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Q9C0B1

- FTO_HUMAN

UniProt

Q9C0B1 - FTO_HUMAN

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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

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
Complete GO annotation...

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
Complete GO annotation...

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. 1 Publication
Mutagenesisi108 – 1081Y → A: Abolishes enzyme activity. 1 Publication
Mutagenesisi114 – 1141F → D: Perturbs interaction between N-terminal and C-terminal domains and strongly reduces enzyme activity. 1 Publication
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. 1 Publication
Mutagenesisi392 – 3921C → D: Perturbs interaction between N-terminal and C-terminal domains and strongly reduces enzyme activity. 1 Publication

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

BgeeiQ9C0B1.
CleanExiHS_FTO.
ExpressionAtlasiQ9C0B1. baseline.
GenevestigatoriQ9C0B1.

Organism-specific databases

HPAiCAB017123.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi122520. 17 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.
GeneTreeiENSGT00390000017730.
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

        10         20         30         40         50
MKRTPTAEER EREAKKLRLL EELEDTWLPY LTPKDDEFYQ QWQLKYPKLI
60 70 80 90 100
LREASSVSEE LHKEVQEAFL TLHKHGCLFR DLVRIQGKDL LTPVSRILIG
110 120 130 140 150
NPGCTYKYLN TRLFTVPWPV KGSNIKHTEA EIAAACETFL KLNDYLQIET
160 170 180 190 200
IQALEELAAK EKANEDAVPL CMSADFPRVG MGSSYNGQDE VDIKSRAAYN
210 220 230 240 250
VTLLNFMDPQ KMPYLKEEPY FGMGKMAVSW HHDENLVDRS AVAVYSYSCE
260 270 280 290 300
GPEEESEDDS HLEGRDPDIW HVGFKISWDI ETPGLAIPLH QGDCYFMLDD
310 320 330 340 350
LNATHQHCVL AGSQPRFSST HRVAECSTGT LDYILQRCQL ALQNVCDDVD
360 370 380 390 400
NDDVSLKSFE PAVLKQGEEI HNEVEFEWLR QFWFQGNRYR KCTDWWCQPM
410 420 430 440 450
AQLEALWKKM EGVTNAVLHE VKREGLPVEQ RNEILTAILA SLTARQNLRR
460 470 480 490 500
EWHARCQSRI ARTLPADQKP ECRPYWEKDD ASMPLPFDLT DIVSELRGQL

LEAKP
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. 17 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.
GeneTreei ENSGT00390000017730.
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

Bgeei Q9C0B1.
CleanExi HS_FTO.
ExpressionAtlasi Q9C0B1. baseline.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 91 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