UniProt ID | BCP1_YEAST | |
---|---|---|
UniProt AC | Q06338 | |
Protein Name | Protein BCP1 | |
Gene Name | BCP1 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 283 | |
Subcellular Localization | Cytoplasm . Nucleus . | |
Protein Description | Involved in nuclear export of the lipid kinase MSS4 and of the 60S ribosomal subunit. May also play a role in directing MSS4 to the plasma membrane. Plays a role in actin cytoskeleton organization and vesicular transport.. | |
Protein Sequence | MVQAIKLNDLKNRKRKNVEEENGSDESEIDISSTDSENEEEQNGEEEIVNIDFDFFGGNPEVDFHALKNLLRQLFGPQESTRIQLSSLADLILGSPTTTIKTDGKESDPYCFLSFVDFKANHLSDYVKYLQKVDMRLSTFFKTMIDSGNKNCALVLSERLINMPPEVVPPLYKITLEDVATALGDDKHYDFYIIVTRKYEVNFDTDDDTDSGKRNKNKDERSKKRVKADEVDYFHEEDRFFEKYAKIHFESEAKKGVISSYMILDHEGLVKSIDELETEISTW | |
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 |
---|---|---|---|---|---|
11 | Acetylation | AIKLNDLKNRKRKNV EEEHHHHHHHCCCCC | 58.53 | 25381059 | |
114 | Phosphorylation | SDPYCFLSFVDFKAN CCCEEEEEEEECHHH | 11.72 | 19779198 | |
128 | Acetylation | NHLSDYVKYLQKVDM HCHHHHHHHHHHHHH | 33.73 | 24489116 | |
199 | Phosphorylation | YIIVTRKYEVNFDTD EEEEEEEEEEECCCC | 23.09 | 28889911 | |
205 | Phosphorylation | KYEVNFDTDDDTDSG EEEEECCCCCCCCCC | 36.87 | 22369663 | |
209 | Phosphorylation | NFDTDDDTDSGKRNK ECCCCCCCCCCCCCC | 38.77 | 22369663 | |
211 | Phosphorylation | DTDDDTDSGKRNKNK CCCCCCCCCCCCCCH | 48.59 | 22369663 | |
213 | Acetylation | DDDTDSGKRNKNKDE CCCCCCCCCCCCHHH | 57.67 | 24489116 | |
272 | Phosphorylation | DHEGLVKSIDELETE CCCCHHCCHHHHHHH | 28.00 | 30377154 |
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 BCP1_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of BCP1_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 BCP1_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 THR-205, AND MASSSPECTROMETRY. | |
"Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases."; Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.; Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-205 AND THR-209, ANDMASS 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 THR-205 AND THR-209, ANDMASS SPECTROMETRY. |