| UniProt ID | BBP_YEAST | |
|---|---|---|
| UniProt AC | Q12186 | |
| Protein Name | Branchpoint-bridging protein | |
| Gene Name | MSL5 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 476 | |
| Subcellular Localization | Nucleus . | |
| Protein Description | Required for pre-spliceosome formation, which is the first step of pre-mRNA splicing. 2 commitment complexes, CC1 and CC2, have been defined. CC1 is a basal complex dependent only on the 5'-splice site. CC2 is a complex of lower mobility and is dependent on a branchpoint as well as a 5'-splice site region. This protein is involved in CC2 formation where it binds to the snRNP U1-associated protein PRP40, bridging the U1 snRNP-associated 5'-splice site and the MSL5-associated branch point 3' intron splice site. Involved in nuclear retention of pre-mRNA.. | |
| Protein Sequence | MSFRRINSRYFENRKGSSMEEKKAKVPPNVNLSLWRKNTVESDVHRFNSLPSKISGALTREQIYSYQVMFRIQEITIKLRTNDFVPPSRKNRSPSPPPVYDAQGKRTNTREQRYRKKLEDERIKLVEIALKTIPYFVPPDDYKRPTKFQDKYYIPVDQYPDVNFVGLLLGPRGRTLRKLQEDSNCKIAIRGRGSVKEGKNASDLPPGAMNFEDPLHCLIIADSEDKIQKGIKVCQNIVIKAVTSPEGQNDLKRGQLRELAELNGTLREDNRPCPICGLKDHKRYDCPNRKIPNIQGIVCKICGQTGHFSRDCNSSSQRMSRFDRNATVNNSAPIQSNDVHYNSNTHPIQAPKRSRYDNNSTEPPLKFPASSRYAPSPSPPASHISRQAQNVTPTPPPGLTSSSFSSGVPGIAPPPLQSPPESEQPKFSLPPPPGMTTVQSSIAPPPGLSGPPGFSNNMGNDINKPTPPGLQGPPGL | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 39 | Phosphorylation | LSLWRKNTVESDVHR HHHHCCCCHHCCHHH | 28.78 | 30377154 | |
| 49 | Phosphorylation | SDVHRFNSLPSKISG CCHHHHHCCCHHHCC | 38.66 | 30377154 | |
| 93 | Phosphorylation | PPSRKNRSPSPPPVY CCCCCCCCCCCCCCC | 38.84 | 22369663 | |
| 95 | Phosphorylation | SRKNRSPSPPPVYDA CCCCCCCCCCCCCCC | 51.81 | 22369663 | |
| 100 | Phosphorylation | SPSPPPVYDAQGKRT CCCCCCCCCCCCCCC | 16.01 | 22369663 | |
| 243 | Phosphorylation | NIVIKAVTSPEGQND HEEEEEECCCCCCCH | 43.34 | 23749301 | |
| 244 | Phosphorylation | IVIKAVTSPEGQNDL EEEEEECCCCCCCHH | 17.85 | 22369663 | |
| 327 | Phosphorylation | SRFDRNATVNNSAPI HHCCCCCCCCCCCCC | 27.58 | 28889911 | |
| 336 | Phosphorylation | NNSAPIQSNDVHYNS CCCCCCCCCCCCCCC | 35.40 | 19779198 | |
| 345 | Phosphorylation | DVHYNSNTHPIQAPK CCCCCCCCCCCCCCC | 28.93 | 19779198 | |
| 366 | Acetylation | NSTEPPLKFPASSRY CCCCCCCCCCCCCCC | 55.89 | 24489116 | |
| 373 | Phosphorylation | KFPASSRYAPSPSPP CCCCCCCCCCCCCCC | 25.47 | 22369663 | |
| 376 | Phosphorylation | ASSRYAPSPSPPASH CCCCCCCCCCCCHHH | 29.82 | 22369663 | |
| 378 | Phosphorylation | SRYAPSPSPPASHIS CCCCCCCCCCHHHHH | 48.10 | 22369663 | |
| 382 | Phosphorylation | PSPSPPASHISRQAQ CCCCCCHHHHHHHHC | 27.42 | 29136822 | |
| 385 | Phosphorylation | SPPASHISRQAQNVT CCCHHHHHHHHCCCC | 16.96 | 19779198 |
| 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 BBP_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of BBP_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 BBP_YEAST !! | ||||||
| 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-93; SER-95; SER-376 ANDSER-378, AND MASS SPECTROMETRY. | |
| "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 SER-93; SER-95; SER-376 ANDSER-378, AND MASS SPECTROMETRY. | |
