Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Riboflavin kinase

Gene

Rfk

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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 (By similarity).By similarity

Catalytic activityi

ATP + riboflavin = ADP + FMN.

Cofactori

Zn2+By similarity, Mg2+By similarityNote: Zinc or magnesium.By similarity

Pathwayi

Sites

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

GO - Molecular functioni

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

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. reactive oxygen species metabolic process Source: MGI
  5. riboflavin biosynthetic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Ligandi

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

Enzyme and pathway databases

ReactomeiREACT_324263. 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
KOI-4
Gene namesi
Name:Rfk
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 19

Organism-specific databases

MGIiMGI:1914688. Rfk.

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

  1. mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Mutant embryos die in utero before 7.5 dpc.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 155155Riboflavin kinasePRO_0000194149Add
BLAST

Proteomic databases

MaxQBiQ8CFV9.
PaxDbiQ8CFV9.
PRIDEiQ8CFV9.

PTM databases

PhosphoSiteiQ8CFV9.

Expressioni

Gene expression databases

BgeeiQ8CFV9.
CleanExiMM_RFK.
GenevestigatoriQ8CFV9.

Interactioni

Subunit structurei

Monomer (By similarity). Directly interacts with TNFRSF1A death domain; this interaction may be supported by TRADD. In the absence of TNFRSF1A, interacts with TRADD. Independently of TNFRSF1A, interacts with the NADPH oxidase subunit CYBA.By similarity1 Publication

Protein-protein interaction databases

DIPiDIP-60455N.
STRINGi10090.ENSMUSP00000025617.

Structurei

3D structure databases

ProteinModelPortaliQ8CFV9.
SMRiQ8CFV9. Positions 2-148.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Phylogenomic databases

eggNOGiCOG0196.
GeneTreeiENSGT00390000015537.
HOGENOMiHOG000260803.
HOVERGENiHBG049989.
InParanoidiQ8CFV9.
KOiK00861.
OMAiSLPYFCR.
OrthoDBiEOG7K3TP0.
PhylomeDBiQ8CFV9.
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.

Q8CFV9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRSLPFFCRG QVVRGFGRGS KQLGIPTANF PEQVVDNLPA DVSTGIYYGW
60 70 80 90 100
ASVGSGDVHK MVVSIGWNPY YKNVKKSMET HIIHTFKEDF YGEILNVAIV
110 120 130 140 150
GYLRPEKNFD SLESLISAIQ GDIEEAKKQL DLPEHLKLKD DNFFQVSKGK

IMNGH
Length:155
Mass (Da):17,437
Last modified:October 3, 2003 - v2
Checksum:iAE6577023E3D34CF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK010607 mRNA. Translation: BAB27057.1.
AK002806 mRNA. Translation: BAB22372.1.
AK008352 mRNA. Translation: BAB25622.1.
BC033521 mRNA. Translation: AAH33521.2.
BC051021 mRNA. Translation: AAH51021.1.
AF031380 Genomic DNA. Translation: AAB86494.1.
AF031381 Genomic DNA. Translation: AAB86495.1.
CCDSiCCDS29688.1.
RefSeqiNP_062310.1. NM_019437.3.
UniGeneiMm.7013.

Genome annotation databases

EnsembliENSMUST00000025617; ENSMUSP00000025617; ENSMUSG00000024712.
GeneIDi54391.
KEGGimmu:54391.
UCSCiuc008gxo.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK010607 mRNA. Translation: BAB27057.1.
AK002806 mRNA. Translation: BAB22372.1.
AK008352 mRNA. Translation: BAB25622.1.
BC033521 mRNA. Translation: AAH33521.2.
BC051021 mRNA. Translation: AAH51021.1.
AF031380 Genomic DNA. Translation: AAB86494.1.
AF031381 Genomic DNA. Translation: AAB86495.1.
CCDSiCCDS29688.1.
RefSeqiNP_062310.1. NM_019437.3.
UniGeneiMm.7013.

3D structure databases

ProteinModelPortaliQ8CFV9.
SMRiQ8CFV9. Positions 2-148.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-60455N.
STRINGi10090.ENSMUSP00000025617.

PTM databases

PhosphoSiteiQ8CFV9.

Proteomic databases

MaxQBiQ8CFV9.
PaxDbiQ8CFV9.
PRIDEiQ8CFV9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000025617; ENSMUSP00000025617; ENSMUSG00000024712.
GeneIDi54391.
KEGGimmu:54391.
UCSCiuc008gxo.2. mouse.

Organism-specific databases

CTDi55312.
MGIiMGI:1914688. Rfk.

Phylogenomic databases

eggNOGiCOG0196.
GeneTreeiENSGT00390000015537.
HOGENOMiHOG000260803.
HOVERGENiHBG049989.
InParanoidiQ8CFV9.
KOiK00861.
OMAiSLPYFCR.
OrthoDBiEOG7K3TP0.
PhylomeDBiQ8CFV9.
TreeFamiTF313786.

Enzyme and pathway databases

UniPathwayiUPA00276; UER00406.
ReactomeiREACT_324263. Vitamin B2 (riboflavin) metabolism.

Miscellaneous databases

ChiTaRSiRfk. mouse.
NextBioi311232.
PROiQ8CFV9.
SOURCEiSearch...

Gene expression databases

BgeeiQ8CFV9.
CleanExiMM_RFK.
GenevestigatoriQ8CFV9.

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.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Embryonic stem cell, Kidney and Small intestine.
  2. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Olfactory epithelium and Retina.
  3. Abrantes E.F., Silva A.M., Reis L.F.L.
    Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 79-112 AND 114-155.
    Strain: 129/Sv.
  4. Cited for: INTERACTION WITH CYBA; TNFRSF1A AND TRADD, DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiRIFK_MOUSE
AccessioniPrimary (citable) accession number: Q8CFV9
Secondary accession number(s): O35471, O35472, Q9CQ95
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2003
Last sequence update: October 3, 2003
Last modified: April 1, 2015
This is version 111 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.