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Q8BGW1

- FTO_MOUSE

UniProt

Q8BGW1 - FTO_MOUSE

Protein

Alpha-ketoglutarate-dependent dioxygenase FTO

Gene

Fto

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 88 (01 Oct 2014)
      Sequence version 1 (01 Mar 2003)
      Previous versions | rss
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    Functioni

    Dioxygenase that repairs alkylated DNA and RNA by oxidative demethylation. Has highest activity towards single-stranded RNA containing 3-methyluracil, followed by single-stranded DNA containing 3-methylthymine. Has low demethylase activity towards single-stranded DNA containing 1-methyladenine or 3-methylcytosine. Specifically demethylates N(6)-methyladenosine (m6A) RNA, the most prevalent internal modification of messenger RNA (mRNA) in higher eukaryotes. Has no activity towards 1-methylguanine. Has no detectable activity towards double-stranded DNA. Requires molecular oxygen, alpha-ketoglutarate and iron. Contributes to the regulation of the global metabolic rate, energy expenditure and energy homeostasis. Contributes to the regulation of body size and body fat accumulation.4 Publications

    Cofactori

    Binds 1 Fe2+ ion per subunit.1 Publication

    Enzyme regulationi

    Activated by ascorbate. Inhibited by N-oxalylglycine, fumarate and succinate.1 Publication

    pH dependencei

    Optimum pH is 5.5-6.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei96 – 961SubstrateBy similarity
    Binding sitei108 – 1081SubstrateBy similarity
    Binding sitei202 – 2021Alpha-ketoglutarateBy similarity
    Metal bindingi228 – 2281Iron; catalyticBy similarity
    Metal bindingi230 – 2301Iron; catalyticBy similarity
    Binding sitei292 – 2921Alpha-ketoglutarateBy similarity
    Metal bindingi304 – 3041Iron; catalyticBy similarity
    Binding sitei317 – 3171Alpha-ketoglutarateBy similarity
    Binding sitei319 – 3191Alpha-ketoglutarateBy similarity

    GO - Molecular functioni

    1. DNA-N1-methyladenine dioxygenase activity Source: UniProtKB
    2. ferrous iron binding Source: UniProtKB
    3. oxidative DNA demethylase activity Source: BHF-UCL
    4. oxidative RNA demethylase activity Source: BHF-UCL

    GO - Biological processi

    1. adipose tissue development Source: UniProtKB
    2. DNA dealkylation involved in DNA repair Source: UniProtKB
    3. DNA demethylation Source: BHF-UCL
    4. oxidative demethylation Source: BHF-UCL
    5. oxidative single-stranded DNA demethylation Source: BHF-UCL
    6. oxidative single-stranded RNA demethylation Source: BHF-UCL
    7. regulation of lipid storage Source: UniProtKB
    8. regulation of multicellular organism growth Source: UniProtKB
    9. regulation of respiratory system process Source: UniProtKB
    10. regulation of white fat cell proliferation Source: UniProtKB
    11. RNA repair Source: BHF-UCL
    12. temperature homeostasis Source: UniProtKB

    Keywords - Molecular functioni

    Dioxygenase, Oxidoreductase

    Keywords - Biological processi

    DNA damage, DNA repair, RNA repair

    Keywords - Ligandi

    Iron, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Alpha-ketoglutarate-dependent dioxygenase FTO (EC:1.14.11.-)
    Alternative name(s):
    Fat mass and obesity-associated protein
    Protein fatso
    Gene namesi
    Name:Fto
    Synonyms:Kiaa1752
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 8

    Organism-specific databases

    MGIiMGI:1347093. Fto.

    Subcellular locationi

    Nucleus 3 Publications. Nucleus speckle By similarity

    GO - Cellular componenti

    1. nuclear speck Source: UniProtKB
    2. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Disruption phenotypei

    Elevated perinatal mortality. Mice have normal body weight at birth, but show growth retardation from day 2 onwards, resulting in a weight reduction of 30-40% after 6 weeks, both in males and females. In addition, animals display reduced nose to anus length. Fat mass is reduced by 60% in males and by 23% in females. Lean body mass is reduced by 26% in males and 19% in females. White adipose tissue decreases more and more over time, while brown adipose tissue is not affected. Serum leptin levels are decreased, while serum levels of adiponectin are increased. Mice exhibit significant hyperphagia after correction for body weight. They show increased oxygen consumption, carbon dioxide production and heat generation, indicating increased energy expenditure, in spite of reduced spontaneous locomotor activity. Plasma adrenaline concentrations are significantly increased. Overall glucose metabolism appears normal.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi304 – 3041H → A: Reduced enzyme activity. 1 Publication
    Mutagenesisi313 – 3131R → A: Loss of enzyme activity. 1 Publication
    Mutagenesisi367 – 3671I → A: Reduces enzyme activity by about 60%. 1 Publication
    Mutagenesisi367 – 3671I → F: Alters protein structure and causes an increase in whole body metabolism, leading to a lean phenotype in adult males, but not in females. 1 Publication

    Keywords - Diseasei

    Obesity

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 502502Alpha-ketoglutarate-dependent dioxygenase FTOPRO_0000286164Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei213 – 2131N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ8BGW1.
    PaxDbiQ8BGW1.
    PRIDEiQ8BGW1.

    PTM databases

    PhosphoSiteiQ8BGW1.

    Expressioni

    Tissue specificityi

    Ubiquitous. Detected in brain, brain cortex, hypothalamus, cerebellum, liver, pancreas, heart, kidney, white adipose tissue and skeletal muscle. Most abundant in the brain, particularly in hypothalamic nuclei governing energy balance.2 Publications

    Inductioni

    Down-regulated in fasting animals.1 Publication

    Gene expression databases

    ArrayExpressiQ8BGW1.
    BgeeiQ8BGW1.
    CleanExiMM_FTO.
    GenevestigatoriQ8BGW1.

    Interactioni

    Subunit structurei

    Monomer. May also exist as homodimer.1 Publication

    Protein-protein interaction databases

    BioGridi204941. 1 interaction.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8BGW1.
    SMRiQ8BGW1. Positions 30-500.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni42 – 324283Fe2OG dioxygenase domainBy similarityAdd
    BLAST
    Regioni210 – 22112Loop L1; predicted to block binding of double-stranded DNA or RNABy similarityAdd
    BLAST
    Regioni228 – 2314Substrate bindingBy similarity
    Regioni313 – 3153Alpha-ketoglutarate bindingBy similarity

    Domaini

    The 3D-structure of the Fe2OG dioxygenase domain is similar to that of the Fe2OG dioxygenase domain found in the bacterial DNA repair dioxygenase alkB and its mammalian orthologs, but sequence similarity is very low. As a consequence, the domain is not detected by protein signature databases By similarity.By similarity

    Sequence similaritiesi

    Belongs to the fto family.Curated

    Phylogenomic databases

    eggNOGiNOG45792.
    GeneTreeiENSGT00390000017730.
    HOVERGENiHBG101847.
    InParanoidiQ8BGW1.
    OMAiAVYNYSC.
    OrthoDBiEOG7CK36T.
    PhylomeDBiQ8BGW1.
    TreeFamiTF333296.

    Family and domain databases

    InterProiIPR024366. FTO_C.
    IPR024367. FTO_cat_dom.
    [Graphical view]
    PfamiPF12934. FTO_CTD. 1 hit.
    PF12933. FTO_NTD. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q8BGW1-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MKRVQTAEER EREAKKLRLL EELEDTWLPY LTPKDDEFYQ QWQLKYPKLV    50
    FREAGSIPEE LHKEVPEAFL TLHKHGCLFR DVVRIQGKDV LTPVSRILIG 100
    DPGCTYKYLN TRLFTVPWPV KGCTVKYTEA EIAAACQTFL KLNDYLQVET 150
    IQALEELAVR EKANEDAVPL CMAEFPRAGV GPSCDDEVDL KSRAAYNVTL 200
    LNFMDPQKMP YLKEEPYFGM GKMAVSWHHD ENLVDRSAVA VYSYSCEGSE 250
    DESEDESSFE GRDPDTWHVG FKISWDIETP GLTIPLHQGD CYFMLDDLNA 300
    THQHCVLAGS QPRFSSTHRV AECSTGTLDY ILERCQLALQ NVLNDSDDGD 350
    VSLKSFDPAV LKQGEEIHNE VEFEWLRQFW FQGNRYKLCT DWWCEPMTHL 400
    EGLWKKMESM TNAVLREVKR EGLPVEQRSE ILSAILVPLT VRQNLRKEWH 450
    ARCQSRVVRT LPVQQKPDCR PYWEKDDPSM PLPFDLTDVV SELRGQLLEA 500
    RS 502
    Length:502
    Mass (Da):58,007
    Last modified:March 1, 2003 - v1
    Checksum:i69223B824028D872
    GO
    Isoform 2 (identifier: Q8BGW1-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         453-502: CQSRVVRTLP...LRGQLLEARS → FVLLRGGVWCPCPSSARPAQRTKVEDILS

    Note: No experimental confirmation available.

    Show »
    Length:481
    Mass (Da):55,393
    Checksum:iD79A1C3143BEF2D9
    GO
    Isoform 3 (identifier: Q8BGW1-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         411-413: TNA → VSA
         414-502: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:413
    Mass (Da):47,593
    Checksum:iA3E62B85C8133963
    GO
    Isoform 4 (identifier: Q8BGW1-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         296-316: DDLNATHQHCVLAGSQPRFSS → GNVGSLRVGHLWGFEIHFWIL
         317-502: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:316
    Mass (Da):36,366
    Checksum:iC6C1B6EB7E895140
    GO

    Sequence cautioni

    The sequence BAC98247.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti181 – 1811G → R in BAC32382. (PubMed:16141072)Curated
    Sequence conflicti384 – 3841N → S in CAB59324. (PubMed:10501967)Curated
    Sequence conflicti384 – 3841N → S in BAC98247. (PubMed:14621295)Curated
    Sequence conflicti384 – 3841N → S in BAC40629. (PubMed:16141072)Curated
    Sequence conflicti384 – 3841N → S in AAH22222. (PubMed:15489334)Curated
    Sequence conflicti410 – 4101M → V in BAC98247. (PubMed:14621295)Curated
    Sequence conflicti410 – 4101M → V in BAC40629. (PubMed:16141072)Curated
    Sequence conflicti410 – 4101M → V in AAH22222. (PubMed:15489334)Curated
    Sequence conflicti463 – 4631V → A in BAC40629. (PubMed:16141072)Curated
    Sequence conflicti463 – 4631V → A in AAH22222. (PubMed:15489334)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei296 – 31621DDLNA…PRFSS → GNVGSLRVGHLWGFEIHFWI L in isoform 4. 1 PublicationVSP_025007Add
    BLAST
    Alternative sequencei317 – 502186Missing in isoform 4. 1 PublicationVSP_025008Add
    BLAST
    Alternative sequencei411 – 4133TNA → VSA in isoform 3. 1 PublicationVSP_025009
    Alternative sequencei414 – 50289Missing in isoform 3. 1 PublicationVSP_025010Add
    BLAST
    Alternative sequencei453 – 50250CQSRV…LEARS → FVLLRGGVWCPCPSSARPAQ RTKVEDILS in isoform 2. 1 PublicationVSP_025011Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ237917 mRNA. Translation: CAB59324.1.
    AK129437 mRNA. Translation: BAC98247.1. Different initiation.
    AK036677 mRNA. Translation: BAC29533.1.
    AK040866 mRNA. Translation: BAC30724.1.
    AK045465 mRNA. Translation: BAC32382.1.
    AK049502 mRNA. Translation: BAC33780.1.
    AK088881 mRNA. Translation: BAC40629.1.
    AK161060 mRNA. Translation: BAE36177.1.
    BC022222 mRNA. Translation: AAH22222.1.
    BC057008 mRNA. Translation: AAH57008.1.
    CCDSiCCDS22521.1. [Q8BGW1-1]
    RefSeqiNP_036066.2. NM_011936.2. [Q8BGW1-1]
    UniGeneiMm.4375.

    Genome annotation databases

    EnsembliENSMUST00000069718; ENSMUSP00000068380; ENSMUSG00000055932. [Q8BGW1-1]
    GeneIDi26383.
    KEGGimmu:26383.
    UCSCiuc009msq.2. mouse. [Q8BGW1-4]
    uc009msr.2. mouse. [Q8BGW1-3]
    uc009mss.2. mouse. [Q8BGW1-2]
    uc009mst.2. mouse. [Q8BGW1-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ237917 mRNA. Translation: CAB59324.1 .
    AK129437 mRNA. Translation: BAC98247.1 . Different initiation.
    AK036677 mRNA. Translation: BAC29533.1 .
    AK040866 mRNA. Translation: BAC30724.1 .
    AK045465 mRNA. Translation: BAC32382.1 .
    AK049502 mRNA. Translation: BAC33780.1 .
    AK088881 mRNA. Translation: BAC40629.1 .
    AK161060 mRNA. Translation: BAE36177.1 .
    BC022222 mRNA. Translation: AAH22222.1 .
    BC057008 mRNA. Translation: AAH57008.1 .
    CCDSi CCDS22521.1. [Q8BGW1-1 ]
    RefSeqi NP_036066.2. NM_011936.2. [Q8BGW1-1 ]
    UniGenei Mm.4375.

    3D structure databases

    ProteinModelPortali Q8BGW1.
    SMRi Q8BGW1. Positions 30-500.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 204941. 1 interaction.

    PTM databases

    PhosphoSitei Q8BGW1.

    Proteomic databases

    MaxQBi Q8BGW1.
    PaxDbi Q8BGW1.
    PRIDEi Q8BGW1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000069718 ; ENSMUSP00000068380 ; ENSMUSG00000055932 . [Q8BGW1-1 ]
    GeneIDi 26383.
    KEGGi mmu:26383.
    UCSCi uc009msq.2. mouse. [Q8BGW1-4 ]
    uc009msr.2. mouse. [Q8BGW1-3 ]
    uc009mss.2. mouse. [Q8BGW1-2 ]
    uc009mst.2. mouse. [Q8BGW1-1 ]

    Organism-specific databases

    CTDi 79068.
    MGIi MGI:1347093. Fto.
    Rougei Search...

    Phylogenomic databases

    eggNOGi NOG45792.
    GeneTreei ENSGT00390000017730.
    HOVERGENi HBG101847.
    InParanoidi Q8BGW1.
    OMAi AVYNYSC.
    OrthoDBi EOG7CK36T.
    PhylomeDBi Q8BGW1.
    TreeFami TF333296.

    Miscellaneous databases

    ChiTaRSi FTO. mouse.
    NextBioi 304305.
    PROi Q8BGW1.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8BGW1.
    Bgeei Q8BGW1.
    CleanExi MM_FTO.
    Genevestigatori Q8BGW1.

    Family and domain databases

    InterProi IPR024366. FTO_C.
    IPR024367. FTO_cat_dom.
    [Graphical view ]
    Pfami PF12934. FTO_CTD. 1 hit.
    PF12933. FTO_NTD. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning of Fatso (Fto), a novel gene deleted by the Fused toes (Ft) mouse mutation."
      Peters T., Ausmeier K., Ruether U.
      Mamm. Genome 10:983-986(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Prediction of the coding sequences of mouse homologues of KIAA gene: III. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
      Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Nagase T., Ohara O., Koga H.
      DNA Res. 10:167-180(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Brain.
    3. "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] (ISOFORMS 1; 3 AND 4).
      Strain: C57BL/6J and NOD.
      Tissue: Aorta, Bone, Corpora quadrigemina, Skin, Thymus and Vein.
    4. "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] (ISOFORM 1).
      Strain: C57BL/6 and FVB/N.
      Tissue: Brain and Kidney.
    5. Cited for: FUNCTION, COFACTOR, ENZYME REGULATION, SUBCELLULAR LOCATION, MUTAGENESIS OF HIS-304 AND ARG-313, INDUCTION, TISSUE SPECIFICITY.
    6. "Oxidative demethylation of 3-methylthymine and 3-methyluracil in single-stranded DNA and RNA by mouse and human FTO."
      Jia G., Yang C.G., Yang S., Jian X., Yi C., Zhou Z., He C.
      FEBS Lett. 582:3313-3319(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
    7. Cited for: DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, FUNCTION, TISSUE SPECIFICITY.
    8. "A mouse model for the metabolic effects of the human fat mass and obesity associated FTO gene."
      Church C., Lee S., Bagg E.A., McTaggart J.S., Deacon R., Gerken T., Lee A., Moir L., Mecinovic J., Quwailid M.M., Schofield C.J., Ashcroft F.M., Cox R.D.
      PLoS Genet. 5:E1000599-E1000599(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, CIRCULAR DICHROISM, MUTAGENESIS OF ILE-367.

    Entry informationi

    Entry nameiFTO_MOUSE
    AccessioniPrimary (citable) accession number: Q8BGW1
    Secondary accession number(s): Q3TTZ5
    , Q6ZPI7, Q8BR68, Q8CB66, Q8R250, Q9QZ13
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 2007
    Last sequence update: March 1, 2003
    Last modified: October 1, 2014
    This is version 88 of the entry and version 1 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3