UniProt ID | YBP1_YEAST | |
---|---|---|
UniProt AC | P38315 | |
Protein Name | YAP1-binding protein 1 | |
Gene Name | YBP1 {ECO:0000303|PubMed:12743123} | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 674 | |
Subcellular Localization | Cytoplasm . | |
Protein Description | Involved in oxidative stress response and redox homeostasis. Required for hydrogen peroxide-induced oxidation and nuclear localization (activation) of YAP1. Functions probably in concert with HYP1/GPX3, the actual YAP1 modifying enzyme. YBP1 is not required for HYP1/GPX3-independent, diamide-induced oxidation of YAP1.. | |
Protein Sequence | MEPIDDILFEVTDAFKTQKEDLLELVTLIDIYGEQVNQEGSYEEKTRFIETLNTLLEDNPSTTGEIGWDLPKGLLKFLSKDNVDVNGRLGTNMIVQGVMKCFYAISIQGEPKKCLITGLELLSSLCSKDFSKSDQQNKEDFVDKKANTLPPEGVIENSSNRKDFPSYGESKSSNEFFLKLKSYILFEFIGASLKRISTLFPSKYLGAAVSTIEKFVYSHADTFEDALFLLRRVYTFCRNYIPPDPPKDIQLNEDFTREMFDKVVEEESELQVRLLRRLCTFGISTPIKTVTTNADVKYYCALNQQKFELSAYYTEYLELFCRYYQMAFSLDVDIEGEFQNVIKECRIIYKSVPQEISAVNDEAKLVLERMVYKLAYTFEVQKAAKEKNVGLDYNGVILFSGIHYLETNQHLVKEMNITDAIYLYLRFTTPSLYSKVYYNVAVESVSRYWLWYAITTEPLEDVKKELKNLSVFVTKTLLHVLLQKNCIQVNQQLRMITFTLLTRLLCLIPEKVAFEFILDVLKTSPLPLAKTSVLCVFKDLSRRRISTKDNDSETDLIVEKLSKLKVNDSNKAQQSNIRHYIQLDSSKMKAVHDCCLQTIQDSFTADAKKSDILLLLTYLNIFIVLKKTWDEDLLKIVCSKIDSNLKSVEPDKLPKYKEIVDKNESLNDYFTGIK | |
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 |
---|---|---|---|---|---|
76 | Acetylation | DLPKGLLKFLSKDNV CCCHHHHHHHCCCCC | 49.67 | 24489116 | |
80 | Acetylation | GLLKFLSKDNVDVNG HHHHHHCCCCCCCCC | 56.31 | 24489116 | |
112 | Ubiquitination | ISIQGEPKKCLITGL HHCCCCCCEEEHHHH | 52.39 | 17644757 | |
113 | Ubiquitination | SIQGEPKKCLITGLE HCCCCCCEEEHHHHH | 45.01 | 17644757 | |
128 | Ubiquitination | LLSSLCSKDFSKSDQ HHHHHHCCCCCHHHH | 62.89 | 17644757 | |
132 | Ubiquitination | LCSKDFSKSDQQNKE HHCCCCCHHHHCCHH | 59.03 | 17644757 | |
138 | Ubiquitination | SKSDQQNKEDFVDKK CHHHHCCHHHHHCCC | 55.08 | 17644757 | |
144 | Ubiquitination | NKEDFVDKKANTLPP CHHHHHCCCCCCCCC | 48.78 | 17644757 | |
145 | Ubiquitination | KEDFVDKKANTLPPE HHHHHCCCCCCCCCC | 42.26 | 17644757 | |
197 | Phosphorylation | GASLKRISTLFPSKY HHHHHHHHHHCCHHH | 24.08 | 26447709 | |
198 | Phosphorylation | ASLKRISTLFPSKYL HHHHHHHHHCCHHHH | 30.01 | 26447709 | |
202 | Phosphorylation | RISTLFPSKYLGAAV HHHHHCCHHHHHHHH | 26.97 | 26447709 | |
204 | Phosphorylation | STLFPSKYLGAAVST HHHCCHHHHHHHHHH | 18.08 | 26447709 | |
218 | Phosphorylation | TIEKFVYSHADTFED HHHHHHHHCCCCHHH | 13.59 | 27017623 | |
284 | Phosphorylation | RLCTFGISTPIKTVT HHHHCCCCCCCEEEE | 28.63 | 27017623 | |
538 | Acetylation | TSVLCVFKDLSRRRI HHEEEEECCCCCCCC | 37.04 | 24489116 | |
548 | Acetylation | SRRRISTKDNDSETD CCCCCCCCCCCCCHH | 47.98 | 24489116 | |
552 | Phosphorylation | ISTKDNDSETDLIVE CCCCCCCCCHHHHHH | 48.96 | 21440633 | |
554 | Phosphorylation | TKDNDSETDLIVEKL CCCCCCCHHHHHHHH | 39.80 | 24961812 | |
560 | Acetylation | ETDLIVEKLSKLKVN CHHHHHHHHHCCCCC | 47.36 | 24489116 | |
669 | Phosphorylation | KNESLNDYFTGIK-- CCCCHHHHHCCCC-- | 11.28 | 19684113 | |
671 | Phosphorylation | ESLNDYFTGIK---- CCHHHHHCCCC---- | 31.59 | 19684113 |
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 YBP1_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of YBP1_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 YBP1_YEAST !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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