Q969G6 · RIFK_HUMAN

  • Protein
    Riboflavin kinase
  • Gene
    RFK
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Catalyzes the phosphorylation of riboflavin (vitamin B2) to form flavin-mononucleotide (FMN), hence rate-limiting enzyme in the synthesis of FAD. Essential for TNF-induced reactive oxygen species (ROS) production. Through its interaction with both TNFRSF1A and CYBA, physically and functionally couples TNFRSF1A to NADPH oxidase. TNF-activation of RFK may enhance the incorporation of FAD in NADPH oxidase, a critical step for the assembly and activation of NADPH oxidase.

Catalytic activity

Cofactor

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )
Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Note: Zinc or magnesium.

Pathway

Cofactor biosynthesis; FMN biosynthesis; FMN from riboflavin (ATP route): step 1/1.

Features

Showing features for binding site, active site.

TypeIDPosition(s)Description
Binding site15ATP (UniProtKB | ChEBI)
Binding site21ATP (UniProtKB | ChEBI)
Binding site27ATP (UniProtKB | ChEBI)
Binding site27Mg2+ (UniProtKB | ChEBI)
Binding site29ATP (UniProtKB | ChEBI)
Binding site29Mg2+ (UniProtKB | ChEBI)
Active site79Nucleophile
Binding site82ATP (UniProtKB | ChEBI)
Binding site84ATP (UniProtKB | ChEBI)
Binding site91ATP (UniProtKB | ChEBI)
Binding site104FMN (UniProtKB | ChEBI)
Binding site107FMN (UniProtKB | ChEBI)
Binding site109FMN (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Cellular Componentcytosol
Cellular Componentmitochondrion
Molecular FunctionATP binding
Molecular Functionmetal ion binding
Molecular Functionriboflavin kinase activity
Biological Processapoptotic process
Biological Processflavin adenine dinucleotide biosynthetic process
Biological ProcessFMN biosynthetic process
Biological Processpositive regulation of NAD(P)H oxidase activity
Biological Processreactive oxygen species metabolic process
Biological Processriboflavin biosynthetic process
Biological Processriboflavin metabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Riboflavin kinase
  • EC number
  • Alternative names
    • ATP:riboflavin 5'-phosphotransferase
    • Flavokinase

Gene names

    • Name
      RFK

Organism names

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

Accessions

  • Primary accession
    Q969G6
  • Secondary accessions
    • Q5JSG9
    • Q9NUT7

Proteomes

Organism-specific databases

Subcellular Location

Keywords

Disease & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis79Loss of riboflavin kinase activity. No effect on TNFRSF1A- and CYBA-binding.

Variants

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

The viewer provides 149 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Organism-specific databases

Miscellaneous

Chemistry

Genetic variation databases

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00001941481-155Riboflavin kinase

Proteomic databases

PTM databases

Expression

Tissue specificity

Detected in brain, placenta and urinary bladder.

Gene expression databases

Organism-specific databases

Interaction

Subunit

Monomer. Directly interacts with TNFRSF1A death domain. TNFRSF1A-binding may be supported by TRADD. In the absence of TNFRSF1A, interacts with TRADD. Independently of TNFRSF1A, interacts with the NADPH oxidase subunit CYBA.

Binary interactions

Protein-protein interaction databases

Miscellaneous

Family & Domains

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    155
  • Mass (Da)
    17,623
  • Last updated
    2008-10-14 v2
  • Checksum
    3E038E487E164EBA
MRHLPYFCRGQVVRGFGRGSKQLGIPTANFPEQVVDNLPADISTGIYYGWASVGSGDVHKMVVSIGWNPYYKNTKKSMETHIMHTFKEDFYGEILNVAIVGYLRPEKNFDSLESLISAIQGDIEEAKKRLELPEHLKIKEDNFFQVSKSKIMNGH

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
H7C4G0H7C4G0_HUMANRFK120

Sequence caution

The sequence AAH07069.1 differs from that shown. Reason: Erroneous initiation Extended N-terminus.
The sequence BAA92033.1 differs from that shown. Reason: Erroneous initiation Extended N-terminus.

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict96in Ref. 1; BAA92033

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AK002011
EMBL· GenBank· DDBJ
BAA92033.1
EMBL· GenBank· DDBJ
mRNA Different initiation
AL391868
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
BC007069
EMBL· GenBank· DDBJ
AAH07069.1
EMBL· GenBank· DDBJ
mRNA Different initiation

Genome annotation databases

Similar Proteins

Disclaimer

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