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Protein

cAMP-specific 3',5'-cyclic phosphodiesterase 7B

Gene

PDE7B

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Hydrolyzes the second messenger cAMP, which is a key regulator of many important physiological processes. May be involved in the control of cAMP-mediated neural activity and cAMP metabolism in the brain.

Catalytic activityi

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

Cofactori

a divalent metal cationBy similarityNote: 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

Enzyme regulationi

Inhibited by dipyridamole, IBMX and SCH 51866. Insensitive to zaprinast, rolipram, and milrinone.

Pathwayi: 3',5'-cyclic AMP degradation

This protein is involved in step 1 of the subpathway that synthesizes AMP from 3',5'-cyclic AMP.
Proteins known to be involved in this subpathway in this organism are:
  1. cAMP-specific 3',5'-cyclic phosphodiesterase 4C (PDE4C), cAMP and cAMP-inhibited cGMP 3',5'-cyclic phosphodiesterase 10A (PDE10A), cAMP-specific 3',5'-cyclic phosphodiesterase 4A (PDE4A), High affinity cAMP-specific 3',5'-cyclic phosphodiesterase 7A (PDE7A), cAMP-specific 3',5'-cyclic phosphodiesterase 7B (PDE7B), cAMP-specific 3',5'-cyclic phosphodiesterase 4D (PDE4D), cAMP-specific 3',5'-cyclic phosphodiesterase 4B (PDE4B), High affinity cAMP-specific and IBMX-insensitive 3',5'-cyclic phosphodiesterase 8B (PDE8B), High affinity cAMP-specific and IBMX-insensitive 3',5'-cyclic phosphodiesterase 8A (PDE8A)
This subpathway is part of the pathway 3',5'-cyclic AMP degradation, which is itself part of Purine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes AMP from 3',5'-cyclic AMP, the pathway 3',5'-cyclic AMP degradation and in Purine metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei173Proton donorBy similarity1
Metal bindingi177Divalent metal cation 1By similarity1
Metal bindingi213Divalent metal cation 1By similarity1
Metal bindingi214Divalent metal cation 1By similarity1
Metal bindingi214Divalent metal cation 2By similarity1
Metal bindingi323Divalent metal cation 1By similarity1

GO - Molecular functioni

GO - Biological processi

  • cAMP catabolic process Source: UniProtKB-UniPathway
  • chemical synaptic transmission Source: ProtInc
  • signal transduction Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

cAMP, Metal-binding

Enzyme and pathway databases

BioCyciZFISH:HS10299-MONOMER.
BRENDAi3.1.4.53. 2681.
ReactomeiR-HSA-418555. G alpha (s) signalling events.
UniPathwayiUPA00762; UER00747.

Names & Taxonomyi

Protein namesi
Recommended name:
cAMP-specific 3',5'-cyclic phosphodiesterase 7B (EC:3.1.4.53)
Gene namesi
Name:PDE7B
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:8792. PDE7B.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

DisGeNETi27115.
OpenTargetsiENSG00000171408.
PharmGKBiPA33140.

Chemistry databases

ChEMBLiCHEMBL4716.
DrugBankiDB00201. Caffeine.
DB00651. Dyphylline.
DB00920. Ketotifen.
GuidetoPHARMACOLOGYi1306.

Polymorphism and mutation databases

BioMutaiPDE7B.
DMDMi13626185.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001988361 – 450cAMP-specific 3',5'-cyclic phosphodiesterase 7BAdd BLAST450

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei426PhosphoserineBy similarity1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9NP56.
PaxDbiQ9NP56.
PeptideAtlasiQ9NP56.
PRIDEiQ9NP56.

PTM databases

iPTMnetiQ9NP56.
PhosphoSitePlusiQ9NP56.

Expressioni

Tissue specificityi

Highly expressed in brain. Also expressed in heart, liver, skeletal muscle and pancreas.

Gene expression databases

BgeeiENSG00000171408.
CleanExiHS_PDE7B.
ExpressionAtlasiQ9NP56. baseline and differential.
GenevisibleiQ9NP56. HS.

Organism-specific databases

HPAiHPA023967.

Interactioni

Protein-protein interaction databases

BioGridi118010. 2 interactors.
IntActiQ9NP56. 1 interactor.
STRINGi9606.ENSP00000310661.

Chemistry databases

BindingDBiQ9NP56.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1LXWmodel-A104-433[»]
ProteinModelPortaliQ9NP56.
SMRiQ9NP56.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni172 – 410CatalyticBy similarityAdd BLAST239

Domaini

Composed of a C-terminal catalytic domain containing two putative divalent metal sites and an N-terminal regulatory domain.

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG3689. Eukaryota.
ENOG410XRI7. LUCA.
GeneTreeiENSGT00760000118889.
HOGENOMiHOG000220881.
HOVERGENiHBG053543.
KOiK18436.
PhylomeDBiQ9NP56.
TreeFamiTF314638.

Family and domain databases

Gene3Di1.10.1300.10. 1 hit.
InterProiIPR003607. HD/PDEase_dom.
IPR023088. PDEase.
IPR002073. PDEase_catalytic_dom.
IPR023174. PDEase_CS.
[Graphical view]
PfamiPF00233. PDEase_I. 1 hit.
[Graphical view]
PRINTSiPR00387. PDIESTERASE1.
SMARTiSM00471. HDc. 1 hit.
[Graphical view]
PROSITEiPS00126. PDEASE_I. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9NP56-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSCLMVERCG EILFENPDQN AKCVCMLGDI RLRGQTGVRA ERRGSYPFID
60 70 80 90 100
FRLLNSTTYS GEIGTKKKVK RLLSFQRYFH ASRLLRGIIP QAPLHLLDED
110 120 130 140 150
YLGQARHMLS KVGMWDFDIF LFDRLTNGNS LVTLLCHLFN THGLIHHFKL
160 170 180 190 200
DMVTLHRFLV MVQEDYHSQN PYHNAVHAAD VTQAMHCYLK EPKLASFLTP
210 220 230 240 250
LDIMLGLLAA AAHDVDHPGV NQPFLIKTNH HLANLYQNMS VLENHHWRST
260 270 280 290 300
IGMLRESRLL AHLPKEMTQD IEQQLGSLIL ATDINRQNEF LTRLKAHLHN
310 320 330 340 350
KDLRLEDAQD RHFMLQIALK CADICNPCRI WEMSKQWSER VCEEFYRQGE
360 370 380 390 400
LEQKFELEIS PLCNQQKDSI PSIQIGFMSY IVEPLFREWA HFTGNSTLSE
410 420 430 440 450
NMLGHLAHNK AQWKSLLPRQ HRSRGSSGSG PDHDHAGQGT ESEEQEGDSP
Length:450
Mass (Da):51,835
Last modified:October 1, 2000 - v1
Checksum:iEC142BF3E28D0028
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB038040 mRNA. Translation: BAA96537.1.
AJ251860 mRNA. Translation: CAB92441.1.
AL360178, AL133319, AL138828 Genomic DNA. Translation: CAH73075.1.
AL133319, AL138828, AL360178 Genomic DNA. Translation: CAH73332.1.
AL138828, AL133319, AL360178 Genomic DNA. Translation: CAI95287.1.
CH471051 Genomic DNA. Translation: EAW47957.1.
BC075082 mRNA. Translation: AAH75082.1.
BC075083 mRNA. Translation: AAH75083.1.
CCDSiCCDS5175.1.
PIRiJC7266.
RefSeqiNP_061818.1. NM_018945.3.
UniGeneiHs.744230.

Genome annotation databases

EnsembliENST00000308191; ENSP00000310661; ENSG00000171408.
GeneIDi27115.
KEGGihsa:27115.
UCSCiuc003qgp.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB038040 mRNA. Translation: BAA96537.1.
AJ251860 mRNA. Translation: CAB92441.1.
AL360178, AL133319, AL138828 Genomic DNA. Translation: CAH73075.1.
AL133319, AL138828, AL360178 Genomic DNA. Translation: CAH73332.1.
AL138828, AL133319, AL360178 Genomic DNA. Translation: CAI95287.1.
CH471051 Genomic DNA. Translation: EAW47957.1.
BC075082 mRNA. Translation: AAH75082.1.
BC075083 mRNA. Translation: AAH75083.1.
CCDSiCCDS5175.1.
PIRiJC7266.
RefSeqiNP_061818.1. NM_018945.3.
UniGeneiHs.744230.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1LXWmodel-A104-433[»]
ProteinModelPortaliQ9NP56.
SMRiQ9NP56.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi118010. 2 interactors.
IntActiQ9NP56. 1 interactor.
STRINGi9606.ENSP00000310661.

Chemistry databases

BindingDBiQ9NP56.
ChEMBLiCHEMBL4716.
DrugBankiDB00201. Caffeine.
DB00651. Dyphylline.
DB00920. Ketotifen.
GuidetoPHARMACOLOGYi1306.

PTM databases

iPTMnetiQ9NP56.
PhosphoSitePlusiQ9NP56.

Polymorphism and mutation databases

BioMutaiPDE7B.
DMDMi13626185.

Proteomic databases

MaxQBiQ9NP56.
PaxDbiQ9NP56.
PeptideAtlasiQ9NP56.
PRIDEiQ9NP56.

Protocols and materials databases

DNASUi27115.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000308191; ENSP00000310661; ENSG00000171408.
GeneIDi27115.
KEGGihsa:27115.
UCSCiuc003qgp.4. human.

Organism-specific databases

CTDi27115.
DisGeNETi27115.
GeneCardsiPDE7B.
HGNCiHGNC:8792. PDE7B.
HPAiHPA023967.
MIMi604645. gene.
neXtProtiNX_Q9NP56.
OpenTargetsiENSG00000171408.
PharmGKBiPA33140.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3689. Eukaryota.
ENOG410XRI7. LUCA.
GeneTreeiENSGT00760000118889.
HOGENOMiHOG000220881.
HOVERGENiHBG053543.
KOiK18436.
PhylomeDBiQ9NP56.
TreeFamiTF314638.

Enzyme and pathway databases

UniPathwayiUPA00762; UER00747.
BioCyciZFISH:HS10299-MONOMER.
BRENDAi3.1.4.53. 2681.
ReactomeiR-HSA-418555. G alpha (s) signalling events.

Miscellaneous databases

GenomeRNAii27115.
PROiQ9NP56.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000171408.
CleanExiHS_PDE7B.
ExpressionAtlasiQ9NP56. baseline and differential.
GenevisibleiQ9NP56. HS.

Family and domain databases

Gene3Di1.10.1300.10. 1 hit.
InterProiIPR003607. HD/PDEase_dom.
IPR023088. PDEase.
IPR002073. PDEase_catalytic_dom.
IPR023174. PDEase_CS.
[Graphical view]
PfamiPF00233. PDEase_I. 1 hit.
[Graphical view]
PRINTSiPR00387. PDIESTERASE1.
SMARTiSM00471. HDc. 1 hit.
[Graphical view]
PROSITEiPS00126. PDEASE_I. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPDE7B_HUMAN
AccessioniPrimary (citable) accession number: Q9NP56
Secondary accession number(s): Q5W154
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: October 1, 2000
Last modified: November 2, 2016
This is version 144 of the entry and version 1 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 6
    Human chromosome 6: 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.