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Q04724

- TLE1_HUMAN

UniProt

Q04724 - TLE1_HUMAN

Protein

Transducin-like enhancer protein 1

Gene

TLE1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 156 (01 Oct 2014)
      Sequence version 2 (25 Mar 2003)
      Previous versions | rss
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    Functioni

    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. The effects of full-length TLE family members may be modulated by association with dominant-negative AES. Unusual function as coactivator for ESRRG.1 Publication

    GO - Molecular functioni

    1. chromatin binding Source: Ensembl
    2. protein binding Source: UniProtKB
    3. RNA polymerase II transcription corepressor activity Source: BHF-UCL
    4. transcription factor binding Source: UniProtKB

    GO - Biological processi

    1. multicellular organismal development Source: ProtInc
    2. negative regulation of anoikis Source: UniProtKB
    3. negative regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
    4. negative regulation of transcription, DNA-templated Source: UniProtKB
    5. negative regulation of Wnt signaling pathway Source: UniProtKB
    6. Notch signaling pathway Source: Reactome
    7. organ morphogenesis Source: ProtInc
    8. positive regulation of gene expression Source: UniProtKB
    9. signal transduction Source: ProtInc
    10. Wnt signaling pathway Source: UniProtKB-KW

    Keywords - Molecular functioni

    Repressor

    Keywords - Biological processi

    Transcription, Transcription regulation, Wnt signaling pathway

    Enzyme and pathway databases

    ReactomeiREACT_118780. NOTCH1 Intracellular Domain Regulates Transcription.
    REACT_200731. deactivation of the beta-catenin transactivating complex.
    REACT_200753. formation of the beta-catenin:TCF transactivating complex.
    SignaLinkiQ04724.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Transducin-like enhancer protein 1
    Alternative name(s):
    E(Sp1) homolog
    Enhancer of split groucho-like protein 1
    Short name:
    ESG1
    Gene namesi
    Name:TLE1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:11837. TLE1.

    Subcellular locationi

    Nucleus 1 Publication
    Note: Nuclear and chromatin-associated, depending on isoforms and phosphorylation status. Hyperphosphorylation decreases the affinity for nuclear components.

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. cytosol Source: UniProtKB
    3. nucleolus Source: HPA
    4. nucleoplasm Source: Reactome
    5. nucleus Source: UniProtKB
    6. transcription factor complex Source: Ensembl

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi486 – 4861V → S: Abolishes HESX1 binding. 1 Publication
    Mutagenesisi532 – 5321Y → H: Abolishes HESX1 binding. 1 Publication
    Mutagenesisi702 – 7021L → S: Abolishes HESX1 binding. 1 Publication
    Mutagenesisi715 – 7151S → P: Abolishes HESX1 binding. 1 Publication

    Organism-specific databases

    PharmGKBiPA36539.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 770770Transducin-like enhancer protein 1PRO_0000051276Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei239 – 2391Phosphoserine1 Publication
    Modified residuei259 – 2591Phosphoserine; by CDK1Sequence Analysis
    Modified residuei263 – 2631Phosphoserine; by CDK1Sequence Analysis
    Modified residuei267 – 2671Phosphoserine; by CDK1Sequence Analysis
    Modified residuei286 – 2861Phosphoserine1 Publication

    Post-translational modificationi

    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 RUNX1.1 Publication
    Ubiquitinated by XIAP/BIRC4.1 Publication

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ04724.
    PaxDbiQ04724.
    PRIDEiQ04724.

    PTM databases

    PhosphoSiteiQ04724.

    Expressioni

    Tissue specificityi

    In all tissues examined, mostly in brain, liver and muscle.

    Gene expression databases

    ArrayExpressiQ04724.
    BgeeiQ04724.
    CleanExiHS_TLE1.
    GenevestigatoriQ04724.

    Organism-specific databases

    HPAiCAB011482.
    HPA055160.

    Interactioni

    Subunit structurei

    Homooligomer and heterooligomer with other family members. Binds LEF1, RUNX1, RUNX3, FOXA2, KDM6A, UTY, histone H3, HESX1, ESRRG and the NF-kappa-B subunit RELA. Interacts with HES1 (via WRPW motif).10 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself4EBI-711424,EBI-711424
    HIST2H4BP628056EBI-711424,EBI-302023
    RUNX1Q01196-14EBI-711424,EBI-925940
    RUNX1Q01196-23EBI-711424,EBI-925944
    RUNX3Q137613EBI-711424,EBI-925990
    SIRT1Q96EB64EBI-711424,EBI-1802965
    SYT-SSX2A4PIW011EBI-711424,EBI-6050533

    Protein-protein interaction databases

    BioGridi112943. 98 interactions.
    DIPiDIP-36665N.
    IntActiQ04724. 66 interactions.
    MINTiMINT-190700.
    STRINGi9606.ENSP00000365682.

    Structurei

    Secondary structure

    1
    770
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi22 – 9271
    Helixi93 – 953
    Helixi98 – 11114
    Helixi116 – 13318
    Beta strandi447 – 4504
    Beta strandi452 – 4543
    Beta strandi456 – 4583
    Beta strandi465 – 4684
    Beta strandi473 – 4819
    Beta strandi489 – 4924
    Beta strandi494 – 5029
    Beta strandi504 – 5118
    Beta strandi521 – 5255
    Beta strandi531 – 5388
    Beta strandi542 – 55817
    Beta strandi560 – 5634
    Beta strandi565 – 5717
    Beta strandi573 – 5753
    Beta strandi577 – 5826
    Beta strandi586 – 5938
    Beta strandi598 – 6025
    Turni603 – 6064
    Beta strandi607 – 6126
    Beta strandi619 – 6246
    Beta strandi628 – 6358
    Beta strandi638 – 6447
    Turni645 – 6484
    Beta strandi649 – 6557
    Beta strandi660 – 6656
    Beta strandi669 – 6768
    Beta strandi681 – 6855
    Beta strandi691 – 6944
    Beta strandi701 – 7066
    Beta strandi710 – 7178
    Beta strandi720 – 7267
    Turni727 – 7293
    Beta strandi732 – 7376
    Beta strandi742 – 7476
    Beta strandi753 – 7586
    Beta strandi763 – 7697

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1GXRX-ray1.65A/B443-770[»]
    2CE8X-ray2.03A/B/C/D443-770[»]
    2CE9X-ray2.12A/B/C/D443-770[»]
    4OM2X-ray4.00A/B/C/D1-156[»]
    4OM3X-ray2.86A/B/C/D15-156[»]
    ProteinModelPortaliQ04724.
    SMRiQ04724. Positions 438-770.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ04724.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati470 – 50132WD 1Add
    BLAST
    Repeati528 – 55831WD 2Add
    BLAST
    Repeati572 – 60231WD 3Add
    BLAST
    Repeati614 – 64431WD 4Add
    BLAST
    Repeati696 – 72631WD 5Add
    BLAST
    Repeati737 – 76731WD 6Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni200 – 26869CCN domainAdd
    BLAST

    Motif

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

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi1 – 131131Gln-richAdd
    BLAST
    Compositional biasi132 – 19968Gly/Pro-richAdd
    BLAST
    Compositional biasi269 – 449181Pro/Ser-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the WD repeat Groucho/TLE family.Curated
    Contains 6 WD repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, WD repeat

    Phylogenomic databases

    eggNOGiCOG2319.
    HOGENOMiHOG000293211.
    HOVERGENiHBG004689.
    OMAiPPAMDPL.
    OrthoDBiEOG7HQNC3.
    PhylomeDBiQ04724.
    TreeFamiTF314167.

    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. 6 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.

    Q04724-1 [UniParc]FASTAAdd to Basket

    « Hide

    MFPQSRHPTP HQAAGQPFKF TIPESLDRIK EEFQFLQAQY HSLKLECEKL    50
    ASEKTEMQRH YVMYYEMSYG LNIEMHKQTE IAKRLNTICA QVIPFLSQEH 100
    QQQVAQAVER AKQVTMAELN AIIGQQQLQA QHLSHGHGPP VPLTPHPSGL 150
    QPPGIPPLGG SAGLLALSSA LSGQSHLAIK DDKKHHDAEH HRDREPGTSN 200
    SLLVPDSLRG TDKRRNGPEF SNDIKKRKVD DKDSSHYDSD GDKSDDNLVV 250
    DVSNEDPSSP RASPAHSPRE NGIDKNRLLK KDASSSPAST ASSASSTSLK 300
    SKEMSLHEKA STPVLKSSTP TPRSDMPTPG TSATPGLRPG LGKPPAIDPL 350
    VNQAAAGLRT PLAVPGPYPA PFGMVPHAGM NGELTSPGAA YASLHNMSPQ 400
    MSAAAAAAAV VAYGRSPMVG FDPPPHMRVP TIPPNLAGIP GGKPAYSFHV 450
    TADGQMQPVP FPPDALIGPG IPRHARQINT LNHGEVVCAV TISNPTRHVY 500
    TGGKGCVKVW DISHPGNKSP VSQLDCLNRD NYIRSCKLLP DGCTLIVGGE 550
    ASTLSIWDLA APTPRIKAEL TSSAPACYAL AISPDSKVCF SCCSDGNIAV 600
    WDLHNQTLVR QFQGHTDGAS CIDISNDGTK LWTGGLDNTV RSWDLREGRQ 650
    LQQHDFTSQI FSLGYCPTGE WLAVGMESSN VEVLHVNKPD KYQLHLHESC 700
    VLSLKFAYCG KWFVSTGKDN LLNAWRTPYG ASIFQSKESS SVLSCDISVD 750
    DKYIVTGSGD KKATVYEVIY 770
    Length:770
    Mass (Da):83,201
    Last modified:March 25, 2003 - v2
    Checksum:i695FD1A37410EFE5
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti407 – 4126AAAVVA → RGRRGR in AAA61192. (PubMed:1303260)Curated
    Sequence conflicti464 – 4652DA → TP in AAA61192. (PubMed:1303260)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M99435 mRNA. Translation: AAA61192.1.
    AK290860 mRNA. Translation: BAF83549.1.
    AL365190, AL353682 Genomic DNA. Translation: CAI14977.1.
    AL353682, AL365190 Genomic DNA. Translation: CAI12595.1.
    CH471089 Genomic DNA. Translation: EAW62636.1.
    BC010100 mRNA. Translation: AAH10100.1.
    BC015747 mRNA. Translation: AAH15747.1.
    CCDSiCCDS6661.1.
    PIRiB56695.
    RefSeqiNP_005068.2. NM_005077.3.
    UniGeneiHs.197320.
    Hs.689805.

    Genome annotation databases

    EnsembliENST00000376499; ENSP00000365682; ENSG00000196781.
    GeneIDi7088.
    KEGGihsa:7088.
    UCSCiuc004aly.3. human.

    Polymorphism databases

    DMDMi29840816.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M99435 mRNA. Translation: AAA61192.1 .
    AK290860 mRNA. Translation: BAF83549.1 .
    AL365190 , AL353682 Genomic DNA. Translation: CAI14977.1 .
    AL353682 , AL365190 Genomic DNA. Translation: CAI12595.1 .
    CH471089 Genomic DNA. Translation: EAW62636.1 .
    BC010100 mRNA. Translation: AAH10100.1 .
    BC015747 mRNA. Translation: AAH15747.1 .
    CCDSi CCDS6661.1.
    PIRi B56695.
    RefSeqi NP_005068.2. NM_005077.3.
    UniGenei Hs.197320.
    Hs.689805.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1GXR X-ray 1.65 A/B 443-770 [» ]
    2CE8 X-ray 2.03 A/B/C/D 443-770 [» ]
    2CE9 X-ray 2.12 A/B/C/D 443-770 [» ]
    4OM2 X-ray 4.00 A/B/C/D 1-156 [» ]
    4OM3 X-ray 2.86 A/B/C/D 15-156 [» ]
    ProteinModelPortali Q04724.
    SMRi Q04724. Positions 438-770.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112943. 98 interactions.
    DIPi DIP-36665N.
    IntActi Q04724. 66 interactions.
    MINTi MINT-190700.
    STRINGi 9606.ENSP00000365682.

    PTM databases

    PhosphoSitei Q04724.

    Polymorphism databases

    DMDMi 29840816.

    Proteomic databases

    MaxQBi Q04724.
    PaxDbi Q04724.
    PRIDEi Q04724.

    Protocols and materials databases

    DNASUi 7088.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000376499 ; ENSP00000365682 ; ENSG00000196781 .
    GeneIDi 7088.
    KEGGi hsa:7088.
    UCSCi uc004aly.3. human.

    Organism-specific databases

    CTDi 7088.
    GeneCardsi GC09M084198.
    HGNCi HGNC:11837. TLE1.
    HPAi CAB011482.
    HPA055160.
    MIMi 600189. gene.
    neXtProti NX_Q04724.
    PharmGKBi PA36539.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2319.
    HOGENOMi HOG000293211.
    HOVERGENi HBG004689.
    OMAi PPAMDPL.
    OrthoDBi EOG7HQNC3.
    PhylomeDBi Q04724.
    TreeFami TF314167.

    Enzyme and pathway databases

    Reactomei REACT_118780. NOTCH1 Intracellular Domain Regulates Transcription.
    REACT_200731. deactivation of the beta-catenin transactivating complex.
    REACT_200753. formation of the beta-catenin:TCF transactivating complex.
    SignaLinki Q04724.

    Miscellaneous databases

    EvolutionaryTracei Q04724.
    GeneWikii TLE1.
    GenomeRNAii 7088.
    NextBioi 27723.
    PROi Q04724.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q04724.
    Bgeei Q04724.
    CleanExi HS_TLE1.
    Genevestigatori Q04724.

    Family and domain databases

    Gene3Di 2.130.10.10. 1 hit.
    InterProi IPR005617. 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 ]
    Pfami PF03920. TLE_N. 1 hit.
    PF00400. WD40. 6 hits.
    [Graphical view ]
    PRINTSi PR01850. GROUCHOFAMLY.
    SMARTi SM00320. WD40. 7 hits.
    [Graphical view ]
    SUPFAMi SSF50978. SSF50978. 1 hit.
    PROSITEi PS00678. WD_REPEATS_1. 2 hits.
    PS50082. WD_REPEATS_2. 2 hits.
    PS50294. WD_REPEATS_REGION. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Human homologs of a Drosophila enhancer of split gene product define a novel family of nuclear proteins."
      Stifani S., Blaumueller C.M., Redhead N.J., Hill R.E., Artavanis-Tsakonas S.
      Nat. Genet. 2:119-127(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Fetal brain.
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Mammary gland.
    3. "DNA sequence and analysis of human chromosome 9."
      Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
      , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
      Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Colon and Kidney.
    6. "Transducin-like enhancer of split proteins, the human homologs of Drosophila groucho, interact with hepatic nuclear factor 3beta."
      Wang J.-C., Waltner-Law M., Yamada K., Osawa H., Stifani S., Granner D.K.
      J. Biol. Chem. 275:18418-18423(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 727-739, INTERACTION WITH FOXA2, MODULATION BY AES.
    7. "Molecular interaction between TLE1 and the carboxyl-terminal domain of HES-1 containing the WRPW motif."
      Grbavec D., Stifani S.
      Biochem. Biophys. Res. Commun. 223:701-705(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TLE1.
    8. "The WRPW motif of the hairy-related basic helix-loop-helix repressor proteins acts as a 4-amino-acid transcription repression and protein-protein interaction domain."
      Fisher A.L., Ohsako S., Caudy M.
      Mol. Cell. Biol. 16:2670-2677(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HES1.
    9. "The Groucho/transducin-like enhancer of split transcriptional repressors interact with the genetically defined amino-terminal silencing domain of histone H3."
      Palaparti A., Baratz A., Stifani S.
      J. Biol. Chem. 272:26604-26610(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: OLIGOMERIZATION, ASSOCIATION WITH CHROMATIN, INTERACTION WITH HISTONE H3.
    10. "Transducin-like Enhancer of split 2, a mammalian homologue of Drosophila Groucho, acts as a transcriptional repressor, interacts with Hairy/Enhancer of split proteins, and is expressed during neuronal development."
      Grbavec D., Lo R., Liu Y., Stifani S.
      Eur. J. Biochem. 258:339-349(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: OLIGOMERIZATION, INTERACTION WITH HES1.
    11. "Transcriptional repression by AML1 and LEF-1 is mediated by the TLE/Groucho corepressors."
      Levanon D., Goldstein R.E., Bernstein Y., Tang H., Goldenberg D., Stifani S., Paroush Z., Groner Y.
      Proc. Natl. Acad. Sci. U.S.A. 95:11590-11595(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RUNX1; RUNX3 AND LEF1.
    12. "Groucho/transducin-like enhancer of split (TLE) family members interact with the yeast transcriptional co-repressor SSN6 and mammalian SSN6-related proteins: implications for evolutionary conservation of transcription repression mechanisms."
      Grbavec D., Lo R., Liu Y., Greenfield A., Stifani S.
      Biochem. J. 337:13-17(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH KDM6A AND UTY.
    13. "Inhibition of nuclear factor-kappaB-mediated transcription by association with the amino-terminal enhancer of split, a Groucho-related protein lacking WD40 repeats."
      Tetsuka T., Uranishi H., Imai H., Ono T., Sonta S., Takahashi N., Asamitsu K., Okamoto T.
      J. Biol. Chem. 275:4383-4390(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH RELA.
    14. "Temporal regulation of a paired-like homeodomain repressor/TLE corepressor complex and a related activator is required for pituitary organogenesis."
      Dasen J.S., Martinez-Barbera J.-P., Herman T.S., O'Connell S., Olson L., Ju B., Tollkuhn J., Baek S.H., Rose D.W., Rosenfeld M.G.
      Genes Dev. 15:3193-3207(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HESX1, MUTAGENESIS OF VAL-486; TYR-532; LEU-702 AND SER-715.
    15. "A role for cell cycle-regulated phosphorylation in Groucho-mediated transcriptional repression."
      Nuthall H.N., Joachim K., Palaparti A., Stifani S.
      J. Biol. Chem. 277:51049-51057(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, DEGREE OF PHOSPHORYLATION.
    16. "Identification of PNRC2 and TLE1 as activation function-1 cofactors of the orphan nuclear receptor ERRgamma."
      Hentschke M., Borgmeyer U.
      Biochem. Biophys. Res. Commun. 312:975-982(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ESRRG.
    17. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-239 AND SER-286, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. "XIAP monoubiquitylates Groucho/TLE to promote canonical Wnt signaling."
      Hanson A.J., Wallace H.A., Freeman T.J., Beauchamp R.D., Lee L.A., Lee E.
      Mol. Cell 45:619-628(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION BY XIAP/BIRC4.
    22. "Crystal structure of the C-terminal WD40 repeat domain of the human Groucho/TLE1 transcriptional corepressor."
      Pickles L.M., Roe S.M., Hemingway E.J., Stifani S., Pearl L.H.
      Structure 10:751-761(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 443-770.

    Entry informationi

    Entry nameiTLE1_HUMAN
    AccessioniPrimary (citable) accession number: Q04724
    Secondary accession number(s): A8K495, Q5T3G4, Q969V9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1994
    Last sequence update: March 25, 2003
    Last modified: October 1, 2014
    This is version 156 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 9
      Human chromosome 9: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3