UniProt ID | IBD2_YEAST | |
---|---|---|
UniProt AC | P53892 | |
Protein Name | Protein IBD2 | |
Gene Name | IBD2 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 351 | |
Subcellular Localization | Cytoplasm, cytoskeleton, spindle pole . | |
Protein Description | Part of a checkpoint which monitors spindle integrity and prevents premature exit from mitosis. This cell-cycle arrest depends upon inhibition of the G-protein TEM1 by the BFA1/BUB2 complex.. | |
Protein Sequence | MTPTNQSSGTTNASVEVLSEDGPMPINVMMQEGVKALTKILSNQLQDRQAFQNAPHAMQFVIRNGGKALSNARLEELKDALPKMDSLSLEDELAKIDGQSAYHIDSAEEKETFESKIGQIASRNSADFIIEEDLQNILDDDLKDSELNLDGEEAEIIFDYESQELDTPDGIGEKISQMIESVLPGGFGSEEQGGLRTVTNVEDLDVAEEVTDIDHDTVDAARLHGDGQHSISSRKHSRSKNSKKNGHVRRHDFYDESRDHKSCCPHHHYENLSKLRNYYYHDFEYISRTENRVPDFSVLVNESSPMCLFCEYYMVFGEPPRNMIKWYNRTFGYNRMPNPPRDEQDSRKRNR | |
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 | ------MTPTNQSSG ------CCCCCCCCC | 38.53 | 30377154 | |
4 | Phosphorylation | ----MTPTNQSSGTT ----CCCCCCCCCCC | 36.40 | 30377154 | |
7 | Phosphorylation | -MTPTNQSSGTTNAS -CCCCCCCCCCCCCE | 32.57 | 30377154 | |
38 | Phosphorylation | QEGVKALTKILSNQL HHHHHHHHHHHHHHH | 22.39 | 30377154 | |
42 | Phosphorylation | KALTKILSNQLQDRQ HHHHHHHHHHHHHHH | 26.46 | 28152593 | |
70 | Phosphorylation | RNGGKALSNARLEEL CCCCCHHHHHCHHHH | 33.05 | 21440633 | |
86 | Phosphorylation | DALPKMDSLSLEDEL HHHHHCCCCCHHHHH | 19.16 | 30377154 | |
88 | Phosphorylation | LPKMDSLSLEDELAK HHHCCCCCHHHHHHH | 33.39 | 30377154 | |
100 | Phosphorylation | LAKIDGQSAYHIDSA HHHHCCCCEEECCCH | 36.00 | 22890988 | |
102 | Phosphorylation | KIDGQSAYHIDSAEE HHCCCCEEECCCHHH | 12.45 | 22890988 | |
106 | Phosphorylation | QSAYHIDSAEEKETF CCEEECCCHHHHHHH | 36.66 | 22369663 | |
112 | Phosphorylation | DSAEEKETFESKIGQ CCHHHHHHHHHHHHH | 43.71 | 19779198 | |
115 | Phosphorylation | EEKETFESKIGQIAS HHHHHHHHHHHHHHH | 25.94 | 28889911 | |
125 | Phosphorylation | GQIASRNSADFIIEE HHHHHCCCCCEEEHH | 28.27 | 28889911 | |
211 | Phosphorylation | LDVAEEVTDIDHDTV CCHHHEECCCCCCHH | 30.43 | 22369663 | |
217 | Phosphorylation | VTDIDHDTVDAARLH ECCCCCCHHHHHHHC | 19.50 | 22369663 | |
230 | Phosphorylation | LHGDGQHSISSRKHS HCCCCCCCCCCCCCC | 19.11 | 28889911 | |
232 | Phosphorylation | GDGQHSISSRKHSRS CCCCCCCCCCCCCCC | 27.40 | 28889911 |
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 IBD2_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of IBD2_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 IBD2_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-42; TYR-102; SER-106;THR-211 AND SER-230, 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-106, AND MASSSPECTROMETRY. |