BBP1_YEAST - dbPTM
BBP1_YEAST - PTM Information in dbPTM
Basic Information of Protein
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
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
7Phosphorylation-MNQEDNTGGGGIFG
-CCCCCCCCCCCCCH
49.9128152593
19PhosphorylationIFGLFKWTKDALFGT
CCHHHHCCHHHHCCC
21.4528889911
26PhosphorylationTKDALFGTDISPSMK
CHHHHCCCCCCCCCC
23.8722369663
29PhosphorylationALFGTDISPSMKYKD
HHCCCCCCCCCCCCC
17.4622369663
31PhosphorylationFGTDISPSMKYKDQE
CCCCCCCCCCCCCHH
22.5522369663
51PhosphorylationSRYAQDDTNFSMKFG
HHHCCCCCCCCCCCC
46.5921700874
54PhosphorylationAQDDTNFSMKFGNDS
CCCCCCCCCCCCCCC
24.1128889911
61PhosphorylationSMKFGNDSNRRSTNL
CCCCCCCCCCCCCCC
35.9125704821
65PhosphorylationGNDSNRRSTNLSRSN
CCCCCCCCCCCCCCC
20.5722369663
66PhosphorylationNDSNRRSTNLSRSNS
CCCCCCCCCCCCCCC
38.0622369663
69PhosphorylationNRRSTNLSRSNSWSG
CCCCCCCCCCCCCCC
35.4122369663
71PhosphorylationRSTNLSRSNSWSGLD
CCCCCCCCCCCCCHH
31.6622369663
73PhosphorylationTNLSRSNSWSGLDST
CCCCCCCCCCCHHHH
24.7022369663
75PhosphorylationLSRSNSWSGLDSTLH
CCCCCCCCCHHHHHH
29.3322369663
98PhosphorylationYNENGFNSIVNGDHH
HCCCCCHHHCCCCCC
26.1721551504
106PhosphorylationIVNGDHHSKERIRSL
HCCCCCCCHHHHHHC
32.5621440633
112PhosphorylationHSKERIRSLRSPAPI
CCHHHHHHCCCCCCC
26.2628889911
115PhosphorylationERIRSLRSPAPIVPR
HHHHHCCCCCCCCCC
30.6117330950
143PhosphorylationRLHTKRRTINELSNS
HHHHCCCCHHHHHCC
31.9921440633
148PhosphorylationRRTINELSNSQIPFI
CCCHHHHHCCCCCCC
28.4027017623
150PhosphorylationTINELSNSQIPFIPP
CHHHHHCCCCCCCCC
26.5527017623
179PhosphorylationGVNEVRRSPYKLSVK
CCCCHHCCCCCCCCC
23.2425521595
181PhosphorylationNEVRRSPYKLSVKDI
CCHHCCCCCCCCCCC
26.3028889911
191AcetylationSVKDIPGKFPSPLTK
CCCCCCCCCCCCCCC
49.0724489116
194PhosphorylationDIPGKFPSPLTKRDE
CCCCCCCCCCCCHHH
35.3625521595
197PhosphorylationGKFPSPLTKRDEIDN
CCCCCCCCCHHHCCC
27.6725521595
205PhosphorylationKRDEIDNYYVRDEDA
CHHHCCCEEECCHHH
10.2921700874
206PhosphorylationRDEIDNYYVRDEDAC
HHHCCCEEECCHHHC
8.6821700874
234PhosphorylationFAQMDLNSRDLEDLC
HHHCCCCCCCHHHHH
34.1719779198
309PhosphorylationSHEAELATSRERLYQ
CHHHHHHHHHHHHHC
40.7321700874
310PhosphorylationHEAELATSRERLYQE
HHHHHHHHHHHHHCH
26.9121440633
333PhosphorylationQTLKQRLSDLELKYT
HHHHHHHHHHHHHHH
42.1928889911
374PhosphorylationRNNERKDTSAGSNIF
HCCCCCCCCCCCCCC
24.4220377248
375PhosphorylationNNERKDTSAGSNIFS
CCCCCCCCCCCCCCC
40.5422369663
378PhosphorylationRKDTSAGSNIFSTGQ
CCCCCCCCCCCCCCC
26.8622369663

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
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 !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BBP1_YEAST !!

Disease-associated PTM Sites based on SAP

* 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 !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MPS2_YEASTMPS2physical
10654940
SPC29_YEASTSPC29physical
10654940
KAR1_YEASTKAR1physical
10654940
BBP1_YEASTBBP1physical
11967834
KAR1_YEASTKAR1genetic
10654940
MPS2_YEASTMPS2genetic
10654940
POM34_YEASTPOM34genetic
19571182
SMY2_YEASTSMY2genetic
19571182
EAP1_YEASTEAP1genetic
19571182
SC160_YEASTSCP160genetic
19571182
CDC5_YEASTCDC5physical
15509790
BBP1_YEASTBBP1physical
20139001
MPS2_YEASTMPS2physical
20139001

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of BBP1_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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.

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