UniProt ID | PIP2_YEAST | |
---|---|---|
UniProt AC | P52960 | |
Protein Name | Peroxisome proliferation transcriptional regulator | |
Gene Name | PIP2 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 996 | |
Subcellular Localization | Nucleus. | |
Protein Description | The PIP2-OAF1 heterodimer acts as a transcriptional activator to induce the transcription of genes encoding proteins involved in fatty acid beta-oxidation, a response called oleic acid induction, when cells grow on fatty acids as sole carbon source. Recognizes and binds to the oleate response element (ORE) (or peroxisome box), two inverted CGG triplets spaced by 14 to 18 intervening nucleotides, in the promoter region of a number of genes (such as CTA1, FOX1 to FOX3, FAA2, PAS8, PAS10, etc.) for peroxisomal proteins. Activity is inhibited by OAF1 under non-inducing conditions. Activity is repressed by glucose.. | |
Protein Sequence | MYFTDESSPAMNRVGKKRNRLSFVCQACRKAKTKCDQEKPRCGRCTKQNLFCIYDVARQAAPRNPNKDATIARLKKEIRYWRNKTVDLTQEKKDFYTALKRPTEELAARRTCKSLQENSFPISLYKTHPRLIMTKVMKREINPLSEKYLIFQDTFLKTLIASVLLSCSRNSMIPALNADISRSRTQPCVKNNVVKMREVLLKNSKYESQRKSINEFTDRLLQRKNPEEQIAVNKVISLLYSNRESSYLEDTCPTENDYSDLLKGYINEIEKTLPPKAIIEQYLSHFFEHIFHLIPFASKEMLEESIHTTVQYNELGEVRLSMGTTLIRNKMENLCILLLILRIAYISLTFIEDKIEDYSPYITKEMLEQYPIQSEVIFLAQQILASENWCACANENTISCLLYIWCAFVFSPTEGDFLLEQPSDVIINLVILIGTSIGLHRDPSDFPALNHPEASDKRLLNLRRIQWLSIISMATLESSLKGRLLVSPLSMIDLFIDVRDPNCVEIYKKRVKKDLTGSESDEQLLEIHEIFFHRAQLALFLSDLNNITISYSGSVPMDTLETLRVKANELLKNKFQLRSVDINIYDEEKTFQKLTFNSILNSISLSGQILGKLMMLRASIALMLYFETLAMERSECLSFFYKYFFQCCADTISLIRFFFLYFNGSYEKVLSSLVCFITTKVIQLAVPTTMFTLLVIIMRVELAKNMLLVKCNECNARGDISDLPEIKEKIKSLDTIKENFERLLLEVYLLASQNLRFKYFYIFKMLTLFDVFIQRLRKGQLFSGLFVKVDKDLTTKKIATMLELTLGINLDKSDHLIDRLKGKNLTVNFTLDQLYQIIKEFDRIKNIGVADPQNSLNPSKPNMKDNTPTIELLLNSSVENESVPPYSSSNDPTNVGNASTYSLAHNISNQNNEENMPPSIGSSESNRAAPNLNFMPINNNYNNSGSNINNNDNVKLPSNFKNYYDPPMSSLDISMDVPDIFGSLDFFDYDLLFQND | |
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 |
---|---|---|---|---|---|
2 | Phosphorylation | ------MYFTDESSP ------CCCCCCCCC | 18.39 | 28132839 | |
100 | Acetylation | KDFYTALKRPTEELA HHHHHHHHCCHHHHH | 54.59 | 24489116 | |
158 | Phosphorylation | FQDTFLKTLIASVLL CHHHHHHHHHHHHHH | 26.08 | 21126336 |
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 PIP2_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PIP2_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 PIP2_YEAST !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
OAF1_YEAST | OAF1 | physical | 12709061 | |
OAF1_YEAST | OAF1 | physical | 9288897 | |
PRI1_YEAST | PRI1 | genetic | 8668138 | |
OAF1_YEAST | OAF1 | physical | 18671944 | |
OAF1_YEAST | OAF1 | physical | 18285336 | |
YRM1_YEAST | YRM1 | genetic | 20959818 | |
YPT6_YEAST | YPT6 | genetic | 20959818 | |
CTK1_YEAST | CTK1 | genetic | 21127252 | |
MGA2_YEAST | MGA2 | genetic | 21127252 | |
GPR1_YEAST | GPR1 | genetic | 27708008 | |
UBC3_YEAST | CDC34 | genetic | 27708008 | |
BCP1_YEAST | BCP1 | genetic | 27708008 | |
SPC97_YEAST | SPC97 | genetic | 27708008 | |
CDC6_YEAST | CDC6 | genetic | 27708008 | |
CDC11_YEAST | CDC11 | genetic | 27708008 | |
SEC22_YEAST | SEC22 | genetic | 27708008 | |
CSG2_YEAST | CSG2 | genetic | 27708008 |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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