TCF7_HUMAN - dbPTM
TCF7_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TCF7_HUMAN
UniProt AC P36402
Protein Name Transcription factor 7
Gene Name TCF7
Organism Homo sapiens (Human).
Sequence Length 384
Subcellular Localization Nucleus.
Protein Description Transcriptional activator involved in T-cell lymphocyte differentiation. Necessary for the survival of CD4(+) CD8(+) immature thymocytes. Isoforms lacking the N-terminal CTNNB1 binding domain cannot fulfill this role. Binds to the T-lymphocyte-specific enhancer element (5'-WWCAAAG-3') found in the promoter of the CD3E gene. May also act as feedback transcriptional repressor of CTNNB1 and TCF7L2 target genes. TLE1, TLE2, TLE3 and TLE4 repress transactivation mediated by TCF7 and CTNNB1..
Protein Sequence MPQLDSGGGGAGGGDDLGAPDELLAFQDEGEEQDDKSRDSAAGPERDLAELKSSLVNESEGAAGGAGIPGVPGAGAGARGEAEALGREHAAQRLFPDKLPEPLEDGLKAPECTSGMYKETVYSAFNLLMHYPPPSGAGQHPQPQPPLHKANQPPHGVPQLSLYEHFNSPHPTPAPADISQKQVHRPLQTPDLSGFYSLTSGSMGQLPHTVSWFTHPSLMLGSGVPGHPAAIPHPAIVPPSGKQELQPFDRNLKTQAESKAEKEAKKPTIKKPLNAFMLYMKEMRAKVIAECTLKESAAINQILGRRWHALSREEQAKYYELARKERQLHMQLYPGWSARDNYGKKKRRSREKHQESTTETNWPRELKDGNGQESLSMSSSSSPA
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
6Phosphorylation--MPQLDSGGGGAGG
--CCCCCCCCCCCCC
48.1828634120
36UbiquitinationEGEEQDDKSRDSAAG
CCCCCCHHHCCCCCC
56.53-
36 (in isoform 9)Ubiquitination-56.53-
37PhosphorylationGEEQDDKSRDSAAGP
CCCCCHHHCCCCCCC
48.6030108239
40PhosphorylationQDDKSRDSAAGPERD
CCHHHCCCCCCCHHH
20.9330108239
52UbiquitinationERDLAELKSSLVNES
HHHHHHHHHHHHCCC
29.51-
52 (in isoform 5)Ubiquitination-29.51-
52 (in isoform 9)Ubiquitination-29.51-
98 (in isoform 9)Ubiquitination-67.20-
98UbiquitinationAQRLFPDKLPEPLED
HHHHCCCCCCCCCCC
67.20-
108 (in isoform 9)Ubiquitination-68.38-
108UbiquitinationEPLEDGLKAPECTSG
CCCCCCCCCCCCCCC
68.38-
117PhosphorylationPECTSGMYKETVYSA
CCCCCCHHHHHHHHH
14.81-
161PhosphorylationPHGVPQLSLYEHFNS
CCCCCCCCHHHCCCC
24.5328796482
163PhosphorylationGVPQLSLYEHFNSPH
CCCCCCHHHCCCCCC
12.1828796482
168PhosphorylationSLYEHFNSPHPTPAP
CHHHCCCCCCCCCCC
24.5228796482
172PhosphorylationHFNSPHPTPAPADIS
CCCCCCCCCCCCCCC
29.1128796482
179PhosphorylationTPAPADISQKQVHRP
CCCCCCCCHHCCCCC
31.69-
181UbiquitinationAPADISQKQVHRPLQ
CCCCCCHHCCCCCCC
47.71-
234 (in isoform 12)Phosphorylation-20.5126657352
234 (in isoform 4)Phosphorylation-20.5126657352
234 (in isoform 8)Phosphorylation-20.5126657352
237 (in isoform 10)Ubiquitination-6.57-
241 (in isoform 4)Phosphorylation-41.2529978859
241 (in isoform 8)Phosphorylation-41.2529978859
241 (in isoform 12)Phosphorylation-41.2529978859
242 (in isoform 4)Phosphorylation-44.9629978859
242 (in isoform 8)Phosphorylation-44.9629978859
242 (in isoform 12)Phosphorylation-44.9629978859
243 (in isoform 4)Phosphorylation-61.2226657352
243 (in isoform 8)Phosphorylation-61.2226657352
243 (in isoform 12)Phosphorylation-61.2226657352
247 (in isoform 4)Phosphorylation-45.8126657352
247 (in isoform 8)Phosphorylation-45.8126657352
247 (in isoform 12)Phosphorylation-45.8126657352
250 (in isoform 10)Phosphorylation-51.24-
253UbiquitinationQPFDRNLKTQAESKA
CCCCHHHHHHHHHHH
41.98-
253AcetylationQPFDRNLKTQAESKA
CCCCHHHHHHHHHHH
41.9825953088
253 (in isoform 9)Ubiquitination-41.98-
259UbiquitinationLKTQAESKAEKEAKK
HHHHHHHHHHHHHCC
52.66-
259 (in isoform 9)Ubiquitination-52.66-
271UbiquitinationAKKPTIKKPLNAFML
HCCCCCCHHHHHHHH
51.38-
271 (in isoform 5)Ubiquitination-51.38-
281UbiquitinationNAFMLYMKEMRAKVI
HHHHHHHHHHHHHHH
34.50-
286 (in isoform 9)Ubiquitination-24.65-
286UbiquitinationYMKEMRAKVIAECTL
HHHHHHHHHHHHCCC
24.65-
294 (in isoform 9)Ubiquitination-31.31-
294UbiquitinationVIAECTLKESAAINQ
HHHHCCCCHHHHHHH
31.31-
317UbiquitinationLSREEQAKYYELARK
CCHHHHHHHHHHHHH
48.32-
317 (in isoform 5)Ubiquitination-48.32-
318PhosphorylationSREEQAKYYELARKE
CHHHHHHHHHHHHHH
12.75-
319PhosphorylationREEQAKYYELARKER
HHHHHHHHHHHHHHH
12.08-
333PhosphorylationRQLHMQLYPGWSARD
HHHHHHHCCCCHHHC
5.25-
337PhosphorylationMQLYPGWSARDNYGK
HHHCCCCHHHCCCCH
21.24-
349 (in isoform 7)Phosphorylation-49.1526657352
349 (in isoform 11)Phosphorylation-49.1526657352
349 (in isoform 3)Phosphorylation-49.1526657352
352 (in isoform 9)Ubiquitination-49.86-
356 (in isoform 11)Phosphorylation-33.7829978859
356 (in isoform 3)Phosphorylation-33.7829978859
356 (in isoform 7)Phosphorylation-33.7829978859
357 (in isoform 3)Phosphorylation-28.0929978859
357 (in isoform 7)Phosphorylation-28.0929978859
357 (in isoform 11)Phosphorylation-28.0929978859
358 (in isoform 11)Phosphorylation-50.5226657352
358 (in isoform 7)Phosphorylation-50.5226657352
358 (in isoform 3)Phosphorylation-50.5226657352
362 (in isoform 3)Phosphorylation-10.7626657352
362 (in isoform 7)Phosphorylation-10.7626657352
362 (in isoform 11)Phosphorylation-10.7626657352
365 (in isoform 9)Phosphorylation-56.97-
371 (in isoform 5)Ubiquitination-37.86-

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

Oops, there are no upstream regulatory protein records of TCF7_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TCF7_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 TCF7_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DAZP2_HUMANDAZAP2physical
19304756
CREST_HUMANSS18L1physical
20211142

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TCF7_HUMAN

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Related Literatures of Post-Translational Modification

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