FRAT2_HUMAN
ID FRAT2_HUMAN Reviewed; 233 AA.
AC O75474; Q5JTI0; Q8WUL9; Q9BYG2;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 3.
DT 03-AUG-2022, entry version 151.
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 Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Fetal lung;
RX PubMed=11237732; DOI=10.1006/bbrc.2001.4421;
RA Saitoh T., Moriwaki J., Koike J., Takagi A., Miwa T., Shiokawa K.,
RA Katoh M.;
RT "Molecular cloning and characterization of FRAT2, encoding a positive
RT regulator of the WNT signaling pathway.";
RL Biochem. Biophys. Res. Commun. 281:815-820(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
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).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 121-233.
RX PubMed=9635432; DOI=10.1016/s0092-8674(00)81208-8;
RA Yost C., Farr G.H. III, Pierce S.B., Ferkey D.M., Chen M.M., Kimelman D.;
RT "GBP, an inhibitor of GSK-3, is implicated in Xenopus development and
RT oncogenesis.";
RL Cell 93:1031-1041(1998).
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; AB045118; BAB39165.1; -; mRNA.
DR EMBL; AL355490; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC020165; AAH20165.1; -; mRNA.
DR EMBL; AF062739; AAC39786.1; -; mRNA.
DR CCDS; CCDS7456.1; -.
DR PIR; JC7618; JC7618.
DR RefSeq; NP_036215.1; NM_012083.2.
DR AlphaFoldDB; O75474; -.
DR SMR; O75474; -.
DR BioGRID; 116974; 25.
DR ComplexPortal; CPX-462; Nuclear export complex FRAT2-GSK3B.
DR IntAct; O75474; 13.
DR MINT; O75474; -.
DR STRING; 9606.ENSP00000360058; -.
DR iPTMnet; O75474; -.
DR PhosphoSitePlus; O75474; -.
DR BioMuta; FRAT2; -.
DR EPD; O75474; -.
DR jPOST; O75474; -.
DR MassIVE; O75474; -.
DR MaxQB; O75474; -.
DR PaxDb; O75474; -.
DR PeptideAtlas; O75474; -.
DR PRIDE; O75474; -.
DR ProteomicsDB; 50036; -.
DR Antibodypedia; 30842; 141 antibodies from 24 providers.
DR DNASU; 23401; -.
DR Ensembl; ENST00000371019.4; ENSP00000360058.2; ENSG00000181274.7.
DR GeneID; 23401; -.
DR KEGG; hsa:23401; -.
DR MANE-Select; ENST00000371019.4; ENSP00000360058.2; NM_012083.3; NP_036215.1.
DR UCSC; uc001knd.2; human.
DR CTD; 23401; -.
DR DisGeNET; 23401; -.
DR GeneCards; FRAT2; -.
DR HGNC; HGNC:16048; FRAT2.
DR HPA; ENSG00000181274; Low tissue specificity.
DR MIM; 605006; gene.
DR neXtProt; NX_O75474; -.
DR OpenTargets; ENSG00000181274; -.
DR PharmGKB; PA28362; -.
DR VEuPathDB; HostDB:ENSG00000181274; -.
DR eggNOG; ENOG502S0IC; Eukaryota.
DR GeneTree; ENSGT00390000007081; -.
DR HOGENOM; CLU_101225_1_0_1; -.
DR InParanoid; O75474; -.
DR OMA; YCVEELT; -.
DR OrthoDB; 1477860at2759; -.
DR PhylomeDB; O75474; -.
DR TreeFam; TF330804; -.
DR PathwayCommons; O75474; -.
DR Reactome; R-HSA-196299; Beta-catenin phosphorylation cascade.
DR Reactome; R-HSA-4641262; Disassembly of the destruction complex and recruitment of AXIN to the membrane.
DR SignaLink; O75474; -.
DR SIGNOR; O75474; -.
DR BioGRID-ORCS; 23401; 11 hits in 1076 CRISPR screens.
DR GeneWiki; FRAT2; -.
DR GenomeRNAi; 23401; -.
DR Pharos; O75474; Tbio.
DR PRO; PR:O75474; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; O75474; protein.
DR Bgee; ENSG00000181274; Expressed in blood and 138 other tissues.
DR Genevisible; O75474; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
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..233
FT /note="GSK-3-binding protein FRAT2"
FT /id="PRO_0000087334"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 174..196
FT /note="Involved in GSK-3 binding"
FT /evidence="ECO:0000250"
FT REGION 204..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..24
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 83
FT /note="A -> T (in Ref. 3; AAH20165)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 233 AA; 24051 MW; 01ACC1DEEAB4C16F CRC64;
MPCRREEEEE AGEEAEGEEE EDDSFLLLQQ SVTLGSSGEV DRLVAQIGET LQLDAAQDSP
ASPCAPPGVP LRAPGPLAAA VPADKARPPA VPLLLPPASA ETVGPAPSGA LRCALGDRGR
VRGRAAPYCV AEVAAGPSAL PGPCRRGWLR DAVTSRRLQQ RRWTQAGARA GDDDPHRLLQ
QLVLSGNLIK EAVRRLQRAV AAVAATGPAS APGPGGGRSG PDRIALQPSG SLL
