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Q01064

- PDE1B_HUMAN

UniProt

Q01064 - PDE1B_HUMAN

Protein

Calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1B

Gene

PDE1B

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 139 (01 Oct 2014)
      Sequence version 2 (15 Jul 1998)
      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. Has a preference for cGMP as a substrate.1 Publication

    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

    Type I PDE are activated by the binding of calmodulin in the presence of Ca2+.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei223 – 2231Proton donorBy similarity
    Metal bindingi227 – 2271Divalent metal cation 1
    Metal bindingi263 – 2631Divalent metal cation 1
    Metal bindingi264 – 2641Divalent metal cation 1
    Metal bindingi264 – 2641Divalent metal cation 2
    Metal bindingi370 – 3701Divalent metal cation 1

    GO - Molecular functioni

    1. 3',5'-cyclic-AMP phosphodiesterase activity Source: Ensembl
    2. calcium- and calmodulin-regulated 3',5'-cyclic-GMP phosphodiesterase activity Source: Ensembl
    3. calmodulin-dependent cyclic-nucleotide phosphodiesterase activity Source: ProtInc
    4. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. activation of phospholipase C activity Source: Reactome
    2. apoptotic process Source: ProtInc
    3. blood coagulation Source: Reactome
    4. cAMP catabolic process Source: UniProtKB
    5. cellular response to granulocyte macrophage colony-stimulating factor stimulus Source: UniProtKB
    6. cellular response to macrophage colony-stimulating factor stimulus Source: UniProtKB
    7. cGMP catabolic process Source: UniProtKB
    8. epidermal growth factor receptor signaling pathway Source: Reactome
    9. fibroblast growth factor receptor signaling pathway Source: Reactome
    10. innate immune response Source: Reactome
    11. locomotory behavior Source: Ensembl
    12. monocyte differentiation Source: UniProtKB
    13. neurotrophin TRK receptor signaling pathway Source: Reactome
    14. regulation of dopamine metabolic process Source: Ensembl
    15. regulation of neurotransmitter levels Source: Ensembl
    16. response to amphetamine Source: Ensembl
    17. serotonin metabolic process Source: Ensembl
    18. signal transduction Source: Reactome
    19. visual learning Source: Ensembl

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    Calmodulin-binding, cAMP, cGMP, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_15408. Cam-PDE 1 activation.
    REACT_19327. G alpha (s) signalling events.
    REACT_23767. cGMP effects.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1B (EC:3.1.4.17)
    Short name:
    Cam-PDE 1B
    Alternative name(s):
    63 kDa Cam-PDE
    Gene namesi
    Name:PDE1B
    Synonyms:PDE1B1, PDES1B
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:8775. PDE1B.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. neuronal cell body Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA33123.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 536536Calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1BPRO_0000198789Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei466 – 4661PhosphoserineBy similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ01064.
    PaxDbiQ01064.
    PRIDEiQ01064.

    PTM databases

    PhosphoSiteiQ01064.

    Expressioni

    Gene expression databases

    ArrayExpressiQ01064.
    BgeeiQ01064.
    CleanExiHS_PDE1B.
    GenevestigatoriQ01064.

    Organism-specific databases

    HPAiHPA018492.

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Protein-protein interaction databases

    BioGridi111179. 2 interactions.
    IntActiQ01064. 1 interaction.
    STRINGi9606.ENSP00000243052.

    Structurei

    Secondary structure

    1
    536
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi152 – 1587
    Turni159 – 1624
    Helixi168 – 1747
    Helixi179 – 19012
    Helixi193 – 1964
    Helixi201 – 21515
    Turni216 – 2183
    Beta strandi221 – 2244
    Helixi225 – 24218
    Helixi244 – 2474
    Helixi250 – 26213
    Turni263 – 2664
    Helixi272 – 2787
    Helixi281 – 2866
    Helixi291 – 30313
    Helixi307 – 3093
    Turni311 – 3144
    Helixi317 – 33216
    Helixi336 – 3383
    Helixi339 – 35113
    Helixi358 – 37013
    Helixi373 – 3753
    Helixi378 – 40225
    Helixi414 – 42714
    Helixi429 – 44416
    Helixi476 – 50126

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1LXRmodel-A158-461[»]
    1TAZX-ray1.77A146-506[»]
    ProteinModelPortaliQ01064.
    SMRiQ01064. Positions 146-502.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ01064.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni27 – 4721Calmodulin-bindingSequence AnalysisAdd
    BLAST
    Regioni197 – 496300CatalyticBy similarityAdd
    BLAST

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiNOG139098.
    HOGENOMiHOG000231888.
    HOVERGENiHBG056120.
    InParanoidiQ01064.
    KOiK13755.
    OMAiSTAVHNC.
    OrthoDBiEOG7X9G6J.
    PhylomeDBiQ01064.
    TreeFamiTF314638.

    Family and domain databases

    Gene3Di1.10.1300.10. 2 hits.
    InterProiIPR003607. HD/PDEase_dom.
    IPR023088. PDEase.
    IPR002073. PDEase_catalytic_dom.
    IPR023174. PDEase_CS.
    IPR013706. PDEase_N.
    [Graphical view]
    PfamiPF00233. PDEase_I. 1 hit.
    PF08499. PDEase_I_N. 1 hit.
    [Graphical view]
    PRINTSiPR00387. PDIESTERASE1.
    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 PDE1B1 (identifier: Q01064-1) [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

    MELSPRSPPE MLEESDCPSP LELKSAPSKK MWIKLRSLLR YMVKQLENGE    50
    INIEELKKNL EYTASLLEAV YIDETRQILD TEDELQELRS DAVPSEVRDW 100
    LASTFTQQAR AKGRRAEEKP KFRSIVHAVQ AGIFVERMFR RTYTSVGPTY 150
    STAVLNCLKN LDLWCFDVFS LNQAADDHAL RTIVFELLTR HNLISRFKIP 200
    TVFLMSFLDA LETGYGKYKN PYHNQIHAAD VTQTVHCFLL RTGMVHCLSE 250
    IELLAIIFAA AIHDYEHTGT TNSFHIQTKS ECAIVYNDRS VLENHHISSV 300
    FRLMQDDEMN IFINLTKDEF VELRALVIEM VLATDMSCHF QQVKTMKTAL 350
    QQLERIDKPK ALSLLLHAAD ISHPTKQWLV HSRWTKALME EFFRQGDKEA 400
    ELGLPFSPLC DRTSTLVAQS QIGFIDFIVE PTFSVLTDVA EKSVQPLADE 450
    DSKSKNQPSF QWRQPSLDVE VGDPNPDVVS FRSTWVKRIQ ENKQKWKERA 500
    ASGITNQMSI DELSPCEEEA PPSPAEDEHN QNGNLD 536
    Length:536
    Mass (Da):61,380
    Last modified:July 15, 1998 - v2
    Checksum:iD15211AC32C756A4
    GO
    Isoform PDE1B2 (identifier: Q01064-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-18: MELSPRSPPEMLEESDCP → MANPVPVQRSHLQGPILR
         19-38: Missing.

    Show »
    Length:516
    Mass (Da):59,051
    Checksum:i0A9093462479DC5C
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti225 – 2262QI → SM in AAA58405. (PubMed:9419816)Curated
    Sequence conflicti337 – 3371S → A in AAA58405. (PubMed:9419816)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 1818MELSP…ESDCP → MANPVPVQRSHLQGPILR in isoform PDE1B2. 2 PublicationsVSP_038643Add
    BLAST
    Alternative sequencei19 – 3820Missing in isoform PDE1B2. 2 PublicationsVSP_038644Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U56976 mRNA. Translation: AAC50769.1.
    U86078 mRNA. Translation: AAC51872.1.
    AJ401609 mRNA. Translation: CAC82207.1.
    AK302931 mRNA. Translation: BAG64092.1.
    CH471054 Genomic DNA. Translation: EAW96790.1.
    BC032226 mRNA. Translation: AAH32226.1.
    M94539 mRNA. Translation: AAA58405.1.
    CCDSiCCDS53800.1. [Q01064-2]
    CCDS8882.1. [Q01064-1]
    PIRiJC6129.
    RefSeqiNP_000915.1. NM_000924.3. [Q01064-1]
    NP_001159447.1. NM_001165975.2. [Q01064-2]
    NP_001275697.1. NM_001288768.1.
    NP_001275698.1. NM_001288769.1.
    UniGeneiHs.530871.

    Genome annotation databases

    EnsembliENST00000243052; ENSP00000243052; ENSG00000123360. [Q01064-1]
    ENST00000550620; ENSP00000448519; ENSG00000123360. [Q01064-2]
    GeneIDi5153.
    KEGGihsa:5153.
    UCSCiuc001sgd.2. human. [Q01064-1]
    uc001sge.3. human. [Q01064-2]

    Polymorphism databases

    DMDMi3183514.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U56976 mRNA. Translation: AAC50769.1 .
    U86078 mRNA. Translation: AAC51872.1 .
    AJ401609 mRNA. Translation: CAC82207.1 .
    AK302931 mRNA. Translation: BAG64092.1 .
    CH471054 Genomic DNA. Translation: EAW96790.1 .
    BC032226 mRNA. Translation: AAH32226.1 .
    M94539 mRNA. Translation: AAA58405.1 .
    CCDSi CCDS53800.1. [Q01064-2 ]
    CCDS8882.1. [Q01064-1 ]
    PIRi JC6129.
    RefSeqi NP_000915.1. NM_000924.3. [Q01064-1 ]
    NP_001159447.1. NM_001165975.2. [Q01064-2 ]
    NP_001275697.1. NM_001288768.1.
    NP_001275698.1. NM_001288769.1.
    UniGenei Hs.530871.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1LXR model - A 158-461 [» ]
    1TAZ X-ray 1.77 A 146-506 [» ]
    ProteinModelPortali Q01064.
    SMRi Q01064. Positions 146-502.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111179. 2 interactions.
    IntActi Q01064. 1 interaction.
    STRINGi 9606.ENSP00000243052.

    Chemistry

    BindingDBi Q01064.
    ChEMBLi CHEMBL4425.
    GuidetoPHARMACOLOGYi 1295.

    PTM databases

    PhosphoSitei Q01064.

    Polymorphism databases

    DMDMi 3183514.

    Proteomic databases

    MaxQBi Q01064.
    PaxDbi Q01064.
    PRIDEi Q01064.

    Protocols and materials databases

    DNASUi 5153.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000243052 ; ENSP00000243052 ; ENSG00000123360 . [Q01064-1 ]
    ENST00000550620 ; ENSP00000448519 ; ENSG00000123360 . [Q01064-2 ]
    GeneIDi 5153.
    KEGGi hsa:5153.
    UCSCi uc001sgd.2. human. [Q01064-1 ]
    uc001sge.3. human. [Q01064-2 ]

    Organism-specific databases

    CTDi 5153.
    GeneCardsi GC12P054943.
    HGNCi HGNC:8775. PDE1B.
    HPAi HPA018492.
    MIMi 171891. gene.
    neXtProti NX_Q01064.
    PharmGKBi PA33123.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG139098.
    HOGENOMi HOG000231888.
    HOVERGENi HBG056120.
    InParanoidi Q01064.
    KOi K13755.
    OMAi STAVHNC.
    OrthoDBi EOG7X9G6J.
    PhylomeDBi Q01064.
    TreeFami TF314638.

    Enzyme and pathway databases

    Reactomei REACT_15408. Cam-PDE 1 activation.
    REACT_19327. G alpha (s) signalling events.
    REACT_23767. cGMP effects.

    Miscellaneous databases

    EvolutionaryTracei Q01064.
    GeneWikii PDE1B.
    GenomeRNAii 5153.
    NextBioi 19926.
    PROi Q01064.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q01064.
    Bgeei Q01064.
    CleanExi HS_PDE1B.
    Genevestigatori Q01064.

    Family and domain databases

    Gene3Di 1.10.1300.10. 2 hits.
    InterProi IPR003607. HD/PDEase_dom.
    IPR023088. PDEase.
    IPR002073. PDEase_catalytic_dom.
    IPR023174. PDEase_CS.
    IPR013706. PDEase_N.
    [Graphical view ]
    Pfami PF00233. PDEase_I. 1 hit.
    PF08499. PDEase_I_N. 1 hit.
    [Graphical view ]
    PRINTSi PR00387. PDIESTERASE1.
    SMARTi SM00471. HDc. 1 hit.
    [Graphical view ]
    PROSITEi PS00126. PDEASE_I. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Inhibition of calmodulin-dependent phosphodiesterase induces apoptosis in human leukemic cells."
      Jiang X., Li J., Paskind M., Epstein P.M.
      Proc. Natl. Acad. Sci. U.S.A. 93:11236-11241(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PDE1B1).
    2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PDE1B1).
      Tissue: Brain.
    3. "Isolation and differential tissue distribution of two human cDNAs encoding PDE1 splice variants."
      Fidock M.D., Miller M., Lanfear J.
      Cell. Signal. 14:53-60(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PDE1B2).
      Tissue: Testis.
    4. "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 PDE1B2).
      Tissue: Testis.
    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 PDE1B1).
      Tissue: Brain.
    7. "A polymerase chain reaction strategy to identify and clone cyclic nucleotide phosphodiesterase cDNAs. Molecular cloning of the cDNA encoding the 63-kDa calmodulin-dependent phosphodiesterase."
      Repaske D.R., Swinnen J.V., Jin S.-L.C., van Wyk J.J., Conti M.
      J. Biol. Chem. 267:18683-18688(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 222-337.
    8. Cited for: X-RAY CRYSTALLOGRAPHY (1.77 ANGSTROMS) OF 146-506 IN COMPLEX WITH METAL IONS, COFACTOR, FUNCTION.

    Entry informationi

    Entry nameiPDE1B_HUMAN
    AccessioniPrimary (citable) accession number: Q01064
    Secondary accession number(s): Q92825, Q96KP3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: July 15, 1998
    Last modified: October 1, 2014
    This is version 139 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 12
      Human chromosome 12: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3