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Protein

Alpha-ketoglutarate-dependent dioxygenase FTO

Gene

FTO

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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 (PubMed:18775698, PubMed:20376003). Specifically demethylates N(6)-methyladenosine (m6A) RNA, the most prevalent internal modification of messenger RNA (mRNA) in higher eukaryotes (PubMed:22002720, PubMed:26458103). 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 (PubMed:18775698, PubMed:20376003). In particular, it is involved in the regulation of thermogenesis and the control of adipocyte differentiation into brown or white fat cells (PubMed:26287746).5 Publications

Catalytic activityi

N(6)-methyladenosine in mRNA + 2-oxoglutarate + O2 = adenosine in mRNA + formaldehyde + succinate + CO2.1 Publication

Cofactori

Fe2+1 PublicationNote: 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)DescriptionActionsGraphical viewLength
Binding sitei96Substrate1
Binding sitei108Substrate1
Binding sitei205Alpha-ketoglutarate1
Metal bindingi231Iron; catalytic1
Metal bindingi233Iron; catalytic1
Binding sitei295Alpha-ketoglutarate1
Metal bindingi307Iron; catalytic1
Binding sitei320Alpha-ketoglutarate1
Binding sitei322Alpha-ketoglutarate1

GO - Molecular functioni

  • DNA-N1-methyladenine dioxygenase activity Source: UniProtKB
  • ferrous iron binding Source: UniProtKB
  • oxidative DNA demethylase activity Source: UniProtKB
  • oxidative RNA demethylase activity Source: UniProtKB
  • RNA N6-methyladenosine dioxygenase activity Source: UniProtKB

GO - Biological processi

  • adipose tissue development Source: Ensembl
  • DNA dealkylation involved in DNA repair Source: UniProtKB
  • DNA demethylation Source: BHF-UCL
  • oxidative demethylation Source: BHF-UCL
  • oxidative single-stranded DNA demethylation Source: UniProtKB
  • oxidative single-stranded RNA demethylation Source: UniProtKB
  • regulation of brown fat cell differentiation Source: UniProtKB
  • regulation of lipid storage Source: UniProtKB
  • regulation of multicellular organism growth Source: Ensembl
  • regulation of respiratory system process Source: Ensembl
  • regulation of white fat cell proliferation Source: Ensembl
  • RNA repair Source: BHF-UCL
  • 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

Enzyme and pathway databases

ReactomeiR-HSA-73943. Reversal of alkylation damage by DNA dioxygenases.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-ketoglutarate-dependent dioxygenase FTO (EC:1.14.11.-1 Publication)
Alternative name(s):
Fat mass and obesity-associated protein
Gene namesi
Name:FTO
Synonyms:KIAA1752
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:24678. FTO.

Subcellular locationi

GO - Cellular componenti

  • nuclear speck Source: UniProtKB
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

Growth retardation, developmental delay, and facial dysmorphism (GDFD)3 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:612938
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_063252316R → Q in GDFD; has no residual normal activity, impaired ability to demethylate N(6)-methyladenosine RNAs (m6A) RNAs. 2 PublicationsCorresponds to variant rs121918214dbSNPEnsembl.1
Natural variantiVAR_075468319S → F in GDFD; reduced enzyme activity. 1 Publication1
Natural variantiVAR_075469322R → Q in GDFD. 1 PublicationCorresponds to variant rs745616565dbSNPEnsembl.1
Obesity (OBESITY)1 Publication
Disease susceptibility is associated with variations affecting the gene represented in this entry. A pathogenic intronic FTO variation (rs1421085) disrupts an evolutionarily conserved motif for ARID5B binding. Loss of ARID5B binding results in overexpression of two genes distal to FTO, IRX3 and IRX5. IRX3 and IRX5 overexpression shifts pre-adipocytes differentiation from brown to white fat cells, resulting in increased lipid storage and loss of mitochondrial thermogenesis.1 Publication
Disease descriptionA condition characterized by an increase of body weight beyond the limitation of skeletal and physical requirements, as the result of excessive accumulation of body fat.
See also OMIM:601665

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi96R → M or W: Almost abolishes enzyme activity. 1 Publication1
Mutagenesisi108Y → A: Abolishes enzyme activity. 1 Publication1
Mutagenesisi114F → D: Perturbs interaction between N-terminal and C-terminal domains and strongly reduces enzyme activity. 1 Publication1
Mutagenesisi231 – 233HHD → AHA: Abolishes ability to demethylate N(6)-methyladenosine RNAs (m6A) RNAs. 1 Publication3
Mutagenesisi234E → P: Abolishes enzyme activity. Abolishes ability to demethylate N(6)-methyladenosine RNAs (m6A) RNAs; when associated with Q-322. 1 Publication1
Mutagenesisi392C → D: Perturbs interaction between N-terminal and C-terminal domains and strongly reduces enzyme activity. 1 Publication1

Keywords - Diseasei

Disease mutation, Obesity

Organism-specific databases

DisGeNETi79068.
MalaCardsiFTO.
MIMi601665. phenotype.
612460. phenotype.
612938. phenotype.
OpenTargetsiENSG00000140718.
Orphaneti210144. Lethal polymalformative syndrome, Boissel type.
PharmGKBiPA152208656.

Chemistry databases

ChEMBLiCHEMBL2331065.

Polymorphism and mutation databases

BioMutaiFTO.
DMDMi148841515.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002861631 – 505Alpha-ketoglutarate-dependent dioxygenase FTOAdd BLAST505

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei4PhosphothreonineCombined sources1
Modified residuei216N6-acetyllysineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9C0B1.
MaxQBiQ9C0B1.
PaxDbiQ9C0B1.
PeptideAtlasiQ9C0B1.
PRIDEiQ9C0B1.

PTM databases

iPTMnetiQ9C0B1.
PhosphoSitePlusiQ9C0B1.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiENSG00000140718.
CleanExiHS_FTO.
ExpressionAtlasiQ9C0B1. baseline and differential.
GenevisibleiQ9C0B1. HS.

Organism-specific databases

HPAiCAB017123.
HPA041086.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi122520. 25 interactors.
IntActiQ9C0B1. 2 interactors.
STRINGi9606.ENSP00000418823.

Chemistry databases

BindingDBiQ9C0B1.

Structurei

Secondary structure

1505
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi35 – 37Combined sources3
Helixi38 – 45Combined sources8
Beta strandi49 – 52Combined sources4
Helixi54 – 56Combined sources3
Helixi59 – 74Combined sources16
Beta strandi79 – 85Combined sources7
Beta strandi88 – 101Combined sources14
Beta strandi104 – 108Combined sources5
Beta strandi111 – 114Combined sources4
Helixi130 – 162Combined sources33
Helixi190 – 196Combined sources7
Beta strandi201 – 207Combined sources7
Turni209 – 211Combined sources3
Beta strandi212 – 214Combined sources3
Beta strandi219 – 221Combined sources3
Beta strandi225 – 231Combined sources7
Beta strandi242 – 248Combined sources7
Beta strandi271 – 276Combined sources6
Beta strandi280 – 282Combined sources3
Beta strandi284 – 288Combined sources5
Beta strandi293 – 297Combined sources5
Helixi301 – 304Combined sources4
Beta strandi305 – 310Combined sources6
Beta strandi316 – 322Combined sources7
Turni327 – 329Combined sources3
Helixi331 – 342Combined sources12
Helixi361 – 377Combined sources17
Helixi379 – 384Combined sources6
Turni385 – 387Combined sources3
Helixi389 – 391Combined sources3
Helixi397 – 422Combined sources26
Beta strandi423 – 426Combined sources4
Helixi428 – 457Combined sources30
Helixi459 – 463Combined sources5
Helixi466 – 468Combined sources3
Beta strandi482 – 485Combined sources4
Helixi490 – 500Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3LFMX-ray2.50A32-505[»]
4CXWX-ray3.10A32-505[»]
4CXXX-ray2.76A32-505[»]
4CXYX-ray2.65A32-505[»]
4IDZX-ray2.46A32-505[»]
4IE0X-ray2.53A32-505[»]
4IE4X-ray2.50A32-505[»]
4IE5X-ray1.95A32-505[»]
4IE6X-ray2.50A32-505[»]
4IE7X-ray2.60A32-505[»]
4QHOX-ray2.37A32-505[»]
4QKNX-ray2.20A32-503[»]
4ZS2X-ray2.16A32-505[»]
4ZS3X-ray2.45A32-505[»]
5DABX-ray2.10A32-505[»]
ProteinModelPortaliQ9C0B1.
SMRiQ9C0B1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni32 – 327Fe2OG dioxygenase domainAdd BLAST296
Regioni213 – 224Loop L1; predicted to block binding of double-stranded DNA or RNAAdd BLAST12
Regioni231 – 234Substrate binding4
Regioni316 – 318Alpha-ketoglutarate binding3

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

eggNOGiENOG410IJ5C. Eukaryota.
ENOG4111PKJ. LUCA.
GeneTreeiENSGT00390000017730.
HOGENOMiHOG000273870.
HOVERGENiHBG101847.
InParanoidiQ9C0B1.
KOiK19469.
OMAiPVCIGPD.
OrthoDBiEOG091G08LA.
PhylomeDBiQ9C0B1.
TreeFamiTF333296.

Family and domain databases

InterProiIPR032868. FTO.
IPR024366. FTO_C.
IPR024367. FTO_cat_dom.
[Graphical view]
PANTHERiPTHR31291. PTHR31291. 1 hit.
PfamiPF12934. FTO_CTD. 1 hit.
PF12933. FTO_NTD. 1 hit.
[Graphical view]
SMARTiSM01223. FTO_NTD. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

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 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti316R → W in BAB21843 (PubMed:11214970).Curated1
Sequence conflicti316R → W in AAH03583 (PubMed:15489334).Curated1
Sequence conflicti316R → W in AAH30798 (PubMed:15489334).Curated1
Sequence conflicti316R → W in AAI32893 (PubMed:15489334).Curated1

Polymorphismi

Genetic variations at the FTO locus define the body mass index quantitative trait locus 14 (BMIQ14) [MIMi:612460]. Variance in body mass index is a susceptibility factor for obesity.3 Publications

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_076423271H → P Found in a patient with microcephaly, developmental delay, behavioral abnormalities, dysmorphic facial features, hypotonia and other various phenotypic abnormalities; unknown pathological significance. 1 Publication1
Natural variantiVAR_063252316R → Q in GDFD; has no residual normal activity, impaired ability to demethylate N(6)-methyladenosine RNAs (m6A) RNAs. 2 PublicationsCorresponds to variant rs121918214dbSNPEnsembl.1
Natural variantiVAR_075468319S → F in GDFD; reduced enzyme activity. 1 Publication1
Natural variantiVAR_075469322R → Q in GDFD. 1 PublicationCorresponds to variant rs745616565dbSNPEnsembl.1
Natural variantiVAR_032078405A → V.Corresponds to variant rs16952624dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0250021 – 445Missing in isoform 3. 1 PublicationAdd BLAST445
Alternative sequenceiVSP_0250031 – 399Missing in isoform 4. 1 PublicationAdd BLAST399
Alternative sequenceiVSP_0250041 – 378Missing in isoform 2. 1 PublicationAdd BLAST378
Alternative sequenceiVSP_025005379 – 413LRQFW…KMEGV → MEWRKVSECNSVEPCREVKK WPYRCIHHGKNFSRM in isoform 2. 1 PublicationAdd BLAST35
Alternative sequenceiVSP_025006446 – 455QNLRREWHAR → MACQGREECW in isoform 3. 1 Publication10

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.4. human. [Q9C0B1-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3LFMX-ray2.50A32-505[»]
4CXWX-ray3.10A32-505[»]
4CXXX-ray2.76A32-505[»]
4CXYX-ray2.65A32-505[»]
4IDZX-ray2.46A32-505[»]
4IE0X-ray2.53A32-505[»]
4IE4X-ray2.50A32-505[»]
4IE5X-ray1.95A32-505[»]
4IE6X-ray2.50A32-505[»]
4IE7X-ray2.60A32-505[»]
4QHOX-ray2.37A32-505[»]
4QKNX-ray2.20A32-503[»]
4ZS2X-ray2.16A32-505[»]
4ZS3X-ray2.45A32-505[»]
5DABX-ray2.10A32-505[»]
ProteinModelPortaliQ9C0B1.
SMRiQ9C0B1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122520. 25 interactors.
IntActiQ9C0B1. 2 interactors.
STRINGi9606.ENSP00000418823.

Chemistry databases

BindingDBiQ9C0B1.
ChEMBLiCHEMBL2331065.

PTM databases

iPTMnetiQ9C0B1.
PhosphoSitePlusiQ9C0B1.

Polymorphism and mutation databases

BioMutaiFTO.
DMDMi148841515.

Proteomic databases

EPDiQ9C0B1.
MaxQBiQ9C0B1.
PaxDbiQ9C0B1.
PeptideAtlasiQ9C0B1.
PRIDEiQ9C0B1.

Protocols and materials databases

DNASUi79068.
Structural Biology KnowledgebaseSearch...

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.4. human. [Q9C0B1-1]

Organism-specific databases

CTDi79068.
DisGeNETi79068.
GeneCardsiFTO.
H-InvDBHIX0013037.
HIX0134382.
HIX0204005.
HGNCiHGNC:24678. FTO.
HPAiCAB017123.
HPA041086.
MalaCardsiFTO.
MIMi601665. phenotype.
610966. gene.
612460. phenotype.
612938. phenotype.
neXtProtiNX_Q9C0B1.
OpenTargetsiENSG00000140718.
Orphaneti210144. Lethal polymalformative syndrome, Boissel type.
PharmGKBiPA152208656.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IJ5C. Eukaryota.
ENOG4111PKJ. LUCA.
GeneTreeiENSGT00390000017730.
HOGENOMiHOG000273870.
HOVERGENiHBG101847.
InParanoidiQ9C0B1.
KOiK19469.
OMAiPVCIGPD.
OrthoDBiEOG091G08LA.
PhylomeDBiQ9C0B1.
TreeFamiTF333296.

Enzyme and pathway databases

ReactomeiR-HSA-73943. Reversal of alkylation damage by DNA dioxygenases.

Miscellaneous databases

ChiTaRSiFTO. human.
GeneWikiiFTO_gene.
GenomeRNAii79068.
PROiQ9C0B1.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000140718.
CleanExiHS_FTO.
ExpressionAtlasiQ9C0B1. baseline and differential.
GenevisibleiQ9C0B1. HS.

Family and domain databases

InterProiIPR032868. FTO.
IPR024366. FTO_C.
IPR024367. FTO_cat_dom.
[Graphical view]
PANTHERiPTHR31291. PTHR31291. 1 hit.
PfamiPF12934. FTO_CTD. 1 hit.
PF12933. FTO_NTD. 1 hit.
[Graphical view]
SMARTiSM01223. FTO_NTD. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: November 30, 2016
This is version 112 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

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 one 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.