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Q01064 (PDE1B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 134. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1B

Short name=Cam-PDE 1B
EC=3.1.4.17
Alternative name(s):
63 kDa Cam-PDE
Gene names
Name:PDE1B
Synonyms:PDE1B1, PDES1B
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length536 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.8

Catalytic activity

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

Cofactor

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. Ref.8

Enzyme regulation

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

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the cyclic nucleotide phosphodiesterase family. PDE1 subfamily.

Ontologies

Keywords
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
   LigandCalmodulin-binding
cAMP
cGMP
Metal-binding
   Molecular functionHydrolase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactivation of phospholipase C activity

Traceable author statement. Source: Reactome

apoptotic process

Traceable author statement Ref.1. Source: ProtInc

blood coagulation

Traceable author statement. Source: Reactome

cAMP catabolic process

Inferred from direct assay PubMed 14687666. Source: UniProtKB

cGMP catabolic process

Inferred from direct assay PubMed 14687666. Source: UniProtKB

cellular response to granulocyte macrophage colony-stimulating factor stimulus

Inferred from direct assay PubMed 14687666. Source: UniProtKB

cellular response to macrophage colony-stimulating factor stimulus

Inferred from direct assay PubMed 14687666. Source: UniProtKB

epidermal growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

fibroblast growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

innate immune response

Traceable author statement. Source: Reactome

locomotory behavior

Inferred from electronic annotation. Source: Ensembl

monocyte differentiation

Inferred from expression pattern PubMed 14687666. Source: UniProtKB

neurotrophin TRK receptor signaling pathway

Traceable author statement. Source: Reactome

regulation of dopamine metabolic process

Inferred from electronic annotation. Source: Ensembl

regulation of neurotransmitter levels

Inferred from electronic annotation. Source: Ensembl

response to amphetamine

Inferred from electronic annotation. Source: Ensembl

serotonin metabolic process

Inferred from electronic annotation. Source: Ensembl

signal transduction

Traceable author statement. Source: Reactome

visual learning

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

neuronal cell body

Inferred from electronic annotation. Source: Ensembl

   Molecular_function3',5'-cyclic-AMP phosphodiesterase activity

Inferred from electronic annotation. Source: Ensembl

calcium- and calmodulin-regulated 3',5'-cyclic-GMP phosphodiesterase activity

Inferred from electronic annotation. Source: Ensembl

calmodulin-dependent cyclic-nucleotide phosphodiesterase activity

Traceable author statement Ref.2. Source: ProtInc

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform PDE1B1 (identifier: Q01064-1)

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.
Isoform PDE1B2 (identifier: Q01064-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 536536Calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1B
PRO_0000198789

Regions

Region27 – 4721Calmodulin-binding Potential
Region197 – 496300Catalytic By similarity

Sites

Active site2231Proton donor By similarity
Metal binding2271Divalent metal cation 1
Metal binding2631Divalent metal cation 1
Metal binding2641Divalent metal cation 1
Metal binding2641Divalent metal cation 2
Metal binding3701Divalent metal cation 1

Amino acid modifications

Modified residue4661Phosphoserine By similarity

Natural variations

Alternative sequence1 – 1818MELSP…ESDCP → MANPVPVQRSHLQGPILR in isoform PDE1B2.
VSP_038643
Alternative sequence19 – 3820Missing in isoform PDE1B2.
VSP_038644

Experimental info

Sequence conflict225 – 2262QI → SM in AAA58405. Ref.2
Sequence conflict3371S → A in AAA58405. Ref.2

Secondary structure

................................................ 536
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform PDE1B1 [UniParc].

Last modified July 15, 1998. Version 2.
Checksum: D15211AC32C756A4

FASTA53661,380
        10         20         30         40         50         60 
MELSPRSPPE MLEESDCPSP LELKSAPSKK MWIKLRSLLR YMVKQLENGE INIEELKKNL 

        70         80         90        100        110        120 
EYTASLLEAV YIDETRQILD TEDELQELRS DAVPSEVRDW LASTFTQQAR AKGRRAEEKP 

       130        140        150        160        170        180 
KFRSIVHAVQ AGIFVERMFR RTYTSVGPTY STAVLNCLKN LDLWCFDVFS LNQAADDHAL 

       190        200        210        220        230        240 
RTIVFELLTR HNLISRFKIP TVFLMSFLDA LETGYGKYKN PYHNQIHAAD VTQTVHCFLL 

       250        260        270        280        290        300 
RTGMVHCLSE IELLAIIFAA AIHDYEHTGT TNSFHIQTKS ECAIVYNDRS VLENHHISSV 

       310        320        330        340        350        360 
FRLMQDDEMN IFINLTKDEF VELRALVIEM VLATDMSCHF QQVKTMKTAL QQLERIDKPK 

       370        380        390        400        410        420 
ALSLLLHAAD ISHPTKQWLV HSRWTKALME EFFRQGDKEA ELGLPFSPLC DRTSTLVAQS 

       430        440        450        460        470        480 
QIGFIDFIVE PTFSVLTDVA EKSVQPLADE DSKSKNQPSF QWRQPSLDVE VGDPNPDVVS 

       490        500        510        520        530 
FRSTWVKRIQ ENKQKWKERA ASGITNQMSI DELSPCEEEA PPSPAEDEHN QNGNLD 

« Hide

Isoform PDE1B2 [UniParc].

Checksum: 0A9093462479DC5C
Show »

FASTA51659,051

References

« Hide 'large scale' references
[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]"Identification and characterisation of a human calmodulin-stimulated phosphodiesterase PDE1B1."
Yu J., Frazier A.L.B., Wolda S.L., Florio V.A., Martins T.J., Snyder P.B., Harris E.A.S., McCaw K.N., Farrell C.A., Steiner B., Bentley J.K., Beavo J.A., Ferguson K., Gelinas R.
Cell. Signal. 9:519-529(1997) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"A glutamine switch mechanism for nucleotide selectivity by phosphodiesterases."
Zhang K.Y.J., Card G.L., Suzuki Y., Artis D.R., Fong D., Gillette S., Hsieh D., Neiman J., West B.L., Zhang C., Milburn M.V., Kim S.-H., Schlessinger J., Bollag G.
Mol. Cell 15:279-286(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.77 ANGSTROMS) OF 146-506 IN COMPLEX WITH METAL IONS, COFACTOR, FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRJC6129.
RefSeqNP_000915.1. NM_000924.3.
NP_001159447.1. NM_001165975.2.
NP_001275697.1. NM_001288768.1.
NP_001275698.1. NM_001288769.1.
UniGeneHs.530871.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1LXRmodel-A158-461[»]
1TAZX-ray1.77A146-506[»]
ProteinModelPortalQ01064.
SMRQ01064. Positions 73-502.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111179. 2 interactions.
IntActQ01064. 1 interaction.
STRING9606.ENSP00000243052.

Chemistry

BindingDBQ01064.
ChEMBLCHEMBL4425.
GuidetoPHARMACOLOGY1295.

PTM databases

PhosphoSiteQ01064.

Polymorphism databases

DMDM3183514.

Proteomic databases

PaxDbQ01064.
PRIDEQ01064.

Protocols and materials databases

DNASU5153.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000243052; ENSP00000243052; ENSG00000123360. [Q01064-1]
ENST00000550620; ENSP00000448519; ENSG00000123360. [Q01064-2]
GeneID5153.
KEGGhsa:5153.
UCSCuc001sgd.2. human. [Q01064-1]
uc001sge.3. human. [Q01064-2]

Organism-specific databases

CTD5153.
GeneCardsGC12P054943.
HGNCHGNC:8775. PDE1B.
HPAHPA018492.
MIM171891. gene.
neXtProtNX_Q01064.
PharmGKBPA33123.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG139098.
HOGENOMHOG000231888.
HOVERGENHBG056120.
InParanoidQ01064.
KOK13755.
OMASTAVHNC.
OrthoDBEOG7X9G6J.
PhylomeDBQ01064.
TreeFamTF314638.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_116125. Disease.
REACT_604. Hemostasis.
REACT_6900. Immune System.

Gene expression databases

ArrayExpressQ01064.
BgeeQ01064.
CleanExHS_PDE1B.
GenevestigatorQ01064.

Family and domain databases

Gene3D1.10.1300.10. 2 hits.
InterProIPR003607. HD/PDEase_dom.
IPR023088. PDEase.
IPR002073. PDEase_catalytic_dom.
IPR023174. PDEase_CS.
IPR013706. PDEase_N.
[Graphical view]
PfamPF00233. PDEase_I. 1 hit.
PF08499. PDEase_I_N. 1 hit.
[Graphical view]
PRINTSPR00387. PDIESTERASE1.
SMARTSM00471. HDc. 1 hit.
[Graphical view]
PROSITEPS00126. PDEASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ01064.
GeneWikiPDE1B.
GenomeRNAi5153.
NextBio19926.
PROQ01064.
SOURCESearch...

Entry information

Entry namePDE1B_HUMAN
AccessionPrimary (citable) accession number: Q01064
Secondary accession number(s): Q92825, Q96KP3
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: July 15, 1998
Last modified: April 16, 2014
This is version 134 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM