UniProt ID | TYY1_MOUSE | |
---|---|---|
UniProt AC | Q00899 | |
Protein Name | Transcriptional repressor protein YY1 | |
Gene Name | Yy1 | |
Organism | Mus musculus (Mouse). | |
Sequence Length | 414 | |
Subcellular Localization | Nucleus . Nucleus matrix . Cytoplasm . Associated with the nuclear matrix. In testis, localized to heterochromatin of spermatocytes. | |
Protein Description | Multifunctional transcription factor that exhibits positive and negative control on a large number of cellular and viral genes by binding to sites overlapping the transcription start site. Binds to the consensus sequence 5'-CCGCCATNTT-3'; some genes have been shown to contain a longer binding motif allowing enhanced binding; the initial CG dinucleotide can be methylated greatly reducing the binding affinity. The effect on transcription regulation is depending upon the context in which it binds and diverse mechanisms of action include direct activation or repression, indirect activation or repression via cofactor recruitment, or activation or repression by disruption of binding sites or conformational DNA changes. Its activity is regulated by transcription factors and cytoplasmic proteins that have been shown to abrogate or completely inhibit YY1-mediated activation or repression. Binds to the upstream conserved region (UCR) (5'-CGCCATTTT-3') of Moloney murine leukemia virus (MuLV). Acts synergistically with the SMAD1 and SMAD4 in bone morphogenetic protein (BMP)-mediated cardiac-specific gene expression. [PubMed: 15329343 Binds to SMAD binding elements (SBEs) (5'-GTCT/AGAC-3') within BMP response element (BMPRE) of cardiac activating regions] | |
Protein Sequence | MASGDTLYIATDGSEMPAEIVELHEIEVETIPVETIETTVVGEEEEEDDDDEDGGGGDHGGGGGGHGHAGHHHHHHHHHHHHPPMIALQPLVTDDPTQVHHHQEVILVQTREEVVGGDDSDGLRAEDGFEDQILIPVPAPAGGDDDYIEQTLVTVAAAGKSGGGASSGGGRVKKGGGKKSGKKSYLGGGAGAAGGGGADPGNKKWEQKQVQIKTLEGEFSVTMWSSDEKKDIDHETVVEEQIIGENSPPDYSEYMTGKKLPPGGIPGIDLSDPKQLAEFARMKPRKIKEDDAPRTIACPHKGCTKMFRDNSAMRKHLHTHGPRVHVCAECGKAFVESSKLKRHQLVHTGEKPFQCTFEGCGKRFSLDFNLRTHVRIHTGDRPYVCPFDGCNKKFAQSTNLKSHILTHAKAKNNQ | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
30 | Phosphorylation | LHEIEVETIPVETIE EEEEEEEEEECEEEE | 35.44 | 22482732 | |
120 | Phosphorylation | EVVGGDDSDGLRAED EECCCCCCCCCCCCC | 38.01 | 25521595 | |
183 | Ubiquitination | GGKKSGKKSYLGGGA CCCCCCCCCCCCCCC | 48.10 | 22790023 | |
184 | Phosphorylation | GKKSGKKSYLGGGAG CCCCCCCCCCCCCCC | 29.13 | 26643407 | |
185 | Phosphorylation | KKSGKKSYLGGGAGA CCCCCCCCCCCCCCC | 20.46 | 18846507 | |
203 | Ubiquitination | GGADPGNKKWEQKQV CCCCCCCCCCEECEE | 66.24 | 27667366 | |
247 | Phosphorylation | EQIIGENSPPDYSEY EHHCCCCCCCCHHHH | 33.24 | 27087446 | |
251 | Phosphorylation | GENSPPDYSEYMTGK CCCCCCCHHHHHCCC | 14.80 | 25619855 | |
252 | Phosphorylation | ENSPPDYSEYMTGKK CCCCCCHHHHHCCCC | 29.63 | 25619855 | |
254 | Phosphorylation | SPPDYSEYMTGKKLP CCCCHHHHHCCCCCC | 8.27 | 25619855 | |
256 | Phosphorylation | PDYSEYMTGKKLPPG CCHHHHHCCCCCCCC | 44.97 | 25619855 | |
311 | Phosphorylation | TKMFRDNSAMRKHLH HHHHCCCHHHHHHHH | 27.94 | 29176673 | |
348 | Phosphorylation | KRHQLVHTGEKPFQC CCCCCCCCCCCCEEE | 39.29 | 23140645 | |
365 | Phosphorylation | EGCGKRFSLDFNLRT CCCCCEEEEEEECCE | 30.94 | 28833060 | |
378 | Phosphorylation | RTHVRIHTGDRPYVC CEEEEEECCCCCEEC | 38.10 | 25266776 | |
397 | Phosphorylation | CNKKFAQSTNLKSHI CCHHHHHHHCCHHHH | 18.81 | 22817900 | |
398 | Phosphorylation | NKKFAQSTNLKSHIL CHHHHHHHCCHHHHH | 32.27 | 21183079 | |
402 | Phosphorylation | AQSTNLKSHILTHAK HHHHCCHHHHHHHHH | 20.94 | 21183079 |
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 TYY1_MOUSE !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of TYY1_MOUSE !! |
* 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 TYY1_MOUSE !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
EP300_MOUSE | Ep300 | physical | 17220375 | |
CTCF_MOUSE | Ctcf | physical | 17218270 | |
SP3_MOUSE | Sp3 | physical | 21149256 | |
SMCA4_MOUSE | Smarca4 | physical | 21149256 | |
GON4L_MOUSE | Gon4l | physical | 21454521 | |
HDAC1_MOUSE | Hdac1 | physical | 8917507 | |
MTOR_MOUSE | Mtor | physical | 18046414 | |
PRGC1_MOUSE | Ppargc1a | physical | 18046414 |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry."; Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.; J. Proteome Res. 7:5314-5326(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-247, AND MASSSPECTROMETRY. |