SubmitCancel

Skip Header

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

Q8CFV9

- RIFK_MOUSE

UniProt

Q8CFV9 - RIFK_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Riboflavin kinase
Gene
Rfk
Organism
Mus musculus (Mouse)
Status
Reviewed - 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.

Catalytic activityi

ATP + riboflavin = ADP + FMN.

Cofactori

Zinc or magnesium By similarity.

Pathwayi

Sites

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

GO - Molecular functioni

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

GO - Biological processi

  1. FMN biosynthetic process Source: UniProtKB-UniPathway
  2. positive regulation of NAD(P)H oxidase activity Source: MGI
  3. reactive oxygen species metabolic process Source: MGI
  4. 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_216155. 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: 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 kinase
PRO_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.1 Publication

Protein-protein interaction databases

DIPiDIP-60455N.
STRINGi10090.ENSMUSP00000025617.

Structurei

3D structure databases

ProteinModelPortaliQ8CFV9.
SMRiQ8CFV9. Positions 2-148.

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

MRSLPFFCRG QVVRGFGRGS KQLGIPTANF PEQVVDNLPA DVSTGIYYGW    50
ASVGSGDVHK MVVSIGWNPY YKNVKKSMET HIIHTFKEDF YGEILNVAIV 100
GYLRPEKNFD SLESLISAIQ GDIEEAKKQL DLPEHLKLKD DNFFQVSKGK 150
IMNGH 155
Length:155
Mass (Da):17,437
Last modified:October 3, 2003 - v2
Checksum:iAE6577023E3D34CF
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS29688.1.
RefSeqi NP_062310.1. NM_019437.3.
UniGenei Mm.7013.

3D structure databases

ProteinModelPortali Q8CFV9.
SMRi Q8CFV9. Positions 2-148.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-60455N.
STRINGi 10090.ENSMUSP00000025617.

PTM databases

PhosphoSitei Q8CFV9.

Proteomic databases

MaxQBi Q8CFV9.
PaxDbi Q8CFV9.
PRIDEi Q8CFV9.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000025617 ; ENSMUSP00000025617 ; ENSMUSG00000024712 .
GeneIDi 54391.
KEGGi mmu:54391.
UCSCi uc008gxo.2. mouse.

Organism-specific databases

CTDi 55312.
MGIi MGI:1914688. Rfk.

Phylogenomic databases

eggNOGi COG0196.
GeneTreei ENSGT00390000015537.
HOGENOMi HOG000260803.
HOVERGENi HBG049989.
InParanoidi Q8CFV9.
KOi K00861.
OMAi SLPYFCR.
OrthoDBi EOG7K3TP0.
PhylomeDBi Q8CFV9.
TreeFami TF313786.

Enzyme and pathway databases

UniPathwayi UPA00276 ; UER00406 .
Reactomei REACT_216155. Vitamin B2 (riboflavin) metabolism.

Miscellaneous databases

ChiTaRSi RFK. mouse.
NextBioi 311232.
PROi Q8CFV9.
SOURCEi Search...

Gene expression databases

Bgeei Q8CFV9.
CleanExi MM_RFK.
Genevestigatori Q8CFV9.

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

« 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(2005) [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(2004) [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 (OCT-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: September 3, 2014
This is version 105 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