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Q04724

- TLE1_HUMAN

UniProt

Q04724 - TLE1_HUMAN

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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

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. identical protein binding Source: IntAct
  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
Complete GO annotation...

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
Complete GO annotation...

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

BgeeiQ04724.
CleanExiHS_TLE1.
ExpressionAtlasiQ04724. baseline and differential.
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). Interacts with SIX3.11 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. 105 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 19-135, 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.
GeneTreeiENSGT00550000074465.
HOGENOMiHOG000293211.
HOVERGENiHBG004689.
InParanoidiQ04724.
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

        10         20         30         40         50
MFPQSRHPTP HQAAGQPFKF TIPESLDRIK EEFQFLQAQY HSLKLECEKL
60 70 80 90 100
ASEKTEMQRH YVMYYEMSYG LNIEMHKQTE IAKRLNTICA QVIPFLSQEH
110 120 130 140 150
QQQVAQAVER AKQVTMAELN AIIGQQQLQA QHLSHGHGPP VPLTPHPSGL
160 170 180 190 200
QPPGIPPLGG SAGLLALSSA LSGQSHLAIK DDKKHHDAEH HRDREPGTSN
210 220 230 240 250
SLLVPDSLRG TDKRRNGPEF SNDIKKRKVD DKDSSHYDSD GDKSDDNLVV
260 270 280 290 300
DVSNEDPSSP RASPAHSPRE NGIDKNRLLK KDASSSPAST ASSASSTSLK
310 320 330 340 350
SKEMSLHEKA STPVLKSSTP TPRSDMPTPG TSATPGLRPG LGKPPAIDPL
360 370 380 390 400
VNQAAAGLRT PLAVPGPYPA PFGMVPHAGM NGELTSPGAA YASLHNMSPQ
410 420 430 440 450
MSAAAAAAAV VAYGRSPMVG FDPPPHMRVP TIPPNLAGIP GGKPAYSFHV
460 470 480 490 500
TADGQMQPVP FPPDALIGPG IPRHARQINT LNHGEVVCAV TISNPTRHVY
510 520 530 540 550
TGGKGCVKVW DISHPGNKSP VSQLDCLNRD NYIRSCKLLP DGCTLIVGGE
560 570 580 590 600
ASTLSIWDLA APTPRIKAEL TSSAPACYAL AISPDSKVCF SCCSDGNIAV
610 620 630 640 650
WDLHNQTLVR QFQGHTDGAS CIDISNDGTK LWTGGLDNTV RSWDLREGRQ
660 670 680 690 700
LQQHDFTSQI FSLGYCPTGE WLAVGMESSN VEVLHVNKPD KYQLHLHESC
710 720 730 740 750
VLSLKFAYCG KWFVSTGKDN LLNAWRTPYG ASIFQSKESS SVLSCDISVD
760 770
DKYIVTGSGD KKATVYEVIY
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 19-135, 438-770.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112943. 105 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.
GeneTreei ENSGT00550000074465.
HOGENOMi HOG000293211.
HOVERGENi HBG004689.
InParanoidi Q04724.
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

Bgeei Q04724.
CleanExi HS_TLE1.
ExpressionAtlasi Q04724. baseline and differential.
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

« Hide 'large scale' publications
  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. "Six3 and Six6 activity is modulated by members of the groucho family."
    Lopez-Rios J., Tessmar K., Loosli F., Wittbrodt J., Bovolenta P.
    Development 130:185-195(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SIX3.
  18. "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].
  19. "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.
  20. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. "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].
  22. "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.
  23. "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 29, 2014
This is version 157 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

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