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Q9C0B1

- FTO_HUMAN

UniProt

Q9C0B1 - FTO_HUMAN

Protein

Alpha-ketoglutarate-dependent dioxygenase FTO

Gene

FTO

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 90 (01 Oct 2014)
      Sequence version 3 (29 May 2007)
      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.3 Publications

    Cofactori

    Binds 1 Fe2+ ion per subunit.1 Publication

    Enzyme regulationi

    Activated by ascorbate. Inhibited by N-oxalylglycine, fumarate and succinate By similarity.By similarity

    pH dependencei

    Optimum pH is 5.5-6.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei96 – 961Substrate
    Binding sitei108 – 1081Substrate
    Binding sitei205 – 2051Alpha-ketoglutarate
    Metal bindingi231 – 2311Iron; catalytic
    Metal bindingi233 – 2331Iron; catalytic
    Binding sitei295 – 2951Alpha-ketoglutarate
    Metal bindingi307 – 3071Iron; catalytic
    Binding sitei320 – 3201Alpha-ketoglutarate
    Binding sitei322 – 3221Alpha-ketoglutarate

    GO - Molecular functioni

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

    GO - Biological processi

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

    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
    Gene namesi
    Name:FTO
    Synonyms:KIAA1752
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:24678. FTO.

    Subcellular locationi

    Nucleus 1 Publication. Nucleus speckle 1 Publication

    GO - Cellular componenti

    1. nuclear speck Source: UniProtKB
    2. nucleus Source: BHF-UCL

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Growth retardation developmental delay coarse facies early death (GDFD) [MIM:612938]: A severe polymalformation syndrome characterized by postnatal growth retardation, microcephaly, severe psychomotor delay, functional brain deficits and characteristic facial dysmorphism. In some patients, structural brain malformations, cardiac defects, genital anomalies, and cleft palate are observed. Early death occurs by the age of 3 years.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti316 – 3161R → Q in GDFD; has no residual normal activity, impaired ability to demethylate N(6)-methyladenosine RNAs (m6A) RNAs. 1 Publication
    VAR_063252

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi96 – 961R → M or W: Almost abolishes enzyme activity. 2 Publications
    Mutagenesisi108 – 1081Y → A: Abolishes enzyme activity. 2 Publications
    Mutagenesisi114 – 1141F → D: Perturbs interaction between N-terminal and C-terminal domains and strongly reduces enzyme activity. 2 Publications
    Mutagenesisi231 – 2333HHD → AHA: Abolishes ability to demethylate N(6)-methyladenosine RNAs (m6A) RNAs. 1 Publication
    Mutagenesisi234 – 2341E → P: Abolishes enzyme activity. Abolishes ability to demethylate N(6)-methyladenosine RNAs (m6A) RNAs; when associated with Q-322. 2 Publications
    Mutagenesisi392 – 3921C → D: Perturbs interaction between N-terminal and C-terminal domains and strongly reduces enzyme activity. 2 Publications

    Keywords - Diseasei

    Disease mutation, Obesity

    Organism-specific databases

    MIMi612938. phenotype.
    Orphaneti210144. Lethal polymalformative syndrome, Boissel type.
    PharmGKBiPA152208656.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 505505Alpha-ketoglutarate-dependent dioxygenase FTOPRO_0000286163Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei216 – 2161N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ9C0B1.
    PaxDbiQ9C0B1.
    PRIDEiQ9C0B1.

    PTM databases

    PhosphoSiteiQ9C0B1.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed, with relatively high expression in adrenal glands and brain; especially in hypothalamus and pituitary.2 Publications

    Gene expression databases

    ArrayExpressiQ9C0B1.
    BgeeiQ9C0B1.
    CleanExiHS_FTO.
    GenevestigatoriQ9C0B1.

    Organism-specific databases

    HPAiCAB017123.

    Interactioni

    Subunit structurei

    Monomer. May also exist as homodimer By similarity.By similarity

    Protein-protein interaction databases

    BioGridi122520. 16 interactions.
    IntActiQ9C0B1. 2 interactions.
    STRINGi9606.ENSP00000418823.

    Structurei

    Secondary structure

    1
    505
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi38 – 458
    Beta strandi49 – 524
    Helixi54 – 563
    Helixi59 – 7416
    Beta strandi79 – 857
    Beta strandi88 – 10114
    Beta strandi104 – 1085
    Beta strandi111 – 1144
    Helixi130 – 16233
    Helixi190 – 1967
    Beta strandi201 – 2077
    Turni209 – 2113
    Beta strandi212 – 2143
    Beta strandi219 – 2213
    Beta strandi225 – 2317
    Beta strandi242 – 2487
    Beta strandi271 – 2766
    Beta strandi280 – 2823
    Beta strandi284 – 2885
    Beta strandi293 – 2975
    Helixi301 – 3044
    Beta strandi305 – 3106
    Beta strandi316 – 3227
    Helixi331 – 34212
    Helixi361 – 37717
    Helixi379 – 3846
    Turni385 – 3873
    Helixi389 – 3913
    Helixi397 – 42226
    Beta strandi423 – 4264
    Helixi428 – 45730
    Helixi459 – 4635
    Helixi466 – 4683
    Beta strandi483 – 4853
    Helixi490 – 50011

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3LFMX-ray2.50A32-505[»]
    4IDZX-ray2.46A32-505[»]
    4IE0X-ray2.53A32-505[»]
    4IE4X-ray2.50A32-505[»]
    4IE5X-ray1.95A32-505[»]
    4IE6X-ray2.50A32-505[»]
    4IE7X-ray2.60A32-505[»]
    ProteinModelPortaliQ9C0B1.
    SMRiQ9C0B1. Positions 30-503.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni32 – 327296Fe2OG dioxygenase domainAdd
    BLAST
    Regioni213 – 22412Loop L1; predicted to block binding of double-stranded DNA or RNAAdd
    BLAST
    Regioni231 – 2344Substrate binding
    Regioni316 – 3183Alpha-ketoglutarate binding

    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.1 Publication

    Sequence similaritiesi

    Belongs to the fto family.Curated

    Phylogenomic databases

    eggNOGiNOG45792.
    HOGENOMiHOG000273870.
    HOVERGENiHBG101847.
    InParanoidiQ9C0B1.
    OMAiAVYNYSC.
    OrthoDBiEOG7CK36T.
    PhylomeDBiQ9C0B1.
    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: Q9C0B1-1) [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

    MKRTPTAEER EREAKKLRLL EELEDTWLPY LTPKDDEFYQ QWQLKYPKLI    50
    LREASSVSEE LHKEVQEAFL TLHKHGCLFR DLVRIQGKDL LTPVSRILIG 100
    NPGCTYKYLN TRLFTVPWPV KGSNIKHTEA EIAAACETFL KLNDYLQIET 150
    IQALEELAAK EKANEDAVPL CMSADFPRVG MGSSYNGQDE VDIKSRAAYN 200
    VTLLNFMDPQ KMPYLKEEPY FGMGKMAVSW HHDENLVDRS AVAVYSYSCE 250
    GPEEESEDDS HLEGRDPDIW HVGFKISWDI ETPGLAIPLH QGDCYFMLDD 300
    LNATHQHCVL AGSQPRFSST HRVAECSTGT LDYILQRCQL ALQNVCDDVD 350
    NDDVSLKSFE PAVLKQGEEI HNEVEFEWLR QFWFQGNRYR KCTDWWCQPM 400
    AQLEALWKKM EGVTNAVLHE VKREGLPVEQ RNEILTAILA SLTARQNLRR 450
    EWHARCQSRI ARTLPADQKP ECRPYWEKDD ASMPLPFDLT DIVSELRGQL 500
    LEAKP 505
    Length:505
    Mass (Da):58,282
    Last modified:May 29, 2007 - v3
    Checksum:i3498A92C6E6D81B1
    GO
    Isoform 2 (identifier: Q9C0B1-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-378: Missing.
         379-413: LRQFWFQGNRYRKCTDWWCQPMAQLEALWKKMEGV → MEWRKVSECNSVEPCREVKKWPYRCIHHGKNFSRM

    Note: No experimental confirmation available.

    Show »
    Length:127
    Mass (Da):14,936
    Checksum:i5FA0B71723B0564B
    GO
    Isoform 3 (identifier: Q9C0B1-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-445: Missing.
         446-455: QNLRREWHAR → MACQGREECW

    Note: No experimental confirmation available.

    Show »
    Length:60
    Mass (Da):6,924
    Checksum:i54A786243F09AF34
    GO
    Isoform 4 (identifier: Q9C0B1-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-399: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:106
    Mass (Da):12,218
    Checksum:iAFE4D8E4F34B2F74
    GO

    Sequence cautioni

    The sequence BAB21843.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti316 – 3161R → W in BAB21843. (PubMed:11214970)Curated
    Sequence conflicti316 – 3161R → W in AAH03583. (PubMed:15489334)Curated
    Sequence conflicti316 – 3161R → W in AAH30798. (PubMed:15489334)Curated
    Sequence conflicti316 – 3161R → W in AAI32893. (PubMed:15489334)Curated

    Polymorphismi

    At least one intronic variation within the gene predisposes to childhood and adult obesity.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti316 – 3161R → Q in GDFD; has no residual normal activity, impaired ability to demethylate N(6)-methyladenosine RNAs (m6A) RNAs. 1 Publication
    VAR_063252
    Natural varianti405 – 4051A → V.
    Corresponds to variant rs16952624 [ dbSNP | Ensembl ].
    VAR_032078

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 445445Missing in isoform 3. 1 PublicationVSP_025002Add
    BLAST
    Alternative sequencei1 – 399399Missing in isoform 4. 1 PublicationVSP_025003Add
    BLAST
    Alternative sequencei1 – 378378Missing in isoform 2. 1 PublicationVSP_025004Add
    BLAST
    Alternative sequencei379 – 41335LRQFW…KMEGV → MEWRKVSECNSVEPCREVKK WPYRCIHHGKNFSRM in isoform 2. 1 PublicationVSP_025005Add
    BLAST
    Alternative sequencei446 – 45510QNLRREWHAR → MACQGREECW in isoform 3. 1 PublicationVSP_025006

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB051539 mRNA. Translation: BAB21843.1. Different initiation.
    AC007347 Genomic DNA. No translation available.
    AC007496 Genomic DNA. No translation available.
    AC007909 Genomic DNA. No translation available.
    BC003583 mRNA. Translation: AAH03583.1.
    BC030798 mRNA. Translation: AAH30798.1.
    BC132892 mRNA. Translation: AAI32893.1.
    BC137091 mRNA. Translation: AAI37092.1.
    CCDSiCCDS32448.1. [Q9C0B1-1]
    RefSeqiNP_001073901.1. NM_001080432.2. [Q9C0B1-1]
    UniGeneiHs.528833.

    Genome annotation databases

    EnsembliENST00000431610; ENSP00000415636; ENSG00000140718. [Q9C0B1-4]
    ENST00000460382; ENSP00000417422; ENSG00000140718. [Q9C0B1-4]
    ENST00000463855; ENSP00000417843; ENSG00000140718. [Q9C0B1-2]
    ENST00000471389; ENSP00000418823; ENSG00000140718. [Q9C0B1-1]
    GeneIDi79068.
    KEGGihsa:79068.
    UCSCiuc002ehr.3. human. [Q9C0B1-1]
    uc010cbz.3. human. [Q9C0B1-4]

    Polymorphism databases

    DMDMi148841515.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB051539 mRNA. Translation: BAB21843.1 . Different initiation.
    AC007347 Genomic DNA. No translation available.
    AC007496 Genomic DNA. No translation available.
    AC007909 Genomic DNA. No translation available.
    BC003583 mRNA. Translation: AAH03583.1 .
    BC030798 mRNA. Translation: AAH30798.1 .
    BC132892 mRNA. Translation: AAI32893.1 .
    BC137091 mRNA. Translation: AAI37092.1 .
    CCDSi CCDS32448.1. [Q9C0B1-1 ]
    RefSeqi NP_001073901.1. NM_001080432.2. [Q9C0B1-1 ]
    UniGenei Hs.528833.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3LFM X-ray 2.50 A 32-505 [» ]
    4IDZ X-ray 2.46 A 32-505 [» ]
    4IE0 X-ray 2.53 A 32-505 [» ]
    4IE4 X-ray 2.50 A 32-505 [» ]
    4IE5 X-ray 1.95 A 32-505 [» ]
    4IE6 X-ray 2.50 A 32-505 [» ]
    4IE7 X-ray 2.60 A 32-505 [» ]
    ProteinModelPortali Q9C0B1.
    SMRi Q9C0B1. Positions 30-503.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 122520. 16 interactions.
    IntActi Q9C0B1. 2 interactions.
    STRINGi 9606.ENSP00000418823.

    Chemistry

    ChEMBLi CHEMBL2331065.

    PTM databases

    PhosphoSitei Q9C0B1.

    Polymorphism databases

    DMDMi 148841515.

    Proteomic databases

    MaxQBi Q9C0B1.
    PaxDbi Q9C0B1.
    PRIDEi Q9C0B1.

    Protocols and materials databases

    DNASUi 79068.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000431610 ; ENSP00000415636 ; ENSG00000140718 . [Q9C0B1-4 ]
    ENST00000460382 ; ENSP00000417422 ; ENSG00000140718 . [Q9C0B1-4 ]
    ENST00000463855 ; ENSP00000417843 ; ENSG00000140718 . [Q9C0B1-2 ]
    ENST00000471389 ; ENSP00000418823 ; ENSG00000140718 . [Q9C0B1-1 ]
    GeneIDi 79068.
    KEGGi hsa:79068.
    UCSCi uc002ehr.3. human. [Q9C0B1-1 ]
    uc010cbz.3. human. [Q9C0B1-4 ]

    Organism-specific databases

    CTDi 79068.
    GeneCardsi GC16P053737.
    H-InvDB HIX0013037.
    HIX0134382.
    HIX0204005.
    HGNCi HGNC:24678. FTO.
    HPAi CAB017123.
    MIMi 610966. gene.
    612938. phenotype.
    neXtProti NX_Q9C0B1.
    Orphaneti 210144. Lethal polymalformative syndrome, Boissel type.
    PharmGKBi PA152208656.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG45792.
    HOGENOMi HOG000273870.
    HOVERGENi HBG101847.
    InParanoidi Q9C0B1.
    OMAi AVYNYSC.
    OrthoDBi EOG7CK36T.
    PhylomeDBi Q9C0B1.
    TreeFami TF333296.

    Miscellaneous databases

    ChiTaRSi FTO. human.
    GeneWikii FTO_gene.
    GenomeRNAii 79068.
    NextBioi 67845.
    PROi Q9C0B1.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9C0B1.
    Bgeei Q9C0B1.
    CleanExi HS_FTO.
    Genevestigatori Q9C0B1.

    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. "Prediction of the coding sequences of unidentified human genes. XIX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
      Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.
      DNA Res. 7:347-355(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Brain.
    2. "The sequence and analysis of duplication-rich human chromosome 16."
      Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
      , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
      Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Tissue: Brain.
    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] (ISOFORMS 2; 3 AND 4).
      Tissue: Cervix, Eye and Lung.
    4. Cited for: INVOLVEMENT IN PREDISPOSITION OF OBESITY, TISSUE SPECIFICITY.
    5. Cited for: INVOLVEMENT IN PREDISPOSITION OF OBESITY, 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. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-216, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. "N6-methyladenosine in nuclear RNA is a major substrate of the obesity-associated FTO."
      Jia G., Fu Y., Zhao X., Dai Q., Zheng G., Yang Y., Yi C., Lindahl T., Pan T., Yang Y.G., He C.
      Nat. Chem. Biol. 7:885-887(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF 231-HIS--ASP-233, CHARACTERIZATION OF VARIANT GDFD GLN-316.
    10. "Crystal structure of the FTO protein reveals basis for its substrate specificity."
      Han Z., Niu T., Chang J., Lei X., Zhao M., Wang Q., Cheng W., Wang J., Feng Y., Chai J.
      Nature 464:1205-1209(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 32-505 IN COMPLEX WITH IRON IONS; N-OXALYLGLYCINE AND 3-METHYLTHYMIDINE, CATALYTIC ACTIVITY, FUNCTION, COFACTOR, ENZYME REGULATION, MUTAGENESIS OF ARG-96; TYR-108; PHE-114; GLU-234 AND CYS-392, CIRCULAR DICHROISM, DOMAIN.
    11. "Loss-of-function mutation in the dioxygenase-encoding FTO gene causes severe growth retardation and multiple malformations."
      Boissel S., Reish O., Proulx K., Kawagoe-Takaki H., Sedgwick B., Yeo G.S., Meyre D., Golzio C., Molinari F., Kadhom N., Etchevers H.C., Saudek V., Farooqi I.S., Froguel P., Lindahl T., O'Rahilly S., Munnich A., Colleaux L.
      Am. J. Hum. Genet. 85:106-111(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT GDFD GLN-316, CHARACTERIZATION OF VARIANT GDFD GLN-316.

    Entry informationi

    Entry nameiFTO_HUMAN
    AccessioniPrimary (citable) accession number: Q9C0B1
    Secondary accession number(s): A2RUH1
    , B2RNS0, Q0P676, Q7Z785
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 2007
    Last sequence update: May 29, 2007
    Last modified: October 1, 2014
    This is version 90 of the entry and version 3 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 16
      Human chromosome 16: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3