| UniProt ID | AP1_YEAST | |
|---|---|---|
| UniProt AC | P19880 | |
| Protein Name | AP-1-like transcription factor YAP1 {ECO:0000305} | |
| Gene Name | YAP1 {ECO:0000303|PubMed:2542125} | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 650 | |
| Subcellular Localization | Nucleus . Cytoplasm . Oxidized YAP1 is found predominantly in the nucleus, while reduced YAP1 is continuously exported to the cytoplasm by CRM1/exportin 1. Nuclear import requires the karyopherin PSE1/KAP121 and is independent on YAP1 oxidation state | |
| Protein Description | Transcription activator involved in oxidative stress response and redox homeostasis. Regulates the transcription of genes encoding antioxidant enzymes and components of the cellular thiol-reducing pathways, including the thioredoxin system (TRX2, TRR1), the glutaredoxin system (GSH1, GLR1), superoxide dismutase (SOD1, SOD2), glutathione peroxidase (GPX2), and thiol-specific peroxidases (TSA1, AHP1). The induction of some of these genes requires the cooperative action of both, YAP1 and SKN7. Preferentially binds to promoters with the core binding site 5'-TTA[CG]TAA-3'. Activity of the transcription factor is controlled through oxidation of specific cysteine residues resulting in the alteration of its subcellular location. Oxidative stress (as well as carbon stress, but not increased temperature, acidic pH, or ionic stress) induces nuclear accumulation and as a result YAP1 transcriptional activity. Activation by hydrogen peroxide or thiol-reactive chemicals elicit distinct adaptive gene responses. Nuclear export is restored when disulfide bonds are reduced by thioredoxin (TRX2), whose expression is controlled by YAP1, providing a mechanism for negative autoregulation. When overexpressed, YAP1 confers pleiotropic drug-resistance and increases cellular tolerance to cadmium, iron chelators and zinc.. | |
| Protein Sequence | MSVSTAKRSLDVVSPGSLAEFEGSKSRHDEIENEHRRTGTRDGEDSEQPKKKGSKTSKKQDLDPETKQKRTAQNRAAQRAFRERKERKMKELEKKVQSLESIQQQNEVEATFLRDQLITLVNELKKYRPETRNDSKVLEYLARRDPNLHFSKNNVNHSNSEPIDTPNDDIQENVKQKMNFTFQYPLDNDNDNDNSKNVGKQLPSPNDPSHSAPMPINQTQKKLSDATDSSSATLDSLSNSNDVLNNTPNSSTSMDWLDNVIYTNRFVSGDDGSNSKTKNLDSNMFSNDFNFENQFDEQVSEFCSKMNQVCGTRQCPIPKKPISALDKEVFASSSILSSNSPALTNTWESHSNITDNTPANVIATDATKYENSFSGFGRLGFDMSANHYVVNDNSTGSTDSTGSTGNKNKKNNNNSDDVLPFISESPFDMNQVTNFFSPGSTGIGNNAASNTNPSLLQSSKEDIPFINANLAFPDDNSTNIQLQPFSESQSQNKFDYDMFFRDSSKEGNNLFGEFLEDDDDDKKAANMSDDESSLIKNQLINEEPELPKQYLQSVPGNESEISQKNGSSLQNADKINNGNDNDNDNDVVPSKEGSLLRCSEIWDRITTHPKYSDIDVDGLCSELMAKAKCSERGVVINAEDVQLALNKHMN | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 5 | Phosphorylation | ---MSVSTAKRSLDV ---CCHHHCCHHCCC | 30377154 | ||
| 7 | Ubiquitination | -MSVSTAKRSLDVVS -CCHHHCCHHCCCCC | 17644757 | ||
| 9 | Phosphorylation | SVSTAKRSLDVVSPG CHHHCCHHCCCCCCC | 22890988 | ||
| 14 | Phosphorylation | KRSLDVVSPGSLAEF CHHCCCCCCCCHHHC | 22369663 | ||
| 17 | Phosphorylation | LDVVSPGSLAEFEGS CCCCCCCCHHHCCCC | 22369663 | ||
| 24 | Phosphorylation | SLAEFEGSKSRHDEI CHHHCCCCCCCCHHH | 22369663 | ||
| 25 | Ubiquitination | LAEFEGSKSRHDEIE HHHCCCCCCCCHHHH | 17644757 | ||
| 26 | Phosphorylation | AEFEGSKSRHDEIEN HHCCCCCCCCHHHHH | 19779198 | ||
| 40 | Phosphorylation | NEHRRTGTRDGEDSE HHHHCCCCCCCCCCC | 23749301 | ||
| 46 | Phosphorylation | GTRDGEDSEQPKKKG CCCCCCCCCCCCCCC | 27214570 | ||
| 135 | Phosphorylation | RPETRNDSKVLEYLA CCCCCCHHHHHHHHH | 28889911 | ||
| 140 | Phosphorylation | NDSKVLEYLARRDPN CHHHHHHHHHHHCCC | 22369663 | ||
| 158 | Phosphorylation | SKNNVNHSNSEPIDT CCCCCCCCCCCCCCC | 24961812 | ||
| 160 | Phosphorylation | NNVNHSNSEPIDTPN CCCCCCCCCCCCCCC | 24961812 | ||
| 165 | Phosphorylation | SNSEPIDTPNDDIQE CCCCCCCCCCHHHHH | 22369663 | ||
| 204 | Phosphorylation | NVGKQLPSPNDPSHS CCCCCCCCCCCCCCC | 22369663 | ||
| 209 | Phosphorylation | LPSPNDPSHSAPMPI CCCCCCCCCCCCCCC | 22369663 | ||
| 211 | Phosphorylation | SPNDPSHSAPMPINQ CCCCCCCCCCCCCCH | 22369663 | ||
| 219 | Phosphorylation | APMPINQTQKKLSDA CCCCCCHHHHHHHHC | 22369663 | ||
| 221 | Ubiquitination | MPINQTQKKLSDATD CCCCHHHHHHHHCCC | 23749301 | ||
| 268 | Phosphorylation | IYTNRFVSGDDGSNS EEECCCCCCCCCCCC | 30377154 | ||
| 273 | Phosphorylation | FVSGDDGSNSKTKNL CCCCCCCCCCCCCCC | 28889911 | ||
| 276 | Ubiquitination | GDDGSNSKTKNLDSN CCCCCCCCCCCCCCC | 23749301 | ||
| 372 | Phosphorylation | DATKYENSFSGFGRL CCCCCCCCCCCCCCC | 28889911 | ||
| 384 | Phosphorylation | GRLGFDMSANHYVVN CCCCEECCCCEEEEC | 22369663 | ||
| 388 | Phosphorylation | FDMSANHYVVNDNST EECCCCEEEECCCCC | 22369663 | ||
| 394 | Phosphorylation | HYVVNDNSTGSTDST EEEECCCCCCCCCCC | 22369663 | ||
| 395 | Phosphorylation | YVVNDNSTGSTDSTG EEECCCCCCCCCCCC | 22369663 | ||
| 397 | Phosphorylation | VNDNSTGSTDSTGST ECCCCCCCCCCCCCC | 22369663 | ||
| 398 | Phosphorylation | NDNSTGSTDSTGSTG CCCCCCCCCCCCCCC | 22369663 | ||
| 400 | Phosphorylation | NSTGSTDSTGSTGNK CCCCCCCCCCCCCCC | 22369663 | ||
| 401 | Phosphorylation | STGSTDSTGSTGNKN CCCCCCCCCCCCCCC | 22369663 | ||
| 403 | Phosphorylation | GSTDSTGSTGNKNKK CCCCCCCCCCCCCCC | 22369663 | ||
| 404 | Phosphorylation | STDSTGSTGNKNKKN CCCCCCCCCCCCCCC | 22369663 | ||
| 496 | Phosphorylation | QSQNKFDYDMFFRDS HCCCCCCCEEECCCC | 22369663 | ||
| 503 | Phosphorylation | YDMFFRDSSKEGNNL CEEECCCCCCCCCCC | 22369663 | ||
| 504 | Phosphorylation | DMFFRDSSKEGNNLF EEECCCCCCCCCCCH | 22369663 | ||
| 528 | Phosphorylation | DKKAANMSDDESSLI CHHHHCCCCCHHHHH | 22369663 | ||
| 532 | Phosphorylation | ANMSDDESSLIKNQL HCCCCCHHHHHHHHH | 22369663 | ||
| 533 | Phosphorylation | NMSDDESSLIKNQLI CCCCCHHHHHHHHHH | 22369663 | ||
| 559 | Phosphorylation | QSVPGNESEISQKNG HCCCCCHHHHHHHCC | 19779198 | ||
| 562 | Phosphorylation | PGNESEISQKNGSSL CCCHHHHHHHCCCCC | 27017623 | ||
| 590 | Phosphorylation | NDNDVVPSKEGSLLR CCCCCCCCCCCCEEE | 22369663 | ||
| 591 | Ubiquitination | DNDVVPSKEGSLLRC CCCCCCCCCCCEEEH | 23749301 | ||
| 594 | Phosphorylation | VVPSKEGSLLRCSEI CCCCCCCCEEEHHHH | 22369663 | ||
| 599 | Phosphorylation | EGSLLRCSEIWDRIT CCCEEEHHHHHHHHH | 21440633 |
| 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 AP1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of AP1_YEAST !! | ||||||
* 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 AP1_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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