TF7L1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: TF7L1_MOUSE
• UniProt AC: Q9Z1J1
• Protein Name: Transcription factor 7-like 1
• Gene Name: Tcf7l1
• Organism: Mus musculus (Mouse).
• Sequence Length: 584
• Subcellular Localization: Nucleus.
• Protein Description: Participates in the Wnt signaling pathway. Binds to DNA and acts as a repressor in the absence of CTNNB1, and as an activator in its presence. Necessary for the terminal differentiation of epidermal cells, the formation of keratohyalin granules and the development of the barrier function of the epidermis..
• Protein Sequence: MPQLGGGRGGAGGGGGGSGAGATSGGDDLGANDELIPFQDEGGEEQEPSSDTASAQRDLDEVKSSLVNESENQSSSSDSEAERRPQPARDAFQKPRDYFAEVRRPQDGAFFKGGAYPGYPFLMIPDLSSPYLSNGPLSPGGARTYLQMKWPLLDVPSSATVKDTRSPSPAHLSNKVPVVQHPHHMHPLTPLITYSNDHFSPASPPTHLSPEIDPKTGIPRPPHPSELSPYYPLSPGAVGQIPHPLGWLVPQQGQPMYSLPPGGFRHPYPALAMNASMSSLVSSRFPHMVAPAHPGLPTSGIPHPAIVSPIVKQEPAAPSLSPAVSAKSPVTVKKEEEKKPHVKKPLNAFMLYMKEMRAKVVAECTLKESAAINQILGRKWHNLSREEQAKYYELARKERQLHAQLYPTWSARDNYGKKKKRKREKQLSQTQSQQQIQEAEGALASKSKKPCIQYLPPEKPCDSPASSHGSALDSPATPSAALASPAAPAATHSEQAQPLSLTTKPEARAQLALHSAAFLSAKAAASNSSQMGSQPPLLSRPLPLGSMPAALLTSPPTFPATLHAHQALPVLQAQPLSLVTKSAH

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
64	Phosphorylation	RDLDEVKSSLVNESE HCHHHHHHHHCCCCC	33.80	26160508
65	Phosphorylation	DLDEVKSSLVNESEN CHHHHHHHHCCCCCC	30.53	26160508
70	Phosphorylation	KSSLVNESENQSSSS HHHHCCCCCCCCCCC	36.32	26160508
74	Phosphorylation	VNESENQSSSSDSEA CCCCCCCCCCCCHHH	43.71	25619855
75	Phosphorylation	NESENQSSSSDSEAE CCCCCCCCCCCHHHH	24.89	25619855
76	Phosphorylation	ESENQSSSSDSEAER CCCCCCCCCCHHHHH	43.33	25619855
77	Phosphorylation	SENQSSSSDSEAERR CCCCCCCCCHHHHHC	47.29	25619855
79	Phosphorylation	NQSSSSDSEAERRPQ CCCCCCCHHHHHCCC	40.43	26160508
138	Phosphorylation	YLSNGPLSPGGARTY CCCCCCCCCCCHHHH	25.32	29514104
143	Dimethylation	PLSPGGARTYLQMKW CCCCCCHHHHEEECC	27.46	-
143	Methylation	PLSPGGARTYLQMKW CCCCCCHHHHEEECC	27.46	54541713
164	Phosphorylation	SSATVKDTRSPSPAH CCCCCCCCCCCCHHH	27.59	21454597
166	Phosphorylation	ATVKDTRSPSPAHLS CCCCCCCCCCHHHHC	31.64	24899341
168	Phosphorylation	VKDTRSPSPAHLSNK CCCCCCCCHHHHCCC	35.65	24899341
173	Phosphorylation	SPSPAHLSNKVPVVQ CCCHHHHCCCCCCCC	25.41	29550500
189	Phosphorylation	PHHMHPLTPLITYSN CCCCCCCCCEEEECC	22.09	26060331
193	Phosphorylation	HPLTPLITYSNDHFS CCCCCEEEECCCCCC	28.69	26060331
194	Phosphorylation	PLTPLITYSNDHFSP CCCCEEEECCCCCCC	9.85	26060331
195	Phosphorylation	LTPLITYSNDHFSPA CCCEEEECCCCCCCC	27.42	26060331
200	Phosphorylation	TYSNDHFSPASPPTH EECCCCCCCCCCCCC	19.01	26060331
203	Phosphorylation	NDHFSPASPPTHLSP CCCCCCCCCCCCCCC	34.49	26060331
319	Phosphorylation	KQEPAAPSLSPAVSA CCCCCCCCCCCCCCC	36.43	26060331
321	Phosphorylation	EPAAPSLSPAVSAKS CCCCCCCCCCCCCCC	18.36	22006019
325	Phosphorylation	PSLSPAVSAKSPVTV CCCCCCCCCCCCCCC	31.89	26060331
328	Phosphorylation	SPAVSAKSPVTVKKE CCCCCCCCCCCCCCH	25.07	26060331
384	Phosphorylation	GRKWHNLSREEQAKY CHHHHCCCHHHHHHH	42.85	20139300
391	Phosphorylation	SREEQAKYYELARKE CHHHHHHHHHHHHHH	12.75	20139300
392	Phosphorylation	REEQAKYYELARKER HHHHHHHHHHHHHHH	12.08	20139300
428	Phosphorylation	RKREKQLSQTQSQQQ HHHHHHHHHHHHHHH	28.78	29514104
539	Phosphorylation	GSQPPLLSRPLPLGS CCCCCCCCCCCCCCC	39.26	-
546	Phosphorylation	SRPLPLGSMPAALLT CCCCCCCCCCHHHHC	29.31	-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of TF7L1_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of TF7L1_MOUSE !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of TF7L1_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of TF7L1_MOUSE !!

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.