Q04724 (TLE1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	770 AA.
Sequence status	Complete.
Protein existence	Evidence 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.20
Sequence similarities	Belongs to the WD repeat Groucho/TLE family. Contains 6 WD repeats.

Ontologies

Keywords
Biological process	Transcription Transcription regulation Wnt signaling pathway
Cellular component	Nucleus
Domain	Repeat WD repeat
Molecular function	Repressor
PTM	Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	Notch signaling pathway Traceable author statement. Source: Reactome Wnt receptor signaling pathway Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of I-kappaB kinase/NF-kappaB cascade Inferred from direct assay PubMed 17680780. Source: UniProtKB negative regulation of Wnt receptor signaling pathway Non-traceable author statement Ref.11. Source: UniProtKB negative regulation of anoikis Inferred from mutant phenotype PubMed 15006356PubMed 22952044. Source: UniProtKB organ morphogenesis Traceable author statement PubMed 8808280. Source: ProtInc positive regulation of gene expression Inferred from mutant phenotype PubMed 15006356. Source: UniProtKB
Cellular_component	cytosol Inferred from mutant phenotype PubMed 22952044. Source: UniProtKB nucleoplasm Traceable author statement. Source: Reactome transcription factor complex Inferred from electronic annotation. Source: Compara
Molecular_function	RNA polymerase II transcription corepressor activity Inferred from direct assay Ref.6. Source: BHF-UCL chromatin binding Inferred from electronic annotation. Source: Compara transcription factor binding Inferred from direct assay Ref.11. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
RUNX1	Q01196-1	4	EBI-711424,EBI-925940
RUNX1	Q01196-2	3	EBI-711424,EBI-925944
RUNX3	Q13761	3	EBI-711424,EBI-925990
SIRT1	Q96EB6	4	EBI-711424,EBI-1802965
SYT-SSX2	A4PIW0	11	EBI-711424,EBI-6050533

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 770

770

Transducin-like enhancer protein 1

PRO_0000051276

Regions

Repeat

470 – 501

32

WD 1

Repeat

528 – 558

31

WD 2

Repeat

572 – 602

31

WD 3

Repeat

614 – 644

31

WD 4

Repeat

696 – 726

31

WD 5

Repeat

737 – 767

31

WD 6

Region

200 – 268

69

CCN domain

Motif

225 – 228

4

Nuclear localization signal Potential

Compositional bias

1 – 131

131

Gln-rich

Compositional bias

132 – 199

68

Gly/Pro-rich

Compositional bias

269 – 449

181

Pro/Ser-rich

Amino acid modifications

Modified residue

239

1

Phosphoserine Ref.19

Modified residue

259

1

Phosphoserine; by CDK1 Potential

Modified residue

263

1

Phosphoserine; by CDK1 Potential

Modified residue

267

1

Phosphoserine; by CDK1 Potential

Modified residue

284

1

Phosphoserine By similarity

Modified residue

286

1

Phosphoserine Ref.19

Experimental info

Mutagenesis

486

1

V → S: Abolishes HESX1 binding. Ref.14

Mutagenesis

532

1

Y → H: Abolishes HESX1 binding. Ref.14

Mutagenesis

702

1

L → S: Abolishes HESX1 binding. Ref.14

Mutagenesis

715

1

S → P: Abolishes HESX1 binding. Ref.14

Sequence conflict

407 – 412

6

AAAVVA → RGRRGR in AAA61192. Ref.1

Sequence conflict

464 – 465

2

DA → TP in AAA61192. Ref.1

Secondary structure

1

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770

Helix Strand Turn

Details...

Beta strand

447 – 450

4

Beta strand

452 – 454

3

Beta strand

456 – 458

3

Beta strand

465 – 468

4

Beta strand

473 – 481

9

Beta strand

489 – 492

4

Beta strand

494 – 502

9

Beta strand

504 – 511

8

Beta strand

521 – 525

5

Beta strand

531 – 538

8

Beta strand

542 – 558

17

Beta strand

560 – 563

4

Beta strand

565 – 571

7

Beta strand

573 – 575

3

Beta strand

577 – 582

6

Beta strand

586 – 593

8

Beta strand

598 – 602

5

Turn

603 – 606

4

Beta strand

607 – 612

6

Beta strand

619 – 624

6

Beta strand

628 – 635

8

Beta strand

638 – 644

7

Turn

645 – 648

4

Beta strand

649 – 655

7

Beta strand

660 – 665

6

Beta strand

669 – 676

8

Beta strand

681 – 685

5

Beta strand

691 – 694

4

Beta strand

701 – 706

6

Beta strand

710 – 717

8

Beta strand

720 – 726

7

Turn

727 – 729

3

Beta strand

732 – 737

6

Beta strand

742 – 747

6

Beta strand

753 – 758

6

Beta strand

763 – 769

7

Sequences

	Sequence		Length	Mass (Da)
	Q04724 [UniParc]. Last modified March 25, 2003. Version 2. Checksum: 695FD1A37410EFE5	FASTA	770	83,201
	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

References

	« Hide 'large scale' referencesShow '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. , 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]	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. , 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]	"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.
[18]	"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].
[19]	"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, MASS SPECTROMETRY.
[20]	"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.
[21]	"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.

IPI

IPI00413270.

PIR

B56695.

RefSeq

NP_005068.2. NM_005077.3.

UniGene

Hs.197320.
Hs.689805.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

Q04724.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-36665N.

IntAct

Q04724. 48 interactions.

MINT

MINT-190700.

STRING

9606.ENSP00000365682.

PTM databases

PhosphoSite

Q04724.

Polymorphism databases

DMDM

29840816.

Proteomic databases

PaxDb

Q04724.

PRIDE

Q04724.

Protocols and materials databases

DNASU

7088.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000376499; ENSP00000365682; ENSG00000196781.

GeneID

7088.

KEGG

hsa:7088.

UCSC

uc004aly.3. human.

Organism-specific databases

CTD

7088.

GeneCards

GC09M084198.

HGNC

HGNC:11837. TLE1.

HPA

CAB011482.

MIM

600189. gene.

neXtProt

NX_Q04724.

PharmGKB

PA36539.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG2319.

HOGENOM

HOG000293211.

HOVERGEN

HBG004689.

OMA

AMDPLVN.

OrthoDB

EOG4MGS6V.

PhylomeDB

Q04724.

Enzyme and pathway databases

Pathway_Interaction_DB

wnt_canonical_pathway. Canonical Wnt signaling pathway.
ps1pathway. Presenilin action in Notch and Wnt signaling.

Reactome

REACT_111102. Signal Transduction.

Gene expression databases

ArrayExpress

Q04724.

Bgee

Q04724.

CleanEx

HS_TLE1.

Genevestigator

Q04724.

GermOnline

ENSG00000196781. Homo sapiens.

Family and domain databases

Gene3D

2.130.10.10. 1 hit.

InterPro

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]

Pfam

PF03920. TLE_N. 1 hit.
PF00400. WD40. 6 hits.
[Graphical view]

PRINTS

PR01850. GROUCHOFAMLY.

SMART

SM00320. WD40. 7 hits.
[Graphical view]

SUPFAM

SSF50978. WD40_like. 1 hit.

PROSITE

PS00678. WD_REPEATS_1. 2 hits.
PS50082. WD_REPEATS_2. 2 hits.
PS50294. WD_REPEATS_REGION. 2 hits.
[Graphical view]

ProtoNet

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Other

EvolutionaryTrace

Q04724.

GenomeRNAi

7088.

NextBio

27723.

SOURCE

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Entry information

Entry name

TLE1_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 142 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.