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Q04726 (TLE3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 151. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Transducin-like enhancer protein 3
Alternative name(s):
Enhancer of split groucho-like protein 3
Short name=ESG3
Gene names
Name:TLE3
Synonyms:KIAA1547
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length772 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Transcriptional corepressor that binds to a number of transcription factors. Inhibits the transcriptional activation mediated 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 By similarity.

Subunit structure

Homotetramer and heterooligomer with other family members. Binds LEF1, TCF7 and TCF7L1 By similarity. Binds FOXA2. Interacts with XIAP/BIRC4 and TCF7L2/TCF4. Ref.6 Ref.18

Subcellular location

Nucleus.

Tissue specificity

Placenta and lung.

Post-translational modification

Ubiquitinated by XIAP/BIRC4. This ubiquitination does not affect its stability, nuclear localization, or capacity to tetramerize but inhibits its interaction with TCF7L2/TCF4. Ref.18

Sequence similarities

Belongs to the WD repeat Groucho/TLE family.

Contains 7 WD repeats.

Sequence caution

The sequence BAB13373.1 differs from that shown. Reason: Erroneous initiation.

Alternative products

This entry describes 7 isoforms produced by alternative splicing. [Align] [Select]

Note: Experimental confirmation may be lacking for some isoforms.
Isoform 1 (identifier: Q04726-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q04726-2)

The sequence of this isoform differs from the canonical sequence as follows:
     342-353: Missing.
Isoform 3 (identifier: Q04726-3)

The sequence of this isoform differs from the canonical sequence as follows:
     351-353: Missing.
     417-421: Missing.
Note: Contains a N6-acetyllysine at position 343.
Isoform 4 (identifier: Q04726-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-8: MYPQGRHP → MPPPPPLSCLRGLQ
     127-127: Missing.
     417-421: Missing.
Isoform 5 (identifier: Q04726-5)

The sequence of this isoform differs from the canonical sequence as follows:
     351-353: Missing.
Note: No experimental confirmation available. Contains a N6-acetyllysine at position 343.
Isoform 6 (identifier: Q04726-6)

The sequence of this isoform differs from the canonical sequence as follows:
     416-420: Missing.
Note: No experimental confirmation available.
Isoform 7 (identifier: Q04726-7)

The sequence of this isoform differs from the canonical sequence as follows:
     1-8: MYPQGRHP → M
     351-353: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 772772Transducin-like enhancer protein 3
PRO_0000051280

Regions

Repeat484 – 52239WD 1
Repeat530 – 56940WD 2
Repeat574 – 61340WD 3
Repeat616 – 65540WD 4
Repeat657 – 69640WD 5
Repeat698 – 73740WD 6
Repeat739 – 77133WD 7
Region199 – 26870CCN domain
Motif225 – 2284Nuclear localization signal Potential
Compositional bias1 – 131131Gln-rich
Compositional bias132 – 19867Gly/Pro-rich
Compositional bias269 – 451183Pro/Ser-rich
Compositional bias401 – 4099Poly-Ala

Amino acid modifications

Modified residue2031Phosphoserine Ref.8 Ref.10 Ref.13 Ref.15 Ref.17
Modified residue2071Phosphoserine Ref.10
Modified residue2171Phosphoserine Ref.7
Modified residue2401Phosphoserine Ref.17
Modified residue2451Phosphoserine Ref.17
Modified residue2591Phosphothreonine Ref.10 Ref.13 Ref.15 Ref.17
Modified residue2631Phosphoserine Ref.10 Ref.15 Ref.17
Modified residue2671Phosphoserine Ref.10 Ref.15 Ref.17
Modified residue2861Phosphoserine Ref.8 Ref.10 Ref.13 Ref.17
Modified residue3121Phosphothreonine Ref.10
Modified residue3171Phosphoserine Ref.10
Modified residue3191Phosphothreonine Ref.10
Modified residue3211Phosphothreonine Ref.10
Modified residue3281Phosphothreonine Ref.10 Ref.13 Ref.15
Modified residue3341Phosphothreonine Ref.8 Ref.10 Ref.13 Ref.15
Modified residue4131Phosphoserine Ref.10

Natural variations

Alternative sequence1 – 88MYPQGRHP → MPPPPPLSCLRGLQ in isoform 4.
VSP_007023
Alternative sequence1 – 88MYPQGRHP → M in isoform 7.
VSP_055168
Alternative sequence1271Missing in isoform 4.
VSP_007024
Alternative sequence342 – 35312Missing in isoform 2.
VSP_006788
Alternative sequence351 – 3533Missing in isoform 3, isoform 5 and isoform 7.
VSP_006789
Alternative sequence416 – 4205Missing in isoform 6.
VSP_054598
Alternative sequence417 – 4215Missing in isoform 3 and isoform 4.
VSP_006790
Natural variant2291A → V. Ref.1
Corresponds to variant rs1057864 [ dbSNP | Ensembl ].
VAR_053421

Experimental info

Sequence conflict3581R → C in BAG60692. Ref.3
Sequence conflict3651S → G in BAG60692. Ref.3
Sequence conflict4091A → T in AAH41831. Ref.5
Sequence conflict4871E → G in AAA61194. Ref.1
Sequence conflict4981T → S in AAA61194. Ref.1
Sequence conflict5351I → M in AAA61194. Ref.1
Sequence conflict5411L → H in AAA61194. Ref.1
Sequence conflict5491V → E in BAG60692. Ref.3
Sequence conflict5531A → G in AAA61194. Ref.1
Sequence conflict6921D → H in AAA61194. Ref.1
Sequence conflict7361F → S in AAA61194. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 10, 2002. Version 2.
Checksum: A2A469D73BF04A43

FASTA77283,417
        10         20         30         40         50         60 
MYPQGRHPAP HQPGQPGFKF TVAESCDRIK DEFQFLQAQY HSLKVEYDKL ANEKTEMQRH 

        70         80         90        100        110        120 
YVMYYEMSYG LNIEMHKQTE IAKRLNTILA QIMPFLSQEH QQQVAQAVER AKQVTMTELN 

       130        140        150        160        170        180 
AIIGQQQLQA QHLSHATHGP PVQLPPHPSG LQPPGIPPVT GSSSGLLALG ALGSQAHLTV 

       190        200        210        220        230        240 
KDEKNHHELD HRERESSANN SVSPSESLRA SEKHRGSADY SMEAKKRKAE EKDSLSRYDS 

       250        260        270        280        290        300 
DGDKSDDLVV DVSNEDPATP RVSPAHSPPE NGLDKARSLK KDAPTSPASV ASSSSTPSSK 

       310        320        330        340        350        360 
TKDLGHNDKS STPGLKSNTP TPRNDAPTPG TSTTPGLRSM PGKPPGMDPI GIMASALRTP 

       370        380        390        400        410        420 
ISITSSYAAP FAMMSHHEMN GSLTSPGAYA GLHNIPPQMS AAAAAAAAAY GRSPMVSFGA 

       430        440        450        460        470        480 
VGFDPHPPMR ATGLPSSLAS IPGGKPAYSF HVSADGQMQP VPFPHDALAG PGIPRHARQI 

       490        500        510        520        530        540 
NTLSHGEVVC AVTISNPTRH VYTGGKGCVK IWDISQPGSK SPISQLDCLN RDNYIRSCKL 

       550        560        570        580        590        600 
LPDGRTLIVG GEASTLTIWD LASPTPRIKA ELTSSAPACY ALAISPDAKV CFSCCSDGNI 

       610        620        630        640        650        660 
AVWDLHNQTL VRQFQGHTDG ASCIDISHDG TKLWTGGLDN TVRSWDLREG RQLQQHDFTS 

       670        680        690        700        710        720 
QIFSLGYCPT GEWLAVGMES SNVEVLHHTK PDKYQLHLHE SCVLSLKFAY CGKWFVSTGK 

       730        740        750        760        770 
DNLLNAWRTP YGASIFQSKE SSSVLSCDIS ADDKYIVTGS GDKKATVYEV IY 

« Hide

Isoform 2 [UniParc].

Checksum: 5CA1DDAE26C00E19
Show »

FASTA76082,222
Isoform 3 [UniParc].

Checksum: EF5606A1D9C7C2BA
Show »

FASTA76482,654
Isoform 4 [UniParc].

Checksum: F10C1C00DE38D280
Show »

FASTA77283,348
Isoform 5 [UniParc].

Checksum: 9E7895DE647F9D9E
Show »

FASTA76983,115
Isoform 6 [UniParc].

Checksum: 7081DB8CE8BF2EAD
Show »

FASTA76782,955
Isoform 7 [UniParc].

Checksum: E82ECE78C54894E1
Show »

FASTA76282,279

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] (ISOFORM 1), VARIANT VAL-229.
Tissue: Fetal brain.
[2]"Prediction of the coding sequences of unidentified human genes. XVIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.
DNA Res. 7:273-281(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Brain.
[3]"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] (ISOFORMS 5 AND 7).
Tissue: Trachea.
[4]"Analysis of the DNA sequence and duplication history of human chromosome 15."
Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A. expand/collapse author list , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
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] (ISOFORMS 3; 4 AND 6).
Tissue: Pancreas and Testis.
[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 324-338 AND 521-531, INTERACTION WITH FOXA2.
[7]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-217, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203; SER-286 AND THR-334, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203; SER-207; THR-259; SER-263; SER-267; SER-286; THR-312; SER-317; THR-319; THR-321; THR-328; THR-334 AND SER-413, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"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].
[12]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203; THR-259; SER-286; THR-328 AND THR-334, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[14]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-343 (ISOFORMS 3 AND 5), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203; THR-259; SER-263; SER-267; THR-328 AND THR-334, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"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].
[17]"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-203; SER-240; SER-245; THR-259; SER-263; SER-267 AND SER-286, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"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: SUBUNIT, UBIQUITINATION BY XIAP/BIRC4, INTERACTION WITH XIAP/BIRC4 AND TCF7L2/TCF4.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M99438 mRNA. Translation: AAA61194.1.
AB046767 mRNA. Translation: BAB13373.1. Different initiation.
AK315058 mRNA. No translation available.
AK298482 mRNA. Translation: BAG60692.1.
AC026583 Genomic DNA. No translation available.
AC068327 Genomic DNA. No translation available.
BC015729 mRNA. No translation available.
BC041831 mRNA. Translation: AAH41831.1.
BC043247 mRNA. Translation: AAH43247.1.
CCDSCCDS45293.1. [Q04726-1]
CCDS45294.1. [Q04726-5]
CCDS58375.1. [Q04726-2]
CCDS61692.1. [Q04726-3]
PIRD56695.
RefSeqNP_001098662.1. NM_001105192.2. [Q04726-5]
NP_001269908.1. NM_001282979.1. [Q04726-3]
NP_001269909.1. NM_001282980.1. [Q04726-6]
NP_001269910.1. NM_001282981.1.
NP_001269911.1. NM_001282982.1.
NP_005069.2. NM_005078.3. [Q04726-1]
NP_065959.1. NM_020908.2. [Q04726-2]
UniGeneHs.287362.

3D structure databases

ProteinModelPortalQ04726.
SMRQ04726. Positions 443-772.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112945. 27 interactions.
IntActQ04726. 9 interactions.
MINTMINT-2805536.
STRING9606.ENSP00000319233.

PTM databases

PhosphoSiteQ04726.

Polymorphism databases

DMDM20532417.

Proteomic databases

MaxQBQ04726.
PaxDbQ04726.
PRIDEQ04726.

Protocols and materials databases

DNASU7090.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000317509; ENSP00000319233; ENSG00000140332. [Q04726-2]
ENST00000440567; ENSP00000415057; ENSG00000140332.
ENST00000451782; ENSP00000394717; ENSG00000140332. [Q04726-5]
ENST00000557907; ENSP00000453107; ENSG00000140332. [Q04726-3]
ENST00000557997; ENSP00000453083; ENSG00000140332. [Q04726-3]
ENST00000558379; ENSP00000453435; ENSG00000140332.
ENST00000558939; ENSP00000452871; ENSG00000140332. [Q04726-1]
ENST00000559048; ENSP00000453760; ENSG00000140332. [Q04726-4]
GeneID7090.
KEGGhsa:7090.
UCSCuc002asl.2. human. [Q04726-4]
uc002asm.2. human. [Q04726-1]
uc002asn.2. human. [Q04726-2]
uc002asp.2. human. [Q04726-3]

Organism-specific databases

CTD7090.
GeneCardsGC15M070341.
HGNCHGNC:11839. TLE3.
HPAHPA054116.
MIM600190. gene.
neXtProtNX_Q04726.
PharmGKBPA36541.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2319.
HOGENOMHOG000293211.
HOVERGENHBG004689.
InParanoidQ04726.
OrthoDBEOG7HQNC3.
PhylomeDBQ04726.
TreeFamTF314167.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_116125. Disease.
SignaLinkQ04726.

Gene expression databases

ArrayExpressQ04726.
BgeeQ04726.
CleanExHS_TLE3.
GenevestigatorQ04726.

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. 5 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

GeneWikiTLE3.
GenomeRNAi7090.
NextBio27731.
PROQ04726.
SOURCESearch...

Entry information

Entry nameTLE3_HUMAN
AccessionPrimary (citable) accession number: Q04726
Secondary accession number(s): B4DPT0 expand/collapse secondary AC list , E9PD64, F8W964, Q6PI57, Q8IVV6, Q8WVR2, Q9HCM5
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: May 10, 2002
Last modified: July 9, 2014
This is version 151 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

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 15

Human chromosome 15: entries, gene names and cross-references to MIM