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Entry version 120 (18 Sep 2019)
Sequence version 1 (01 Mar 2003)
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Protein

Alpha-ketoglutarate-dependent dioxygenase FTO

Gene

Fto

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

RNA demethylase that mediates oxidative demethylation of different RNA species, such as mRNAs, tRNAs and snRNAs, and acts as a regulator of fat mass, adipogenesis and energy homeostasis (PubMed:17991826, PubMed:18775698, PubMed:28002401). Specifically demethylates N6-methyladenosine (m6A) RNA, the most prevalent internal modification of messenger RNA (mRNA) in higher eukaryotes (PubMed:28002401). M6A demethylation by FTO affects mRNA expression and stability (By similarity). Also able to demethylate m6A in U6 small nuclear RNA (snRNA) (By similarity). Mediates demethylation of N6,2'-O-dimethyladenosine cap (m6A(m)), by demethylating the N6-methyladenosine at the second transcribed position of mRNAs and U6 snRNA (PubMed:28002401). Demethylation of m6A(m) in the 5'-cap by FTO affects mRNA stability by promoting susceptibility to decapping (By similarity). Also acts as a tRNA demethylase by removing N1-methyladenine from various tRNAs (By similarity). Has no activity towards 1-methylguanine (By similarity). Has no detectable activity towards double-stranded DNA (By similarity). Also able to repair alkylated DNA and RNA by oxidative demethylation: demethylates single-stranded RNA containing 3-methyluracil, single-stranded DNA containing 3-methylthymine and has low demethylase activity towards single-stranded DNA containing 1-methyladenine or 3-methylcytosine (PubMed:17991826, PubMed:18775698). Ability to repair alkylated DNA and RNA is however unsure in vivo (PubMed:17991826, PubMed:18775698). Involved in the regulation of fat mass, adipogenesis and body weight, thereby contributing to the regulation of body size and body fat accumulation (PubMed:19234441, PubMed:19680540, PubMed:21076408, PubMed:23817550, PubMed:23300482). Involved in the regulation of thermogenesis and the control of adipocyte differentiation into brown or white fat cells (PubMed:19234441, PubMed:19680540). Regulates activity of the dopaminergic midbrain circuitry via its ability to demethylate m6A in mRNAs (PubMed:23817550).By similarity8 Publications

Caution

Many publications have reported a critical role of Fto in regulating fat mass, adipogenesis and total body weight (PubMed:19234441, PubMed:19680540, PubMed:21076408, PubMed:23817550, PubMed:23300482). However, some reports suggest that some effects are indirect and caused by impaired expression of adjacent genes such as Irx3 and Rpgrip1l (PubMed:24807221, PubMed:24646999).7 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Fe2+1 PublicationNote: Binds 1 Fe2+ ion per subunit.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Activated by ascorbate (PubMed:17991826). Inhibited by N-oxalylglycine, fumarate and succinate (PubMed:17991826).1 Publication

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>pH dependencei

Optimum pH is 5.5-6.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei96SubstrateBy similarity1
Binding sitei108SubstrateBy similarity1
Binding sitei202Alpha-ketoglutarateBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi228Iron; catalyticBy similarity1
Metal bindingi230Iron; catalyticBy similarity1
Binding sitei292Alpha-ketoglutarateBy similarity1
Metal bindingi304Iron; catalyticBy similarity1
Binding sitei317Alpha-ketoglutarateBy similarity1
Binding sitei319Alpha-ketoglutarateBy similarity1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionDioxygenase, Oxidoreductase
LigandIron, Metal-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-MMU-73943 Reversal of alkylation damage by DNA dioxygenases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Alpha-ketoglutarate-dependent dioxygenase FTOCurated
Alternative name(s):
Fat mass and obesity-associated protein1 Publication
Protein fatso1 Publication
U6 small nuclear RNA (2'-O-methyladenosine-N(6)-)-demethylase FTOCurated (EC:1.14.11.-By similarity)
U6 small nuclear RNA N(6)-methyladenosine-demethylase FTOCurated (EC:1.14.11.-By similarity)
mRNA (2'-O-methyladenosine-N(6)-)-demethylase FTOCurated (EC:1.14.11.-By similarity)
Short name:
m6A(m)-demethylase FTOCurated
mRNA N(6)-methyladenosine demethylase FTOCurated (EC:1.14.11.531 Publication)
tRNA N1-methyl adenine demethylase FTOCurated (EC:1.14.11.-By similarity)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Fto1 PublicationImported
Synonyms:Kiaa17521 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiMus musculus (Mouse)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10090 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000589 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 8

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...
MGIi
MGI:1347093 Fto

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Elevated perinatal mortality (PubMed:19234441). 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 (PubMed:19234441). In addition, animals display reduced nose to anus length (PubMed:19234441). Fat mass is reduced by 60% in males and by 23% in females (PubMed:19234441). Lean body mass is reduced by 26% in males and 19% in females (PubMed:19234441). White adipose tissue decreases more and more over time, while brown adipose tissue is not affected (PubMed:19234441). Serum leptin levels are decreased, while serum levels of adiponectin are increased (PubMed:19234441). Mice exhibit significant hyperphagia after correction for body weight (PubMed:19234441). They show increased oxygen consumption, carbon dioxide production and heat generation, indicating increased energy expenditure, in spite of reduced spontaneous locomotor activity (PubMed:19234441). Plasma adrenaline concentrations are significantly increased (PubMed:19234441). Overall glucose metabolism appears normal (PubMed:19234441). Conditional deletion in the adult affects body composition and metabolism, and causes a small reduction in food intake and weight gain (PubMed:23300482). Mice with conditional deletion in dopaminergic neurons show abnormal dopamine signaling pathways, including impaired dopamine receptor type 2 (D2R) and type 3 (D3R) signaling and the related locomotion function (PubMed:23817550). Deficient mice show increased N6-methyladenosine (m6A) in a subset of mRNAs important for neuronal signaling, including many in the dopaminergic signaling pathway (PubMed:23817550). Knockout cells show strongly increased levels of N6,2'-O-dimethyladenosine cap (m6A(m)) mRNAs (PubMed:28002401).4 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi304H → A: Reduced enzyme activity. 1 Publication1
Mutagenesisi313R → A: Loss of enzyme activity. 1 Publication1
Mutagenesisi367I → A: Reduces enzyme activity by about 60%. 1 Publication1
Mutagenesisi367I → 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 Publication1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL3611964

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002861641 – 502Alpha-ketoglutarate-dependent dioxygenase FTOAdd BLAST502

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei213N6-acetyllysineBy similarity1

Keywords - PTMi

Acetylation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
Q8BGW1

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
Q8BGW1

PeptideAtlas

More...
PeptideAtlasi
Q8BGW1

PRoteomics IDEntifications database

More...
PRIDEi
Q8BGW1

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q8BGW1

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
Q8BGW1

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>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

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Down-regulated in fasting animals.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSMUSG00000055932 Expressed in 290 organ(s), highest expression level in superior colliculus

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q8BGW1 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q8BGW1 MM

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Monomer (PubMed:19680540). May also exist as homodimer (PubMed:19680540).

1 Publication

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
204941, 1 interactor

STRING: functional protein association networks

More...
STRINGi
10090.ENSMUSP00000068380

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
Q8BGW1

Database of comparative protein structure models

More...
ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni32 – 324Fe2OG dioxygenase domainBy similarityAdd BLAST293
Regioni210 – 221Loop L1; predicted to block binding of double-stranded DNA or RNABy similarityAdd BLAST12
Regioni228 – 231Substrate bindingBy similarity4
Regioni313 – 315Alpha-ketoglutarate bindingBy similarity3

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>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

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the fto family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG410IJ5C Eukaryota
ENOG4111PKJ LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00390000017730

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q8BGW1

KEGG Orthology (KO)

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KOi
K19469

Identification of Orthologs from Complete Genome Data

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OMAi
WFQGKRY

Database of Orthologous Groups

More...
OrthoDBi
1300974at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q8BGW1

TreeFam database of animal gene trees

More...
TreeFami
TF333296

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.20.58.1470, 1 hit
2.60.120.590, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR037151 AlkB-like_sf
IPR032868 FTO
IPR024366 FTO_C
IPR038413 FTO_C_sf
IPR024367 FTO_cat_dom

The PANTHER Classification System

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PANTHERi
PTHR31291 PTHR31291, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF12934 FTO_CTD, 1 hit
PF12933 FTO_NTD, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM01223 FTO_NTD, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (4+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry describes 4 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 4 described isoforms and 2 potential isoforms that are computationally mapped.Show allAlign All

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

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali 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
MKRVQTAEER EREAKKLRLL EELEDTWLPY LTPKDDEFYQ QWQLKYPKLV
60 70 80 90 100
FREAGSIPEE LHKEVPEAFL TLHKHGCLFR DVVRIQGKDV LTPVSRILIG
110 120 130 140 150
DPGCTYKYLN TRLFTVPWPV KGCTVKYTEA EIAAACQTFL KLNDYLQVET
160 170 180 190 200
IQALEELAVR EKANEDAVPL CMAEFPRAGV GPSCDDEVDL KSRAAYNVTL
210 220 230 240 250
LNFMDPQKMP YLKEEPYFGM GKMAVSWHHD ENLVDRSAVA VYSYSCEGSE
260 270 280 290 300
DESEDESSFE GRDPDTWHVG FKISWDIETP GLTIPLHQGD CYFMLDDLNA
310 320 330 340 350
THQHCVLAGS QPRFSSTHRV AECSTGTLDY ILERCQLALQ NVLNDSDDGD
360 370 380 390 400
VSLKSFDPAV LKQGEEIHNE VEFEWLRQFW FQGNRYKLCT DWWCEPMTHL
410 420 430 440 450
EGLWKKMESM TNAVLREVKR EGLPVEQRSE ILSAILVPLT VRQNLRKEWH
460 470 480 490 500
ARCQSRVVRT LPVQQKPDCR PYWEKDDPSM PLPFDLTDVV SELRGQLLEA

RS
Length:502
Mass (Da):58,007
Last modified:March 1, 2003 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> 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

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
D3Z127D3Z127_MOUSE
Alpha-ketoglutarate-dependent dioxy...
Fto
149Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
E9Q1E4E9Q1E4_MOUSE
Alpha-ketoglutarate-dependent dioxy...
Fto
270Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti181G → R in BAC32382 (PubMed:16141072).Curated1
Sequence conflicti384N → S in CAB59324 (PubMed:10501967).Curated1
Sequence conflicti384N → S in BAC98247 (PubMed:14621295).Curated1
Sequence conflicti384N → S in BAC40629 (PubMed:16141072).Curated1
Sequence conflicti384N → S in AAH22222 (PubMed:15489334).Curated1
Sequence conflicti410M → V in BAC98247 (PubMed:14621295).Curated1
Sequence conflicti410M → V in BAC40629 (PubMed:16141072).Curated1
Sequence conflicti410M → V in AAH22222 (PubMed:15489334).Curated1
Sequence conflicti463V → A in BAC40629 (PubMed:16141072).Curated1
Sequence conflicti463V → A in AAH22222 (PubMed:15489334).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_025007296 – 316DDLNA…PRFSS → GNVGSLRVGHLWGFEIHFWI L in isoform 4. 1 PublicationAdd BLAST21
Alternative sequenceiVSP_025008317 – 502Missing in isoform 4. 1 PublicationAdd BLAST186
Alternative sequenceiVSP_025009411 – 413TNA → VSA in isoform 3. 1 Publication3
Alternative sequenceiVSP_025010414 – 502Missing in isoform 3. 1 PublicationAdd BLAST89
Alternative sequenceiVSP_025011453 – 502CQSRV…LEARS → FVLLRGGVWCPCPSSARPAQ RTKVEDILS in isoform 2. 1 PublicationAdd BLAST50

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
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

The Consensus CDS (CCDS) project

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CCDSi
CCDS22521.1 [Q8BGW1-1]

NCBI Reference Sequences

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RefSeqi
NP_036066.2, NM_011936.2 [Q8BGW1-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSMUST00000069718; ENSMUSP00000068380; ENSMUSG00000055932 [Q8BGW1-1]
ENSMUST00000125471; ENSMUSP00000147563; ENSMUSG00000055932 [Q8BGW1-4]
ENSMUST00000128081; ENSMUSP00000147548; ENSMUSG00000055932 [Q8BGW1-2]
ENSMUST00000136802; ENSMUSP00000147603; ENSMUSG00000055932 [Q8BGW1-3]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
26383

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
mmu:26383

UCSC genome browser

More...
UCSCi
uc009msq.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

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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]

3D structure databases

SMRiQ8BGW1
ModBaseiSearch...

Protein-protein interaction databases

BioGridi204941, 1 interactor
STRINGi10090.ENSMUSP00000068380

Chemistry databases

ChEMBLiCHEMBL3611964

PTM databases

iPTMnetiQ8BGW1
PhosphoSitePlusiQ8BGW1

Proteomic databases

EPDiQ8BGW1
PaxDbiQ8BGW1
PeptideAtlasiQ8BGW1
PRIDEiQ8BGW1

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000069718; ENSMUSP00000068380; ENSMUSG00000055932 [Q8BGW1-1]
ENSMUST00000125471; ENSMUSP00000147563; ENSMUSG00000055932 [Q8BGW1-4]
ENSMUST00000128081; ENSMUSP00000147548; ENSMUSG00000055932 [Q8BGW1-2]
ENSMUST00000136802; ENSMUSP00000147603; ENSMUSG00000055932 [Q8BGW1-3]
GeneIDi26383
KEGGimmu:26383
UCSCiuc009msq.2 mouse [Q8BGW1-4]
uc009msr.2 mouse [Q8BGW1-3]
uc009mss.2 mouse [Q8BGW1-2]
uc009mst.2 mouse [Q8BGW1-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
79068
MGIiMGI:1347093 Fto

Rodent Unidentified Gene-Encoded large proteins database

More...
Rougei
Search...

Phylogenomic databases

eggNOGiENOG410IJ5C Eukaryota
ENOG4111PKJ LUCA
GeneTreeiENSGT00390000017730
InParanoidiQ8BGW1
KOiK19469
OMAiWFQGKRY
OrthoDBi1300974at2759
PhylomeDBiQ8BGW1
TreeFamiTF333296

Enzyme and pathway databases

ReactomeiR-MMU-73943 Reversal of alkylation damage by DNA dioxygenases

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
Fto mouse

Protein Ontology

More...
PROi
PR:Q8BGW1

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000055932 Expressed in 290 organ(s), highest expression level in superior colliculus
ExpressionAtlasiQ8BGW1 baseline and differential
GenevisibleiQ8BGW1 MM

Family and domain databases

Gene3Di1.20.58.1470, 1 hit
2.60.120.590, 1 hit
InterProiView protein in InterPro
IPR037151 AlkB-like_sf
IPR032868 FTO
IPR024366 FTO_C
IPR038413 FTO_C_sf
IPR024367 FTO_cat_dom
PANTHERiPTHR31291 PTHR31291, 1 hit
PfamiView protein in Pfam
PF12934 FTO_CTD, 1 hit
PF12933 FTO_NTD, 1 hit
SMARTiView protein in SMART
SM01223 FTO_NTD, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiFTO_MOUSE
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q8BGW1
Secondary accession number(s): Q3TTZ5
, Q6ZPI7, Q8BR68, Q8CB66, Q8R250, Q9QZ13
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 1, 2007
Last sequence update: March 1, 2003
Last modified: September 18, 2019
This is version 120 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
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