TF7L2_HUMAN - dbPTM
TF7L2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TF7L2_HUMAN
UniProt AC Q9NQB0
Protein Name Transcription factor 7-like 2
Gene Name TCF7L2
Organism Homo sapiens (Human).
Sequence Length 619
Subcellular Localization Nucleus, PML body . Diffuse pattern. Colocalizes with SUMO1 and PIAS4 in a subset of PML (promyelocytic leukemia) nuclear bodies.
Protein Description Participates in the Wnt signaling pathway and modulates MYC expression by binding to its promoter in a sequence-specific manner. Acts as repressor in the absence of CTNNB1, and as activator in its presence. Activates transcription from promoters with several copies of the Tcf motif 5'-CCTTTGATC-3' in the presence of CTNNB1. TLE1, TLE2, TLE3 and TLE4 repress transactivation mediated by TCF7L2/TCF4 and CTNNB1. Expression of dominant-negative mutants results in cell-cycle arrest in G1. Necessary for the maintenance of the epithelial stem-cell compartment of the small intestine..
Protein Sequence MPQLNGGGGDDLGANDELISFKDEGEQEEKSSENSSAERDLADVKSSLVNESETNQNSSSDSEAERRPPPRSESFRDKSRESLEEAAKRQDGGLFKGPPYPGYPFIMIPDLTSPYLPNGSLSPTARTLHFQSGSTHYSAYKTIEHQIAVQYLQMKWPLLDVQAGSLQSRQALKDARSPSPAHIVSNKVPVVQHPHHVHPLTPLITYSNEHFTPGNPPPHLPADVDPKTGIPRPPHPPDISPYYPLSPGTVGQIPHPLGWLVPQQGQPVYPITTGGFRHPYPTALTVNASMSRFPPHMVPPHHTLHTTGIPHPAIVTPTVKQESSQSDVGSLHSSKHQDSKKEEEKKKPHIKKPLNAFMLYMKEMRAKVVAECTLKESAAINQILGRRWHALSREEQAKYYELARKERQLHMQLYPGWSARDNYGKKKKRKRDKQPGETNEHSECFLNPCLSLPPITDLSAPKKCRARFGLDQQNNWCGPCRRKKKCVRYIQGEGSCLSPPSSDGSLLDSPPPSPNLLGSPPRDAKSQTEQTQPLSLSLKPDPLAHLSMMPPPPALLLAEATHKASALCPNGALDLPPAALQPAAPSSSIAQPSTSSLHSHSSLAGTQPQPLSLVTKSLE
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
20PhosphorylationGANDELISFKDEGEQ
CCCCCEEECCCCCHH		38.5824719451
22SumoylationNDELISFKDEGEQEE
CCCEEECCCCCHHHH		48.3428112733
31PhosphorylationEGEQEEKSSENSSAE
CCHHHHHHCCCCHHH		46.2825159151
32PhosphorylationGEQEEKSSENSSAER
CHHHHHHCCCCHHHH		52.4428985074
35PhosphorylationEEKSSENSSAERDLA
HHHHCCCCHHHHHHH		27.2025159151
36PhosphorylationEKSSENSSAERDLAD
HHHCCCCHHHHHHHH		45.8123312004
45 (in isoform 10)Ubiquitination-34.57-
46PhosphorylationRDLADVKSSLVNESE
HHHHHHHHHHHCCCC		28.8421406692
47PhosphorylationDLADVKSSLVNESET
HHHHHHHHHHCCCCC		30.5321406692
51UbiquitinationVKSSLVNESETNQNS
HHHHHHCCCCCCCCC		42.3321906983
52PhosphorylationKSSLVNESETNQNSS
HHHHHCCCCCCCCCC		44.5130576142
54PhosphorylationSLVNESETNQNSSSD
HHHCCCCCCCCCCCC		51.9230576142
58PhosphorylationESETNQNSSSDSEAE
CCCCCCCCCCCCHHH		22.8123927012
59PhosphorylationSETNQNSSSDSEAER
CCCCCCCCCCCHHHH		45.7923927012
60PhosphorylationETNQNSSSDSEAERR
CCCCCCCCCCHHHHC		45.0023927012
62PhosphorylationNQNSSSDSEAERRPP
CCCCCCCCHHHHCCC		40.4330576142
74PhosphorylationRPPPRSESFRDKSRE
CCCCCCHHHHHHHHH		27.1627251275
79PhosphorylationSESFRDKSRESLEEA
CHHHHHHHHHHHHHH		45.6425159151
82PhosphorylationFRDKSRESLEEAAKR
HHHHHHHHHHHHHHH		39.7128985074
88UbiquitinationESLEEAAKRQDGGLF
HHHHHHHHHCCCCCC		58.6021906983
88 (in isoform 10)Ubiquitination-58.6021906983
88 (in isoform 1)Ubiquitination-58.6021906983
88 (in isoform 2)Ubiquitination-58.6021906983
88 (in isoform 3)Ubiquitination-58.6021906983
88 (in isoform 4)Ubiquitination-58.6021906983
88 (in isoform 5)Ubiquitination-58.6021906983
88 (in isoform 6)Ubiquitination-58.6021906983
88 (in isoform 7)Ubiquitination-58.6021906983
88 (in isoform 8)Ubiquitination-58.6021906983
88 (in isoform 9)Ubiquitination-58.6021906983
112PhosphorylationFIMIPDLTSPYLPNG
EEECCCCCCCCCCCC		34.7325627689
113PhosphorylationIMIPDLTSPYLPNGS
EECCCCCCCCCCCCC		20.8825627689
113 (in isoform 10)Phosphorylation-20.8825159151
113 (in isoform 11)Phosphorylation-20.8825159151
113 (in isoform 12)Phosphorylation-20.8825159151
113 (in isoform 13)Phosphorylation-20.8825159151
113 (in isoform 14)Phosphorylation-20.8825159151
113 (in isoform 15)Phosphorylation-20.8825159151
113 (in isoform 16)Phosphorylation-20.8825159151
113 (in isoform 8)Phosphorylation-20.8825159151
120PhosphorylationSPYLPNGSLSPTART
CCCCCCCCCCCCCEE		32.1128450419
122PhosphorylationYLPNGSLSPTARTLH
CCCCCCCCCCCEEEE		23.1529496963
122 (in isoform 10)Phosphorylation-23.1525627689
122 (in isoform 11)Phosphorylation-23.1525627689
122 (in isoform 12)Phosphorylation-23.1525627689
122 (in isoform 13)Phosphorylation-23.1525627689
122 (in isoform 14)Phosphorylation-23.1525627689
122 (in isoform 15)Phosphorylation-23.1525627689
122 (in isoform 16)Phosphorylation-23.1525627689
122 (in isoform 8)Phosphorylation-23.1525627689
124PhosphorylationPNGSLSPTARTLHFQ
CCCCCCCCCEEEEEC		25.9528450419
126MethylationGSLSPTARTLHFQSG
CCCCCCCEEEEECCC		40.0554559899
132 (in isoform 10)Ubiquitination-33.4921906983
132 (in isoform 8)Ubiquitination-33.4921906983
151PhosphorylationEHQIAVQYLQMKWPL
HHHHHHHHHHHHCCC		7.72-
154 (in isoform 11)Phosphorylation-4.5328348404
156 (in isoform 11)Phosphorylation-5.3928348404
165PhosphorylationLLDVQAGSLQSRQAL
CHHHCCCCHHHHHHH		26.6728122231
168PhosphorylationVQAGSLQSRQALKDA
HCCCCHHHHHHHHHC		31.4928122231
173AcetylationLQSRQALKDARSPSP
HHHHHHHHHCCCCCH		52.9762154805
177PhosphorylationQALKDARSPSPAHIV
HHHHHCCCCCHHHHH		31.3022167270
179PhosphorylationLKDARSPSPAHIVSN
HHHCCCCCHHHHHCC		35.6525159151
185PhosphorylationPSPAHIVSNKVPVVQ
CCHHHHHCCCCCCCC		30.2627251275
195 (in isoform 11)Phosphorylation-33.2130622161
197 (in isoform 11)Phosphorylation-4.5230622161
201PhosphorylationPHHVHPLTPLITYSN
CCCCCCCCCEEEECC		22.0912556497
212PhosphorylationTYSNEHFTPGNPPPH
EECCCCCCCCCCCCC		31.9910919662
243PhosphorylationPPDISPYYPLSPGTV
CCCCCCCCCCCCCCC		10.9026074081
246PhosphorylationISPYYPLSPGTVGQI
CCCCCCCCCCCCCCC		19.4426074081
249PhosphorylationYYPLSPGTVGQIPHP
CCCCCCCCCCCCCCC		25.5026074081
308 (in isoform 10)Ubiquitination-32.3621906983
312 (in isoform 8)Ubiquitination-20.5121906983
320SumoylationAIVTPTVKQESSQSD
CEECCCCCCCCCCCC		51.32-
320SumoylationAIVTPTVKQESSQSD
CEECCCCCCCCCCCC		51.3212727872
323PhosphorylationTPTVKQESSQSDVGS
CCCCCCCCCCCCHHH		31.0521406692
324PhosphorylationPTVKQESSQSDVGSL
CCCCCCCCCCCHHHC		32.7121406692
326PhosphorylationVKQESSQSDVGSLHS
CCCCCCCCCHHHCCC		35.8930206219
330PhosphorylationSSQSDVGSLHSSKHQ
CCCCCHHHCCCCCCC		23.8230206219
333PhosphorylationSDVGSLHSSKHQDSK
CCHHHCCCCCCCCCH		46.5021406692
334PhosphorylationDVGSLHSSKHQDSKK
CHHHCCCCCCCCCHH		24.3321406692
335UbiquitinationVGSLHSSKHQDSKKE
HHHCCCCCCCCCHHH		48.582190698
335 (in isoform 1)Ubiquitination-48.5821906983
335 (in isoform 2)Ubiquitination-48.5821906983
335 (in isoform 3)Ubiquitination-48.5821906983
335 (in isoform 4)Ubiquitination-48.5821906983
335 (in isoform 5)Ubiquitination-48.5821906983
335 (in isoform 6)Ubiquitination-48.5821906983
335 (in isoform 7)Ubiquitination-48.5821906983
335 (in isoform 9)Ubiquitination-48.5821906983
352UbiquitinationKKKPHIKKPLNAFML
HHCCCCCHHHHHHHH		54.88-
362AcetylationNAFMLYMKEMRAKVV
HHHHHHHHHHHHHHH		34.50-
367AcetylationYMKEMRAKVVAECTL
HHHHHHHHHHHCCCC		27.20-
398UbiquitinationLSREEQAKYYELARK
CCHHHHHHHHHHHHH		48.32-
399PhosphorylationSREEQAKYYELARKE
CHHHHHHHHHHHHHH		12.75-
400PhosphorylationREEQAKYYELARKER
HHHHHHHHHHHHHHH		12.08-
414PhosphorylationRQLHMQLYPGWSARD
HHHHHHHCCCCHHHC		5.25-
418PhosphorylationMQLYPGWSARDNYGK
HHHCCCCHHHCCCCC		21.24-
420 (in isoform 13)Phosphorylation-27.4821815630
443 (in isoform 7)Phosphorylation-31.0621815630
468 (in isoform 4)Phosphorylation-12.7522468782
485 (in isoform 2)Phosphorylation-40.7822468782
489PhosphorylationRKKKCVRYIQGEGSC
CCCCCEEEECCCCCC		4.17-
526PhosphorylationSPPRDAKSQTEQTQP
CCCCCCCCCCCCCCC		44.0224173317
528PhosphorylationPRDAKSQTEQTQPLS
CCCCCCCCCCCCCCC		36.8324173317
535PhosphorylationTEQTQPLSLSLKPDP
CCCCCCCCCCCCCCC		23.6924719451
537PhosphorylationQTQPLSLSLKPDPLA
CCCCCCCCCCCCCCC		30.8524719451
539SumoylationQPLSLSLKPDPLAHL
CCCCCCCCCCCCCCC		43.9628112733
563AcetylationLLAEATHKASALCPN
HHHHHCHHHHHCCCC		39.427465867
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
58SPhosphorylationKinaseCK2-FAMILY-GPS
58SPhosphorylationKinaseCK2_GROUP-PhosphoELM
59SPhosphorylationKinaseCK2-FAMILY-GPS
59SPhosphorylationKinaseCK2_GROUP-PhosphoELM
60SPhosphorylationKinaseCK2-FAMILY-GPS
60SPhosphorylationKinaseCK2_GROUP-PhosphoELM
177SPhosphorylationKinaseTNIKQ9UKE5
PSP
201TPhosphorylationKinaseNLKQ9UBE8
Uniprot
212TPhosphorylationKinaseNLKQ9UBE8
Uniprot
-KUbiquitinationE3 ubiquitin ligaseRNF138Q8WVD3
PMID:16714285
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
201TPhosphorylation

12556497
212TPhosphorylation

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 TF7L2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PLAK_HUMANJUPphysical
11711551
PSN1_HUMANPSEN1physical
11504726
CTNB1_HUMANCTNNB1physical
19304756
DAZP2_HUMANDAZAP2physical
19304756
XRCC6_HUMANXRCC6physical
17283121
XRCC5_HUMANXRCC5physical
17283121
PARP1_HUMANPARP1physical
17283121
CTNB1_HUMANCTNNB1physical
17283121
MD2L2_HUMANMAD2L2physical
19443654
CTNB1_HUMANCTNNB1physical
19443654
KAISO_HUMANZBTB33physical
21670201
DAXX_HUMANDAXXphysical
16569639
CTNB1_HUMANCTNNB1physical
16569639
UBC9_HUMANUBE2Iphysical
21988832
CTNB1_HUMANCTNNB1physical
22155184
DAXX_HUMANDAXXphysical
19563778
HBP1_HUMANHBP1physical
11500377
CTNB1_HUMANCTNNB1physical
16630820
CDC73_HUMANCDC73physical
16630820
RN138_HUMANRNF138physical
16714285
HIC1_HUMANHIC1physical
16724116
CTNB1_HUMANCTNNB1physical
17050667
EP300_HUMANEP300physical
17050667
CTNB1_HUMANCTNNB1physical
17914096
KMT5A_HUMANSETD8physical
21282610
LEF1_HUMANLEF1physical
24748645
RNF43_HUMANRNF43physical
26350900
CTNB1_HUMANCTNNB1physical
26350900
CTBP1_HUMANCTBP1physical
26350900
TLE3_HUMANTLE3physical
22304967
XIAP_HUMANXIAPphysical
22304967
CTNB1_HUMANCTNNB1physical
22304967
ANM6_HUMANPRMT6physical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
Note=Constitutive activation and subsequent transactivation of target genes may lead to the maintenance of stem-cell characteristics (cycling and longevity) in cells that should normally undergo terminal differentiation and constitute the primary transforming event in colorectal cancer (CRC).
125853
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TF7L2_HUMAN

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Related Literatures of Post-Translational Modification
Sumoylation
ReferencePubMed
"Sumoylation is involved in beta-catenin-dependent activation of Tcf-4.";
Yamamoto H., Ihara M., Matsuura Y., Kikuchi A.;
EMBO J. 22:2047-2059(2003).
Cited for: SUMOYLATION AT LYS-320, INTERACTION WITH PIAS4, FUNCTION, SUBCELLULARLOCATION, AND MUTAGENESIS OF LYS-320 AND GLU-322.

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