Q8BGW1 (FTO_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Alpha-ketoglutarate-dependent dioxygenase FTO
EC=1.14.11.-

Alternative name(s):
Fat mass and obesity-associated protein
Protein fatso

Gene names

Name:	Fto
Synonyms:	Kiaa1752

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	502 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. 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. Ref.5 Ref.6 Ref.7 Ref.8
Cofactor	Binds 1 Fe2+ ion per subunit. Ref.5
Enzyme regulation	Activated by ascorbate. Inhibited by N-oxalylglycine, fumarate and succinate. Ref.5
Subunit structure	Monomer. May also exist as homodimer. Ref.8
Subcellular location	Nucleus Ref.5 Ref.7 Ref.8.
Tissue specificity	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. Ref.5 Ref.7
Induction	Down-regulated in fasting animals. Ref.5
Domain	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.
Disruption phenotype	Elevated perinatal mortality. Mice have normal body weight at birth, but show growth retardation from day 2 onwards, resulting in a weight reduction of 30-40% after 6 weeks, both in males and females. In addition, animals display reduced nose to anus length. Fat mass is reduced by 60% in males and by 23% in females. Lean body mass is reduced by 26% in males and 19% in females. White adipose tissue decreases more and more over time, while brown adipose tissue is not affected. Serum leptin levels are decreased, while serum levels of adiponectin are increased. Mice exhibit significant hyperphagia after correction for body weight. They show increased oxygen consumption, carbon dioxide production and heat generation, indicating increased energy expenditure, in spite of reduced spontaneous locomotor activity. Plasma adrenaline concentrations are significantly increased. Overall glucose metabolism appears normal. Ref.7
Sequence similarities	Belongs to the fto family.
Biophysicochemical properties	pH dependence: Optimum pH is 5.5-6. Ref.6
Sequence caution	The sequence BAC98247.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Biological process	DNA damage DNA repair RNA repair
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Disease	Obesity
Ligand	Iron Metal-binding
Molecular function	Dioxygenase Oxidoreductase
PTM	Acetylation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA dealkylation involved in DNA repair Inferred from sequence or structural similarity. Source: UniProtKB RNA repair Inferred from direct assay Ref.6. Source: BHF-UCL adipose tissue development Inferred from mutant phenotype Ref.7. Source: UniProtKB oxidative single-stranded DNA demethylation Inferred from direct assay Ref.6. Source: BHF-UCL oxidative single-stranded RNA demethylation Inferred from direct assay Ref.6. Source: BHF-UCL regulation of lipid storage Inferred from mutant phenotype Ref.7. Source: UniProtKB regulation of multicellular organism growth Inferred from mutant phenotype Ref.7. Source: UniProtKB regulation of respiratory system process Inferred from mutant phenotype Ref.7. Source: UniProtKB regulation of white fat cell proliferation Inferred from mutant phenotype Ref.7. Source: UniProtKB temperature homeostasis Inferred from mutant phenotype Ref.7. Source: UniProtKB
Cellular_component	nucleus Inferred from direct assay Ref.7. Source: UniProtKB
Molecular_function	DNA-N1-methyladenine dioxygenase activity Inferred from direct assay Ref.5. Source: UniProtKB ferrous iron binding Inferred from sequence or structural similarity. Source: UniProtKB oxidative DNA demethylase activity Inferred from direct assay Ref.6. Source: BHF-UCL oxidative RNA demethylase activity Inferred from direct assay Ref.6. Source: BHF-UCL oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q8BGW1-1)

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.

Isoform 2 (identifier: Q8BGW1-2)

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

Note: No experimental confirmation available.

Isoform 3 (identifier: Q8BGW1-3)

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

Note: No experimental confirmation available.

Isoform 4 (identifier: Q8BGW1-4)

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

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 502	502	Alpha-ketoglutarate-dependent dioxygenase FTO		PRO_0000286164
Regions
	Region	42 – 324	283	Fe2OG dioxygenase domain By similarity
	Region	210 – 221	12	Loop L1; predicted to block binding of double-stranded DNA or RNA By similarity
	Region	228 – 231	4	Substrate binding By similarity
	Region	313 – 315	3	Alpha-ketoglutarate binding By similarity
Sites
	Metal binding	228	1	Iron; catalytic By similarity
	Metal binding	230	1	Iron; catalytic By similarity
	Metal binding	304	1	Iron; catalytic By similarity
	Binding site	96	1	Substrate By similarity
	Binding site	108	1	Substrate By similarity
	Binding site	202	1	Alpha-ketoglutarate By similarity
	Binding site	292	1	Alpha-ketoglutarate By similarity
	Binding site	317	1	Alpha-ketoglutarate By similarity
	Binding site	319	1	Alpha-ketoglutarate By similarity
Amino acid modifications
	Modified residue	213	1	N6-acetyllysine By similarity
Natural variations
	Alternative sequence	296 – 316	21	DDLNA…PRFSS → GNVGSLRVGHLWGFEIHFWI L in isoform 4.		VSP_025007
	Alternative sequence	317 – 502	186	Missing in isoform 4.		VSP_025008
	Alternative sequence	411 – 413	3	TNA → VSA in isoform 3.		VSP_025009
	Alternative sequence	414 – 502	89	Missing in isoform 3.		VSP_025010
	Alternative sequence	453 – 502	50	CQSRV…LEARS → FVLLRGGVWCPCPSSARPAQ RTKVEDILS in isoform 2.		VSP_025011
Experimental info
	Mutagenesis	304	1	H → A: Reduced enzyme activity. Ref.5
	Mutagenesis	313	1	R → A: Loss of enzyme activity. Ref.5
	Mutagenesis	367	1	I → A: Reduces enzyme activity by about 60%. Ref.8
	Mutagenesis	367	1	I → F: Alters protein structure and causes an increase in whole body metabolism, leading to a lean phenotype in adult males, but not in females. Ref.8
	Sequence conflict	181	1	G → R in BAC32382. Ref.3
	Sequence conflict	384	1	N → S in CAB59324. Ref.1
	Sequence conflict	384	1	N → S in BAC98247. Ref.2
	Sequence conflict	384	1	N → S in BAC40629. Ref.3
	Sequence conflict	384	1	N → S in AAH22222. Ref.4
	Sequence conflict	410	1	M → V in BAC98247. Ref.2
	Sequence conflict	410	1	M → V in BAC40629. Ref.3
	Sequence conflict	410	1	M → V in AAH22222. Ref.4
	Sequence conflict	463	1	V → A in BAC40629. Ref.3
	Sequence conflict	463	1	V → A in AAH22222. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: 69223B824028D872	FASTA	502	58,007
	10 20 30 40 50 60 MKRVQTAEER EREAKKLRLL EELEDTWLPY LTPKDDEFYQ QWQLKYPKLV FREAGSIPEE 70 80 90 100 110 120 LHKEVPEAFL TLHKHGCLFR DVVRIQGKDV LTPVSRILIG DPGCTYKYLN TRLFTVPWPV 130 140 150 160 170 180 KGCTVKYTEA EIAAACQTFL KLNDYLQVET IQALEELAVR EKANEDAVPL CMAEFPRAGV 190 200 210 220 230 240 GPSCDDEVDL KSRAAYNVTL LNFMDPQKMP YLKEEPYFGM GKMAVSWHHD ENLVDRSAVA 250 260 270 280 290 300 VYSYSCEGSE DESEDESSFE GRDPDTWHVG FKISWDIETP GLTIPLHQGD CYFMLDDLNA 310 320 330 340 350 360 THQHCVLAGS QPRFSSTHRV AECSTGTLDY ILERCQLALQ NVLNDSDDGD VSLKSFDPAV 370 380 390 400 410 420 LKQGEEIHNE VEFEWLRQFW FQGNRYKLCT DWWCEPMTHL EGLWKKMESM TNAVLREVKR 430 440 450 460 470 480 EGLPVEQRSE ILSAILVPLT VRQNLRKEWH ARCQSRVVRT LPVQQKPDCR PYWEKDDPSM 490 500 PLPFDLTDVV SELRGQLLEA RS
	Isoform 2 [UniParc]. Checksum: D79A1C3143BEF2D9	FASTA	481	55,393
	10 20 30 40 50 60 MKRVQTAEER EREAKKLRLL EELEDTWLPY LTPKDDEFYQ QWQLKYPKLV FREAGSIPEE 70 80 90 100 110 120 LHKEVPEAFL TLHKHGCLFR DVVRIQGKDV LTPVSRILIG DPGCTYKYLN TRLFTVPWPV 130 140 150 160 170 180 KGCTVKYTEA EIAAACQTFL KLNDYLQVET IQALEELAVR EKANEDAVPL CMAEFPRAGV 190 200 210 220 230 240 GPSCDDEVDL KSRAAYNVTL LNFMDPQKMP YLKEEPYFGM GKMAVSWHHD ENLVDRSAVA 250 260 270 280 290 300 VYSYSCEGSE DESEDESSFE GRDPDTWHVG FKISWDIETP GLTIPLHQGD CYFMLDDLNA 310 320 330 340 350 360 THQHCVLAGS QPRFSSTHRV AECSTGTLDY ILERCQLALQ NVLNDSDDGD VSLKSFDPAV 370 380 390 400 410 420 LKQGEEIHNE VEFEWLRQFW FQGNRYKLCT DWWCEPMTHL EGLWKKMESM TNAVLREVKR 430 440 450 460 470 480 EGLPVEQRSE ILSAILVPLT VRQNLRKEWH ARFVLLRGGV WCPCPSSARP AQRTKVEDIL S
	Isoform 3 [UniParc]. Checksum: A3E62B85C8133963	FASTA	413	47,593
	10 20 30 40 50 60 MKRVQTAEER EREAKKLRLL EELEDTWLPY LTPKDDEFYQ QWQLKYPKLV FREAGSIPEE 70 80 90 100 110 120 LHKEVPEAFL TLHKHGCLFR DVVRIQGKDV LTPVSRILIG DPGCTYKYLN TRLFTVPWPV 130 140 150 160 170 180 KGCTVKYTEA EIAAACQTFL KLNDYLQVET IQALEELAVR EKANEDAVPL CMAEFPRAGV 190 200 210 220 230 240 GPSCDDEVDL KSRAAYNVTL LNFMDPQKMP YLKEEPYFGM GKMAVSWHHD ENLVDRSAVA 250 260 270 280 290 300 VYSYSCEGSE DESEDESSFE GRDPDTWHVG FKISWDIETP GLTIPLHQGD CYFMLDDLNA 310 320 330 340 350 360 THQHCVLAGS QPRFSSTHRV AECSTGTLDY ILERCQLALQ NVLNDSDDGD VSLKSFDPAV 370 380 390 400 410 LKQGEEIHNE VEFEWLRQFW FQGNRYKLCT DWWCEPMTHL EGLWKKMESM VSA
	Isoform 4 [UniParc]. Checksum: C6C1B6EB7E895140	FASTA	316	36,366
	10 20 30 40 50 60 MKRVQTAEER EREAKKLRLL EELEDTWLPY LTPKDDEFYQ QWQLKYPKLV FREAGSIPEE 70 80 90 100 110 120 LHKEVPEAFL TLHKHGCLFR DVVRIQGKDV LTPVSRILIG DPGCTYKYLN TRLFTVPWPV 130 140 150 160 170 180 KGCTVKYTEA EIAAACQTFL KLNDYLQVET IQALEELAVR EKANEDAVPL CMAEFPRAGV 190 200 210 220 230 240 GPSCDDEVDL KSRAAYNVTL LNFMDPQKMP YLKEEPYFGM GKMAVSWHHD ENLVDRSAVA 250 260 270 280 290 300 VYSYSCEGSE DESEDESSFE GRDPDTWHVG FKISWDIETP GLTIPLHQGD CYFMLGNVGS 310 LRVGHLWGFE IHFWIL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning of Fatso (Fto), a novel gene deleted by the Fused toes (Ft) mouse mutation." Peters T., Ausmeier K., Ruether U. Mamm. Genome 10:983-986(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	"Prediction of the coding sequences of mouse homologues of KIAA gene: III. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries." Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Nagase T., Ohara O., Koga H. DNA Res. 10:167-180(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Brain.
[3]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4). Strain: C57BL/6J and NOD. Tissue: Aorta, Bone, Corpora quadrigemina, Skin, Thymus and Vein.
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Strain: C57BL/6 and FVB/N. Tissue: Brain and Kidney.
[5]	"The obesity-associated FTO gene encodes a 2-oxoglutarate-dependent nucleic acid demethylase." Gerken T., Girard C.A., Tung Y.C., Webby C.J., Saudek V., Hewitson K.S., Yeo G.S., McDonough M.A., Cunliffe S., McNeill L.A., Galvanovskis J., Rorsman P., Robins P., Prieur X., Coll A.P., Ma M., Jovanovic Z., Farooqi I.S. , Sedgwick B., Barroso I., Lindahl T., Ponting C.P., Ashcroft F.M., O'Rahilly S., Schofield C.J. Science 318:1469-1472(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, COFACTOR, ENZYME REGULATION, SUBCELLULAR LOCATION, MUTAGENESIS OF HIS-304 AND ARG-313, INDUCTION, TISSUE SPECIFICITY.
[6]	"Oxidative demethylation of 3-methylthymine and 3-methyluracil in single-stranded DNA and RNA by mouse and human FTO." Jia G., Yang C.G., Yang S., Jian X., Yi C., Zhou Z., He C. FEBS Lett. 582:3313-3319(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
[7]	"Inactivation of the Fto gene protects from obesity." Fischer J., Koch L., Emmerling C., Vierkotten J., Peters T., Bruning J.C., Ruther U. Nature 458:894-898(2009) [PubMed] [Europe PMC] [Abstract] Cited for: DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, FUNCTION, TISSUE SPECIFICITY.
[8]	"A mouse model for the metabolic effects of the human fat mass and obesity associated FTO gene." Church C., Lee S., Bagg E.A., McTaggart J.S., Deacon R., Gerken T., Lee A., Moir L., Mecinovic J., Quwailid M.M., Schofield C.J., Ashcroft F.M., Cox R.D. PLoS Genet. 5:E1000599-E1000599(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, CIRCULAR DICHROISM, MUTAGENESIS OF ILE-367.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00280462. IPI00845534. IPI00845571. IPI00845590.
RefSeq	NP_036066.2. NM_011936.2.
UniGene	Mm.4375.
3D structure databases
ProteinModelPortal	Q8BGW1.
SMR	Q8BGW1. Positions 30-496.
ModBase	Search...
PTM databases
PhosphoSite	Q8BGW1.
Proteomic databases
PaxDb	Q8BGW1.
PRIDE	Q8BGW1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000069718; ENSMUSP00000068380; ENSMUSG00000055932.
GeneID	26383.
KEGG	mmu:26383.
UCSC	uc009msq.2. mouse. uc009msr.2. mouse. uc009mss.2. mouse. uc009mst.2. mouse.
Organism-specific databases
CTD	79068.
MGI	MGI:1347093. Fto.
Rouge	Search...
Phylogenomic databases
eggNOG	NOG45792.
GeneTree	ENSGT00390000017730.
HOVERGEN	HBG101847.
InParanoid	Q8BGW1.
OMA	AVYNYSC.
OrthoDB	EOG4SF969.
Gene expression databases
ArrayExpress	Q8BGW1.
Bgee	Q8BGW1.
CleanEx	MM_FTO.
Genevestigator	Q8BGW1.
Family and domain databases
InterPro	IPR024366. FTO_C. IPR024367. FTO_cat_dom. [Graphical view]
Pfam	PF12934. FTO_CTD. 1 hit. PF12933. FTO_NTD. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	FTO. mouse.
NextBio	304305.
SOURCE	Search...

Entry information

Entry name

FTO_MOUSE

Accession

Primary (citable) accession number: Q8BGW1
Secondary accession number(s): Q3TTZ5 , Q6ZPI7, Q8BR68, Q8CB66, Q8R250, Q9QZ13

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 2007
Last sequence update:	March 1, 2003
Last modified:	April 3, 2013
This is version 76 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program