P36959 · GMPR1_HUMAN
- ProteinGMP reductase 1
- GeneGMPR
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids345 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes the irreversible NADPH-dependent deamination of GMP to IMP. It functions in the conversion of nucleobase, nucleoside and nucleotide derivatives of G to A nucleotides, and in maintaining the intracellular balance of A and G nucleotides.
Catalytic activity
- IMP + NADP+ + NH4+ = GMP + 2 H+ + NADPH
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 26-27 | NADP+ (UniProtKB | ChEBI); ligand shared between two neighboring subunits | ||||
Sequence: SR | ||||||
Binding site | 78 | NADP+ (UniProtKB | ChEBI); ligand shared between two neighboring subunits; in other chain | ||||
Sequence: K | ||||||
Binding site | 129-131 | NADP+ (UniProtKB | ChEBI); ligand shared between two neighboring subunits; in other chain | ||||
Sequence: DVA | ||||||
Binding site | 180-181 | NADP+ (UniProtKB | ChEBI); ligand shared between two neighboring subunits; in other chain | ||||
Sequence: VG | ||||||
Binding site | 181 | K+ (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 183 | K+ (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Active site | 186 | Thioimidate intermediate | ||||
Sequence: C | ||||||
Binding site | 186 | K+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Active site | 188 | Proton donor/acceptor | ||||
Sequence: T | ||||||
Binding site | 189 | K+ (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 219-221 | GMP (UniProtKB | ChEBI) | ||||
Sequence: DGG | ||||||
Binding site | 242-243 | GMP (UniProtKB | ChEBI) | ||||
Sequence: GG | ||||||
Binding site | 268-270 | GMP (UniProtKB | ChEBI) | ||||
Sequence: GMS | ||||||
Binding site | 269 | NADP+ (UniProtKB | ChEBI); ligand shared between two neighboring subunits; in other chain | ||||
Sequence: M | ||||||
Binding site | 285-286 | NADP+ (UniProtKB | ChEBI); ligand shared between two neighboring subunits; in other chain | ||||
Sequence: YR | ||||||
Binding site | 286-290 | GMP (UniProtKB | ChEBI) | ||||
Sequence: RASEG | ||||||
Binding site | 314-317 | NADP+ (UniProtKB | ChEBI); ligand shared between two neighboring subunits | ||||
Sequence: STCT |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | GMP reductase complex | |
Molecular Function | GMP reductase activity | |
Molecular Function | metal ion binding | |
Biological Process | purine nucleobase metabolic process | |
Biological Process | purine nucleotide metabolic process | |
Biological Process | response to cold |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameGMP reductase 1
- EC number
- Short namesGMPR 1
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP36959
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_003969 | 234 | in dbSNP:rs760571328 | |||
Sequence: A → T | ||||||
Natural variant | VAR_003970 | 256 | in dbSNP:rs1042391 | |||
Sequence: F → I |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 417 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000093723 | 1-345 | UniProt | GMP reductase 1 | |||
Sequence: MPRIDADLKLDFKDVLLRPKRSSLKSRAEVDLERTFTFRNSKQTYSGIPIIVANMDTVGTFEMAAVMSQHSMFTAIHKHYSLDDWKLFATNHPECLQNVAVSSGSGQNDLEKMTSILEAVPQVKFICLDVANGYSEHFVEFVKLVRAKFPEHTIMAGNVVTGEMVEELILSGADIIKVGVGPGSVCTTRTKTGVGYPQLSAVIECADSAHGLKGHIISDGGCTCPGDVAKAFGAGADFVMLGGMFSGHTECAGEVFERNGRKLKLFYGMSSDTAMNKHAGGVAEYRASEGKTVEVPYKGDVENTILDILGGLRSTCTYVGAAKLKELSRRATFIRVTQQHNTVFS | |||||||
Modified residue (large scale data) | 345 | PRIDE | Phosphoserine | ||||
Sequence: S |
Proteomic databases
PTM databases
Interaction
Subunit
Homotetramer.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P36959 | GMPR2 Q9P2T1 | 2 | EBI-10484590, EBI-2806548 |
Protein-protein interaction databases
Miscellaneous
Structure
Sequence
- Sequence statusComplete
- Length345
- Mass (Da)37,419
- Last updated1994-06-01 v1
- Checksum217E1A5A599CA510
Polymorphism
At least two different alleles are known.
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
L35304 EMBL· GenBank· DDBJ | AAA52503.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M27941 EMBL· GenBank· DDBJ | AAA53106.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M24470 EMBL· GenBank· DDBJ | AAA52498.1 EMBL· GenBank· DDBJ | mRNA | ||
AL009031 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL138883 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC008281 EMBL· GenBank· DDBJ | AAH08281.1 EMBL· GenBank· DDBJ | mRNA |