TLE2_HUMAN - dbPTM
TLE2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TLE2_HUMAN
UniProt AC Q04725
Protein Name Transducin-like enhancer protein 2
Gene Name TLE2
Organism Homo sapiens (Human).
Sequence Length 743
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 MYPQGRHPTPLQSGQPFKFSILEICDRIKEEFQFLQAQYHSLKLECEKLASEKTEMQRHYVMYYEMSYGLNIEMHKQAEIVKRLSGICAQIIPFLTQEHQQQVLQAVERAKQVTVGELNSLIGQQLQPLSHHAPPVPLTPRPAGLVGGSATGLLALSGALAAQAQLAAAVKEDRAGVEAEGSRVERAPSRSASPSPPESLVEEERPSGPGGGGKQRADEKEPSGPYESDEDKSDYNLVVDEDQPSEPPSPATTPCGKVPICIPARRDLVDSPASLASSLGSPLPRAKELILNDLPASTPASKSCDSSPPQDASTPGPSSASHLCQLAAKPAPSTDSVALRSPLTLSSPFTTSFSLGSHSTLNGDLSVPSSYVSLHLSPQVSSSVVYGRSPVMAFESHPHLRGSSVSSSLPSIPGGKPAYSFHVSADGQMQPVPFPSDALVGAGIPRHARQLHTLAHGEVVCAVTISGSTQHVYTGGKGCVKVWDVGQPGAKTPVAQLDCLNRDNYIRSCKLLPDGRSLIVGGEASTLSIWDLAAPTPRIKAELTSSAPACYALAVSPDAKVCFSCCSDGNIVVWDLQNQTMVRQFQGHTDGASCIDISDYGTRLWTGGLDNTVRCWDLREGRQLQQHDFSSQIFSLGHCPNQDWLAVGMESSNVEILHVRKPEKYQLHLHESCVLSLKFASCGRWFVSTGKDNLLNAWRTPYGASIFQSKESSSVLSCDISRNNKYIVTGSGDKKATVYEVVY
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
12 (in isoform 2)Phosphorylation-46.8722210691
13 (in isoform 2)Phosphorylation-47.2622210691
29UbiquitinationLEICDRIKEEFQFLQ
HHHHHHHHHHHHHHH		52.68-
53UbiquitinationCEKLASEKTEMQRHY
HHHHHCCCHHHHHHH		47.49-
68PhosphorylationVMYYEMSYGLNIEMH
HHHHHHHHCCCCHHH		25.0758505
82UbiquitinationHKQAEIVKRLSGICA
HHHHHHHHHHHHHHH		53.97-
182PhosphorylationAGVEAEGSRVERAPS
CCCCCCCCCCCCCCC		25.34-
191PhosphorylationVERAPSRSASPSPPE
CCCCCCCCCCCCCCH		37.1224719451
193PhosphorylationRAPSRSASPSPPESL
CCCCCCCCCCCCHHH		27.4526657352
195PhosphorylationPSRSASPSPPESLVE
CCCCCCCCCCHHHCC		51.0626657352
199PhosphorylationASPSPPESLVEEERP
CCCCCCHHHCCCCCC		43.4124719451
207PhosphorylationLVEEERPSGPGGGGK
HCCCCCCCCCCCCCC		64.9323312004
223PhosphorylationRADEKEPSGPYESDE
CCCCCCCCCCCCCCC		54.1925278378
226PhosphorylationEKEPSGPYESDEDKS
CCCCCCCCCCCCCCC		31.4325278378
228PhosphorylationEPSGPYESDEDKSDY
CCCCCCCCCCCCCCC		40.2221815630
233PhosphorylationYESDEDKSDYNLVVD
CCCCCCCCCCCEECC		58.6125278378
235PhosphorylationSDEDKSDYNLVVDED
CCCCCCCCCEECCCC		19.9325278378
245PhosphorylationVVDEDQPSEPPSPAT
ECCCCCCCCCCCCCC		58.0425278378
249PhosphorylationDQPSEPPSPATTPCG
CCCCCCCCCCCCCCC		37.5725278378
252PhosphorylationSEPPSPATTPCGKVP
CCCCCCCCCCCCCCC		34.3525278378
253PhosphorylationEPPSPATTPCGKVPI
CCCCCCCCCCCCCCE		20.7725278378
271PhosphorylationARRDLVDSPASLASS
CCHHHCCCHHHHHHH		18.1926055452
274PhosphorylationDLVDSPASLASSLGS
HHCCCHHHHHHHHCC		28.0528464451
277PhosphorylationDSPASLASSLGSPLP
CCHHHHHHHHCCCCH		31.2423909892
278PhosphorylationSPASLASSLGSPLPR
CHHHHHHHHCCCCHH		31.0122210691
281PhosphorylationSLASSLGSPLPRAKE
HHHHHHCCCCHHHHH		28.6726055452
287UbiquitinationGSPLPRAKELILNDL
CCCCHHHHHHHHHCC		55.09-
297PhosphorylationILNDLPASTPASKSC
HHHCCCCCCCCHHCC		32.7428555341
298PhosphorylationLNDLPASTPASKSCD
HHCCCCCCCCHHCCC		25.6121815630
301O-linked_GlycosylationLPASTPASKSCDSSP
CCCCCCCHHCCCCCC		26.7228657654
301PhosphorylationLPASTPASKSCDSSP
CCCCCCCHHCCCCCC		26.7228348404
303PhosphorylationASTPASKSCDSSPPQ
CCCCCHHCCCCCCCC		22.2123312004
306PhosphorylationPASKSCDSSPPQDAS
CCHHCCCCCCCCCCC		49.4228348404
307PhosphorylationASKSCDSSPPQDAST
CHHCCCCCCCCCCCC		27.6128348404
313PhosphorylationSSPPQDASTPGPSSA
CCCCCCCCCCCCCCH		43.3423312004
314PhosphorylationSPPQDASTPGPSSAS
CCCCCCCCCCCCCHH		33.7023312004
318PhosphorylationDASTPGPSSASHLCQ
CCCCCCCCCHHHHHH		44.4423312004
319PhosphorylationASTPGPSSASHLCQL
CCCCCCCCHHHHHHH		36.6023312004
321PhosphorylationTPGPSSASHLCQLAA
CCCCCCHHHHHHHHC		20.9528464451
334O-linked_GlycosylationAAKPAPSTDSVALRS
HCCCCCCCCCCEECC		31.1028657654
389PhosphorylationSSVVYGRSPVMAFES
CCEECCCCCEEEECC		19.9228555341
477UbiquitinationQHVYTGGKGCVKVWD
EEEEECCCCEEEEEE		50.94-
481UbiquitinationTGGKGCVKVWDVGQP
ECCCCEEEEEECCCC		41.50-
491UbiquitinationDVGQPGAKTPVAQLD
ECCCCCCCCCCHHEE		60.31-
492PhosphorylationVGQPGAKTPVAQLDC
CCCCCCCCCCHHEEC		23.5929632367
505PhosphorylationDCLNRDNYIRSCKLL
ECCCCCCCHHHCEEC		11.2929632367
508PhosphorylationNRDNYIRSCKLLPDG
CCCCCHHHCEECCCC		13.1729632367
510UbiquitinationDNYIRSCKLLPDGRS
CCCHHHCEECCCCCE		55.06-
540UbiquitinationAAPTPRIKAELTSSA
CCCCCCCEEEECCCC		36.77-
569UbiquitinationCFSCCSDGNIVVWDL
EEEECCCCCEEEEEC		14.9621890473
665PhosphorylationHVRKPEKYQLHLHES
EECCCCCEEEEEECH		18.0426699800
672PhosphorylationYQLHLHESCVLSLKF
EEEEEECHHHHEEEE		9.9726699800
676PhosphorylationLHESCVLSLKFASCG
EECHHHHEEEECCCC		14.7626699800
681PhosphorylationVLSLKFASCGRWFVS
HHEEEECCCCCEEEE		21.9024719451
691AcetylationRWFVSTGKDNLLNAW
CEEEECCHHHHHHHH		43.4630797605
691UbiquitinationRWFVSTGKDNLLNAW
CEEEECCHHHHHHHH		43.4621890473
695 (in isoform 3)Phosphorylation-5.2926503514
703 (in isoform 3)Phosphorylation-17.6626503514
710UbiquitinationGASIFQSKESSSVLS
CCHHCCCCCCCCCEE		51.32-
712PhosphorylationSIFQSKESSSVLSCD
HHCCCCCCCCCEEEE		31.48-
725UbiquitinationCDISRNNKYIVTGSG
EECCCCCEEEEECCC		39.64-
726PhosphorylationDISRNNKYIVTGSGD
ECCCCCEEEEECCCC		11.62-
729PhosphorylationRNNKYIVTGSGDKKA
CCCEEEEECCCCCEE		18.97-
731PhosphorylationNKYIVTGSGDKKATV
CEEEEECCCCCEEEE		34.16-
734UbiquitinationIVTGSGDKKATVYEV
EEECCCCCEEEEEEE		48.08-
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
228SPhosphorylationKinaseCK2-Uniprot
249SPhosphorylationKinaseCDK1P06493
Uniprot
253TPhosphorylationKinaseCDK1P06493
Uniprot
-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 TLE2_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 TLE2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TLE2_HUMANTLE2physical
9874198
TLE1_HUMANTLE1physical
9874198
VENTX_HUMANVENTXphysical
20211142
TLX3_HUMANTLX3physical
20211142
BARH1_HUMANBARHL1physical
20211142
LEF1_HUMANLEF1physical
15768032
ORF50_HHV8PORF50physical
19939918
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 TLE2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-271 AND SER-281, ANDMASS SPECTROMETRY.

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