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Protein

Transducin-like enhancer protein 3

Gene

Tle3

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Transcriptional corepressor that binds to a number of transcription factors. Inhibits the transcriptional activation mediated by CTNNB1 and TCF family members in Wnt signaling. The effects of full-length TLE family members may be modulated by association with dominant-negative AES (By similarity).By similarity

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Transcription, Transcription regulation, Wnt signaling pathway

Enzyme and pathway databases

ReactomeiR-RNO-201722. Formation of the beta-catenin:TCF transactivating complex.
R-RNO-3769402. Deactivation of the beta-catenin transactivating complex.
R-RNO-4641265. Repression of WNT target genes.

Names & Taxonomyi

Protein namesi
Recommended name:
Transducin-like enhancer protein 3
Short name:
rTLE3
Gene namesi
Name:Tle3
Synonyms:Esp3
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 8

Organism-specific databases

RGDi620292. Tle3.

Subcellular locationi

GO - Cellular componenti

  • nucleus Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 764764Transducin-like enhancer protein 3PRO_0000051282Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei203 – 2031PhosphoserineCombined sources
Modified residuei207 – 2071PhosphoserineBy similarity
Modified residuei211 – 2111PhosphoserineBy similarity
Modified residuei217 – 2171PhosphoserineCombined sources
Modified residuei232 – 2321N6-acetyllysineBy similarity
Modified residuei240 – 2401PhosphoserineBy similarity
Modified residuei245 – 2451PhosphoserineCombined sources
Modified residuei259 – 2591PhosphothreonineCombined sources
Modified residuei263 – 2631PhosphoserineCombined sources
Modified residuei267 – 2671PhosphoserineCombined sources
Modified residuei275 – 2751N6-acetyllysineBy similarity
Modified residuei286 – 2861PhosphoserineBy similarity
Modified residuei312 – 3121PhosphothreonineBy similarity
Modified residuei317 – 3171PhosphoserineBy similarity
Modified residuei319 – 3191PhosphothreonineBy similarity
Modified residuei321 – 3211PhosphothreonineBy similarity
Modified residuei328 – 3281PhosphothreonineBy similarity
Modified residuei334 – 3341PhosphothreonineBy similarity
Modified residuei410 – 4101PhosphoserineBy similarity

Post-translational modificationi

Ubiquitinated by XIAP/BIRC4. This ubiquitination does not affect its stability, nuclear localization, or capacity to tetramerize but inhibits its interaction with TCF7L2/TCF4 (By similarity).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ9JIT3.
PRIDEiQ9JIT3.

PTM databases

iPTMnetiQ9JIT3.
PhosphoSiteiQ9JIT3.

Expressioni

Tissue specificityi

Highly expressed in adrenal gland, small intestine, kidney, lung, ovary and thyroid. Detected at lower levels in pituitary, hippocampus, cortex, cerebellum and testis.

Inductioni

By kainic acid in the dentate gyrus.

Gene expression databases

GenevisibleiQ9JIT3. RN.

Interactioni

Subunit structurei

Homotetramer and heterooligomer with other family members. Binds LEF1, TCF7, TCF7L1, TCF7L2 and FOXA2. Interacts with XIAP/BIRC4 and TCF7L2/TCF4. Interacts with TBX18 (via engrailed homology 1 repressor motif), leading to decreased of TBX18 transcriptional activity.By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000018467.

Structurei

3D structure databases

ProteinModelPortaliQ9JIT3.
SMRiQ9JIT3. Positions 435-764.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati476 – 51439WD 1Add
BLAST
Repeati522 – 56140WD 2Add
BLAST
Repeati566 – 60540WD 3Add
BLAST
Repeati608 – 64740WD 4Add
BLAST
Repeati649 – 68840WD 5Add
BLAST
Repeati690 – 72940WD 6Add
BLAST
Repeati731 – 76333WD 7Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 131131Q domainBy similarityAdd
BLAST
Regioni132 – 19968GP domainBy similarityAdd
BLAST
Regioni200 – 26869CcN domainBy similarityAdd
BLAST
Regioni269 – 444176SP domainBy similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi225 – 2284Nuclear localization signalSequence analysis

Domaini

WD repeat Groucho/TLE family members are characterized by 5 regions, a glutamine-rich Q domain, a glycine/proline-rich GP domain, a central CcN domain, containing a nuclear localization signal, and a serine/proline-rich SP domain. The most highly conserved are the N-terminal Q domain and the C-terminal WD-repeat domain.1 Publication

Sequence similaritiesi

Belongs to the WD repeat Groucho/TLE family.Curated
Contains 7 WD repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, WD repeat

Phylogenomic databases

eggNOGiKOG0639. Eukaryota.
ENOG410XPX3. LUCA.
GeneTreeiENSGT00550000074465.
HOGENOMiHOG000293211.
HOVERGENiHBG004689.
InParanoidiQ9JIT3.
OMAiHDLDHRE.
OrthoDBiEOG7HQNC3.
PhylomeDBiQ9JIT3.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
InterProiIPR005617. Groucho/TLE_N.
IPR009146. Groucho_enhance.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF03920. TLE_N. 1 hit.
PF00400. WD40. 2 hits.
[Graphical view]
PRINTSiPR01850. GROUCHOFAMLY.
SMARTiSM00320. WD40. 7 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
PROSITEiPS00678. WD_REPEATS_1. 2 hits.
PS50082. WD_REPEATS_2. 2 hits.
PS50294. WD_REPEATS_REGION. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9JIT3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MYPQGRHPAP HQPGQPGFKF TVAESCDRIK DEFQFLQAQY HSLKVEYDKL
60 70 80 90 100
ANEKTEMQRH YVMYYEMSYG LNIEMHKQTE IAKRLNTILA QIMPFLSQEH
110 120 130 140 150
QQQVAQAVER AKQVTMTELN AIIGQQQLQA QHLSHATHGP PVQLPPHPSG
160 170 180 190 200
LQPPGIPPVT GSSSGLLALG ALGSQAHLAV KDEKNHHELD HRERESSTNN
210 220 230 240 250
SVSPSESLRA SEKHRGSADY SMEAKKRKAE EKDSLSRYDS DGDKSDDLVV
260 270 280 290 300
DVSNEDPATP RVSPAHSPPE NGLDKARGLK KDAPTSPASV ASSSSTPSSK
310 320 330 340 350
TKDLGHNDKS STPGLKSNTP TPRNDAPTPG TSTTPGLRSM PGKPPGMDPI
360 370 380 390 400
ASALRTPISL TSSYAAPFAM MSHHEMNGSL TSPSAYAGLH NIPSQMSAAA
410 420 430 440 450
AAAAAAYGRS PMVGFDPHPP MRATGLPSSL ASIPGGKPAY SFHVSADGQM
460 470 480 490 500
QPVPFPHDAL AGPGIPRHAR QINTLSHGEV VCAVTISNPT RHVYTGGKGC
510 520 530 540 550
VKIWDISQPG SKSPISQLDC LNRDNYIRSC KLLPDGRTLI VGGEASTLTI
560 570 580 590 600
WDLASPTPRI KAELTSSAPA CYALAISPDA KVCFSCCSDG NIAVWDLHNQ
610 620 630 640 650
TLVRQFQGHT DGASCIDISH DGTKLWTGGL DNTVRSWDLR EGRQLQQHDF
660 670 680 690 700
TSQIFSLGYC PTGEWLAVGM ESSNVEVLHH TKPDKYQLHL HESCVLSLKF
710 720 730 740 750
AYCGKWFVST GKDNLLNAWR TPYGASIFQS KESSSVLSCD ISADDKYIVT
760
GSGDKKATVY EVIY
Length:764
Mass (Da):82,644
Last modified:October 1, 2000 - v1
Checksum:i7C5EAAEC9AA1A2DB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF186092 mRNA. Translation: AAF75590.1.
RefSeqiNP_445852.1. NM_053400.1.
UniGeneiRn.24106.

Genome annotation databases

EnsembliENSRNOT00000018467; ENSRNOP00000018467; ENSRNOG00000013013.
GeneIDi84424.
KEGGirno:84424.
UCSCiRGD:620292. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF186092 mRNA. Translation: AAF75590.1.
RefSeqiNP_445852.1. NM_053400.1.
UniGeneiRn.24106.

3D structure databases

ProteinModelPortaliQ9JIT3.
SMRiQ9JIT3. Positions 435-764.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000018467.

PTM databases

iPTMnetiQ9JIT3.
PhosphoSiteiQ9JIT3.

Proteomic databases

PaxDbiQ9JIT3.
PRIDEiQ9JIT3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000018467; ENSRNOP00000018467; ENSRNOG00000013013.
GeneIDi84424.
KEGGirno:84424.
UCSCiRGD:620292. rat.

Organism-specific databases

CTDi7090.
RGDi620292. Tle3.

Phylogenomic databases

eggNOGiKOG0639. Eukaryota.
ENOG410XPX3. LUCA.
GeneTreeiENSGT00550000074465.
HOGENOMiHOG000293211.
HOVERGENiHBG004689.
InParanoidiQ9JIT3.
OMAiHDLDHRE.
OrthoDBiEOG7HQNC3.
PhylomeDBiQ9JIT3.

Enzyme and pathway databases

ReactomeiR-RNO-201722. Formation of the beta-catenin:TCF transactivating complex.
R-RNO-3769402. Deactivation of the beta-catenin transactivating complex.
R-RNO-4641265. Repression of WNT target genes.

Miscellaneous databases

PROiQ9JIT3.

Gene expression databases

GenevisibleiQ9JIT3. RN.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
InterProiIPR005617. Groucho/TLE_N.
IPR009146. Groucho_enhance.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF03920. TLE_N. 1 hit.
PF00400. WD40. 2 hits.
[Graphical view]
PRINTSiPR01850. GROUCHOFAMLY.
SMARTiSM00320. WD40. 7 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
PROSITEiPS00678. WD_REPEATS_1. 2 hits.
PS50082. WD_REPEATS_2. 2 hits.
PS50294. WD_REPEATS_REGION. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "rTLE3, a newly identified transducin-like enhancer of split, is induced by depolarization in brain."
    Feldman J.D., Vician L., Crispino M., Hoe W., Baudry M., Herschman H.R.
    J. Neurochem. 74:1838-1847(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain cortex.
  2. "The Groucho/TLE/Grg family of transcriptional co-repressors."
    Jennings B.H., Ish-Horowicz D.
    Genome Biol. 9:R205.1-R205.7(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  3. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203; SER-217; SER-245; THR-259; SER-263 AND SER-267, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiTLE3_RAT
AccessioniPrimary (citable) accession number: Q9JIT3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 28, 2003
Last sequence update: October 1, 2000
Last modified: July 6, 2016
This is version 116 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. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.