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Q8BGW1

- FTO_MOUSE

UniProt

Q8BGW1 - FTO_MOUSE

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Protein

Alpha-ketoglutarate-dependent dioxygenase FTO

Gene

Fto

Organism
Mus musculus (Mouse)
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.4 Publications

Cofactori

Binds 1 Fe2+ ion per subunit.1 Publication

Enzyme regulationi

Activated by ascorbate. Inhibited by N-oxalylglycine, fumarate and succinate.1 Publication

pH dependencei

Optimum pH is 5.5-6.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei96 – 961SubstrateBy similarity
Binding sitei108 – 1081SubstrateBy similarity
Binding sitei202 – 2021Alpha-ketoglutarateBy similarity
Metal bindingi228 – 2281Iron; catalyticBy similarity
Metal bindingi230 – 2301Iron; catalyticBy similarity
Binding sitei292 – 2921Alpha-ketoglutarateBy similarity
Metal bindingi304 – 3041Iron; catalyticBy similarity
Binding sitei317 – 3171Alpha-ketoglutarateBy similarity
Binding sitei319 – 3191Alpha-ketoglutarateBy similarity

GO - Molecular functioni

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

GO - Biological processi

  1. adipose tissue development Source: UniProtKB
  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: BHF-UCL
  6. oxidative single-stranded RNA demethylation Source: BHF-UCL
  7. regulation of lipid storage Source: UniProtKB
  8. regulation of multicellular organism growth Source: UniProtKB
  9. regulation of respiratory system process Source: UniProtKB
  10. regulation of white fat cell proliferation Source: UniProtKB
  11. RNA repair Source: BHF-UCL
  12. temperature homeostasis Source: UniProtKB
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
Protein fatso
Gene namesi
Name:Fto
Synonyms:Kiaa1752
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 8

Organism-specific databases

MGIiMGI:1347093. Fto.

Subcellular locationi

Nucleus 3 Publications. Nucleus speckle By similarity

GO - Cellular componenti

  1. nuclear speck Source: UniProtKB
  2. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Disruption phenotypei

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.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi304 – 3041H → A: Reduced enzyme activity. 1 Publication
Mutagenesisi313 – 3131R → A: Loss of enzyme activity. 1 Publication
Mutagenesisi367 – 3671I → A: Reduces enzyme activity by about 60%. 1 Publication
Mutagenesisi367 – 3671I → 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 Publication

Keywords - Diseasei

Obesity

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 502502Alpha-ketoglutarate-dependent dioxygenase FTOPRO_0000286164Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei213 – 2131N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ8BGW1.
PaxDbiQ8BGW1.
PRIDEiQ8BGW1.

PTM databases

PhosphoSiteiQ8BGW1.

Expressioni

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

Inductioni

Down-regulated in fasting animals.1 Publication

Gene expression databases

BgeeiQ8BGW1.
CleanExiMM_FTO.
ExpressionAtlasiQ8BGW1. baseline and differential.
GenevestigatoriQ8BGW1.

Interactioni

Subunit structurei

Monomer. May also exist as homodimer.1 Publication

Protein-protein interaction databases

BioGridi204941. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliQ8BGW1.
SMRiQ8BGW1. Positions 30-500.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni42 – 324283Fe2OG dioxygenase domainBy similarityAdd
BLAST
Regioni210 – 22112Loop L1; predicted to block binding of double-stranded DNA or RNABy similarityAdd
BLAST
Regioni228 – 2314Substrate bindingBy similarity
Regioni313 – 3153Alpha-ketoglutarate bindingBy similarity

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).By similarity

Sequence similaritiesi

Belongs to the fto family.Curated

Phylogenomic databases

eggNOGiNOG45792.
GeneTreeiENSGT00390000017730.
HOVERGENiHBG101847.
InParanoidiQ8BGW1.
OMAiAVYNYSC.
OrthoDBiEOG7CK36T.
PhylomeDBiQ8BGW1.
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: Q8BGW1-1) [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
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
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

Sequence cautioni

The sequence BAC98247.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti181 – 1811G → R in BAC32382. (PubMed:16141072)Curated
Sequence conflicti384 – 3841N → S in CAB59324. (PubMed:10501967)Curated
Sequence conflicti384 – 3841N → S in BAC98247. (PubMed:14621295)Curated
Sequence conflicti384 – 3841N → S in BAC40629. (PubMed:16141072)Curated
Sequence conflicti384 – 3841N → S in AAH22222. (PubMed:15489334)Curated
Sequence conflicti410 – 4101M → V in BAC98247. (PubMed:14621295)Curated
Sequence conflicti410 – 4101M → V in BAC40629. (PubMed:16141072)Curated
Sequence conflicti410 – 4101M → V in AAH22222. (PubMed:15489334)Curated
Sequence conflicti463 – 4631V → A in BAC40629. (PubMed:16141072)Curated
Sequence conflicti463 – 4631V → A in AAH22222. (PubMed:15489334)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei296 – 31621DDLNA…PRFSS → GNVGSLRVGHLWGFEIHFWI L in isoform 4. 1 PublicationVSP_025007Add
BLAST
Alternative sequencei317 – 502186Missing in isoform 4. 1 PublicationVSP_025008Add
BLAST
Alternative sequencei411 – 4133TNA → VSA in isoform 3. 1 PublicationVSP_025009
Alternative sequencei414 – 50289Missing in isoform 3. 1 PublicationVSP_025010Add
BLAST
Alternative sequencei453 – 50250CQSRV…LEARS → FVLLRGGVWCPCPSSARPAQ RTKVEDILS in isoform 2. 1 PublicationVSP_025011Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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]
UniGeneiMm.4375.

Genome annotation databases

EnsembliENSMUST00000069718; ENSMUSP00000068380; ENSMUSG00000055932. [Q8BGW1-1]
GeneIDi26383.
KEGGimmu:26383.
UCSCiuc009msq.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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS22521.1. [Q8BGW1-1 ]
RefSeqi NP_036066.2. NM_011936.2. [Q8BGW1-1 ]
UniGenei Mm.4375.

3D structure databases

ProteinModelPortali Q8BGW1.
SMRi Q8BGW1. Positions 30-500.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 204941. 1 interaction.

PTM databases

PhosphoSitei Q8BGW1.

Proteomic databases

MaxQBi Q8BGW1.
PaxDbi Q8BGW1.
PRIDEi Q8BGW1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000069718 ; ENSMUSP00000068380 ; ENSMUSG00000055932 . [Q8BGW1-1 ]
GeneIDi 26383.
KEGGi mmu:26383.
UCSCi uc009msq.2. mouse. [Q8BGW1-4 ]
uc009msr.2. mouse. [Q8BGW1-3 ]
uc009mss.2. mouse. [Q8BGW1-2 ]
uc009mst.2. mouse. [Q8BGW1-1 ]

Organism-specific databases

CTDi 79068.
MGIi MGI:1347093. Fto.
Rougei Search...

Phylogenomic databases

eggNOGi NOG45792.
GeneTreei ENSGT00390000017730.
HOVERGENi HBG101847.
InParanoidi Q8BGW1.
OMAi AVYNYSC.
OrthoDBi EOG7CK36T.
PhylomeDBi Q8BGW1.
TreeFami TF333296.

Miscellaneous databases

ChiTaRSi FTO. mouse.
NextBioi 304305.
PROi Q8BGW1.
SOURCEi Search...

Gene expression databases

Bgeei Q8BGW1.
CleanExi MM_FTO.
ExpressionAtlasi Q8BGW1. baseline and differential.
Genevestigatori Q8BGW1.

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. "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. 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. 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.

Entry informationi

Entry nameiFTO_MOUSE
AccessioniPrimary (citable) accession number: Q8BGW1
Secondary accession number(s): Q3TTZ5
, Q6ZPI7, Q8BR68, Q8CB66, Q8R250, Q9QZ13
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 2007
Last sequence update: March 1, 2003
Last modified: October 29, 2014
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3