray2.90A/B/C/D/E/F/G/H/I/J/K/L654-1073[»]
    ProteinModelPortaliQ13370.
    SMRiQ13370. Positions 656-1073.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ13370.

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei88 – 10821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei117 – 13721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei152 – 17221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei192 – 21221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei220 – 24021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei247 – 26721HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 2525Interaction with RAPGEF3Add
    BLAST
    Regioni436 – 46025Interaction with PIK3R6Add
    BLAST
    Regioni713 – 1072360CatalyticBy similarityAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi1077 – 10804Poly-Glu

    Sequence similaritiesi

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG145074.
    HOGENOMiHOG000060144.
    HOVERGENiHBG053541.
    InParanoidiQ13370.
    KOiK13296.
    OMAiSIHESEY.
    PhylomeDBiQ13370.
    TreeFamiTF329631.

    Family and domain databases

    Gene3Di1.10.1300.10. 2 hits.
    InterProiIPR003607. HD/PDEase_dom.
    IPR002073. PDEase_catalytic_dom.
    IPR023174. PDEase_CS.
    [Graphical view]
    PfamiPF00233. PDEase_I. 1 hit.
    [Graphical view]
    SMARTiSM00471. HDc. 1 hit.
    [Graphical view]
    PROSITEiPS00126. PDEASE_I. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q13370-1) [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

    MRRDERDAKA MRSLQPPDGA GSPPESLRNG YVKSCVSPLR QDPPRGFFFH     50
    LCRFCNVELR PPPASPQQPR RCSPFCRARL SLGALAAFVL ALLLGAEPES 100
    WAAGAAWLRT LLSVCSHSLS PLFSIACAFF FLTCFLTRTK RGPGPGRSCG 150
    SWWLLALPAC CYLGDFLVWQ WWSWPWGDGD AGSAAPHTPP EAAAGRLLLV 200
    LSCVGLLLTL AHPLRLRHCV LVLLLASFVW WVSFTSLGSL PSALRPLLSG 250
    LVGGAGCLLA LGLDHFFQIR EAPLHPRLSS AAEEKVPVIR PRRRSSCVSL 300
    GETAASYYGS CKIFRRPSLP CISREQMILW DWDLKQWYKP HYQNSGGGNG 350
    VDLSVLNEAR NMVSDLLTDP SLPPQVISSL RSISSLMGAF SGSCRPKINP 400
    LTPFPGFYPC SEIEDPAEKG DRKLNKGLNR NSLPTPQLRR SSGTSGLLPV 450
    EQSSRWDRNN GKRPHQEFGI SSQGCYLNGP FNSNLLTIPK QRSSSVSLTH 500
    HVGLRRAGVL SSLSPVNSSN HGPVSTGSLT NRSPIEFPDT ADFLNKPSVI 550
    LQRSLGNAPN TPDFYQQLRN SDSNLCNSCG HQMLKYVSTS ESDGTDCCSG 600
    KSGEEENIFS KESFKLMETQ QEEETEKKDS RKLFQEGDKW LTEEAQSEQQ 650
    TNIEQEVSLD LILVEEYDSL IEKMSNWNFP IFELVEKMGE KSGRILSQVM 700
    YTLFQDTGLL EIFKIPTQQF MNYFRALENG YRDIPYHNRI HATDVLHAVW 750
    YLTTRPVPGL QQIHNGCGTG NETDSDGRIN HGRIAYISSK SCSNPDESYG 800
    CLSSNIPALE LMALYVAAAM HDYDHPGRTN AFLVATNAPQ AVLYNDRSVL 850
    ENHHAASAWN LYLSRPEYNF LLHLDHVEFK RFRFLVIEAI LATDLKKHFD 900
    FLAEFNAKAN DVNSNGIEWS NENDRLLVCQ VCIKLADING PAKVRDLHLK 950
    WTEGIVNEFY EQGDEEANLG LPISPFMDRS SPQLAKLQES FITHIVGPLC 1000
    NSYDAAGLLP GQWLEAEEDN DTESGDDEDG EELDTEDEEM ENNLNPKPPR 1050
    RKSRRRIFCQ LMHHLTENHK IWKEIVEEEE KCKADGNKLQ VENSSLPQAD 1100
    EIQVIEEADE EE 1112
    Length:1,112
    Mass (Da):124,333
    Last modified:April 3, 2007 - v2
    Checksum:i55451C3DA142EF6A
    GO
    Isoform 2 (identifier: Q13370-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         376-426: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:1,061
    Mass (Da):118,809
    Checksum:i755DBD55004867DC
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti84 – 841A → D in AAC50724. (PubMed:8884271)Curated
    Sequence conflicti84 – 841A → D in BAA09306. (PubMed:8706823)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti87 – 871A → V.1 Publication
    Corresponds to variant rs1056584 [ dbSNP | Ensembl ].
    VAR_031462

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei376 – 42651Missing in isoform 2. 1 PublicationVSP_054138Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U38178 Genomic DNA. Translation: AAC50724.1.
    D50640 Genomic DNA. Translation: BAA09306.1.
    X95520 mRNA. Translation: CAA64774.1.
    AY459346 mRNA. Translation: AAR24292.1.
    AC018795 Genomic DNA. No translation available.
    AC087207 Genomic DNA. No translation available.
    AC090835 Genomic DNA. No translation available.
    CH471064 Genomic DNA. Translation: EAW68474.1.
    BC136565 mRNA. Translation: AAI36566.1.
    BC136566 mRNA. Translation: AAI36567.1.
    BC144248 mRNA. Translation: AAI44249.1.
    CCDSiCCDS7817.1. [Q13370-1]
    PIRiS70522.
    RefSeqiNP_000913.2. NM_000922.3. [Q13370-1]
    UniGeneiHs.445711.

    Genome annotation databases

    EnsembliENST00000282096; ENSP00000282096; ENSG00000152270. [Q13370-1]
    ENST00000455098; ENSP00000388644; ENSG00000152270. [Q13370-2]
    GeneIDi5140.
    KEGGihsa:5140.
    UCSCiuc001mln.3. human. [Q13370-1]

    Polymorphism databases

    DMDMi143811435.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U38178 Genomic DNA. Translation: AAC50724.1 .
    D50640 Genomic DNA. Translation: BAA09306.1 .
    X95520 mRNA. Translation: CAA64774.1 .
    AY459346 mRNA. Translation: AAR24292.1 .
    AC018795 Genomic DNA. No translation available.
    AC087207 Genomic DNA. No translation available.
    AC090835 Genomic DNA. No translation available.
    CH471064 Genomic DNA. Translation: EAW68474.1 .
    BC136565 mRNA. Translation: AAI36566.1 .
    BC136566 mRNA. Translation: AAI36567.1 .
    BC144248 mRNA. Translation: AAI44249.1 .
    CCDSi CCDS7817.1. [Q13370-1 ]
    PIRi S70522.
    RefSeqi NP_000913.2. NM_000922.3. [Q13370-1 ]
    UniGenei Hs.445711.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1SO2 X-ray 2.40 A/B/C/D 654-1073 [» ]
    1SOJ X-ray 2.90 A/B/C/D/E/F/G/H/I/J/K/L 654-1073 [» ]
    ProteinModelPortali Q13370.
    SMRi Q13370. Positions 656-1073.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111166. 3 interactions.
    IntActi Q13370. 3 interactions.
    STRINGi 9606.ENSP00000282096.

    Chemistry

    BindingDBi Q13370.
    ChEMBLi CHEMBL2095153.
    GuidetoPHARMACOLOGYi 1299.

    PTM databases

    PhosphoSitei Q13370.

    Polymorphism databases

    DMDMi 143811435.

    Proteomic databases

    MaxQBi Q13370.
    PaxDbi Q13370.
    PRIDEi Q13370.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000282096 ; ENSP00000282096 ; ENSG00000152270 . [Q13370-1 ]
    ENST00000455098 ; ENSP00000388644 ; ENSG00000152270 . [Q13370-2 ]
    GeneIDi 5140.
    KEGGi hsa:5140.
    UCSCi uc001mln.3. human. [Q13370-1 ]

    Organism-specific databases

    CTDi 5140.
    GeneCardsi GC11P014621.
    HGNCi HGNC:8779. PDE3B.
    HPAi CAB009497.
    HPA024342.
    MIMi 602047. gene.
    neXtProti NX_Q13370.
    PharmGKBi PA33127.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG145074.
    HOGENOMi HOG000060144.
    HOVERGENi HBG053541.
    InParanoidi Q13370.
    KOi K13296.
    OMAi SIHESEY.
    PhylomeDBi Q13370.
    TreeFami TF329631.

    Enzyme and pathway databases

    Reactomei REACT_1451. PDE3B signalling.
    REACT_19327. G alpha (s) signalling events.
    REACT_23767. cGMP effects.
    SignaLinki Q13370.

    Miscellaneous databases

    ChiTaRSi PDE3B. human.
    EvolutionaryTracei Q13370.
    GenomeRNAii 5140.
    NextBioi 19820.
    PROi Q13370.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q13370.
    Bgeei Q13370.
    CleanExi HS_PDE3B.
    Genevestigatori Q13370.

    Family and domain databases

    Gene3Di 1.10.1300.10. 2 hits.
    InterProi IPR003607. HD/PDEase_dom.
    IPR002073. PDEase_catalytic_dom.
    IPR023174. PDEase_CS.
    [Graphical view ]
    Pfami PF00233. PDEase_I. 1 hit.
    [Graphical view ]
    SMARTi SM00471. HDc. 1 hit.
    [Graphical view ]
    PROSITEi PS00126. PDEASE_I. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Characterization of the cDNA and gene encoding human PDE3B, the cGIP1 isoform of the human cyclic GMP-inhibited cyclic nucleotide phosphodiesterase family."
      Miki T., Taira M., Hockman S., Shimada F., Lieman J., Napolitano M., Ward D., Taira M., Makino H., Manganiello V.C.
      Genomics 36:476-485(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Tissue: Adipose tissue.
    2. "Differential expression of cGMP-inhibited cyclic nucleotide phosphodiesterases in human hepatoma cell lines."
      Murata T., Taira M., Manganiello V.C.
      FEBS Lett. 390:29-33(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Molecular cloning and chromosomal assignment of the human homologue of the rat cGMP-inhibited phosphodiesterase 1 (PDE3A) -- a gene involved in fat metabolism located at 11p15.1."
      Loebbert R.W., Winterpacht A., Seipel B., Zabel B.U.
      Genomics 37:211-218(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT VAL-87.
    4. "Importance of cAMP-response element-binding protein in regulation of expression of the murine cyclic nucleotide phosphodiesterase 3B (Pde3b) gene in differentiating 3T3-L1 preadipocytes."
      Liu H., Tang J.R., Choi Y.H., Napolitano M., Hockman S., Taira M., Degerman E., Manganiello V.C.
      J. Biol. Chem. 281:21096-21113(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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] (ISOFORMS 1 AND 2).
    8. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-442, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "A phosphodiesterase 3B-based signaling complex integrates exchange protein activated by cAMP 1 and phosphatidylinositol 3-kinase signals in human arterial endothelial cells."
      Wilson L.S., Baillie G.S., Pritchard L.M., Umana B., Terrin A., Zaccolo M., Houslay M.D., Maurice D.H.
      J. Biol. Chem. 286:16285-16296(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH RAPGEF3 AND PIK3R6, MUTAGENESIS OF ARG-2; ARG-3; ARG-6; ALA-8; LYS-9; ALA-10; ARG-12; ARG-439; ARG-440; SER-445 AND PRO-449.
    11. "Crystal structure of human phosphodiesterase 3B: atomic basis for substrate and inhibitor specificity."
      Scapin G., Patel S.B., Chung C., Varnerin J.P., Edmondson S.D., Mastracchio A., Parmee E.R., Singh S.B., Becker J.W., Van der Ploeg L.H., Tota M.R.
      Biochemistry 43:6091-6100(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 654-1073 IN COMPLEX WITH METAL IONS AND INHIBITORS, FUNCTION, COFACTOR.

    Entry informationi

    Entry nameiPDE3B_HUMAN
    AccessioniPrimary (citable) accession number: Q13370
    Secondary accession number(s): B7ZM37
    , O00639, Q14408, Q6SEI4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: April 3, 2007
    Last modified: October 1, 2014
    This is version 140 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 11
      Human chromosome 11: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3