Q04724 · TLE1_HUMAN
- ProteinTransducin-like enhancer protein 1
- GeneTLE1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids770 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Transcriptional corepressor that binds to a number of transcription factors. Inhibits NF-kappa-B-regulated gene expression. Inhibits the transcriptional activation mediated by FOXA2, and by CTNNB1 and TCF family members in Wnt signaling. Enhances FOXG1/BF-1- and HES1-mediated transcriptional repression (By similarity).
The effects of full-length TLE family members may be modulated by association with dominant-negative AES. Unusual function as coactivator for ESRRG
The effects of full-length TLE family members may be modulated by association with dominant-negative AES. Unusual function as coactivator for ESRRG
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | beta-catenin-TCF complex | |
Cellular Component | cytosol | |
Cellular Component | nucleoplasm | |
Cellular Component | nucleus | |
Cellular Component | transcription regulator complex | |
Molecular Function | DNA-binding transcription factor binding | |
Molecular Function | identical protein binding | |
Molecular Function | transcription corepressor activity | |
Biological Process | animal organ morphogenesis | |
Biological Process | negative regulation of anoikis | |
Biological Process | negative regulation of canonical NF-kappaB signal transduction | |
Biological Process | negative regulation of canonical Wnt signaling pathway | |
Biological Process | negative regulation of DNA-templated transcription | |
Biological Process | negative regulation of Wnt signaling pathway | |
Biological Process | positive regulation of gene expression | |
Biological Process | signal transduction | |
Biological Process | Wnt signaling pathway |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameTransducin-like enhancer protein 1
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ04724
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Nuclear and chromatin-associated, depending on isoforms and phosphorylation status. Hyperphosphorylation decreases the affinity for nuclear components.
Keywords
- Cellular component
Disease & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 486 | Abolishes HESX1 binding. | ||||
Sequence: V → S | ||||||
Mutagenesis | 532 | Abolishes HESX1 binding. | ||||
Sequence: Y → H | ||||||
Mutagenesis | 702 | Abolishes HESX1 binding. | ||||
Sequence: L → S | ||||||
Mutagenesis | 715 | Abolishes HESX1 binding. | ||||
Sequence: S → P |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 770 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000051276 | 1-770 | UniProt | Transducin-like enhancer protein 1 | |||
Sequence: MFPQSRHPTPHQAAGQPFKFTIPESLDRIKEEFQFLQAQYHSLKLECEKLASEKTEMQRHYVMYYEMSYGLNIEMHKQTEIAKRLNTICAQVIPFLSQEHQQQVAQAVERAKQVTMAELNAIIGQQQLQAQHLSHGHGPPVPLTPHPSGLQPPGIPPLGGSAGLLALSSALSGQSHLAIKDDKKHHDAEHHRDREPGTSNSLLVPDSLRGTDKRRNGPEFSNDIKKRKVDDKDSSHYDSDGDKSDDNLVVDVSNEDPSSPRASPAHSPRENGIDKNRLLKKDASSSPASTASSASSTSLKSKEMSLHEKASTPVLKSSTPTPRSDMPTPGTSATPGLRPGLGKPPAIDPLVNQAAAGLRTPLAVPGPYPAPFGMVPHAGMNGELTSPGAAYASLHNMSPQMSAAAAAAAVVAYGRSPMVGFDPPPHMRVPTIPPNLAGIPGGKPAYSFHVTADGQMQPVPFPPDALIGPGIPRHARQINTLNHGEVVCAVTISNPTRHVYTGGKGCVKVWDISHPGNKSPVSQLDCLNRDNYIRSCKLLPDGCTLIVGGEASTLSIWDLAAPTPRIKAELTSSAPACYALAISPDSKVCFSCCSDGNIAVWDLHNQTLVRQFQGHTDGASCIDISNDGTKLWTGGLDNTVRSWDLREGRQLQQHDFTSQIFSLGYCPTGEWLAVGMESSNVEVLHVNKPDKYQLHLHESCVLSLKFAYCGKWFVSTGKDNLLNAWRTPYGASIFQSKESSSVLSCDISVDDKYIVTGSGDKKATVYEVIY | |||||||
Modified residue | 239 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 244 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 258 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 259 | UniProt | Phosphoserine; by CDK1 | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 259 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 263 | UniProt | Phosphoserine; by CDK1 | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 263 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 267 | UniProt | Phosphoserine; by CDK1 | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 267 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 284 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 285 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 286 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 286 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 328 | PRIDE | Phosphothreonine | ||||
Sequence: T |
Post-translational modification
Phosphorylated, probably by CDK1. The degree of phosphorylation varies throughout the cell cycle, and is highest at the G2/M transition. Becomes hyperphosphorylated in response to cell differentiation and interaction with HES1 or RUNX1.
Ubiquitinated by XIAP/BIRC4.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
In all tissues examined, mostly in brain, liver and muscle.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Homooligomer and heterooligomer with other family members. Binds RUNX1, RUNX3, FOXA2, KDM6A, UTY, histone H3, HESX1, ESRRG and the NF-kappa-B subunit RELA. Interacts with HES1 (via WRPW motif). Binds TCF7, LEF1, TCF7L1 and TCF7L2 (By similarity).
Interacts with SIX3. Interacts with EFNB1. Interacts with TLE4 (By similarity).
Interacts with FOXG1/BF-1; the interaction is inhibited by TLE6/GRG6 (By similarity).
Interacts with SIX3. Interacts with EFNB1. Interacts with TLE4 (By similarity).
Interacts with FOXG1/BF-1; the interaction is inhibited by TLE6/GRG6 (By similarity).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q04724 | ATXN10 Q9UBB4 | 3 | EBI-711424, EBI-702390 | |
BINARY | Q04724 | DAZAP2 Q15038 | 3 | EBI-711424, EBI-724310 | |
BINARY | Q04724 | FOXG1 P55316 | 2 | EBI-711424, EBI-715416 | |
BINARY | Q04724 | GRN P28799 | 3 | EBI-711424, EBI-747754 | |
BINARY | Q04724 | H4C9 P62805 | 6 | EBI-711424, EBI-302023 | |
BINARY | Q04724 | HES6 Q96HZ4 | 3 | EBI-711424, EBI-7469266 | |
BINARY | Q04724 | HEXB P07686 | 3 | EBI-711424, EBI-7133736 | |
BINARY | Q04724 | NOD2 Q9HC29 | 2 | EBI-711424, EBI-7445625 | |
BINARY | Q04724 | PRKN O60260-5 | 3 | EBI-711424, EBI-21251460 | |
BINARY | Q04724 | RNF11 Q9Y3C5 | 3 | EBI-711424, EBI-396669 | |
BINARY | Q04724 | RUNX1 Q01196-1 | 4 | EBI-711424, EBI-925940 | |
BINARY | Q04724 | RUNX1 Q01196-2 | 3 | EBI-711424, EBI-925944 | |
BINARY | Q04724 | RUNX3 Q13761 | 3 | EBI-711424, EBI-925990 | |
BINARY | Q04724 | SIRT1 Q96EB6 | 4 | EBI-711424, EBI-1802965 | |
BINARY | Q04724 | SYT-SSX2 A4PIW0 | 11 | EBI-711424, EBI-6050533 | |
BINARY | Q04724 | TLE1 Q04724 | 4 | EBI-711424, EBI-711424 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, motif, repeat.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-131 | Q domain | ||||
Sequence: MFPQSRHPTPHQAAGQPFKFTIPESLDRIKEEFQFLQAQYHSLKLECEKLASEKTEMQRHYVMYYEMSYGLNIEMHKQTEIAKRLNTICAQVIPFLSQEHQQQVAQAVERAKQVTMAELNAIIGQQQLQAQ | ||||||
Region | 128-157 | Disordered | ||||
Sequence: LQAQHLSHGHGPPVPLTPHPSGLQPPGIPP | ||||||
Region | 132-199 | GP domain | ||||
Sequence: HLSHGHGPPVPLTPHPSGLQPPGIPPLGGSAGLLALSSALSGQSHLAIKDDKKHHDAEHHRDREPGTS | ||||||
Compositional bias | 140-154 | Pro residues | ||||
Sequence: PVPLTPHPSGLQPPG | ||||||
Region | 176-348 | Disordered | ||||
Sequence: HLAIKDDKKHHDAEHHRDREPGTSNSLLVPDSLRGTDKRRNGPEFSNDIKKRKVDDKDSSHYDSDGDKSDDNLVVDVSNEDPSSPRASPAHSPRENGIDKNRLLKKDASSSPASTASSASSTSLKSKEMSLHEKASTPVLKSSTPTPRSDMPTPGTSATPGLRPGLGKPPAID | ||||||
Compositional bias | 177-197 | Basic and acidic residues | ||||
Sequence: LAIKDDKKHHDAEHHRDREPG | ||||||
Region | 200-268 | CcN domain | ||||
Sequence: NSLLVPDSLRGTDKRRNGPEFSNDIKKRKVDDKDSSHYDSDGDKSDDNLVVDVSNEDPSSPRASPAHSP | ||||||
Compositional bias | 208-250 | Basic and acidic residues | ||||
Sequence: LRGTDKRRNGPEFSNDIKKRKVDDKDSSHYDSDGDKSDDNLVV | ||||||
Motif | 225-228 | Nuclear localization signal | ||||
Sequence: KKRK | ||||||
Compositional bias | 251-265 | Polar residues | ||||
Sequence: DVSNEDPSSPRASPA | ||||||
Region | 269-450 | SP domain | ||||
Sequence: RENGIDKNRLLKKDASSSPASTASSASSTSLKSKEMSLHEKASTPVLKSSTPTPRSDMPTPGTSATPGLRPGLGKPPAIDPLVNQAAAGLRTPLAVPGPYPAPFGMVPHAGMNGELTSPGAAYASLHNMSPQMSAAAAAAAVVAYGRSPMVGFDPPPHMRVPTIPPNLAGIPGGKPAYSFHV | ||||||
Compositional bias | 282-301 | Polar residues | ||||
Sequence: DASSSPASTASSASSTSLKS | ||||||
Compositional bias | 311-331 | Polar residues | ||||
Sequence: STPVLKSSTPTPRSDMPTPGT | ||||||
Repeat | 470-501 | WD 1 | ||||
Sequence: GIPRHARQINTLNHGEVVCAVTISNPTRHVYT | ||||||
Repeat | 528-558 | WD 2 | ||||
Sequence: NRDNYIRSCKLLPDGCTLIVGGEASTLSIWD | ||||||
Repeat | 572-602 | WD 3 | ||||
Sequence: SSAPACYALAISPDSKVCFSCCSDGNIAVWD | ||||||
Repeat | 614-644 | WD 4 | ||||
Sequence: GHTDGASCIDISNDGTKLWTGGLDNTVRSWD | ||||||
Repeat | 696-726 | WD 5 | ||||
Sequence: LHESCVLSLKFAYCGKWFVSTGKDNLLNAWR | ||||||
Repeat | 737-767 | WD 6 | ||||
Sequence: KESSSVLSCDISVDDKYIVTGSGDKKATVYE |
Domain
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.
Sequence similarities
Belongs to the WD repeat Groucho/TLE family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length770
- Mass (Da)83,201
- Last updated2003-03-25 v2
- Checksum695FD1A37410EFE5
Computationally mapped potential isoform sequences
There are 6 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
Q5T3G2 | Q5T3G2_HUMAN | TLE1 | 170 | ||
Q5T3G3 | Q5T3G3_HUMAN | TLE1 | 242 | ||
F6T2C8 | F6T2C8_HUMAN | TLE1 | 146 | ||
A0A669KBK8 | A0A669KBK8_HUMAN | TLE1 | 192 | ||
A0A669KBB1 | A0A669KBB1_HUMAN | TLE1 | 41 | ||
A0A669KAE5 | A0A669KAE5_HUMAN | TLE1 | 209 |
Features
Showing features for compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 140-154 | Pro residues | ||||
Sequence: PVPLTPHPSGLQPPG | ||||||
Compositional bias | 177-197 | Basic and acidic residues | ||||
Sequence: LAIKDDKKHHDAEHHRDREPG | ||||||
Compositional bias | 208-250 | Basic and acidic residues | ||||
Sequence: LRGTDKRRNGPEFSNDIKKRKVDDKDSSHYDSDGDKSDDNLVV | ||||||
Compositional bias | 251-265 | Polar residues | ||||
Sequence: DVSNEDPSSPRASPA | ||||||
Compositional bias | 282-301 | Polar residues | ||||
Sequence: DASSSPASTASSASSTSLKS | ||||||
Compositional bias | 311-331 | Polar residues | ||||
Sequence: STPVLKSSTPTPRSDMPTPGT | ||||||
Sequence conflict | 407-412 | in Ref. 1; AAA61192 | ||||
Sequence: AAAVVA → RGRRGR | ||||||
Sequence conflict | 464-465 | in Ref. 1; AAA61192 | ||||
Sequence: DA → TP |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M99435 EMBL· GenBank· DDBJ | AAA61192.1 EMBL· GenBank· DDBJ | mRNA | ||
AK290860 EMBL· GenBank· DDBJ | BAF83549.1 EMBL· GenBank· DDBJ | mRNA | ||
AL365190 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL353682 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471089 EMBL· GenBank· DDBJ | EAW62636.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC010100 EMBL· GenBank· DDBJ | AAH10100.1 EMBL· GenBank· DDBJ | mRNA | ||
BC015747 EMBL· GenBank· DDBJ | AAH15747.1 EMBL· GenBank· DDBJ | mRNA |