TLE2_MOUSE
ID TLE2_MOUSE Reviewed; 767 AA.
AC Q9WVB2;
DT 10-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Transducin-like enhancer protein 2;
GN Name=Tle2; Synonyms=Grg2;
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].
RX PubMed=11486032; DOI=10.1128/mcb.21.17.5935-5945.2001;
RA Dang J., Inukai T., Kurosawa H., Goi K., Inaba T., Lenny N.T.,
RA Downing J.R., Stifani S., Look A.T.;
RT "The E2A-HLF oncoprotein activates Groucho-related genes and suppresses
RT Runx1.";
RL Mol. Cell. Biol. 21:5935-5945(2001).
RN [2]
RP REVIEW.
RX PubMed=18254933; DOI=10.1186/gb-2008-9-1-205;
RA Jennings B.H., Ish-Horowicz D.;
RT "The Groucho/TLE/Grg family of transcriptional co-repressors.";
RL Genome Biol. 9:R205.1-R205.7(2008).
RN [3]
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=23990468; DOI=10.1074/jbc.m113.461848;
RA Kogawa M., Hisatake K., Atkins G.J., Findlay D.M., Enoki Y., Sato T.,
RA Gray P.C., Kanesaki-Yatsuka Y., Anderson P.H., Wada S., Kato N., Fukuda A.,
RA Katayama S., Tsujimoto M., Yoda T., Suda T., Okazaki Y., Matsumoto M.;
RT "The paired-box homeodomain transcription factor Pax6 binds to the upstream
RT region of the TRAP gene promoter and suppresses receptor activator of NF-
RT kappaB ligand (RANKL)-induced osteoclast differentiation.";
RL J. Biol. Chem. 288:31299-31312(2013).
CC -!- FUNCTION: Transcriptional corepressor that binds to a number of
CC transcription factors. Inhibits the transcriptional activation mediated
CC by CTNNB1 and TCF family members in Wnt signaling. The effects of full-
CC length TLE family members may be modulated by association with
CC dominant-negative AES (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homooligomer and heterooligomer with other family members (By
CC similarity). Binds LEF1, TCF7, TCF7L1, TCF7L2, UTY, HES1 and HES5 (By
CC similarity). {ECO:0000250|UniProtKB:Q04725}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- TISSUE SPECIFICITY: Expressed in bone marrow-derived macrophages.
CC {ECO:0000269|PubMed:23990468}.
CC -!- INDUCTION: Repressed during TNFSF11/RANKL-induced osteoclast
CC differentiation. {ECO:0000269|PubMed:23990468}.
CC -!- DOMAIN: WD repeat Groucho/TLE family members are characterized by 5
CC regions, a glutamine-rich Q domain, a glycine/proline-rich GP domain, a
CC central CcN domain, containing a nuclear localization signal, and a
CC serine/proline-rich SP domain. The most highly conserved are the N-
CC terminal Q domain and the C-terminal WD-repeat domain.
CC {ECO:0000305|PubMed:18254933}.
CC -!- PTM: Ubiquitinated by XIAP/BIRC4. {ECO:0000250|UniProtKB:Q04725}.
CC -!- SIMILARITY: Belongs to the WD repeat Groucho/TLE family. {ECO:0000305}.
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DR EMBL; AF145958; AAD37694.1; -; mRNA.
DR CCDS; CCDS24063.1; -.
DR RefSeq; NP_062699.1; NM_019725.2.
DR RefSeq; XP_006513647.1; XM_006513584.2.
DR AlphaFoldDB; Q9WVB2; -.
DR SMR; Q9WVB2; -.
DR STRING; 10090.ENSMUSP00000121125; -.
DR iPTMnet; Q9WVB2; -.
DR PhosphoSitePlus; Q9WVB2; -.
DR MaxQB; Q9WVB2; -.
DR PaxDb; Q9WVB2; -.
DR PeptideAtlas; Q9WVB2; -.
DR PRIDE; Q9WVB2; -.
DR ProteomicsDB; 260660; -.
DR Antibodypedia; 23107; 210 antibodies from 31 providers.
DR DNASU; 21886; -.
DR Ensembl; ENSMUST00000146358; ENSMUSP00000121125; ENSMUSG00000034771.
DR GeneID; 21886; -.
DR KEGG; mmu:21886; -.
DR UCSC; uc007gis.2; mouse.
DR CTD; 7089; -.
DR MGI; MGI:104635; Tle2.
DR VEuPathDB; HostDB:ENSMUSG00000034771; -.
DR eggNOG; KOG0639; Eukaryota.
DR GeneTree; ENSGT01030000234519; -.
DR InParanoid; Q9WVB2; -.
DR OMA; GENREHT; -.
DR OrthoDB; 546143at2759; -.
DR PhylomeDB; Q9WVB2; -.
DR TreeFam; TF314167; -.
DR Reactome; R-MMU-201722; Formation of the beta-catenin:TCF transactivating complex.
DR Reactome; R-MMU-3769402; Deactivation of the beta-catenin transactivating complex.
DR Reactome; R-MMU-4641265; Repression of WNT target genes.
DR BioGRID-ORCS; 21886; 1 hit in 71 CRISPR screens.
DR PRO; PR:Q9WVB2; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q9WVB2; protein.
DR Bgee; ENSMUSG00000034771; Expressed in cerebellar cortex and 212 other tissues.
DR ExpressionAtlas; Q9WVB2; baseline and differential.
DR Genevisible; Q9WVB2; MM.
DR GO; GO:0005925; C:focal adhesion; ISO:MGI.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005667; C:transcription regulator complex; IBA:GO_Central.
DR GO; GO:0003714; F:transcription corepressor activity; ISO:MGI.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; ISO:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR005617; Groucho/TLE_N.
DR InterPro; IPR009146; Groucho_enhance.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR10814; PTHR10814; 1.
DR Pfam; PF03920; TLE_N; 2.
DR Pfam; PF00400; WD40; 3.
DR PRINTS; PR01850; GROUCHOFAMLY.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 3.
DR PROSITE; PS50294; WD_REPEATS_REGION; 2.
PE 2: Evidence at transcript level;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Repressor;
KW Transcription; Transcription regulation; Ubl conjugation; WD repeat;
KW Wnt signaling pathway.
FT CHAIN 1..767
FT /note="Transducin-like enhancer protein 2"
FT /id="PRO_0000051279"
FT REPEAT 479..517
FT /note="WD 1"
FT REPEAT 525..564
FT /note="WD 2"
FT REPEAT 569..608
FT /note="WD 3"
FT REPEAT 611..650
FT /note="WD 4"
FT REPEAT 693..732
FT /note="WD 5"
FT REPEAT 734..766
FT /note="WD 6"
FT REGION 1..152
FT /note="Q domain"
FT /evidence="ECO:0000250|UniProtKB:Q04724"
FT REGION 153..215
FT /note="GP domain"
FT /evidence="ECO:0000250|UniProtKB:Q04724"
FT REGION 198..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 216..279
FT /note="CcN domain"
FT /evidence="ECO:0000250|UniProtKB:Q04724"
FT REGION 264..283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 280..447
FT /note="SP domain"
FT /evidence="ECO:0000250|UniProtKB:Q04724"
FT REGION 296..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 238..242
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 226..257
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 321..346
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 253
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000255"
FT MOD_RES 274
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000255"
FT MOD_RES 278
FT /note="Phosphothreonine; by CDK1"
FT /evidence="ECO:0000255"
FT MOD_RES 306
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q04725"
SQ SEQUENCE 767 AA; 82623 MW; 2BECE931EE993C44 CRC64;
MYPQGRHPTP LQSGQPFKFS VLEICDRIKE EFQFLQAQYH SLKLECEKLA SEKTEMQRHY
VMAAPHQCPQ GGTSYPHWPR LSPLQYYEMS YGLNIEMHKQ AEIVKRLSAI CAQMVPFLTQ
EHQQQVLQAV DRAKQVTVGE LNSLLGQQNQ LQPLSHAPPV PLTPRPAGLV GAGATGLLAL
SGALAAQAQL VAAVKEDRVG VDAEGSRVDR AASRSSSPSP PESLVEEDHP SSRGGSGKQQ
RAEDKDLSGP YDSEEDKSDY NLVVDEDQPS EPPSPVTTPC GKAPLCIPAR RDLTDSPASL
ASSLGSPLPR SKDIALNDLP TGTPASRSCG TSPPQDSSTP GPSSASHLCQ LAAQPAAPTD
SIALRSPLTL SSPFTSSFSL GSHSTLNGDL SMPGSYVGLH LSPQVSSSVV YGRSPLQMAF
ESHPHLRGSS VSLPGIPVAK PAYSFHVSAD GQMQPVPFPS DALVGTGIPR HARQLHTLAH
GEVVCAVTIS SSTQHVYTGG KGCVKVWDVG QPGSKTPVAQ LDCLNRDNYI RSCKLLPDGQ
SLIVGGEAST LSIWDLAAPT PRIKAELTSS APACYALAVS PDAKVCFSCC SDGNIVVWDL
QNQAMVRQFQ GHTDGASCID ISDYGTRLWT GGLDNTVRCW DLREGRQLQQ HDFSSQIFSL
GHCPNQDWLA VGMESSHVEV LHVRKPEKYQ LRLHESCVLS LKFASCGRWF VSTGKDNLLN
AWRTPYGASI FQSKESSSVL SCDISRNNKY IVTGSGDKKA TVYEVVY
