UniProt ID | BBP1_YEAST | |
---|---|---|
UniProt AC | Q12365 | |
Protein Name | Spindle pole component BBP1 | |
Gene Name | BBP1 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 385 | |
Subcellular Localization | Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body . Associates with the periphary of the central plaque. | |
Protein Description | Component of the spindle pole body (SPB) required for insertion of the nascent SPB into the nuclear envelope and for the proper execution of spindle pole body (SPB) duplication. Connects the central plaque of the SPB with the half-bridge. Required for proper localization of CDC5 at the SPB and for proper M-phase progression.. | |
Protein Sequence | MNQEDNTGGGGIFGLFKWTKDALFGTDISPSMKYKDQEERRDRSRYAQDDTNFSMKFGNDSNRRSTNLSRSNSWSGLDSTLHRKYELLPEYNENGFNSIVNGDHHSKERIRSLRSPAPIVPREPLRNEPTDTFGHRLHTKRRTINELSNSQIPFIPPQEDDPLLSKLFNKDGVNEVRRSPYKLSVKDIPGKFPSPLTKRDEIDNYYVRDEDACHKNREYKKAYFDLFAQMDLNSRDLEDLCEDVREQREQFHRNEQTYKQAYEEMRAELVNELKKSKTLFENYYSLGQKYKSLKKVLDQTISHEAELATSRERLYQEEDLKNFEIQTLKQRLSDLELKYTNLQIEKDMQRDNYESEIHDLLLQLSLRNNERKDTSAGSNIFSTGQ | |
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 | -MNQEDNTGGGGIFG -CCCCCCCCCCCCCH | 49.91 | 28152593 | |
19 | Phosphorylation | IFGLFKWTKDALFGT CCHHHHCCHHHHCCC | 21.45 | 28889911 | |
26 | Phosphorylation | TKDALFGTDISPSMK CHHHHCCCCCCCCCC | 23.87 | 22369663 | |
29 | Phosphorylation | ALFGTDISPSMKYKD HHCCCCCCCCCCCCC | 17.46 | 22369663 | |
31 | Phosphorylation | FGTDISPSMKYKDQE CCCCCCCCCCCCCHH | 22.55 | 22369663 | |
51 | Phosphorylation | SRYAQDDTNFSMKFG HHHCCCCCCCCCCCC | 46.59 | 21700874 | |
54 | Phosphorylation | AQDDTNFSMKFGNDS CCCCCCCCCCCCCCC | 24.11 | 28889911 | |
61 | Phosphorylation | SMKFGNDSNRRSTNL CCCCCCCCCCCCCCC | 35.91 | 25704821 | |
65 | Phosphorylation | GNDSNRRSTNLSRSN CCCCCCCCCCCCCCC | 20.57 | 22369663 | |
66 | Phosphorylation | NDSNRRSTNLSRSNS CCCCCCCCCCCCCCC | 38.06 | 22369663 | |
69 | Phosphorylation | NRRSTNLSRSNSWSG CCCCCCCCCCCCCCC | 35.41 | 22369663 | |
71 | Phosphorylation | RSTNLSRSNSWSGLD CCCCCCCCCCCCCHH | 31.66 | 22369663 | |
73 | Phosphorylation | TNLSRSNSWSGLDST CCCCCCCCCCCHHHH | 24.70 | 22369663 | |
75 | Phosphorylation | LSRSNSWSGLDSTLH CCCCCCCCCHHHHHH | 29.33 | 22369663 | |
98 | Phosphorylation | YNENGFNSIVNGDHH HCCCCCHHHCCCCCC | 26.17 | 21551504 | |
106 | Phosphorylation | IVNGDHHSKERIRSL HCCCCCCCHHHHHHC | 32.56 | 21440633 | |
112 | Phosphorylation | HSKERIRSLRSPAPI CCHHHHHHCCCCCCC | 26.26 | 28889911 | |
115 | Phosphorylation | ERIRSLRSPAPIVPR HHHHHCCCCCCCCCC | 30.61 | 17330950 | |
143 | Phosphorylation | RLHTKRRTINELSNS HHHHCCCCHHHHHCC | 31.99 | 21440633 | |
148 | Phosphorylation | RRTINELSNSQIPFI CCCHHHHHCCCCCCC | 28.40 | 27017623 | |
150 | Phosphorylation | TINELSNSQIPFIPP CHHHHHCCCCCCCCC | 26.55 | 27017623 | |
179 | Phosphorylation | GVNEVRRSPYKLSVK CCCCHHCCCCCCCCC | 23.24 | 25521595 | |
181 | Phosphorylation | NEVRRSPYKLSVKDI CCHHCCCCCCCCCCC | 26.30 | 28889911 | |
191 | Acetylation | SVKDIPGKFPSPLTK CCCCCCCCCCCCCCC | 49.07 | 24489116 | |
194 | Phosphorylation | DIPGKFPSPLTKRDE CCCCCCCCCCCCHHH | 35.36 | 25521595 | |
197 | Phosphorylation | GKFPSPLTKRDEIDN CCCCCCCCCHHHCCC | 27.67 | 25521595 | |
205 | Phosphorylation | KRDEIDNYYVRDEDA CHHHCCCEEECCHHH | 10.29 | 21700874 | |
206 | Phosphorylation | RDEIDNYYVRDEDAC HHHCCCEEECCHHHC | 8.68 | 21700874 | |
234 | Phosphorylation | FAQMDLNSRDLEDLC HHHCCCCCCCHHHHH | 34.17 | 19779198 | |
309 | Phosphorylation | SHEAELATSRERLYQ CHHHHHHHHHHHHHC | 40.73 | 21700874 | |
310 | Phosphorylation | HEAELATSRERLYQE HHHHHHHHHHHHHCH | 26.91 | 21440633 | |
333 | Phosphorylation | QTLKQRLSDLELKYT HHHHHHHHHHHHHHH | 42.19 | 28889911 | |
374 | Phosphorylation | RNNERKDTSAGSNIF HCCCCCCCCCCCCCC | 24.42 | 20377248 | |
375 | Phosphorylation | NNERKDTSAGSNIFS CCCCCCCCCCCCCCC | 40.54 | 22369663 | |
378 | Phosphorylation | RKDTSAGSNIFSTGQ CCCCCCCCCCCCCCC | 26.86 | 22369663 |
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 BBP1_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of BBP1_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 BBP1_YEAST !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
MPS2_YEAST | MPS2 | physical | 10654940 | |
SPC29_YEAST | SPC29 | physical | 10654940 | |
KAR1_YEAST | KAR1 | physical | 10654940 | |
BBP1_YEAST | BBP1 | physical | 11967834 | |
KAR1_YEAST | KAR1 | genetic | 10654940 | |
MPS2_YEAST | MPS2 | genetic | 10654940 | |
POM34_YEAST | POM34 | genetic | 19571182 | |
SMY2_YEAST | SMY2 | genetic | 19571182 | |
EAP1_YEAST | EAP1 | genetic | 19571182 | |
SC160_YEAST | SCP160 | genetic | 19571182 | |
CDC5_YEAST | CDC5 | physical | 15509790 | |
BBP1_YEAST | BBP1 | physical | 20139001 | |
MPS2_YEAST | MPS2 | physical | 20139001 |
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 SER-71 AND SER-73, AND MASSSPECTROMETRY. | |
"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-115, AND MASSSPECTROMETRY. | |
"Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway."; Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.; Mol. Cell. Proteomics 4:310-327(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73, AND MASSSPECTROMETRY. |