A0A1B0GW84 · A0A1B0GW84_HUMAN
- ProteinPhosphodiesterase
- GenePDE4D
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids699 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score3/5
Function
Catalytic activity
- 3',5'-cyclic AMP + H2O = AMP + H+This reaction proceeds in the forward direction.
Cofactor
Note: 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.
Pathway
Purine metabolism; 3',5'-cyclic AMP degradation; AMP from 3',5'-cyclic AMP: step 1/1.
Features
Showing features for active site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 352 | Proton donor | ||||
Sequence: H | ||||||
Binding site | 352-356 | AMP (UniProtKB | ChEBI) | ||||
Sequence: HNNIH | ||||||
Binding site | 356 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 392 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 393 | AMP (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 393 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 393 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 510 | AMP (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 510 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 561 | AMP (UniProtKB | ChEBI) | ||||
Sequence: Q |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | plasma membrane | |
Molecular Function | 3',5'-cyclic-AMP phosphodiesterase activity | |
Molecular Function | metal ion binding | |
Biological Process | cAMP catabolic process | |
Biological Process | signal transduction |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePhosphodiesterase
- EC number
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionA0A1B0GW84
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Disease & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 589 variants from UniProt as well as other sources including ClinVar and dbSNP.
Genetic variation databases
PTM/Processing
Features
Showing features for modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Modified residue (large scale data) | 54 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 61 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 80 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 85 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 87 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 92 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 145 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 195 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 215 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 226 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 238 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 252 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 263 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 264 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 265 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 270 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 547 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 605 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 607 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 636 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 642 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 644 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 651 | PRIDE | Phosphoserine | ||||
Sequence: S |
Proteomic databases
Expression
Gene expression databases
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 233-254 | Disordered | ||||
Sequence: EVEIPSPTQKEKEKKKRPMSQI | ||||||
Compositional bias | 235-252 | Basic and acidic residues | ||||
Sequence: EIPSPTQKEKEKKKRPMS | ||||||
Domain | 276-605 | PDEase | ||||
Sequence: VKTEQEDVLAKELEDVNKWGLHVFRIAELSGNRPLTVIMHTIFQERDLLKTFKIPVDTLITYLMTLEDHYHADVAYHNNIHAADVVQSTHVLLSTPALEAVFTDLEILAAIFASAIHDVDHPGVSNQFLINTNSELALMYNDSSVLENHHLAVGFKLLQEENCDIFQNLTKKQRQSLRKMVIDIVLATDMSKHMNLLADLKTMVETKKVTSSGVLLLDNYSDRIQVLQNMVHCADLSNPTKPLQLYRQWTDRIMEEFFRQGDRERERGMEISPMCDKHNASVEKSQVGFIDYIVHPLWETWADLVHPDAQDILDTLEDNREWYQSTIPQS | ||||||
Region | 600-619 | Disordered | ||||
Sequence: STIPQSPSPAPDDPEEGRQG | ||||||
Region | 625-699 | Disordered | ||||
Sequence: QFELTLEEDGESDTEKDSGSQVEEDTSCSDSKTLCTQDSESTEIPLDEQVEEEAVGEEEESQPEACVIDDRSPDT | ||||||
Compositional bias | 648-667 | Polar residues | ||||
Sequence: EDTSCSDSKTLCTQDSESTE | ||||||
Compositional bias | 668-688 | Acidic residues | ||||
Sequence: IPLDEQVEEEAVGEEEESQPE |
Sequence similarities
Belongs to the cyclic nucleotide phosphodiesterase family. PDE4 subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length699
- Mass (Da)79,202
- Last updated2016-10-05 v1
- Checksum11BC344036C9896B
Computationally mapped potential isoform sequences
There are 6 potential isoforms mapped to this entry
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 235-252 | Basic and acidic residues | ||||
Sequence: EIPSPTQKEKEKKKRPMS | ||||||
Compositional bias | 648-667 | Polar residues | ||||
Sequence: EDTSCSDSKTLCTQDSESTE | ||||||
Compositional bias | 668-688 | Acidic residues | ||||
Sequence: IPLDEQVEEEAVGEEEESQPE |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AC008791 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC008804 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC008829 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC008833 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC020924 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC092343 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
KC876983 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
KF510911 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. |