P52758 · RIDA_HUMAN

  • Protein
    2-iminobutanoate/2-iminopropanoate deaminase
  • Gene
    RIDA
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

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).

Catalytic activity

GO annotations

AspectTerm
Cellular Componentcytoplasm
Cellular Componentcytosol
Cellular Componentextracellular exosome
Cellular Componentmitochondrial matrix
Cellular Componentmitochondrion
Cellular Componentnucleus
Cellular Componentperoxisome
Molecular Function2-iminobutanoate deaminase activity
Molecular Function2-iminopropanoate deaminase activity
Molecular Functiondeaminase activity
Molecular FunctionmRNA binding
Molecular FunctionRNA binding
Molecular FunctionRNA endonuclease activity, producing 3'-phosphomonoesters
Biological ProcessL-threonine catabolic process to glycine
Biological Processlipid metabolic process
Biological ProcessmRNA catabolic process
Biological ProcessmRNA destabilization
Biological Processnegative regulation of translation
Biological Processorganonitrogen compound catabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    2-iminobutanoate/2-iminopropanoate deaminase
  • EC number
  • Alternative names
    • 14.5 kDa translational inhibitor protein
      (hp14.5
      ; p14.5
      )
    • Heat-responsive protein 12
    • Reactive intermediate imine deaminase A homolog
    • Translation inhibitor L-PSP ribonuclease
    • UK114 antigen homolog

Gene names

    • Name
      RIDA
    • Synonyms
      HRSP12

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo

Accessions

  • Primary accession
    P52758
  • Secondary accessions
    • Q6FHU9
    • Q6IBG0

Proteomes

Organism-specific databases

Subcellular Location

Cytoplasm
Nucleus
Peroxisome
Mitochondrion
Note: Mostly cytoplasmic but, in less differentiated cells occasionally nuclear.

Keywords

Disease & Variants

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 151 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Organism-specific databases

Miscellaneous

Genetic variation databases

PTM/Processing

Features

Showing features for initiator methionine, modified residue, chain, modified residue (large scale data).

TypeIDPosition(s)SourceDescription
Initiator methionine1UniProtRemoved
Modified residue2UniProtN-acetylserine
ChainPRO_00001703082-137UniProt2-iminobutanoate/2-iminopropanoate deaminase
Modified residue13UniProtN6-succinyllysine
Modified residue60UniProtN6-succinyllysine
Modified residue67UniProtN6-succinyllysine
Modified residue74UniProtPhosphothreonine
Modified residue (large scale data)110PRIDEPhosphotyrosine
Modified residue136UniProtPhosphoserine
Modified residue (large scale data)136PRIDEPhosphoserine

Keywords

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

Homotrimer (PubMed:14997576).
Interacts with YTHDF2 (PubMed:30930054).

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY P52758BANP Q8N9N5-23EBI-1045080, EBI-11524452

Protein-protein interaction databases

Miscellaneous

Family & Domains

Sequence similarities

Belongs to the RutC family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    137
  • Mass (Da)
    14,494
  • Last updated
    1996-10-01 v1
  • Checksum
    DD0740621E8BE6AD
MSSLIRRVISTAKAPGAIGPYSQAVLVDRTIYISGQIGMDPSSGQLVSGGVAEEAKQALKNMGEILKAAGCDFTNVVKTTVLLADINDFNTVNEIYKQYFKSNFPARAAYQVAALPKGSRIEIEAVAIQGPLTTASL

Computationally mapped potential isoform sequences

There are 3 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
H0YBX3H0YBX3_HUMANRIDA127
H0YB34H0YB34_HUMANRIDA148
E5RIP8E5RIP8_HUMANRIDA42

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict84in Ref. 3; CAG46453

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
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

Genome annotation databases

Similar Proteins

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