FRAT1_MOUSE
ID FRAT1_MOUSE Reviewed; 274 AA.
AC P70339;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2004, sequence version 2.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Proto-oncogene FRAT1;
DE AltName: Full=Frequently rearranged in advanced T-cell lymphomas 1;
DE Short=FRAT-1;
GN Name=Frat1;
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 [MRNA], AND INVOLVEMENT IN T-CELL LYMPHOMA.
RC TISSUE=Testis, and Thymus;
RX PubMed=9034327; DOI=10.1093/emboj/16.3.441;
RA Jonkers J., Korswagen H.C., Acton D., Breuer M., Berns A.;
RT "Activation of a novel proto-oncogene, Frat1, contributes to progression of
RT mouse T-cell lymphomas.";
RL EMBO J. 16:441-450(1997).
RN [2]
RP SEQUENCE REVISION TO 132, FUNCTION, PHOSPHORYLATION, AND SUBCELLULAR
RP LOCATION.
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-243 AND SER-246, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Positively regulates the Wnt signaling pathway by stabilizing
CC beta-catenin through the association with GSK-3. May play a role in
CC tumor progression and collaborate with PIM1 and MYC in lymphomagenesis.
CC {ECO:0000269|PubMed:15073180}.
CC -!- SUBUNIT: Binds DVL1. Binds GSK-3 and prevent GSK-3-dependent
CC phosphorylation.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15073180}.
CC -!- TISSUE SPECIFICITY: Highly expressed in testis. Lower level of
CC expression in spleen, thymus and brain.
CC -!- DEVELOPMENTAL STAGE: Expressed at low levels during embryonic
CC development.
CC -!- PTM: Phosphorylated. {ECO:0000269|PubMed:15073180}.
CC -!- DISEASE: Note=Activation contributes to progression of mouse T-cell
CC lymphomas (PubMed:9034327). {ECO:0000269|PubMed:9034327}.
CC -!- SIMILARITY: Belongs to the GSK-3-binding protein family. {ECO:0000305}.
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DR EMBL; U58974; AAB72010.2; -; mRNA.
DR CCDS; CCDS84438.1; -.
DR RefSeq; NP_032069.2; NM_008043.3.
DR AlphaFoldDB; P70339; -.
DR SMR; P70339; -.
DR ComplexPortal; CPX-108; Nuclear export complex Frat1-Gsk3b.
DR CORUM; P70339; -.
DR iPTMnet; P70339; -.
DR PhosphoSitePlus; P70339; -.
DR PRIDE; P70339; -.
DR ProteomicsDB; 267516; -.
DR DNASU; 14296; -.
DR Ensembl; ENSMUST00000087155; ENSMUSP00000147726; ENSMUSG00000067199.
DR GeneID; 14296; -.
DR KEGG; mmu:14296; -.
DR UCSC; uc008hmi.2; mouse.
DR CTD; 10023; -.
DR MGI; MGI:109450; Frat1.
DR VEuPathDB; HostDB:ENSMUSG00000067199; -.
DR GeneTree; ENSGT00390000007081; -.
DR InParanoid; P70339; -.
DR OMA; PCRQHPE; -.
DR OrthoDB; 1477860at2759; -.
DR PhylomeDB; P70339; -.
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; 14296; 3 hits in 17 CRISPR screens.
DR PRO; PR:P70339; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; P70339; protein.
DR Bgee; ENSMUSG00000067199; Expressed in spermatid and 115 other tissues.
DR ExpressionAtlas; P70339; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:1904886; P:beta-catenin destruction complex disassembly; ISO:MGI.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; ISO:MGI.
DR GO; GO:0000578; P:embryonic axis specification; IDA:MGI.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; ISO:MGI.
DR GO; GO:0006611; P:protein export from nucleus; IDA:MGI.
DR GO; GO:0046825; P:regulation of protein export from nucleus; ISO:MGI.
DR InterPro; IPR008014; GSK3-bd.
DR PANTHER; PTHR35154; PTHR35154; 1.
DR Pfam; PF05350; GSK-3_bind; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Phosphoprotein; Proto-oncogene; Reference proteome;
KW Wnt signaling pathway.
FT CHAIN 1..274
FT /note="Proto-oncogene FRAT1"
FT /id="PRO_0000087333"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 55..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 132..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 191..214
FT /note="Involved in GSK-3 binding"
FT /evidence="ECO:0000250"
FT REGION 232..274
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"
FT COMPBIAS 179..194
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 243
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 246
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 274 AA; 28875 MW; 1C0482997EA95323 CRC64;
MPCRREEEEE AGDEAEGEED DDSFLLLQQS VTLGGSTDVD QLIVQIGETL QLDAAHDRPA
SPCAAPGPPP PQVLAALPAD KTGTPARRLL RPTGSAETGN PAPPGAVRCV LGERGRVRGR
SAPYCVAEIS PGASALPQQP GLDGPPGTGK LSTPQPLSGP CRRGWLRNAA ASRRLQQRRG
SQPETRTGDD DDPHRLLQQL VLSGNLIKEA VRRLHSRQLQ LHAKLPAHPF LGPLSAPVHE
PPSPGSPRAA CSDPGAFMGR AQLRTGDDLL VPGS
