FRAT2_MOUSE
ID FRAT2_MOUSE Reviewed; 231 AA.
AC Q8K025;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=GSK-3-binding protein FRAT2;
DE AltName: Full=Frequently rearranged in advanced T-cell lymphomas 2;
DE Short=FRAT-2;
GN Name=Frat2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/Ola;
RX PubMed=15073180; DOI=10.1074/jbc.m400439200;
RA van Amerongen R., van der Gulden H., Bleeker F., Jonkers J., Berns A.;
RT "Characterization and functional analysis of the murine Frat2 gene.";
RL J. Biol. Chem. 279:26967-26974(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and Colon;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Positively regulates the Wnt signaling pathway by stabilizing
CC beta-catenin through the association with GSK-3.
CC -!- SUBUNIT: Binds GSK-3 and prevents GSK-3-dependent phosphorylation.
CC -!- SIMILARITY: Belongs to the GSK-3-binding protein family. {ECO:0000305}.
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DR EMBL; AY518895; AAR99812.1; -; Genomic_DNA.
DR EMBL; AK081171; BAC38155.1; -; mRNA.
DR EMBL; BC034214; AAH34214.1; -; mRNA.
DR EMBL; BC085510; AAH85510.1; -; mRNA.
DR CCDS; CCDS29813.1; -.
DR RefSeq; NP_808271.1; NM_177603.3.
DR AlphaFoldDB; Q8K025; -.
DR SMR; Q8K025; -.
DR ComplexPortal; CPX-110; Nuclear export complex Frat2-Gsk3b.
DR STRING; 10090.ENSMUSP00000052788; -.
DR PhosphoSitePlus; Q8K025; -.
DR PaxDb; Q8K025; -.
DR PRIDE; Q8K025; -.
DR ProteomicsDB; 271801; -.
DR Antibodypedia; 30842; 141 antibodies from 24 providers.
DR DNASU; 212398; -.
DR Ensembl; ENSMUST00000059231; ENSMUSP00000052788; ENSMUSG00000047604.
DR GeneID; 212398; -.
DR KEGG; mmu:212398; -.
DR UCSC; uc008hmj.3; mouse.
DR CTD; 23401; -.
DR MGI; MGI:2673967; Frat2.
DR VEuPathDB; HostDB:ENSMUSG00000047604; -.
DR eggNOG; ENOG502S0IC; Eukaryota.
DR GeneTree; ENSGT00390000007081; -.
DR HOGENOM; CLU_101225_1_0_1; -.
DR InParanoid; Q8K025; -.
DR OMA; YCVEELT; -.
DR OrthoDB; 1477860at2759; -.
DR PhylomeDB; Q8K025; -.
DR TreeFam; TF330804; -.
DR Reactome; R-MMU-196299; Beta-catenin phosphorylation cascade.
DR Reactome; R-MMU-4641262; Disassembly of the destruction complex and recruitment of AXIN to the membrane.
DR BioGRID-ORCS; 212398; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Frat2; mouse.
DR PRO; PR:Q8K025; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q8K025; protein.
DR Bgee; ENSMUSG00000047604; Expressed in spermatid and 158 other tissues.
DR Genevisible; Q8K025; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IC:ComplexPortal.
DR GO; GO:1904886; P:beta-catenin destruction complex disassembly; IC:ComplexPortal.
DR GO; GO:0046825; P:regulation of protein export from nucleus; IC:ComplexPortal.
DR GO; GO:0016055; P:Wnt signaling pathway; IGI:MGI.
DR InterPro; IPR039202; FRAT2.
DR InterPro; IPR008014; GSK3-bd.
DR PANTHER; PTHR35154; PTHR35154; 1.
DR PANTHER; PTHR35154:SF2; PTHR35154:SF2; 1.
DR Pfam; PF05350; GSK-3_bind; 2.
PE 2: Evidence at transcript level;
KW Reference proteome; Wnt signaling pathway.
FT CHAIN 1..231
FT /note="GSK-3-binding protein FRAT2"
FT /id="PRO_0000087335"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 53..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 172..194
FT /note="Involved in GSK-3 binding"
FT /evidence="ECO:0000250"
FT REGION 203..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..23
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 231 AA; 23914 MW; 6C2C0164B9476C37 CRC64;
MPCRREEEEE AGDEAEGEED DDSFLLLQQS VTLGGSTDVD RLIVQIGETL QLDTAHDRPA
SPCAAPGPPP APPRVLAALS ADKTGTPARR LLRPTGSAET GDPAPPGAVR CVLGERGRVR
GRSAPYCVAE IAPGASALPG PGRRGWLPGS VASHRIQQRR WTAGGARAAD DDPHRLLQQL
VLSGNLIKEA VRRLQRAVAA VAATSPASAP GSGGGRSGPD SVTLQPSGAW L
