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Q04724 (TLE1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 154. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Transducin-like enhancer protein 1
Alternative name(s):
E(Sp1) homolog
Enhancer of split groucho-like protein 1
Short name=ESG1
Gene names
Name:TLE1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length770 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. The effects of full-length TLE family members may be modulated by association with dominant-negative AES. Unusual function as coactivator for ESRRG. Ref.13

Subunit structure

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). Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.16

Subcellular location

Nucleus. Note: Nuclear and chromatin-associated, depending on isoforms and phosphorylation status. Hyperphosphorylation decreases the affinity for nuclear components. Ref.15

Tissue specificity

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

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. Ref.15

Ubiquitinated by XIAP/BIRC4. Ref.21

Sequence similarities

Belongs to the WD repeat Groucho/TLE family.

Contains 6 WD repeats.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
Wnt signaling pathway
   Cellular componentNucleus
   DomainRepeat
WD repeat
   Molecular functionRepressor
   PTMPhosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processNotch signaling pathway

Traceable author statement. Source: Reactome

Wnt signaling pathway

Inferred from electronic annotation. Source: UniProtKB-KW

multicellular organismal development

Traceable author statement PubMed 8365415. Source: ProtInc

negative regulation of I-kappaB kinase/NF-kappaB signaling

Inferred from direct assay PubMed 17680780. Source: UniProtKB

negative regulation of Wnt signaling pathway

Non-traceable author statement Ref.11. Source: UniProtKB

negative regulation of anoikis

Inferred from mutant phenotype PubMed 15006356PubMed 22952044. Source: UniProtKB

negative regulation of transcription, DNA-templated

Inferred from direct assay Ref.11. Source: UniProtKB

organ morphogenesis

Traceable author statement PubMed 8808280. Source: ProtInc

positive regulation of gene expression

Inferred from mutant phenotype PubMed 15006356. Source: UniProtKB

signal transduction

Traceable author statement PubMed 8808280. Source: ProtInc

   Cellular_componentcytoplasm

Inferred from direct assay. Source: HPA

cytosol

Inferred from mutant phenotype PubMed 22952044. Source: UniProtKB

nucleolus

Inferred from direct assay. Source: HPA

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from mutant phenotype PubMed 22952044. Source: UniProtKB

transcription factor complex

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionRNA polymerase II transcription corepressor activity

Inferred from direct assay Ref.6. Source: BHF-UCL

chromatin binding

Inferred from electronic annotation. Source: Ensembl

protein binding

Inferred from physical interaction Ref.11. Source: UniProtKB

transcription factor binding

Inferred from direct assay Ref.11. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 770770Transducin-like enhancer protein 1
PRO_0000051276

Regions

Repeat470 – 50132WD 1
Repeat528 – 55831WD 2
Repeat572 – 60231WD 3
Repeat614 – 64431WD 4
Repeat696 – 72631WD 5
Repeat737 – 76731WD 6
Region200 – 26869CCN domain
Motif225 – 2284Nuclear localization signal Potential
Compositional bias1 – 131131Gln-rich
Compositional bias132 – 19968Gly/Pro-rich
Compositional bias269 – 449181Pro/Ser-rich

Amino acid modifications

Modified residue2391Phosphoserine Ref.20
Modified residue2591Phosphoserine; by CDK1 Potential
Modified residue2631Phosphoserine; by CDK1 Potential
Modified residue2671Phosphoserine; by CDK1 Potential
Modified residue2861Phosphoserine Ref.20

Experimental info

Mutagenesis4861V → S: Abolishes HESX1 binding. Ref.14
Mutagenesis5321Y → H: Abolishes HESX1 binding. Ref.14
Mutagenesis7021L → S: Abolishes HESX1 binding. Ref.14
Mutagenesis7151S → P: Abolishes HESX1 binding. Ref.14
Sequence conflict407 – 4126AAAVVA → RGRRGR in AAA61192. Ref.1
Sequence conflict464 – 4652DA → TP in AAA61192. Ref.1

Secondary structure

........................................................................... 770
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q04724 [UniParc].

Last modified March 25, 2003. Version 2.
Checksum: 695FD1A37410EFE5

FASTA77083,201
        10         20         30         40         50         60 
MFPQSRHPTP HQAAGQPFKF TIPESLDRIK EEFQFLQAQY HSLKLECEKL ASEKTEMQRH 

        70         80         90        100        110        120 
YVMYYEMSYG LNIEMHKQTE IAKRLNTICA QVIPFLSQEH QQQVAQAVER AKQVTMAELN 

       130        140        150        160        170        180 
AIIGQQQLQA QHLSHGHGPP VPLTPHPSGL QPPGIPPLGG SAGLLALSSA LSGQSHLAIK 

       190        200        210        220        230        240 
DDKKHHDAEH HRDREPGTSN SLLVPDSLRG TDKRRNGPEF SNDIKKRKVD DKDSSHYDSD 

       250        260        270        280        290        300 
GDKSDDNLVV DVSNEDPSSP RASPAHSPRE NGIDKNRLLK KDASSSPAST ASSASSTSLK 

       310        320        330        340        350        360 
SKEMSLHEKA STPVLKSSTP TPRSDMPTPG TSATPGLRPG LGKPPAIDPL VNQAAAGLRT 

       370        380        390        400        410        420 
PLAVPGPYPA PFGMVPHAGM NGELTSPGAA YASLHNMSPQ MSAAAAAAAV VAYGRSPMVG 

       430        440        450        460        470        480 
FDPPPHMRVP TIPPNLAGIP GGKPAYSFHV TADGQMQPVP FPPDALIGPG IPRHARQINT 

       490        500        510        520        530        540 
LNHGEVVCAV TISNPTRHVY TGGKGCVKVW DISHPGNKSP VSQLDCLNRD NYIRSCKLLP 

       550        560        570        580        590        600 
DGCTLIVGGE ASTLSIWDLA APTPRIKAEL TSSAPACYAL AISPDSKVCF SCCSDGNIAV 

       610        620        630        640        650        660 
WDLHNQTLVR QFQGHTDGAS CIDISNDGTK LWTGGLDNTV RSWDLREGRQ LQQHDFTSQI 

       670        680        690        700        710        720 
FSLGYCPTGE WLAVGMESSN VEVLHVNKPD KYQLHLHESC VLSLKFAYCG KWFVSTGKDN 

       730        740        750        760        770 
LLNAWRTPYG ASIFQSKESS SVLSCDISVD DKYIVTGSGD KKATVYEVIY 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS6661.1.
PIRB56695.
RefSeqNP_005068.2. NM_005077.3.
UniGeneHs.197320.
Hs.689805.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalQ04724.
SMRQ04724. Positions 438-770.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112943. 98 interactions.
DIPDIP-36665N.
IntActQ04724. 62 interactions.
MINTMINT-190700.
STRING9606.ENSP00000365682.

PTM databases

PhosphoSiteQ04724.

Polymorphism databases

DMDM29840816.

Proteomic databases

MaxQBQ04724.
PaxDbQ04724.
PRIDEQ04724.

Protocols and materials databases

DNASU7088.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000376499; ENSP00000365682; ENSG00000196781.
GeneID7088.
KEGGhsa:7088.
UCSCuc004aly.3. human.

Organism-specific databases

CTD7088.
GeneCardsGC09M084198.
HGNCHGNC:11837. TLE1.
HPACAB011482.
HPA055160.
MIM600189. gene.
neXtProtNX_Q04724.
PharmGKBPA36539.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2319.
HOGENOMHOG000293211.
HOVERGENHBG004689.
OMAPPAMDPL.
OrthoDBEOG7HQNC3.
PhylomeDBQ04724.
TreeFamTF314167.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_116125. Disease.
SignaLinkQ04724.

Gene expression databases

ArrayExpressQ04724.
BgeeQ04724.
CleanExHS_TLE1.
GenevestigatorQ04724.

Family and domain databases

Gene3D2.130.10.10. 1 hit.
InterProIPR005617. 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]
PfamPF03920. TLE_N. 1 hit.
PF00400. WD40. 6 hits.
[Graphical view]
PRINTSPR01850. GROUCHOFAMLY.
SMARTSM00320. WD40. 7 hits.
[Graphical view]
SUPFAMSSF50978. SSF50978. 1 hit.
PROSITEPS00678. WD_REPEATS_1. 2 hits.
PS50082. WD_REPEATS_2. 2 hits.
PS50294. WD_REPEATS_REGION. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ04724.
GeneWikiTLE1.
GenomeRNAi7088.
NextBio27723.
PROQ04724.
SOURCESearch...

Entry information

Entry nameTLE1_HUMAN
AccessionPrimary (citable) accession number: Q04724
Secondary accession number(s): A8K495, Q5T3G4, Q969V9
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: March 25, 2003
Last modified: July 9, 2014
This is version 154 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM