TLE3_HUMAN - dbPTM
TLE3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TLE3_HUMAN
UniProt AC Q04726
Protein Name Transducin-like enhancer protein 3
Gene Name TLE3
Organism Homo sapiens (Human).
Sequence Length 772
Subcellular Localization Nucleus.
Protein Description 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)..
Protein Sequence MYPQGRHPAPHQPGQPGFKFTVAESCDRIKDEFQFLQAQYHSLKVEYDKLANEKTEMQRHYVMYYEMSYGLNIEMHKQTEIAKRLNTILAQIMPFLSQEHQQQVAQAVERAKQVTMTELNAIIGQQQLQAQHLSHATHGPPVQLPPHPSGLQPPGIPPVTGSSSGLLALGALGSQAHLTVKDEKNHHELDHRERESSANNSVSPSESLRASEKHRGSADYSMEAKKRKAEEKDSLSRYDSDGDKSDDLVVDVSNEDPATPRVSPAHSPPENGLDKARSLKKDAPTSPASVASSSSTPSSKTKDLGHNDKSSTPGLKSNTPTPRNDAPTPGTSTTPGLRSMPGKPPGMDPIGIMASALRTPISITSSYAAPFAMMSHHEMNGSLTSPGAYAGLHNIPPQMSAAAAAAAAAYGRSPMVSFGAVGFDPHPPMRATGLPSSLASIPGGKPAYSFHVSADGQMQPVPFPHDALAGPGIPRHARQINTLSHGEVVCAVTISNPTRHVYTGGKGCVKIWDISQPGSKSPISQLDCLNRDNYIRSCKLLPDGRTLIVGGEASTLTIWDLASPTPRIKAELTSSAPACYALAISPDAKVCFSCCSDGNIAVWDLHNQTLVRQFQGHTDGASCIDISHDGTKLWTGGLDNTVRSWDLREGRQLQQHDFTSQIFSLGYCPTGEWLAVGMESSNVEVLHHTKPDKYQLHLHESCVLSLKFAYCGKWFVSTGKDNLLNAWRTPYGASIFQSKESSSVLSCDISADDKYIVTGSGDKKATVYEVIY
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
6Methylation--MYPQGRHPAPHQP
--CCCCCCCCCCCCC		27.63115367979
19MethylationQPGQPGFKFTVAESC
CCCCCCCEEEEECCC		46.14115918565
30AcetylationAESCDRIKDEFQFLQ
ECCCHHHHHHHHHHH		52.6926051181
30UbiquitinationAESCDRIKDEFQFLQ
ECCCHHHHHHHHHHH		52.6921890473
49UbiquitinationSLKVEYDKLANEKTE
HCHHHHHHHHCCCHH		48.90-
69PhosphorylationVMYYEMSYGLNIEMH
HHHHHHHHCCCCCHH		25.07-
179PhosphorylationLGSQAHLTVKDEKNH
HCCEEEEEECCCCCC		18.6824719451
184UbiquitinationHLTVKDEKNHHELDH
EEEECCCCCCCCCCH		72.25-
196PhosphorylationLDHRERESSANNSVS
CCHHHHHHHCCCCCC		40.7622167270
197PhosphorylationDHRERESSANNSVSP
CHHHHHHHCCCCCCH		30.2022167270
201PhosphorylationRESSANNSVSPSESL
HHHHCCCCCCHHHHH		24.6329255136
203PhosphorylationSSANNSVSPSESLRA
HHCCCCCCHHHHHHH		23.6419664994
205PhosphorylationANNSVSPSESLRASE
CCCCCCHHHHHHHHH		32.1029255136
207PhosphorylationNSVSPSESLRASEKH
CCCCHHHHHHHHHHH		27.7429255136
211PhosphorylationPSESLRASEKHRGSA
HHHHHHHHHHHCCCC		40.5225159151
213AcetylationESLRASEKHRGSADY
HHHHHHHHHCCCCCC		35.797681763
215MethylationLRASEKHRGSADYSM
HHHHHHHCCCCCCCH		52.40115918569
217PhosphorylationASEKHRGSADYSMEA
HHHHHCCCCCCCHHH		20.2325159151
220PhosphorylationKHRGSADYSMEAKKR
HHCCCCCCCHHHHHH		15.0530576142
221PhosphorylationHRGSADYSMEAKKRK
HCCCCCCCHHHHHHH		15.6425159151
225AcetylationADYSMEAKKRKAEEK
CCCCHHHHHHHHHHH		39.5425953088
226AcetylationDYSMEAKKRKAEEKD
CCCHHHHHHHHHHHH		67.2025953088
228AcetylationSMEAKKRKAEEKDSL
CHHHHHHHHHHHHHH		69.8625953088
232AcetylationKKRKAEEKDSLSRYD
HHHHHHHHHHHHCCC		44.0923749302
234PhosphorylationRKAEEKDSLSRYDSD
HHHHHHHHHHCCCCC		39.0330576142
236PhosphorylationAEEKDSLSRYDSDGD
HHHHHHHHCCCCCCC		32.5221815630
238PhosphorylationEKDSLSRYDSDGDKS
HHHHHHCCCCCCCCC		19.2022167270
240PhosphorylationDSLSRYDSDGDKSDD
HHHHCCCCCCCCCCC		34.2622167270
245PhosphorylationYDSDGDKSDDLVVDV
CCCCCCCCCCEEEEC		40.8922167270
253O-linked_GlycosylationDDLVVDVSNEDPATP
CCEEEECCCCCCCCC		30.0030059200
253PhosphorylationDDLVVDVSNEDPATP
CCEEEECCCCCCCCC		30.0029255136
259PhosphorylationVSNEDPATPRVSPAH
CCCCCCCCCCCCCCC		19.6019664994
263PhosphorylationDPATPRVSPAHSPPE
CCCCCCCCCCCCCCC		20.0429255136
267PhosphorylationPRVSPAHSPPENGLD
CCCCCCCCCCCCCHH		44.2329255136
275AcetylationPPENGLDKARSLKKD
CCCCCHHHHHHHCCC		51.2225953088
278PhosphorylationNGLDKARSLKKDAPT
CCHHHHHHHCCCCCC		49.7723927012
285PhosphorylationSLKKDAPTSPASVAS
HHCCCCCCCCHHHHC		49.4129255136
286PhosphorylationLKKDAPTSPASVASS
HCCCCCCCCHHHHCC		19.8719664994
289O-linked_GlycosylationDAPTSPASVASSSST
CCCCCCHHHHCCCCC		22.9230059200
289PhosphorylationDAPTSPASVASSSST
CCCCCCHHHHCCCCC		22.9222167270
292PhosphorylationTSPASVASSSSTPSS
CCCHHHHCCCCCCCC		28.7030266825
293PhosphorylationSPASVASSSSTPSSK
CCHHHHCCCCCCCCC		20.6922167270
294PhosphorylationPASVASSSSTPSSKT
CHHHHCCCCCCCCCC		35.4222167270
295PhosphorylationASVASSSSTPSSKTK
HHHHCCCCCCCCCCC		46.4123459991
296PhosphorylationSVASSSSTPSSKTKD
HHHCCCCCCCCCCCC		29.1922167270
298PhosphorylationASSSSTPSSKTKDLG
HCCCCCCCCCCCCCC		44.5522167270
299PhosphorylationSSSSTPSSKTKDLGH
CCCCCCCCCCCCCCC		45.6122167270
300AcetylationSSSTPSSKTKDLGHN
CCCCCCCCCCCCCCC		65.0225953088
301PhosphorylationSSTPSSKTKDLGHND
CCCCCCCCCCCCCCC		31.5725002506
302UbiquitinationSTPSSKTKDLGHNDK
CCCCCCCCCCCCCCC		55.48-
309AcetylationKDLGHNDKSSTPGLK
CCCCCCCCCCCCCCC		52.1823749302
309UbiquitinationKDLGHNDKSSTPGLK
CCCCCCCCCCCCCCC		52.18-
310PhosphorylationDLGHNDKSSTPGLKS
CCCCCCCCCCCCCCC		42.1620044836
311PhosphorylationLGHNDKSSTPGLKSN
CCCCCCCCCCCCCCC		44.3423927012
312PhosphorylationGHNDKSSTPGLKSNT
CCCCCCCCCCCCCCC		28.5923401153
316AcetylationKSSTPGLKSNTPTPR
CCCCCCCCCCCCCCC		47.8025953088
316UbiquitinationKSSTPGLKSNTPTPR
CCCCCCCCCCCCCCC		47.80-
317PhosphorylationSSTPGLKSNTPTPRN
CCCCCCCCCCCCCCC		51.4826055452
319PhosphorylationTPGLKSNTPTPRNDA
CCCCCCCCCCCCCCC		35.3123401153
321PhosphorylationGLKSNTPTPRNDAPT
CCCCCCCCCCCCCCC		32.6120044836
328PhosphorylationTPRNDAPTPGTSTTP
CCCCCCCCCCCCCCC		35.7519664994
328 (in isoform 2)Phosphorylation-35.7525849741
331PhosphorylationNDAPTPGTSTTPGLR
CCCCCCCCCCCCCHH		24.8923401153
332O-linked_GlycosylationDAPTPGTSTTPGLRS
CCCCCCCCCCCCHHC		35.8830059200
332PhosphorylationDAPTPGTSTTPGLRS
CCCCCCCCCCCCHHC		35.8829255136
332 (in isoform 2)Phosphorylation-35.8825849741
333O-linked_GlycosylationAPTPGTSTTPGLRSM
CCCCCCCCCCCHHCC		36.5330059200
333PhosphorylationAPTPGTSTTPGLRSM
CCCCCCCCCCCHHCC		36.5323401153
333 (in isoform 2)Phosphorylation-36.5325849741
334PhosphorylationPTPGTSTTPGLRSMP
CCCCCCCCCCHHCCC		18.3519664994
334 (in isoform 2)Phosphorylation-18.3525849741
336 (in isoform 7)Acetylation-31.4619608861
338MethylationTSTTPGLRSMPGKPP
CCCCCCHHCCCCCCC		36.50115386189
339PhosphorylationSTTPGLRSMPGKPPG
CCCCCHHCCCCCCCC		34.0826074081
343AcetylationGLRSMPGKPPGMDPI
CHHCCCCCCCCCCHH		42.0119608861
343UbiquitinationGLRSMPGKPPGMDPI
CHHCCCCCCCCCCHH		42.01-
343 (in isoform 2)Phosphorylation-42.0129083192
343 (in isoform 3)Acetylation-42.0119608861
343 (in isoform 5)Acetylation-42.0119608861
355PhosphorylationDPIGIMASALRTPIS
CHHHHHHHHHCCCEE		15.5129255136
359O-linked_GlycosylationIMASALRTPISITSS
HHHHHHCCCEEECCC		26.3130059200
362O-linked_GlycosylationSALRTPISITSSYAA
HHHCCCEEECCCCHH		22.4830059200
367PhosphorylationPISITSSYAAPFAMM
CEEECCCCHHCHHHC		13.4222210691
375PhosphorylationAAPFAMMSHHEMNGS
HHCHHHCCCCCCCCC		14.4928348404
382PhosphorylationSHHEMNGSLTSPGAY
CCCCCCCCCCCCCCC		24.3827251275
384PhosphorylationHEMNGSLTSPGAYAG
CCCCCCCCCCCCCCC		34.2727251275
385PhosphorylationEMNGSLTSPGAYAGL
CCCCCCCCCCCCCCC		26.9927251275
410 (in isoform 3)Phosphorylation-14.3525159151
413PhosphorylationAAAAYGRSPMVSFGA
HHHHHCCCCCEEECC		17.0010997877
413 (in isoform 6)Phosphorylation-17.0025159151
417PhosphorylationYGRSPMVSFGAVGFD
HCCCCCEEECCCCCC		16.2327732954
418 (in isoform 4)Phosphorylation-5.0525159151
430MethylationFDPHPPMRATGLPSS
CCCCCCCCCCCCCHH		34.47115918573
445AcetylationLASIPGGKPAYSFHV
HHCCCCCCCCEEEEE		32.1826051181
484PhosphorylationARQINTLSHGEVVCA
HHHCCCCCCCEEEEE		27.66-
493PhosphorylationGEVVCAVTISNPTRH
CEEEEEEEECCCCCE		10.5227251275
494 (in isoform 2)Ubiquitination-2.7721890473
495PhosphorylationVVCAVTISNPTRHVY
EEEEEEECCCCCEEE		27.6527251275
498PhosphorylationAVTISNPTRHVYTGG
EEEECCCCCEEEECC		37.3427251275
506AcetylationRHVYTGGKGCVKIWD
CEEEECCCCEEEEEE		50.9426051181
506UbiquitinationRHVYTGGKGCVKIWD
CEEEECCCCEEEEEE		50.9422053931
510UbiquitinationTGGKGCVKIWDISQP
ECCCCEEEEEECCCC		42.00-
515PhosphorylationCVKIWDISQPGSKSP
EEEEEECCCCCCCCC		28.0529978859
519PhosphorylationWDISQPGSKSPISQL
EECCCCCCCCCCHHH		36.3229978859
520UbiquitinationDISQPGSKSPISQLD
ECCCCCCCCCCHHHH		67.19-
521PhosphorylationISQPGSKSPISQLDC
CCCCCCCCCCHHHHH		29.2121815630
524PhosphorylationPGSKSPISQLDCLNR
CCCCCCCHHHHHCCC		28.2429978859
539UbiquitinationDNYIRSCKLLPDGRT
CCCHHHCEECCCCCE		55.06-
643MethylationGGLDNTVRSWDLREG
CCCCCCCEEECCCCC		29.96-
694PhosphorylationHHTKPDKYQLHLHES
ECCCCCCEEEEEECH		24.5626699800
701PhosphorylationYQLHLHESCVLSLKF
EEEEEECHHHHEEEE		9.9726699800
705PhosphorylationLHESCVLSLKFAYCG
EECHHHHEEEEEECC		14.7626699800
708 (in isoform 2)Ubiquitination-7.7021890473
712 (in isoform 3)Ubiquitination-19.9721890473
717UbiquitinationYCGKWFVSTGKDNLL
ECCCEEHHCCHHHHH		23.2021890473
717UbiquitinationYCGKWFVSTGKDNLL
ECCCEEHHCCHHHHH		23.2021890473
720AcetylationKWFVSTGKDNLLNAW
CEEHHCCHHHHHHHH		43.4630797611
720UbiquitinationKWFVSTGKDNLLNAW
CEEHHCCHHHHHHHH		43.4622053931
720 (in isoform 1)Ubiquitination-43.4621890473
720 (in isoform 4)Ubiquitination-43.4621890473
739UbiquitinationGASIFQSKESSSVLS
CCCHHCCCCCCCCEE		51.32-
741PhosphorylationSIFQSKESSSVLSCD
CHHCCCCCCCCEEEE		31.48-
763UbiquitinationIVTGSGDKKATVYEV
EEECCCCCEEEEEEE		48.08-
764SumoylationVTGSGDKKATVYEVI
EECCCCCEEEEEEEC		54.77-
764SumoylationVTGSGDKKATVYEVI
EECCCCCEEEEEEEC		54.77-
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
-KUbiquitinationE3 ubiquitin ligaseXIAPP98170
PMID:22304967
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TLE3_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of TLE3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FOXG1_MOUSEFoxg1physical
11238932
A4_HUMANAPPphysical
21832049
COPD_HUMANARCN1physical
22863883
COPB_HUMANCOPB1physical
22863883
COPG1_HUMANCOPG1physical
22863883
COPZ1_HUMANCOPZ1physical
22863883
KLC1_HUMANKLC1physical
22863883
SAHH_HUMANAHCYphysical
26344197
IPYR_HUMANPPA1physical
26344197
RPE_HUMANRPEphysical
26344197
STAM1_HUMANSTAMphysical
26344197
TLE3_HUMANTLE3physical
22304967
TLE4_HUMANTLE4physical
28514442
MYH2_HUMANMYH2physical
28514442
MYH1_HUMANMYH1physical
28514442
MYH4_HUMANMYH4physical
28514442
MYH3_HUMANMYH3physical
28514442
MYH7_HUMANMYH7physical
28514442
ACTS_HUMANACTA1physical
28514442
MYH8_HUMANMYH8physical
28514442
TITIN_HUMANTTNphysical
28514442
TLE1_HUMANTLE1physical
28514442
TLE2_HUMANTLE2physical
28514442
MYL1_HUMANMYL1physical
28514442
AT2A1_HUMANATP2A1physical
28514442
LDHC_HUMANLDHCphysical
28514442
CO1A1_HUMANCOL1A1physical
28514442
EF1A2_HUMANEEF1A2physical
28514442
PYGM_HUMANPYGMphysical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TLE3_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-343, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals 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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203; THR-259; SER-286;THR-328 AND THR-334, AND MASS SPECTROMETRY.
"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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203, AND MASSSPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203; THR-285; SER-286;SER-289; SER-299; THR-328 AND THR-334, AND MASS SPECTROMETRY.
"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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203; SER-207; SER-240;THR-259; SER-263; SER-267; SER-286; SER-311; THR-312; SER-317;THR-319; THR-321; THR-328; THR-334 AND SER-413, AND MASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-286, AND MASSSPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient 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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-317; THR-328 ANDTHR-334, AND MASS SPECTROMETRY.
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203; SER-205; SER-286AND SER-292, AND MASS SPECTROMETRY.
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-201; SER-203 ANDSER-207, AND MASS SPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203 AND THR-334, ANDMASS SPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203; SER-217; SER-240;THR-259; SER-263 AND SER-267, AND MASS SPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203; SER-240; SER-245;SER-263; SER-267 AND SER-286, AND MASS SPECTROMETRY.

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