TCF7L2
entrez
6934
canonical
uniprot
Q9NQB0
canonical
ensembl
ENSG00000148737
resolver
ensp
ENSP00000277945
resolver
ensp
ENSP00000344823
resolver
ensp
ENSP00000347949
resolver
ensp
ENSP00000348274
resolver
ensp
ENSP00000358396
resolver
ensp
ENSP00000358402
resolver
ensp
ENSP00000358404
resolver
ensp
ENSP00000440547
resolver
ensp
ENSP00000443626
resolver
ensp
ENSP00000446172
resolver
ensp
ENSP00000486891
resolver
ensp
ENSP00000490478
resolver
ensp
ENSP00000515891
resolver
ensp
ENSP00000537624
resolver
ensp
ENSP00000652724
resolver
ensp
ENSP00000652725
resolver
ensp
ENSP00000652726
resolver
enst
ENST00000277945
resolver
enst
ENST00000369389
resolver
enst
ENST00000369395
resolver
enst
ENST00000534894
resolver
enst
ENST00000545257
resolver
enst
ENST00000704414
resolver
genesymbol
TCF7L2
resolver
genesymbol_syn
TCF4
resolver
hgnc
HGNC:11641
resolver
uniprot
A0A0A0MTI4
resolver
uniprot
A0A0A0MTL7
resolver
uniprot
A0A994J711
resolver
uniprot
A0ACM8QBN5
resolver
uniprot
A0ACM8QIH5
resolver
uniprot
A0ACM8QJQ0
resolver
uniprot
B4DJZ2
resolver
uniprot
B4DRJ8
resolver
uniprot
B7Z9Z6
resolver
uniprot
B9X074
resolver
uniprot
C6ZRJ7
resolver
uniprot
C6ZRJ8
resolver
uniprot
C6ZRJ9
resolver
uniprot
C6ZRK0
resolver
uniprot
C6ZRK1
resolver
uniprot
C6ZRK2
resolver
uniprot
C6ZRK5
resolver
uniprot
E2GH14
resolver
uniprot
E2GH19
resolver
uniprot
E2GH20
resolver
uniprot
E2GH24
resolver
uniprot
E2GH25
resolver
uniprot
E9PFH9
resolver
uniprot
F8W742
resolver
uniprot
F8W7T5
resolver
uniprot
O00185
resolver
uniprot
Q5JRY4
resolver
uniprot
Q5JRY5
resolver
uniprot
Q5VVR7
resolver
uniprot
Q6FHW4
resolver
uniprot
Q9NQB1
resolver
uniprot
Q9NQB2
resolver
uniprot
Q9NQB3
resolver
uniprot
Q9NQB4
resolver
uniprot
Q9NQB5
resolver
uniprot
Q9NQB6
resolver
uniprot
Q9NQB7
resolver
uniprot
Q9ULC2
resolver
uniprot_entry
A0A0A0MTI4_HUMAN
resolver
uniprot_entry
A0A0A0MTL7_HUMAN
resolver
uniprot_entry
A0A994J711_HUMAN
resolver
uniprot_entry
A0ACM8QBN5_HUMAN
resolver
uniprot_entry
A0ACM8QIH5_HUMAN
resolver
uniprot_entry
A0ACM8QJQ0_HUMAN
resolver
uniprot_entry
B4DJZ2_HUMAN
resolver
uniprot_entry
C6ZRJ7_HUMAN
resolver
uniprot_entry
C6ZRK1_HUMAN
resolver
uniprot_entry
C6ZRK2_HUMAN
resolver
uniprot_entry
C6ZRK5_HUMAN
resolver
uniprot_entry
Q5JRY4_HUMAN
resolver
uniprot_entry
Q5VVR7_HUMAN
resolver
uniprot_entry
Q6FHW4_HUMAN
resolver
uniprot_entry
TF7L2_HUMAN
resolver
uniprot_sec
B4DRJ8
resolver
uniprot_sec
B7Z9Z6
resolver
uniprot_sec
B9X074
resolver
uniprot_sec
C6ZRJ8
resolver
uniprot_sec
C6ZRJ9
resolver
uniprot_sec
C6ZRK0
resolver
uniprot_sec
E2GH14
resolver
uniprot_sec
E2GH19
resolver
uniprot_sec
E2GH20
resolver
uniprot_sec
E2GH24
resolver
uniprot_sec
E2GH25
resolver
uniprot_sec
E9PFH9
resolver
uniprot_sec
F8W742
resolver
uniprot_sec
F8W7T5
resolver
uniprot_sec
O00185
resolver
uniprot_sec
Q5JRY5
resolver
uniprot_sec
Q9NQB1
resolver
uniprot_sec
Q9NQB2
resolver
uniprot_sec
Q9NQB3
resolver
uniprot_sec
Q9NQB4
resolver
uniprot_sec
Q9NQB5
resolver
uniprot_sec
Q9NQB6
resolver
uniprot_sec
Q9NQB7
resolver
uniprot_sec
Q9ULC2
resolver
amino_acid_sequence
MPQLNGGGGDDLGANDELISFKDEGEQEEKSSENSSAERDLADVKSSLVNESETNQNSSSDSEAERRPPPRSESFRDKSRESLEEAAKRQDGGLFKGPPYPGYPFIMIPDLTSPYLPNGSLSPTARTLHFQSGSTHYSAYKTIEHQIAVQYLQMKWPLLDVQAGSLQSRQALKDARSPSPAHIVSNKVPVVQHPHHVHPLTPLITYSNEHFTPGNPPPHLPADVDPKTGIPRPPHPPDISPYYPLSPGTVGQIPHPLGWLVPQQGQPVYPITTGGFRHPYPTALTVNASMSRFPPHMVPPHHTLHTTGIPHPAIVTPTVKQESSQSDVGSLHSSKHQDSKKEEEKKKPHIKKPLNAFMLYMKEMRAKVVAECTLKESAAINQILGRRWHALSREEQAKYYELARKERQLHMQLYPGWSARDNYGKKKKRKRDKQPGETNEHSECFLNPCLSLPPITDLSAPKKCRARFGLDQQNNWCGPCRRKKKCVRYIQGEGSCLSPPSSDGSLLDSPPPSPNLLGSPPRDAKSQTEQTQPLSLSLKPDPLAHLSMMPPPPALLLAEATHKASALCPNGALDLPPAALQPAAPSSSIAQPSTSSLHSHSSLAGTQPQPLSLVTKSLE
uniprot
proteins
disease_involvement
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).; DISEASE: Type 2 diabetes mellitus (T2D) [MIM:125853]: A multifactorial disorder of glucose homeostasis caused by a lack of sensitivity to insulin. Affected individuals usually have an obese body habitus and manifestations of a metabolic syndrome characterized by diabetes, insulin resistance, hypertension and hypertriglyceridemia. The disease results in long-term complications that affect the eyes, kidneys, nerves, and blood vessels. {ECO:0000269|PubMed:16415884, ECO:0000269|PubMed:24390345}. Note=Disease susceptibility is associated with variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Participates in the Wnt signaling pathway and modulates MYC expression by binding to its promoter in a sequence-specific manner. Acts as a 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. {ECO:0000269|PubMed:12408868, ECO:0000269|PubMed:12727872, ECO:0000269|PubMed:19443654, ECO:0000269|PubMed:22699938, ECO:0000269|PubMed:9727977}.
uniprot
proteins
mass_dalton
67919
uniprot
proteins
mutagenesis
MUTAGEN 10..11; /note="DD->AA: Reduces CTNNB1 binding."; /evidence="ECO:0000269|PubMed:10080941"; MUTAGEN 16; /note="D->A: Abolishes CTNNB1 binding."; /evidence="ECO:0000269|PubMed:10080941"; MUTAGEN 17; /note="E->A: Reduces CTNNB1 binding."; /evidence="ECO:0000269|PubMed:10080941"; MUTAGEN 19; /note="I->A: Reduces transcription activation."; /evidence="ECO:0000269|PubMed:11713476"; MUTAGEN 21; /note="F->A: Reduces transcription activation."; /evidence="ECO:0000269|PubMed:11713476"; MUTAGEN 23..24; /note="DE->AA: Reduces CTNNB1 binding."; /evidence="ECO:0000269|PubMed:10080941"; MUTAGEN 24; /note="E->A: Reduces CTNNB1 binding, and abolishes CTNNB1 binding; when associated with A-26; A-28 and A-29."; /evidence="ECO:0000269|PubMed:11713475"; MUTAGEN 26; /note="E->A: Abolishes CTNNB1 binding; when associated with A-24; A-28 and A-29."; /evidence="ECO:0000269|PubMed:11713475"; MUTAGEN 28; /note="E->A: Abolishes CTNNB1 binding; when associated with A-24; A-26 and A-29."; /evidence="ECO:0000269|PubMed:11713475"; MUTAGEN 29; /note="E->A: Reduces CTNNB1 binding, and abolishes CTNNB1 binding; when associated with A-24; A-26 and A-28."; /evidence="ECO:0000269|PubMed:11713475"; MUTAGEN 48; /note="L->A: Abolishes CTNNB1 binding."; /evidence="ECO:0000269|PubMed:10080941"; MUTAGEN 201; /note="T->V: Reduced phosphorylation by NLK and enhanced DNA-binding; when associated with V-212."; /evidence="ECO:0000269|PubMed:12556497"; MUTAGEN 212; /note="T->V: Reduced phosphorylation by NLK and enhanced DNA-binding; when associated with V-201."; /evidence="ECO:0000269|PubMed:12556497"; MUTAGEN 320; /note="K->R: Loss of sumoylation. No effect on localization to nuclear bodies."; /evidence="ECO:0000269|PubMed:12727872"; MUTAGEN 322; /note="E->A: Loss of sumoylation."; /evidence="ECO:0000269|PubMed:12727872
uniprot
proteins
post_translational_modification
PTM: In vitro, phosphorylated by TNIK. {ECO:0000269|PubMed:12556497}.; PTM: Phosphorylated at Thr-201 and/or Thr-212 by NLK. Phosphorylation by NLK at these sites inhibits DNA-binding by TCF7L2/TCF4, thereby preventing transcriptional activation of target genes of the canonical Wnt/beta-catenin signaling pathway. {ECO:0000269|PubMed:12556497}.; PTM: Polysumoylated. Sumoylation is enhanced by PIAS family members and desumoylation is enhanced by SENP2. Sumoylation/desumoylation regulates TCF7L2/TCF4 transcription activity in the Wnt/beta-catenin signaling pathway without altering interaction with CTNNB1 nor binding to DNA. {ECO:0000269|PubMed:12727872}.
uniprot
proteins
protein_family
TCF/LEF family
uniprot
proteins
pubmed
10080941
uniprot
proteins
pubmed
10919662
uniprot
proteins
pubmed
11266540
uniprot
proteins
pubmed
11713475
uniprot
proteins
pubmed
11713476
uniprot
proteins
pubmed
12408868
uniprot
proteins
pubmed
12446687
uniprot
proteins
pubmed
12556497
uniprot
proteins
pubmed
12727872
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15164054
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16415884
uniprot
proteins
pubmed
16434966
uniprot
proteins
pubmed
16714285
uniprot
proteins
pubmed
16959974
uniprot
proteins
pubmed
17052462
uniprot
proteins
pubmed
17873903
uniprot
proteins
pubmed
19304756
uniprot
proteins
pubmed
19443654
uniprot
proteins
pubmed
19602480
uniprot
proteins
pubmed
19816403
uniprot
proteins
pubmed
21256126
uniprot
proteins
pubmed
21454679
uniprot
proteins
pubmed
22155184
uniprot
proteins
pubmed
22258766
uniprot
proteins
pubmed
22304967
uniprot
proteins
pubmed
22699938
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
24390345
uniprot
proteins
pubmed
24589551
uniprot
proteins
pubmed
28112733
uniprot
proteins
pubmed
28829046
uniprot
proteins
pubmed
29061846
uniprot
proteins
pubmed
29739711
uniprot
proteins
pubmed
9065401
uniprot
proteins
pubmed
9727977
uniprot
proteins
pubmed
9916915
uniprot
proteins
sequence_length
619
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus, PML body {ECO:0000269|PubMed:12727872, ECO:0000269|PubMed:22699938, ECO:0000269|PubMed:9916915}. Nucleus {ECO:0000269|PubMed:19304756}. Note=Diffuse pattern. Colocalizes with SUMO1 and PIAS4 in a subset of PML (promyelocytic leukemia) nuclear bodies.
uniprot
proteins