UniProt ID | LDB17_YEAST | |
---|---|---|
UniProt AC | Q12342 | |
Protein Name | Protein LDB17 | |
Gene Name | LDB17 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 491 | |
Subcellular Localization | Cytoplasm . Bud . Bud neck . | |
Protein Description | May be involved in protein-linked oligosaccharide phosphorylation since the deletion reduces the negative charge of the cell surface.. | |
Protein Sequence | MILDPLSPNIENHTQDEIIEFWEKTESIANIPKENLDESHVNSSLVAYLKFATDSYKVFINTDRDLYRMSLILLESSLFEFKKEFCLSKLQSLLNIDLLEMNMKFIIVYILLCEAKKNVYSLEIMLKFQGFTVFYNTLYTQFAYLSKYGKERTVASKHQYNSNNSSTGTSLDSLDRSLTDIDLGIIDEMKQISTVLMDLLFQIMKYCKCVIANLQIVDDFFVYYMMESMRSDTMDDMFNNAEFKLLLALNEQYMMFAKEYDIENKVYKYLINGSVSRCFTELLLLKFNRASDPPLQIMMCKIIYLILTPRGDYSPMNFFYTNDLRVLIDVLIRELQNISEDEEVLRNTLLRVLIPLLKNTQLSKTHYRKDDLNKLLNYLSTLDNICVDSPALHEHQVTVALSRKCLQQIPWLETPSTPSDGGSSVSSNNTSRNSSIVALGTPDNQNILARKGHLYSNRELDVSAESLTKRKAKAPPPPPPPPPSRKCGTPK | |
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 |
---|---|---|---|---|---|
7 | Phosphorylation | -MILDPLSPNIENHT -CCCCCCCCCCCCCC | 22.68 | 21440633 | |
434 | Phosphorylation | SNNTSRNSSIVALGT CCCCCCCCEEEEECC | 21.97 | 19779198 | |
435 | Phosphorylation | NNTSRNSSIVALGTP CCCCCCCEEEEECCC | 25.32 | 25752575 | |
441 | Phosphorylation | SSIVALGTPDNQNIL CEEEEECCCCCCCCH | 28.46 | 29688323 | |
455 | Phosphorylation | LARKGHLYSNRELDV HHHCCCCCCCCCCCC | 9.75 | 19823750 | |
456 | Phosphorylation | ARKGHLYSNRELDVS HHCCCCCCCCCCCCC | 35.45 | 19823750 | |
463 | Phosphorylation | SNRELDVSAESLTKR CCCCCCCCHHHHHCC | 26.45 | 22369663 | |
466 | Phosphorylation | ELDVSAESLTKRKAK CCCCCHHHHHCCCCC | 40.84 | 22369663 | |
468 | Phosphorylation | DVSAESLTKRKAKAP CCCHHHHHCCCCCCC | 37.77 | 22890988 |
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 LDB17_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of LDB17_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 LDB17_YEAST !! |
Kegg Drug | ||||||
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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 SER-7; SER-435; SER-463 ANDSER-466, AND MASS SPECTROMETRY. | |
"Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae."; Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.; J. Proteome Res. 6:1190-1197(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-463 AND SER-466, ANDMASS SPECTROMETRY. |