LEF1_HUMAN - dbPTM
LEF1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LEF1_HUMAN
UniProt AC Q9UJU2
Protein Name Lymphoid enhancer-binding factor 1
Gene Name LEF1
Organism Homo sapiens (Human).
Sequence Length 399
Subcellular Localization Nucleus . Found in nuclear bodies upon PIASG binding..
Protein Description Participates in the Wnt signaling pathway. Activates transcription of target genes in the presence of CTNNB1 and EP300. May play a role in hair cell differentiation and follicle morphogenesis. TLE1, TLE2, TLE3 and TLE4 repress transactivation mediated by LEF1 and CTNNB1. Regulates T-cell receptor alpha enhancer function. Binds DNA in a sequence-specific manner. PIAG antagonizes both Wnt-dependent and Wnt-independent activation by LEF1 (By similarity). Isoform 3 lacks the CTNNB1 interaction domain and may be an antagonist for Wnt signaling. Isoform 5 transcriptionally activates the fibronectin promoter, binds to and represses transcription from the E-cadherin promoter in a CTNNB1-independent manner, and is involved in reducing cellular aggregation and increasing cell migration of pancreatic cancer cells. Isoform 1 transcriptionally activates MYC and CCND1 expression and enhances proliferation of pancreatic tumor cells..
Protein Sequence MPQLSGGGGGGGGDPELCATDEMIPFKDEGDPQKEKIFAEISHPEEEGDLADIKSSLVNESEIIPASNGHEVARQAQTSQEPYHDKAREHPDDGKHPDGGLYNKGPSYSSYSGYIMMPNMNNDPYMSNGSLSPPIPRTSNKVPVVQPSHAVHPLTPLITYSDEHFSPGSHPSHIPSDVNSKQGMSRHPPAPDIPTFYPLSPGGVGQITPPLGWQGQPVYPITGGFRQPYPSSLSVDTSMSRFSHHMIPGPPGPHTTGIPHPAIVTPQVKQEHPHTDSDLMHVKPQHEQRKEQEPKRPHIKKPLNAFMLYMKEMRANVVAECTLKESAAINQILGRRWHALSREEQAKYYELARKERQLHMQLYPGWSARDNYGKKKKRKREKLQESASGTGPRMTAAYI
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
5Phosphorylation---MPQLSGGGGGGG
---CCCCCCCCCCCC		30.0924850871
15 (in isoform 7)Phosphorylation-39.4724719451
27SumoylationTDEMIPFKDEGDPQK
CCCEECCCCCCCHHH		49.90-
36UbiquitinationEGDPQKEKIFAEISH
CCCHHHHEEEEECCC		50.59-
42PhosphorylationEKIFAEISHPEEEGD
HEEEEECCCCHHCCC		25.2128464451
54UbiquitinationEGDLADIKSSLVNES
CCCHHHHHHHHCCHH		34.24-
55PhosphorylationGDLADIKSSLVNESE
CCHHHHHHHHCCHHH		29.2826714015
56PhosphorylationDLADIKSSLVNESEI
CHHHHHHHHCCHHHC		31.1926714015
61PhosphorylationKSSLVNESEIIPASN
HHHHCCHHHCCCCCC		28.9722817900
78PhosphorylationEVARQAQTSQEPYHD
HHHHHHCCCCCCCCH		35.0827811184
79PhosphorylationVARQAQTSQEPYHDK
HHHHHCCCCCCCCHH		22.0730576142
83PhosphorylationAQTSQEPYHDKAREH
HCCCCCCCCHHHHHC		23.1527811184
86AcetylationSQEPYHDKAREHPDD
CCCCCCHHHHHCCCC		35.7123749302
86UbiquitinationSQEPYHDKAREHPDD
CCCCCCHHHHHCCCC		35.71-
95AcetylationREHPDDGKHPDGGLY
HHCCCCCCCCCCCCC		59.9823749302
95UbiquitinationREHPDDGKHPDGGLY
HHCCCCCCCCCCCCC		59.9819608861
102PhosphorylationKHPDGGLYNKGPSYS
CCCCCCCCCCCCCCC		20.3627642862
114PhosphorylationSYSSYSGYIMMPNMN
CCCCCCCEEECCCCC		4.62-
125PhosphorylationPNMNNDPYMSNGSLS
CCCCCCCCCCCCCCC		18.9525841592
127PhosphorylationMNNDPYMSNGSLSPP
CCCCCCCCCCCCCCC		32.0025841592
130PhosphorylationDPYMSNGSLSPPIPR
CCCCCCCCCCCCCCC		29.8925841592
132PhosphorylationYMSNGSLSPPIPRTS
CCCCCCCCCCCCCCC		30.2628464451
138PhosphorylationLSPPIPRTSNKVPVV
CCCCCCCCCCCCCCC		31.1528122231
139PhosphorylationSPPIPRTSNKVPVVQ
CCCCCCCCCCCCCCC		35.6128122231
140 (in isoform 7)Phosphorylation-49.05-
148PhosphorylationKVPVVQPSHAVHPLT
CCCCCCCHHCCCCCC		13.6430576142
155PhosphorylationSHAVHPLTPLITYSD
HHCCCCCCCCEEECC		22.0930576142
159PhosphorylationHPLTPLITYSDEHFS
CCCCCCEEECCCCCC		25.3428796482
160PhosphorylationPLTPLITYSDEHFSP
CCCCCEEECCCCCCC		13.7130576142
161PhosphorylationLTPLITYSDEHFSPG
CCCCEEECCCCCCCC		28.0730576142
166PhosphorylationTYSDEHFSPGSHPSH
EECCCCCCCCCCCCC		30.2030576142
169PhosphorylationDEHFSPGSHPSHIPS
CCCCCCCCCCCCCCC		35.2926074081
172PhosphorylationFSPGSHPSHIPSDVN
CCCCCCCCCCCCCCC		28.7330576142
176PhosphorylationSHPSHIPSDVNSKQG
CCCCCCCCCCCCCCC		54.2928122231
180PhosphorylationHIPSDVNSKQGMSRH
CCCCCCCCCCCCCCC		26.6328122231
195PhosphorylationPPAPDIPTFYPLSPG
CCCCCCCCEEECCCC		35.8126552605
197PhosphorylationAPDIPTFYPLSPGGV
CCCCCCEEECCCCCC		13.0226552605
200PhosphorylationIPTFYPLSPGGVGQI
CCCEEECCCCCCCCC		19.5926552605
208 (in isoform 6)Phosphorylation-15.80-
208 (in isoform 5)Phosphorylation-15.80-
208PhosphorylationPGGVGQITPPLGWQG
CCCCCCCCCCCCCCC		15.8028464451
226MethylationYPITGGFRQPYPSSL
EECCCCCCCCCCCCC		39.58115389193
237PhosphorylationPSSLSVDTSMSRFSH
CCCCEECCCCHHCCC		24.95-
238PhosphorylationSSLSVDTSMSRFSHH
CCCEECCCCHHCCCC		15.42-
240PhosphorylationLSVDTSMSRFSHHMI
CEECCCCHHCCCCCC		29.91-
241MethylationSVDTSMSRFSHHMIP
EECCCCHHCCCCCCC		28.57115389201
265PhosphorylationIPHPAIVTPQVKQEH
CCCCCCCCCCCCCCC		11.24-
269SumoylationAIVTPQVKQEHPHTD
CCCCCCCCCCCCCCC		44.73-
283AcetylationDSDLMHVKPQHEQRK
CCCCCCCCHHHHHHH		25.0425953088
283UbiquitinationDSDLMHVKPQHEQRK
CCCCCCCCHHHHHHH		25.04-
295UbiquitinationQRKEQEPKRPHIKKP
HHHHHCCCCCCCCHH		77.22-
301UbiquitinationPKRPHIKKPLNAFML
CCCCCCCHHHHHHHH		54.88-
311UbiquitinationNAFMLYMKEMRANVV
HHHHHHHHHHHHCEE		34.50-
324UbiquitinationVVAECTLKESAAINQ
EEEEEECCHHHHHHH		31.31-
347UbiquitinationLSREEQAKYYELARK
CCHHHHHHHHHHHHH		48.32-
348PhosphorylationSREEQAKYYELARKE
CHHHHHHHHHHHHHH		12.75-
349PhosphorylationREEQAKYYELARKER
HHHHHHHHHHHHHHH		12.08-
363AcetylationRQLHMQLYPGWSARD
HHHHHHHCCCCHHHC		5.25-
363PhosphorylationRQLHMQLYPGWSARD
HHHHHHHCCCCHHHC		5.25-
366PhosphorylationHMQLYPGWSARDNYG
HHHHCCCCHHHCCCC		5.59-
366 (in isoform 6)Phosphorylation-5.59-
367PhosphorylationMQLYPGWSARDNYGK
HHHCCCCHHHCCCCH		21.24-
373 (in isoform 6)Ubiquitination-41.37-
382UbiquitinationKKKRKREKLQESASG
HHHHHHHHHHHHHCC		60.55-
382AcetylationKKKRKREKLQESASG
HHHHHHHHHHHHHCC		60.5525953088
386PhosphorylationKREKLQESASGTGPR
HHHHHHHHHCCCCCC		18.12-
390PhosphorylationLQESASGTGPRMTAA
HHHHHCCCCCCCCEE		41.33-
393MethylationSASGTGPRMTAAYI-
HHCCCCCCCCEECC-		36.11115389209
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
42SPhosphorylationKinaseCSNK2A1P68400
GPS
61SPhosphorylationKinaseCSNK2A1P68400
GPS
132SPhosphorylationKinaseNLKQ9UBE8
PSP
155TPhosphorylationKinaseNLKQ9UBE8
Uniprot
166SPhosphorylationKinaseNLKQ9UBE8
Uniprot
200SPhosphorylationKinaseNLKQ9UBE8
PSP
265TPhosphorylationKinaseNLKQ9UBE8
PSP
-KUbiquitinationE3 ubiquitin ligaseRNF138Q8WVD3
PMID:16714285
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
155TPhosphorylation

12556497
166SPhosphorylation

12556497
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 LEF1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UBF1_HUMANUBTFphysical
12748295
EP300_HUMANEP300physical
12446687
CTNB1_HUMANCTNNB1physical
8757136
IMA1_MOUSEKpna2physical
8631802
IMA5_MOUSEKpna1physical
8631802
SMAD2_HUMANSMAD2physical
10890911
SMAD3_HUMANSMAD3physical
10890911
SMAD4_HUMANSMAD4physical
10890911
CTNB1_HUMANCTNNB1physical
10890911
CTNB1_HUMANCTNNB1physical
16510874
DAZP2_HUMANDAZAP2physical
19304756
ZBTB3_HUMANZBTB3physical
20211142
CTNB1_HUMANCTNNB1physical
16510875
HDAC1_HUMANHDAC1physical
10958684
E2F1_HUMANE2F1physical
17980157
MYB_HUMANMYBphysical
21795403
KMT5A_HUMANSETD8physical
21282610
CTNB1_HUMANCTNNB1physical
18296023
CTNB1_HUMANCTNNB1physical
9419974
HINT1_HUMANHINT1physical
16014379
FHIT_HUMANFHITphysical
18077326
CTNB1_HUMANCTNNB1physical
15525529
NRARP_XENLAnrarpphysical
16228014
CDX1_HUMANCDX1physical
15143193
PITX2_HUMANPITX2physical
15728254
STA5A_HUMANSTAT5Aphysical
24394665
NARF_HUMANNARFphysical
24394665
RN138_HUMANRNF138physical
16714285
NLK_HUMANNLKphysical
24394665
ANM6_HUMANPRMT6physical
26186194
CTNB1_HUMANCTNNB1physical
21743491
ANM6_HUMANPRMT6physical
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 LEF1_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-95, 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-132, AND MASSSPECTROMETRY.

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