O95861 · BPNT1_HUMAN
- Protein3'(2'),5'-bisphosphate nucleotidase 1
- GeneBPNT1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids308 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Phosphatase that converts 3'(2')-phosphoadenosine 5'-phosphate (PAP) to AMP and inositol 1,4-bisphosphate (Ins(1,4)P2) to inositol 4-phosphate (PubMed:10675562).
Is also able to hydrolyze adenosine 3'-phosphate 5'-phosphosulfate (PAPS) to adenosine 5'-phosphosulfate (APS) (By similarity).
Probably prevents the toxic accumulation of PAP, a compound which inhibits a variety of proteins, including PAPS-utilizing enzymes such as sulfotransferases, and RNA processing enzymes. Could also play a role in inositol recycling and phosphoinositide metabolism. Is not active on 3'-AMP, inositol-1-phosphate and inositol-1,4,5-triphosphate (PubMed:10675562).
Is also able to hydrolyze adenosine 3'-phosphate 5'-phosphosulfate (PAPS) to adenosine 5'-phosphosulfate (APS) (By similarity).
Probably prevents the toxic accumulation of PAP, a compound which inhibits a variety of proteins, including PAPS-utilizing enzymes such as sulfotransferases, and RNA processing enzymes. Could also play a role in inositol recycling and phosphoinositide metabolism. Is not active on 3'-AMP, inositol-1-phosphate and inositol-1,4,5-triphosphate (PubMed:10675562).
Miscellaneous
Since this enzyme is sensitive to subtherapeutic concentrations of lithium, it is a potential target of lithium therapy, which could explain some of the side effects of this therapy.
Catalytic activity
- adenosine 3',5'-bisphosphate + H2O = AMP + phosphateThis reaction proceeds in the forward direction.
- 1D-myo-inositol 1,3,4-trisphosphate + H2O = 1D-myo-inositol 3,4-bisphosphate + phosphateThis reaction proceeds in the forward direction.
Cofactor
Note: Binds 3 Mg2+ ions per subunit.
Activity regulation
Is very sensitive to inhibition by Li+ (IC50=0.3 mM for hydrolysis of PAP; IC50=0.6 mM for hydrolysis of inositol-1,4-bis-phosphate). Is not affected by high Na+ concentrations.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
0.4 μM | 1D-myo-inositol 1,4-bisphosphate |
Vmax | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|
1.1 μmol/min/mg | with adenosine 3',5'-bisphosphate as substrate | ||||
0.2 μmol/min/mg | with 1D-myo-inositol 1,4-bisphosphate as substrate |
KM for adenosine 3',5'-bisphosphate is below 1 uM.
Features
Showing features for active site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 51 | Proton acceptor | ||||
Sequence: D | ||||||
Binding site | 74 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 74 | Mg2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 117 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 117 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 119 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: L | ||||||
Binding site | 120 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Active site | 122 | Proton acceptor | ||||
Sequence: T | ||||||
Binding site | 195 | AMP (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 198 | AMP (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 220 | AMP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 224 | AMP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 247 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | 3'(2'),5'-bisphosphate nucleotidase activity | |
Molecular Function | inositol-1,4-bisphosphate 1-phosphatase activity | |
Molecular Function | metal ion binding | |
Biological Process | 3'-phosphoadenosine 5'-phosphosulfate metabolic process | |
Biological Process | nervous system development | |
Biological Process | nucleobase-containing compound metabolic process | |
Biological Process | phosphatidylinositol phosphate biosynthetic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended name3'(2'),5'-bisphosphate nucleotidase 1
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionO95861
- Secondary accessions
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 354 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Initiator methionine | 1 | UniProt | Removed | ||||
Sequence: M | |||||||
Modified residue | 2 | UniProt | N-acetylalanine | ||||
Sequence: A | |||||||
Chain | PRO_0000142527 | 2-308 | UniProt | 3'(2'),5'-bisphosphate nucleotidase 1 | |||
Sequence: ASSNTVLMRLVASAYSIAQKAGMIVRRVIAEGDLGIVEKTCATDLQTKADRLAQMSICSSLARKFPKLTIIGEEDLPSEEVDQELIEDSQWEEILKQPCPSQYSAIKEEDLVVWVDPLDGTKEYTEGLLDNVTVLIGIAYEGKAIAGVINQPYYNYEAGPDAVLGRTIWGVLGLGAFGFQLKEVPAGKHIITTTRSHSNKLVTDCVAAMNPDAVLRVGGAGNKIIQLIEGKASAYVFASPGCKKWDTCAPEVILHAVGGKLTDIHGNVLQYHKDVKHMNSAGVLATLRNYDYYASRVPESIKNALVP | |||||||
Modified residue | 122 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 240 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 240 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 244 | UniProt | N6-succinyllysine | ||||
Sequence: K |
Keywords
- PTM
Proteomic databases
2D gel databases
PTM databases
Expression
Tissue specificity
Highly expressed in kidney, liver, pancreas and heart. Detected at lower levels in brain, placenta, lung and skeletal muscle.
Gene expression databases
Organism-specific databases
Structure
Sequence & Isoforms
- Sequence statusComplete
This entry describes 4 isoforms produced by Alternative splicing.
O95861-1
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.
- Name1
- Length308
- Mass (Da)33,392
- Last updated1999-05-01 v1
- ChecksumA5952F5E31C8CFCB
O95861-2
- Name2
- Differences from canonical
- 277-308: KHMNSAGVLATLRNYDYYASRVPESIKNALVP → SHRTWPKPDFFRAQFFLESHSCFSRNFKNVSTPIKNIYDVIIYAYETDL
O95861-3
- Name3
- Differences from canonical
- 1-55: Missing
O95861-4
- Name4
- Differences from canonical
- 76-111: Missing
Computationally mapped potential isoform sequences
There are 5 potential isoforms mapped to this entry
Features
Showing features for alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_054807 | 1-55 | in isoform 3 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_054808 | 76-111 | in isoform 4 | |||
Sequence: Missing | ||||||
Sequence conflict | 221 | in Ref. 6; AAH17801 | ||||
Sequence: A → V | ||||||
Sequence conflict | 260 | in Ref. 2; CAB65115 | ||||
Sequence: G → S | ||||||
Alternative sequence | VSP_009937 | 277-308 | in isoform 2 | |||
Sequence: KHMNSAGVLATLRNYDYYASRVPESIKNALVP → SHRTWPKPDFFRAQFFLESHSCFSRNFKNVSTPIKNIYDVIIYAYETDL |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF125042 EMBL· GenBank· DDBJ | AAD17329.1 EMBL· GenBank· DDBJ | mRNA | ||
AJ249339 EMBL· GenBank· DDBJ | CAB65115.1 EMBL· GenBank· DDBJ | mRNA | ||
AK291943 EMBL· GenBank· DDBJ | BAF84632.1 EMBL· GenBank· DDBJ | mRNA | ||
AK298476 EMBL· GenBank· DDBJ | BAG60687.1 EMBL· GenBank· DDBJ | mRNA | ||
AK300777 EMBL· GenBank· DDBJ | BAG62441.1 EMBL· GenBank· DDBJ | mRNA | ||
AC103590 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471100 EMBL· GenBank· DDBJ | EAW93306.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471100 EMBL· GenBank· DDBJ | EAW93308.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC017801 EMBL· GenBank· DDBJ | AAH17801.1 EMBL· GenBank· DDBJ | mRNA |