P52758 · RIDA_HUMAN
- Protein2-iminobutanoate/2-iminopropanoate deaminase
- GeneRIDA
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids137 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes the hydrolytic deamination of enamine/imine intermediates that form during the course of normal metabolism. May facilitate the release of ammonia from these potentially toxic reactive metabolites, reducing their impact on cellular components. It may act on enamine/imine intermediates formed by several types of pyridoxal-5'-phosphate-dependent dehydratases including L-threonine dehydratase.
Also promotes endoribonucleolytic cleavage of some transcripts by promoting recruitment of the ribonuclease P/MRP complex (PubMed:30930054, PubMed:8973653).
Acts by bridging YTHDF2 and the ribonuclease P/MRP complex (PubMed:30930054).
RIDA/HRSP12 binds to N6-methyladenosine (m6A)-containing mRNAs containing a 5'-GGUUC-3' motif: cooperative binding of RIDA/HRSP12 and YTHDF2 to such transcripts lead to recruitment of the ribonuclease P/MRP complex and subsequent endoribonucleolytic cleavage (PubMed:30930054).
Acts by bridging YTHDF2 and the ribonuclease P/MRP complex (PubMed:30930054).
RIDA/HRSP12 binds to N6-methyladenosine (m6A)-containing mRNAs containing a 5'-GGUUC-3' motif: cooperative binding of RIDA/HRSP12 and YTHDF2 to such transcripts lead to recruitment of the ribonuclease P/MRP complex and subsequent endoribonucleolytic cleavage (PubMed:30930054).
Catalytic activity
- 2-iminobutanoate + H2O = 2-oxobutanoate + NH4+
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Cellular Component | extracellular exosome | |
Cellular Component | mitochondrial matrix | |
Cellular Component | mitochondrion | |
Cellular Component | nucleus | |
Cellular Component | peroxisome | |
Molecular Function | 2-iminobutanoate deaminase activity | |
Molecular Function | 2-iminopropanoate deaminase activity | |
Molecular Function | deaminase activity | |
Molecular Function | mRNA binding | |
Molecular Function | RNA binding | |
Molecular Function | RNA endonuclease activity, producing 3'-phosphomonoesters | |
Biological Process | L-threonine catabolic process to glycine | |
Biological Process | lipid metabolic process | |
Biological Process | mRNA catabolic process | |
Biological Process | mRNA destabilization | |
Biological Process | negative regulation of translation | |
Biological Process | organonitrogen compound catabolic process |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended name2-iminobutanoate/2-iminopropanoate deaminase
- 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 accessionP52758
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Mostly cytoplasmic but, in less differentiated cells occasionally nuclear.
Keywords
- Cellular component
Disease & Variants
Variants
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The viewer provides 151 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-acetylserine | ||||
Sequence: S | |||||||
Chain | PRO_0000170308 | 2-137 | UniProt | 2-iminobutanoate/2-iminopropanoate deaminase | |||
Sequence: SSLIRRVISTAKAPGAIGPYSQAVLVDRTIYISGQIGMDPSSGQLVSGGVAEEAKQALKNMGEILKAAGCDFTNVVKTTVLLADINDFNTVNEIYKQYFKSNFPARAAYQVAALPKGSRIEIEAVAIQGPLTTASL | |||||||
Modified residue | 13 | UniProt | N6-succinyllysine | ||||
Sequence: K | |||||||
Modified residue | 60 | UniProt | N6-succinyllysine | ||||
Sequence: K | |||||||
Modified residue | 67 | UniProt | N6-succinyllysine | ||||
Sequence: K | |||||||
Modified residue | 74 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 110 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 136 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 136 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed predominantly in liver and kidney. Lower levels in lung and brain.
Developmental stage
Up-regulated during cellular differentiation.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P52758 | BANP Q8N9N5-2 | 3 | EBI-1045080, EBI-11524452 |
Protein-protein interaction databases
Miscellaneous
Structure
Sequence
- Sequence statusComplete
- Length137
- Mass (Da)14,494
- Last updated1996-10-01 v1
- ChecksumDD0740621E8BE6AD
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 84 | in Ref. 3; CAG46453 | ||||
Sequence: A → V |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X95384 EMBL· GenBank· DDBJ | CAA64670.1 EMBL· GenBank· DDBJ | mRNA | ||
AY026764 EMBL· GenBank· DDBJ | AAK01939.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CR456844 EMBL· GenBank· DDBJ | CAG33125.1 EMBL· GenBank· DDBJ | mRNA | ||
CR541652 EMBL· GenBank· DDBJ | CAG46453.1 EMBL· GenBank· DDBJ | mRNA | ||
CH471060 EMBL· GenBank· DDBJ | EAW91774.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC010280 EMBL· GenBank· DDBJ | AAH10280.1 EMBL· GenBank· DDBJ | mRNA | ||
BC012592 EMBL· GenBank· DDBJ | AAH12592.1 EMBL· GenBank· DDBJ | mRNA | ||
BC093059 EMBL· GenBank· DDBJ | AAH93059.1 EMBL· GenBank· DDBJ | mRNA |