TLE1_HUMAN - dbPTM
TLE1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TLE1_HUMAN
UniProt AC Q04724
Protein Name Transducin-like enhancer protein 1
Gene Name TLE1
Organism Homo sapiens (Human).
Sequence Length 770
Subcellular Localization Nucleus . Nuclear and chromatin-associated, depending on isoforms and phosphorylation status. Hyperphosphorylation decreases the affinity for nuclear components.
Protein Description 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..
Protein Sequence MFPQSRHPTPHQAAGQPFKFTIPESLDRIKEEFQFLQAQYHSLKLECEKLASEKTEMQRHYVMYYEMSYGLNIEMHKQTEIAKRLNTICAQVIPFLSQEHQQQVAQAVERAKQVTMAELNAIIGQQQLQAQHLSHGHGPPVPLTPHPSGLQPPGIPPLGGSAGLLALSSALSGQSHLAIKDDKKHHDAEHHRDREPGTSNSLLVPDSLRGTDKRRNGPEFSNDIKKRKVDDKDSSHYDSDGDKSDDNLVVDVSNEDPSSPRASPAHSPRENGIDKNRLLKKDASSSPASTASSASSTSLKSKEMSLHEKASTPVLKSSTPTPRSDMPTPGTSATPGLRPGLGKPPAIDPLVNQAAAGLRTPLAVPGPYPAPFGMVPHAGMNGELTSPGAAYASLHNMSPQMSAAAAAAAVVAYGRSPMVGFDPPPHMRVPTIPPNLAGIPGGKPAYSFHVTADGQMQPVPFPPDALIGPGIPRHARQINTLNHGEVVCAVTISNPTRHVYTGGKGCVKVWDISHPGNKSPVSQLDCLNRDNYIRSCKLLPDGCTLIVGGEASTLSIWDLAAPTPRIKAELTSSAPACYALAISPDSKVCFSCCSDGNIAVWDLHNQTLVRQFQGHTDGASCIDISNDGTKLWTGGLDNTVRSWDLREGRQLQQHDFTSQIFSLGYCPTGEWLAVGMESSNVEVLHVNKPDKYQLHLHESCVLSLKFAYCGKWFVSTGKDNLLNAWRTPYGASIFQSKESSSVLSCDISVDDKYIVTGSGDKKATVYEVIY
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--MFPQSRHPTPHQA
--CCCCCCCCCCCCC		34.26115918557
30UbiquitinationPESLDRIKEEFQFLQ
CHHHHHHHHHHHHHH		52.68-
54UbiquitinationCEKLASEKTEMQRHY
HHHHHCCCHHHHHHH		47.49-
69PhosphorylationVMYYEMSYGLNIEMH
HHHHHHHHCCCCEEH		25.07-
201PhosphorylationREPGTSNSLLVPDSL
CCCCCCCCCCCCHHH		23.8928555341
211PhosphorylationVPDSLRGTDKRRNGP
CCHHHCCCCCCCCCC		31.7328555341
234PhosphorylationRKVDDKDSSHYDSDG
CCCCCCCCCCCCCCC		25.4223663014
235PhosphorylationKVDDKDSSHYDSDGD
CCCCCCCCCCCCCCC		35.8823663014
237PhosphorylationDDKDSSHYDSDGDKS
CCCCCCCCCCCCCCC		21.0623663014
239PhosphorylationKDSSHYDSDGDKSDD
CCCCCCCCCCCCCCC		36.0127362937
244PhosphorylationYDSDGDKSDDNLVVD
CCCCCCCCCCCEEEE		55.7420164059
245PhosphorylationDSDGDKSDDNLVVDV
CCCCCCCCCCEEEEC		55.33-
249PhosphorylationDKSDDNLVVDVSNED
CCCCCCEEEECCCCC		4.3015367661
253PhosphorylationDNLVVDVSNEDPSSP
CCEEEECCCCCCCCC		30.0021406692
254PhosphorylationNLVVDVSNEDPSSPR
CEEEECCCCCCCCCC		58.50-
258PhosphorylationDVSNEDPSSPRASPA
ECCCCCCCCCCCCCC		66.3525849741
259PhosphorylationVSNEDPSSPRASPAH
CCCCCCCCCCCCCCC		24.6423663014
263PhosphorylationDPSSPRASPAHSPRE
CCCCCCCCCCCCCCC		24.7327362937
267PhosphorylationPRASPAHSPRENGID
CCCCCCCCCCCCCCC		27.9727362937
269PhosphorylationASPAHSPRENGIDKN
CCCCCCCCCCCCCHH		53.69-
273PhosphorylationHSPRENGIDKNRLLK
CCCCCCCCCHHHCCC		11.69-
277PhosphorylationENGIDKNRLLKKDAS
CCCCCHHHCCCCCCC		47.33-
281AcetylationDKNRLLKKDASSSPA
CHHHCCCCCCCCCCC		59.5020167786
284PhosphorylationRLLKKDASSSPASTA
HCCCCCCCCCCCCCC		41.2922167270
285PhosphorylationLLKKDASSSPASTAS
CCCCCCCCCCCCCCC		41.9023401153
286PhosphorylationLKKDASSSPASTASS
CCCCCCCCCCCCCCC		23.2219664994
289O-linked_GlycosylationDASSSPASTASSASS
CCCCCCCCCCCCCCC		28.0830620550
289PhosphorylationDASSSPASTASSASS
CCCCCCCCCCCCCCC		28.0830278072
290PhosphorylationASSSPASTASSASST
CCCCCCCCCCCCCCC		32.4430278072
290O-linked_GlycosylationASSSPASTASSASST
CCCCCCCCCCCCCCC		32.4430620550
291AcetylationSSSPASTASSASSTS
CCCCCCCCCCCCCCC		10.05-
292PhosphorylationSSPASTASSASSTSL
CCCCCCCCCCCCCCC		26.9023403867
293O-linked_GlycosylationSPASTASSASSTSLK
CCCCCCCCCCCCCCH		29.7030620550
293PhosphorylationSPASTASSASSTSLK
CCCCCCCCCCCCCCH		29.7023403867
295PhosphorylationASTASSASSTSLKSK
CCCCCCCCCCCCHHC		35.7819664995
296PhosphorylationSTASSASSTSLKSKE
CCCCCCCCCCCHHCC		23.0219664995
297PhosphorylationTASSASSTSLKSKEM
CCCCCCCCCCHHCCC		35.2723403867
298PhosphorylationASSASSTSLKSKEMS
CCCCCCCCCHHCCCC		35.4323403867
299PhosphorylationSSASSTSLKSKEMSL
CCCCCCCCHHCCCCH		8.01-
300PhosphorylationSASSTSLKSKEMSLH
CCCCCCCHHCCCCHH		60.28-
305PhosphorylationSLKSKEMSLHEKAST
CCHHCCCCHHHHCCC		27.8924719451
311PhosphorylationMSLHEKASTPVLKSS
CCHHHHCCCCCCCCC		44.2926657352
312PhosphorylationSLHEKASTPVLKSST
CHHHHCCCCCCCCCC		23.4430266825
315PhosphorylationEKASTPVLKSSTPTP
HHCCCCCCCCCCCCC		4.72-
317PhosphorylationASTPVLKSSTPTPRS
CCCCCCCCCCCCCCC		34.9726074081
318PhosphorylationSTPVLKSSTPTPRSD
CCCCCCCCCCCCCCC		36.5024719451
319PhosphorylationTPVLKSSTPTPRSDM
CCCCCCCCCCCCCCC		37.9723403867
321PhosphorylationVLKSSTPTPRSDMPT
CCCCCCCCCCCCCCC		31.2723532336
322PhosphorylationLKSSTPTPRSDMPTP
CCCCCCCCCCCCCCC		34.67-
328PhosphorylationTPRSDMPTPGTSATP
CCCCCCCCCCCCCCC		27.9324719451
331PhosphorylationSDMPTPGTSATPGLR
CCCCCCCCCCCCCCC		19.1828348404
332PhosphorylationDMPTPGTSATPGLRP
CCCCCCCCCCCCCCC		35.7428348404
334PhosphorylationPTPGTSATPGLRPGL
CCCCCCCCCCCCCCC		20.0428348404
338MethylationTSATPGLRPGLGKPP
CCCCCCCCCCCCCCC		29.20115918549
343MethylationGLRPGLGKPPAIDPL
CCCCCCCCCCCCHHH		53.52115918545
348MethylationLGKPPAIDPLVNQAA
CCCCCCCHHHHHHHH		32.36-
353MethylationAIDPLVNQAAAGLRT
CCHHHHHHHHCCCCC		25.54-
359MethylationNQAAAGLRTPLAVPG
HHHHCCCCCCCCCCC		33.12115918553
369MethylationLAVPGPYPAPFGMVP
CCCCCCCCCCCCCCC		36.27-
416PhosphorylationAVVAYGRSPMVGFDP
HHHHHCCCCCCCCCC		17.0028674419
5042-HydroxyisobutyrylationRHVYTGGKGCVKVWD
CEEEECCCCEEEEEE		50.94-
514UbiquitinationVKVWDISHPGNKSPV
EEEEECCCCCCCCCC		34.32-
519PhosphorylationISHPGNKSPVSQLDC
CCCCCCCCCCHHHHH		34.2428348404
616PhosphorylationVRQFQGHTDGASCID
HHHHCCCCCCCEEEE		42.8424114839
620PhosphorylationQGHTDGASCIDISND
CCCCCCCEEEEECCC		19.6924114839
625PhosphorylationGASCIDISNDGTKLW
CCEEEEECCCCCEEE		25.7224114839
629PhosphorylationIDISNDGTKLWTGGL
EEECCCCCEEECCCC		26.3124114839
641MethylationGGLDNTVRSWDLREG
CCCCCCCEEECCCCC		29.96-
651MethylationDLREGRQLQQHDFTS
CCCCCCCCCCCCCCH		5.22-
692PhosphorylationHVNKPDKYQLHLHES
ECCCCCCEEEEEECH		24.5626699800
699PhosphorylationYQLHLHESCVLSLKF
EEEEEECHHHHEEEE		9.9726699800
703PhosphorylationLHESCVLSLKFAYCG
EECHHHHEEEEECCC		14.7626699800
718AcetylationKWFVSTGKDNLLNAW
CEEHHCCHHHHHHHH		43.4623954790
718UbiquitinationKWFVSTGKDNLLNAW
CEEHHCCHHHHHHHH		43.462189047
728AcetylationLLNAWRTPYGASIFQ
HHHHHCCCCCCCHHC		19.58-
728UbiquitinationLLNAWRTPYGASIFQ
HHHHHCCCCCCCHHC		19.58-
739PhosphorylationSIFQSKESSSVLSCD
CHHCCCCCCCCEEEE		31.48-
762SumoylationVTGSGDKKATVYEVI
EECCCCCEEEEEEEC		54.77-
771UbiquitinationTVYEVIY--------
EEEEECC--------		-
772SumoylationVYEVIY---------
EEEECC---------		-
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
239SPhosphorylationKinaseCSNK2A1P68400
GPS
239SPhosphorylationKinaseHIPK2Q9H2X6
PSP
253SPhosphorylationKinaseCSNK2A1P68400
GPS
259SPhosphorylationKinaseCDK1P06493
Uniprot
263SPhosphorylationKinaseCDK1P06493
Uniprot
267SPhosphorylationKinaseCDK1P06493
Uniprot
286SPhosphorylationKinaseHIPK2Q9H2X6
PSP
289SPhosphorylationKinaseHIPK2Q9H2X6
PSP
-KUbiquitinationE3 ubiquitin ligaseXIAPP98170
PMID:22199232
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TLE1_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 TLE1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HES6_HUMANHES6physical
11551980
FOXA2_HUMANFOXA2physical
10748198
FOXG1_MOUSEFoxg1physical
11238932
UTY_HUMANUTYphysical
9854018
HES1_MOUSEHes1physical
8687460
TF65_HUMANRELAphysical
10660609
HMGB1_HUMANHMGB1physical
11748221
RUNX1_HUMANRUNX1physical
9751710
RUNX3_HUMANRUNX3physical
9751710
CTNB1_HUMANCTNNB1physical
9751710
LEF1_HUMANLEF1physical
9751710
TLE1_HUMANTLE1physical
9874198
TLE2_HUMANTLE2physical
9874198
RUNX2_HUMANRUNX2physical
20160071
HDAC1_HUMANHDAC1physical
19101520
VENTX_HUMANVENTXphysical
20211142
TLX3_HUMANTLX3physical
20211142
BARH1_HUMANBARHL1physical
20211142
K0408_HUMANKIAA0408physical
21900206
TLE1_HUMANTLE1physical
22354967
FOXG1_HUMANFOXG1physical
22354967
AES_HUMANAESphysical
22354967
T7L1A_DANREtcf7l1aphysical
21666599
HHEX_HUMANHHEXphysical
15187083
LEF1_HUMANLEF1physical
15768032
FOXG1_HUMANFOXG1physical
18611861
SSXT_HUMANSS18physical
22439931
ATF2_HUMANATF2physical
22439931
SSX2_HUMANSSX2physical
22439931
HDAC1_HUMANHDAC1physical
22439931
EZH2_HUMANEZH2physical
22439931
TLE1_HUMANTLE1physical
24596249
TFE2_HUMANTCF3physical
24596249
ITF2_HUMANTCF4physical
24596249
HES1_HUMANHES1physical
19321451
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 TLE1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-286, AND MASSSPECTROMETRY.

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