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Q969G6

- RIFK_HUMAN

UniProt

Q969G6 - RIFK_HUMAN

Protein

Riboflavin kinase

Gene

RFK

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. Functioni

    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.1 Publication

    Catalytic activityi

    ATP + riboflavin = ADP + FMN.

    Cofactori

    Zinc or magnesium.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei15 – 151ATP; via amide nitrogen
    Binding sitei21 – 211ATP; via amide nitrogen
    Metal bindingi27 – 271Magnesium
    Binding sitei27 – 271ATP; via amide nitrogen
    Binding sitei29 – 291ATP
    Active sitei79 – 791NucleophileBy similarity
    Binding sitei82 – 821ATP; via amide nitrogen and carbonyl oxygen
    Binding sitei84 – 841ATP; via carbonyl oxygen
    Binding sitei91 – 911ATP
    Binding sitei104 – 1041FMN
    Binding sitei107 – 1071FMN; via amide nitrogen and carbonyl oxygen
    Binding sitei109 – 1091FMN; via amide nitrogen

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. metal ion binding Source: UniProtKB-KW
    3. riboflavin kinase activity Source: UniProtKB

    GO - Biological processi

    1. apoptotic process Source: MGI
    2. FMN biosynthetic process Source: UniProtKB-UniPathway
    3. positive regulation of NAD(P)H oxidase activity Source: MGI
    4. riboflavin biosynthetic process Source: UniProtKB
    5. riboflavin metabolic process Source: Reactome
    6. small molecule metabolic process Source: Reactome
    7. vitamin metabolic process Source: Reactome
    8. water-soluble vitamin metabolic process Source: Reactome

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Ligandi

    ATP-binding, Flavoprotein, FMN, Magnesium, Metal-binding, Nucleotide-binding, Zinc

    Enzyme and pathway databases

    BioCyciMetaCyc:HS05938-MONOMER.
    ReactomeiREACT_11070. Vitamin B2 (riboflavin) metabolism.
    UniPathwayiUPA00276; UER00406.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Riboflavin kinase (EC:2.7.1.26)
    Alternative name(s):
    ATP:riboflavin 5'-phosphotransferase
    Flavokinase
    Gene namesi
    Name:RFK
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:30324. RFK.

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: Reactome
    3. mitochondrion Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi79 – 791E → Q: Loss of kinase activity. No effect on TNFRSF1A- and CYBA-binding. 1 Publication

    Organism-specific databases

    PharmGKBiPA134916697.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 155155Riboflavin kinasePRO_0000194148Add
    BLAST

    Proteomic databases

    MaxQBiQ969G6.
    PaxDbiQ969G6.
    PRIDEiQ969G6.

    PTM databases

    PhosphoSiteiQ969G6.

    Expressioni

    Tissue specificityi

    Detected in brain, placenta and urinary bladder.

    Gene expression databases

    ArrayExpressiQ969G6.
    BgeeiQ969G6.
    CleanExiHS_RFK.
    GenevestigatoriQ969G6.

    Organism-specific databases

    HPAiHPA057163.

    Interactioni

    Subunit structurei

    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.2 Publications

    Protein-protein interaction databases

    BioGridi120594. 3 interactions.
    DIPiDIP-60454N.
    IntActiQ969G6. 3 interactions.
    MINTiMINT-1401441.
    STRINGi9606.ENSP00000257452.

    Structurei

    Secondary structure

    1
    155
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 117
    Beta strandi16 – 183
    Helixi20 – 234
    Helixi32 – 365
    Beta strandi44 – 5310
    Beta strandi59 – 679
    Beta strandi69 – 746
    Beta strandi76 – 849
    Beta strandi93 – 10412
    Helixi112 – 12918
    Helixi133 – 1364
    Helixi137 – 1404
    Helixi142 – 1465

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1NB0X-ray1.70A2-148[»]
    1NB9X-ray1.70A2-148[»]
    1P4MX-ray1.80A2-148[»]
    1Q9SX-ray2.42A1-148[»]
    ProteinModelPortaliQ969G6.
    SMRiQ969G6. Positions 2-148.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ969G6.

    Family & Domainsi

    Phylogenomic databases

    eggNOGiCOG0196.
    HOGENOMiHOG000260803.
    HOVERGENiHBG049989.
    InParanoidiQ969G6.
    KOiK00861.
    OMAiSLPYFCR.
    OrthoDBiEOG7K3TP0.
    PhylomeDBiQ969G6.
    TreeFamiTF313786.

    Family and domain databases

    Gene3Di2.40.30.30. 1 hit.
    InterProiIPR023468. Riboflavin_kinase.
    IPR015865. Riboflavin_kinase_bac/euk.
    IPR023465. Riboflavin_kinase_domain.
    [Graphical view]
    PANTHERiPTHR22749. PTHR22749. 1 hit.
    PfamiPF01687. Flavokinase. 1 hit.
    [Graphical view]
    SMARTiSM00904. Flavokinase. 1 hit.
    [Graphical view]
    SUPFAMiSSF82114. SSF82114. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q969G6-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRHLPYFCRG QVVRGFGRGS KQLGIPTANF PEQVVDNLPA DISTGIYYGW    50
    ASVGSGDVHK MVVSIGWNPY YKNTKKSMET HIMHTFKEDF YGEILNVAIV 100
    GYLRPEKNFD SLESLISAIQ GDIEEAKKRL ELPEHLKIKE DNFFQVSKSK 150
    IMNGH 155
    Length:155
    Mass (Da):17,623
    Last modified:October 14, 2008 - v2
    Checksum:i3E038E487E164EBA
    GO

    Sequence cautioni

    The sequence AAH07069.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence BAA92033.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti96 – 961N → S in BAA92033. (PubMed:14702039)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK002011 mRNA. Translation: BAA92033.1. Different initiation.
    AL391868 Genomic DNA. Translation: CAI40676.1.
    BC007069 mRNA. Translation: AAH07069.1. Different initiation.
    CCDSiCCDS35044.2.
    RefSeqiNP_060809.3. NM_018339.5.
    UniGeneiHs.37558.

    Genome annotation databases

    EnsembliENST00000376736; ENSP00000365926; ENSG00000135002.
    GeneIDi55312.
    KEGGihsa:55312.
    UCSCiuc004akd.2. human.

    Polymorphism databases

    DMDMi209572667.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK002011 mRNA. Translation: BAA92033.1 . Different initiation.
    AL391868 Genomic DNA. Translation: CAI40676.1 .
    BC007069 mRNA. Translation: AAH07069.1 . Different initiation.
    CCDSi CCDS35044.2.
    RefSeqi NP_060809.3. NM_018339.5.
    UniGenei Hs.37558.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1NB0 X-ray 1.70 A 2-148 [» ]
    1NB9 X-ray 1.70 A 2-148 [» ]
    1P4M X-ray 1.80 A 2-148 [» ]
    1Q9S X-ray 2.42 A 1-148 [» ]
    ProteinModelPortali Q969G6.
    SMRi Q969G6. Positions 2-148.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 120594. 3 interactions.
    DIPi DIP-60454N.
    IntActi Q969G6. 3 interactions.
    MINTi MINT-1401441.
    STRINGi 9606.ENSP00000257452.

    Chemistry

    DrugBanki DB00140. Riboflavin.

    PTM databases

    PhosphoSitei Q969G6.

    Polymorphism databases

    DMDMi 209572667.

    Proteomic databases

    MaxQBi Q969G6.
    PaxDbi Q969G6.
    PRIDEi Q969G6.

    Protocols and materials databases

    DNASUi 55312.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000376736 ; ENSP00000365926 ; ENSG00000135002 .
    GeneIDi 55312.
    KEGGi hsa:55312.
    UCSCi uc004akd.2. human.

    Organism-specific databases

    CTDi 55312.
    GeneCardsi GC09M079000.
    H-InvDB HIX0169330.
    HGNCi HGNC:30324. RFK.
    HPAi HPA057163.
    MIMi 613010. gene.
    neXtProti NX_Q969G6.
    PharmGKBi PA134916697.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0196.
    HOGENOMi HOG000260803.
    HOVERGENi HBG049989.
    InParanoidi Q969G6.
    KOi K00861.
    OMAi SLPYFCR.
    OrthoDBi EOG7K3TP0.
    PhylomeDBi Q969G6.
    TreeFami TF313786.

    Enzyme and pathway databases

    UniPathwayi UPA00276 ; UER00406 .
    BioCyci MetaCyc:HS05938-MONOMER.
    Reactomei REACT_11070. Vitamin B2 (riboflavin) metabolism.

    Miscellaneous databases

    EvolutionaryTracei Q969G6.
    GenomeRNAii 55312.
    NextBioi 59546.
    PROi Q969G6.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q969G6.
    Bgeei Q969G6.
    CleanExi HS_RFK.
    Genevestigatori Q969G6.

    Family and domain databases

    Gene3Di 2.40.30.30. 1 hit.
    InterProi IPR023468. Riboflavin_kinase.
    IPR015865. Riboflavin_kinase_bac/euk.
    IPR023465. Riboflavin_kinase_domain.
    [Graphical view ]
    PANTHERi PTHR22749. PTHR22749. 1 hit.
    Pfami PF01687. Flavokinase. 1 hit.
    [Graphical view ]
    SMARTi SM00904. Flavokinase. 1 hit.
    [Graphical view ]
    SUPFAMi SSF82114. SSF82114. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Placenta.
    2. "DNA sequence and analysis of human chromosome 9."
      Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
      , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
      Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Urinary bladder.
    4. Cited for: FUNCTION, INTERACTION WITH CYBA; TNFRSF1A AND TRADD, MUTAGENESIS OF GLU-79.
    5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    6. "Crystal structure of human riboflavin kinase reveals a beta barrel fold and a novel active site arch."
      Karthikeyan S., Zhou Q., Mseeh F., Grishin N.V., Osterman A.L., Zhang H.
      Structure 11:265-273(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 2-148 IN COMPLEX WITH MG-ADP AND RIBOFLAVIN NUCLEOTIDE.

    Entry informationi

    Entry nameiRIFK_HUMAN
    AccessioniPrimary (citable) accession number: Q969G6
    Secondary accession number(s): Q5JSG9, Q9NUT7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 3, 2003
    Last sequence update: October 14, 2008
    Last modified: October 1, 2014
    This is version 124 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 9
      Human chromosome 9: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    4. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references

    External Data

    Dasty 3