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Q04726

- TLE3_HUMAN

UniProt

Q04726 - TLE3_HUMAN

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Protein

Transducin-like enhancer protein 3

Gene

TLE3

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 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).By similarity

GO - Biological processi

  1. Notch signaling pathway Source: Reactome
  2. organ morphogenesis Source: ProtInc
  3. regulation of transcription, DNA-templated Source: UniProtKB-KW
  4. signal transduction Source: ProtInc
  5. transcription, DNA-templated Source: UniProtKB-KW
  6. 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.
SignaLinkiQ04726.

Names & Taxonomyi

Protein namesi
Recommended name:
Transducin-like enhancer protein 3
Alternative name(s):
Enhancer of split groucho-like protein 3
Short name:
ESG3
Gene namesi
Name:TLE3
Synonyms:KIAA1547
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 15

Organism-specific databases

HGNCiHGNC:11839. TLE3.

Subcellular locationi

GO - Cellular componenti

  1. nucleoplasm Source: Reactome
  2. nucleus Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA36541.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 772772Transducin-like enhancer protein 3PRO_0000051280Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei203 – 2031Phosphoserine5 Publications
Modified residuei207 – 2071Phosphoserine1 Publication
Modified residuei217 – 2171Phosphoserine1 Publication
Modified residuei240 – 2401Phosphoserine1 Publication
Modified residuei245 – 2451Phosphoserine1 Publication
Modified residuei259 – 2591Phosphothreonine4 Publications
Modified residuei263 – 2631Phosphoserine3 Publications
Modified residuei267 – 2671Phosphoserine3 Publications
Modified residuei286 – 2861Phosphoserine4 Publications
Modified residuei312 – 3121Phosphothreonine1 Publication
Modified residuei317 – 3171Phosphoserine1 Publication
Modified residuei319 – 3191Phosphothreonine1 Publication
Modified residuei321 – 3211Phosphothreonine1 Publication
Modified residuei328 – 3281Phosphothreonine3 Publications
Modified residuei334 – 3341Phosphothreonine4 Publications
Modified residuei413 – 4131Phosphoserine1 Publication

Post-translational modificationi

Ubiquitinated by XIAP/BIRC4. This ubiquitination does not affect its stability, nuclear localization, or capacity to tetramerize but inhibits its interaction with TCF7L2/TCF4.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ04726.
PaxDbiQ04726.
PRIDEiQ04726.

PTM databases

PhosphoSiteiQ04726.

Expressioni

Tissue specificityi

Placenta and lung.

Gene expression databases

BgeeiQ04726.
CleanExiHS_TLE3.
ExpressionAtlasiQ04726. baseline and differential.
GenevestigatoriQ04726.

Organism-specific databases

HPAiHPA054116.

Interactioni

Subunit structurei

Homotetramer and heterooligomer with other family members. Binds LEF1, TCF7 and TCF7L1 (By similarity). Binds FOXA2. Interacts with XIAP/BIRC4 and TCF7L2/TCF4. Interacts with TBX18 (via engrailed homology 1 repressor motif), leadibg to decreased of TBX18 transcriptional activity.By similarity2 Publications

Protein-protein interaction databases

BioGridi112945. 34 interactions.
IntActiQ04726. 9 interactions.
MINTiMINT-2805536.
STRINGi9606.ENSP00000319233.

Structurei

3D structure databases

ProteinModelPortaliQ04726.
SMRiQ04726. Positions 19-135, 443-772.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati484 – 52239WD 1Add
BLAST
Repeati530 – 56940WD 2Add
BLAST
Repeati574 – 61340WD 3Add
BLAST
Repeati616 – 65540WD 4Add
BLAST
Repeati657 – 69640WD 5Add
BLAST
Repeati698 – 73740WD 6Add
BLAST
Repeati739 – 77133WD 7Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni199 – 26870CCN 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 – 19867Gly/Pro-richAdd
BLAST
Compositional biasi269 – 451183Pro/Ser-richAdd
BLAST
Compositional biasi401 – 4099Poly-Ala

Sequence similaritiesi

Belongs to the WD repeat Groucho/TLE family.Curated
Contains 7 WD repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, WD repeat

Phylogenomic databases

eggNOGiCOG2319.
GeneTreeiENSGT00550000074465.
HOGENOMiHOG000293211.
HOVERGENiHBG004689.
InParanoidiQ04726.
OrthoDBiEOG7HQNC3.
PhylomeDBiQ04726.
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. 5 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]

Sequences (7)i

Sequence statusi: Complete.

This entry describes 7 isoformsi produced by alternative splicing. Align

Note: Experimental confirmation may be lacking for some isoforms.

Isoform 1 (identifier: Q04726-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MYPQGRHPAP HQPGQPGFKF TVAESCDRIK DEFQFLQAQY HSLKVEYDKL
60 70 80 90 100
ANEKTEMQRH YVMYYEMSYG LNIEMHKQTE IAKRLNTILA QIMPFLSQEH
110 120 130 140 150
QQQVAQAVER AKQVTMTELN AIIGQQQLQA QHLSHATHGP PVQLPPHPSG
160 170 180 190 200
LQPPGIPPVT GSSSGLLALG ALGSQAHLTV KDEKNHHELD HRERESSANN
210 220 230 240 250
SVSPSESLRA SEKHRGSADY SMEAKKRKAE EKDSLSRYDS DGDKSDDLVV
260 270 280 290 300
DVSNEDPATP RVSPAHSPPE NGLDKARSLK KDAPTSPASV ASSSSTPSSK
310 320 330 340 350
TKDLGHNDKS STPGLKSNTP TPRNDAPTPG TSTTPGLRSM PGKPPGMDPI
360 370 380 390 400
GIMASALRTP ISITSSYAAP FAMMSHHEMN GSLTSPGAYA GLHNIPPQMS
410 420 430 440 450
AAAAAAAAAY GRSPMVSFGA VGFDPHPPMR ATGLPSSLAS IPGGKPAYSF
460 470 480 490 500
HVSADGQMQP VPFPHDALAG PGIPRHARQI NTLSHGEVVC AVTISNPTRH
510 520 530 540 550
VYTGGKGCVK IWDISQPGSK SPISQLDCLN RDNYIRSCKL LPDGRTLIVG
560 570 580 590 600
GEASTLTIWD LASPTPRIKA ELTSSAPACY ALAISPDAKV CFSCCSDGNI
610 620 630 640 650
AVWDLHNQTL VRQFQGHTDG ASCIDISHDG TKLWTGGLDN TVRSWDLREG
660 670 680 690 700
RQLQQHDFTS QIFSLGYCPT GEWLAVGMES SNVEVLHHTK PDKYQLHLHE
710 720 730 740 750
SCVLSLKFAY CGKWFVSTGK DNLLNAWRTP YGASIFQSKE SSSVLSCDIS
760 770
ADDKYIVTGS GDKKATVYEV IY
Length:772
Mass (Da):83,417
Last modified:May 10, 2002 - v2
Checksum:iA2A469D73BF04A43
GO
Isoform 2 (identifier: Q04726-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     342-353: Missing.

Show »
Length:760
Mass (Da):82,222
Checksum:i5CA1DDAE26C00E19
GO
Isoform 3 (identifier: Q04726-3) [UniParc]FASTAAdd to Basket

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.

Show »
Length:764
Mass (Da):82,654
Checksum:iEF5606A1D9C7C2BA
GO
Isoform 4 (identifier: Q04726-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-8: MYPQGRHP → MPPPPPLSCLRGLQ
     127-127: Missing.
     417-421: Missing.

Show »
Length:772
Mass (Da):83,348
Checksum:iF10C1C00DE38D280
GO
Isoform 5 (identifier: Q04726-5) [UniParc]FASTAAdd to Basket

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.

Show »
Length:769
Mass (Da):83,115
Checksum:i9E7895DE647F9D9E
GO
Isoform 6 (identifier: Q04726-6) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     416-420: Missing.

Note: No experimental confirmation available.

Show »
Length:767
Mass (Da):82,955
Checksum:i7081DB8CE8BF2EAD
GO
Isoform 7 (identifier: Q04726-7) [UniParc]FASTAAdd to Basket

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

Show »
Length:762
Mass (Da):82,279
Checksum:iE82ECE78C54894E1
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti358 – 3581R → C in BAG60692. (PubMed:14702039)Curated
Sequence conflicti365 – 3651S → G in BAG60692. (PubMed:14702039)Curated
Sequence conflicti409 – 4091A → T in AAH41831. (PubMed:15489334)Curated
Sequence conflicti487 – 4871E → G in AAA61194. (PubMed:1303260)Curated
Sequence conflicti498 – 4981T → S in AAA61194. (PubMed:1303260)Curated
Sequence conflicti535 – 5351I → M in AAA61194. (PubMed:1303260)Curated
Sequence conflicti541 – 5411L → H in AAA61194. (PubMed:1303260)Curated
Sequence conflicti549 – 5491V → E in BAG60692. (PubMed:14702039)Curated
Sequence conflicti553 – 5531A → G in AAA61194. (PubMed:1303260)Curated
Sequence conflicti692 – 6921D → H in AAA61194. (PubMed:1303260)Curated
Sequence conflicti736 – 7361F → S in AAA61194. (PubMed:1303260)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti229 – 2291A → V.1 Publication
Corresponds to variant rs1057864 [ dbSNP | Ensembl ].
VAR_053421

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 88MYPQGRHP → MPPPPPLSCLRGLQ in isoform 4. 1 PublicationVSP_007023
Alternative sequencei1 – 88MYPQGRHP → M in isoform 7. 1 PublicationVSP_055168
Alternative sequencei127 – 1271Missing in isoform 4. 1 PublicationVSP_007024
Alternative sequencei342 – 35312Missing in isoform 2. 1 PublicationVSP_006788Add
BLAST
Alternative sequencei351 – 3533Missing in isoform 3, isoform 5 and isoform 7. 2 PublicationsVSP_006789
Alternative sequencei416 – 4205Missing in isoform 6. 1 PublicationVSP_054598
Alternative sequencei417 – 4215Missing in isoform 3 and isoform 4. 1 PublicationVSP_006790

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS45293.1. [Q04726-1]
CCDS45294.1. [Q04726-5]
CCDS58375.1. [Q04726-2]
CCDS61689.1. [Q04726-7]
CCDS61691.1. [Q04726-6]
CCDS61692.1. [Q04726-3]
PIRiD56695.
RefSeqiNP_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. [Q04726-7]
NP_001269911.1. NM_001282982.1.
NP_005069.2. NM_005078.3. [Q04726-1]
NP_065959.1. NM_020908.2. [Q04726-2]
UniGeneiHs.287362.

Genome annotation databases

GeneIDi7090.
KEGGihsa:7090.
UCSCiuc002asl.2. human. [Q04726-4]
uc002asm.2. human. [Q04726-1]
uc002asn.2. human. [Q04726-2]
uc002aso.2. human.
uc002asp.2. human. [Q04726-3]

Polymorphism databases

DMDMi20532417.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS45293.1. [Q04726-1 ]
CCDS45294.1. [Q04726-5 ]
CCDS58375.1. [Q04726-2 ]
CCDS61689.1. [Q04726-7 ]
CCDS61691.1. [Q04726-6 ]
CCDS61692.1. [Q04726-3 ]
PIRi D56695.
RefSeqi NP_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. [Q04726-7 ]
NP_001269911.1. NM_001282982.1.
NP_005069.2. NM_005078.3. [Q04726-1 ]
NP_065959.1. NM_020908.2. [Q04726-2 ]
UniGenei Hs.287362.

3D structure databases

ProteinModelPortali Q04726.
SMRi Q04726. Positions 19-135, 443-772.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112945. 34 interactions.
IntActi Q04726. 9 interactions.
MINTi MINT-2805536.
STRINGi 9606.ENSP00000319233.

PTM databases

PhosphoSitei Q04726.

Polymorphism databases

DMDMi 20532417.

Proteomic databases

MaxQBi Q04726.
PaxDbi Q04726.
PRIDEi Q04726.

Protocols and materials databases

DNASUi 7090.
Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 7090.
KEGGi hsa:7090.
UCSCi uc002asl.2. human. [Q04726-4 ]
uc002asm.2. human. [Q04726-1 ]
uc002asn.2. human. [Q04726-2 ]
uc002aso.2. human.
uc002asp.2. human. [Q04726-3 ]

Organism-specific databases

CTDi 7090.
GeneCardsi GC15M070341.
HGNCi HGNC:11839. TLE3.
HPAi HPA054116.
MIMi 600190. gene.
neXtProti NX_Q04726.
PharmGKBi PA36541.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG2319.
GeneTreei ENSGT00550000074465.
HOGENOMi HOG000293211.
HOVERGENi HBG004689.
InParanoidi Q04726.
OrthoDBi EOG7HQNC3.
PhylomeDBi Q04726.
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 Q04726.

Miscellaneous databases

GeneWikii TLE3.
GenomeRNAii 7090.
NextBioi 27731.
PROi Q04726.
SOURCEi Search...

Gene expression databases

Bgeei Q04726.
CleanExi HS_TLE3.
ExpressionAtlasi Q04726. baseline and differential.
Genevestigatori Q04726.

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. 5 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] (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.
    , 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.
    , 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. 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. 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. 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.

Entry informationi

Entry nameiTLE3_HUMAN
AccessioniPrimary (citable) accession number: Q04726
Secondary accession number(s): B4DPT0
, E9PD64, F8W964, Q6PI57, Q8IVV6, Q8WVR2, Q9HCM5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: May 10, 2002
Last modified: October 29, 2014
This is version 154 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 15
    Human chromosome 15: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3