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Q01064

- PDE1B_HUMAN

UniProt

Q01064 - PDE1B_HUMAN

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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

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

a divalent metal cation1 PublicationNote: 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
Complete GO annotation...

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
Complete GO annotation...

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

BgeeiQ01064.
CleanExiHS_PDE1B.
ExpressionAtlasiQ01064. baseline and differential.
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 – 1587Combined sources
Turni159 – 1624Combined sources
Helixi168 – 1747Combined sources
Helixi179 – 19012Combined sources
Helixi193 – 1964Combined sources
Helixi201 – 21515Combined sources
Turni216 – 2183Combined sources
Beta strandi221 – 2244Combined sources
Helixi225 – 24218Combined sources
Helixi244 – 2474Combined sources
Helixi250 – 26213Combined sources
Turni263 – 2664Combined sources
Helixi272 – 2787Combined sources
Helixi281 – 2866Combined sources
Helixi291 – 30313Combined sources
Helixi307 – 3093Combined sources
Turni311 – 3144Combined sources
Helixi317 – 33216Combined sources
Helixi336 – 3383Combined sources
Helixi339 – 35113Combined sources
Helixi358 – 37013Combined sources
Helixi373 – 3753Combined sources
Helixi378 – 40225Combined sources
Helixi414 – 42714Combined sources
Helixi429 – 44416Combined sources
Helixi476 – 50126Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LXRmodel-A158-461[»]
1TAZX-ray1.77A146-506[»]
4NPVX-ray2.40A142-507[»]
4NPWX-ray1.90A142-507[»]
ProteinModelPortaliQ01064.
SMRiQ01064. Positions 151-502.
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.
GeneTreeiENSGT00760000118889.
HOGENOMiHOG000231888.
HOVERGENiHBG056120.
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

        10         20         30         40         50
MELSPRSPPE MLEESDCPSP LELKSAPSKK MWIKLRSLLR YMVKQLENGE
60 70 80 90 100
INIEELKKNL EYTASLLEAV YIDETRQILD TEDELQELRS DAVPSEVRDW
110 120 130 140 150
LASTFTQQAR AKGRRAEEKP KFRSIVHAVQ AGIFVERMFR RTYTSVGPTY
160 170 180 190 200
STAVLNCLKN LDLWCFDVFS LNQAADDHAL RTIVFELLTR HNLISRFKIP
210 220 230 240 250
TVFLMSFLDA LETGYGKYKN PYHNQIHAAD VTQTVHCFLL RTGMVHCLSE
260 270 280 290 300
IELLAIIFAA AIHDYEHTGT TNSFHIQTKS ECAIVYNDRS VLENHHISSV
310 320 330 340 350
FRLMQDDEMN IFINLTKDEF VELRALVIEM VLATDMSCHF QQVKTMKTAL
360 370 380 390 400
QQLERIDKPK ALSLLLHAAD ISHPTKQWLV HSRWTKALME EFFRQGDKEA
410 420 430 440 450
ELGLPFSPLC DRTSTLVAQS QIGFIDFIVE PTFSVLTDVA EKSVQPLADE
460 470 480 490 500
DSKSKNQPSF QWRQPSLDVE VGDPNPDVVS FRSTWVKRIQ ENKQKWKERA
510 520 530
ASGITNQMSI DELSPCEEEA PPSPAEDEHN QNGNLD
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1LXR model - A 158-461 [» ]
1TAZ X-ray 1.77 A 146-506 [» ]
4NPV X-ray 2.40 A 142-507 [» ]
4NPW X-ray 1.90 A 142-507 [» ]
ProteinModelPortali Q01064.
SMRi Q01064. Positions 151-502.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

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

Chemistry

BindingDBi Q01064.
ChEMBLi CHEMBL2363066.
DrugBanki DB01244. Bepridil.
DB00201. Caffeine.
DB01023. Felodipine.
DB00622. Nicardipine.
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.
GeneTreei ENSGT00760000118889.
HOGENOMi HOG000231888.
HOVERGENi HBG056120.
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

Bgeei Q01064.
CleanExi HS_PDE1B.
ExpressionAtlasi Q01064. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 141 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