Q969G6 · RIFK_HUMAN
- ProteinRiboflavin kinase
- GeneRFK
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids155 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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
- ATP + riboflavin = ADP + FMN + H+This reaction proceeds in the forward direction.
Cofactor
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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 15 | ATP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 21 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 27 | ATP (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 27 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 29 | ATP (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 29 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Active site | 79 | Nucleophile | ||||
Sequence: E | ||||||
Binding site | 82 | ATP (UniProtKB | ChEBI) | ||||
Sequence: I | ||||||
Binding site | 84 | ATP (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 91 | ATP (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 104 | FMN (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 107 | FMN (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 109 | FMN (UniProtKB | ChEBI) | ||||
Sequence: F |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Cellular Component | mitochondrion | |
Molecular Function | ATP binding | |
Molecular Function | metal ion binding | |
Molecular Function | riboflavin kinase activity | |
Biological Process | apoptotic process | |
Biological Process | flavin adenine dinucleotide biosynthetic process | |
Biological Process | FMN biosynthetic process | |
Biological Process | positive regulation of NAD(P)H oxidase activity | |
Biological Process | reactive oxygen species metabolic process | |
Biological Process | riboflavin biosynthetic process | |
Biological Process | riboflavin metabolic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameRiboflavin kinase
- 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 accessionQ969G6
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 79 | Loss of riboflavin kinase activity. No effect on TNFRSF1A- and CYBA-binding. | ||||
Sequence: E → Q |
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.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000194148 | 1-155 | Riboflavin kinase | |||
Sequence: MRHLPYFCRGQVVRGFGRGSKQLGIPTANFPEQVVDNLPADISTGIYYGWASVGSGDVHKMVVSIGWNPYYKNTKKSMETHIMHTFKEDFYGEILNVAIVGYLRPEKNFDSLESLISAIQGDIEEAKKRLELPEHLKIKEDNFFQVSKSKIMNGH |
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
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q969G6 | CNTLN Q9NXG0-2 | 3 | EBI-716872, EBI-9640137 | |
BINARY | Q969G6 | TNFRSF1A P19438 | 4 | EBI-716872, EBI-299451 | |
BINARY | Q969G6 | TNFRSF1A P19438-1 | 2 | EBI-716872, EBI-15795644 |
Protein-protein interaction databases
Miscellaneous
Structure
Sequence
- Sequence statusComplete
- Length155
- Mass (Da)17,623
- Last updated2008-10-14 v2
- Checksum3E038E487E164EBA
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
H7C4G0 | H7C4G0_HUMAN | RFK | 120 |
Sequence caution
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 96 | in Ref. 1; BAA92033 | ||||
Sequence: N → S |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
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 |