| UniProt ID | END3_YEAST | |
|---|---|---|
| UniProt AC | P39013 | |
| Protein Name | Actin cytoskeleton-regulatory complex protein END3 | |
| Gene Name | END3 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 349 | |
| Subcellular Localization |
Cell membrane Peripheral membrane protein Cytoplasmic side. Endosome membrane Peripheral membrane protein Cytoplasmic side. Cytoplasm, cytoskeleton, actin patch. Cytoplasmic and cortical actin patches. |
|
| Protein Description | Component of the PAN1 actin cytoskeleton-regulatory complex required for the internalization of endosomes during actin-coupled endocytosis. The complex links the site of endocytosis to the cell membrane-associated actin cytoskeleton. Mediates uptake of external molecules and vacuolar degradation of plasma membrane proteins. Plays a role in the proper organization of the cell membrane-associated actin cytoskeleton and promotes its destabilization. END3 regulates PAN1 function by preventing phosphorylation of PAN1 by PKR1 and is also involved in the correct localization of SLA1 to the cell cortex, in the bipolar budding of diploid cells and the correct distribution of chitin at the cell surface.. | |
| Protein Sequence | MPKLEQFEIKKYWQIFSGLKPIENKVNHDQVLPILYNSKLDSSVLNKIWFLADIDDDDNLDFEEFVICMRLIFDMVNKNISSVPDELPDWLIPGSKVNLIKERKKRKQIENADLPPKKEIKVDWYMSPDDLNQYEKIYNSCAKLTDGTITFNELSTKLSTKFFNISKTDLNKVWSLINPQNLPSIDRDPTFYFIHCLRQRNDLGAEIPASLPNSLAEVCNKKQLSYDLRSSQPPTKRKEEANEVDNLRDNGQNSSSDSSGSNVLSNEDSIKQKYASLTDDQVANMREQLEGLLNYKKSEKTQGGSKLSKRINIRSITDDLDNIEQQVEVLENYLNNKRHELQALQAEIN | |
| 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 |
|---|---|---|---|---|---|
| 39 | Ubiquitination | LPILYNSKLDSSVLN HHHHCCCCCCHHHHH | 53.31 | 24961812 | |
| 161 | Acetylation | LSTKLSTKFFNISKT HHHHHCCCCCCCCHH | 44.58 | 24489116 | |
| 225 | Phosphorylation | VCNKKQLSYDLRSSQ HHCHHHCCHHCCCCC | 17.69 | 30377154 | |
| 261 | Phosphorylation | SSSDSSGSNVLSNED CCCCCCCCCCCCCHH | 26.22 | 28889911 | |
| 273 | Acetylation | NEDSIKQKYASLTDD CHHHHHHHHHHCCHH | 37.47 | 24489116 | |
| 274 | Phosphorylation | EDSIKQKYASLTDDQ HHHHHHHHHHCCHHH | 10.03 | 25752575 | |
| 276 | Phosphorylation | SIKQKYASLTDDQVA HHHHHHHHCCHHHHH | 28.81 | 17330950 | |
| 278 | Phosphorylation | KQKYASLTDDQVANM HHHHHHCCHHHHHHH | 34.73 | 19795423 | |
| 296 | Succinylation | LEGLLNYKKSEKTQG HHHHHHHHHHCCCCC | 49.07 | 23954790 |
| 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 END3_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of END3_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 END3_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "A multidimensional chromatography technology for in-depthphosphoproteome analysis."; Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; Mol. Cell. Proteomics 7:1389-1396(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-274 AND SER-276, ANDMASS SPECTROMETRY. | |
