| UniProt ID | BRR2_YEAST | |
|---|---|---|
| UniProt AC | P32639 | |
| Protein Name | Pre-mRNA-splicing helicase BRR2 | |
| Gene Name | BRR2 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 2163 | |
| Subcellular Localization | Nucleus . | |
| Protein Description | RNA helicase that plays an essential role in pre-mRNA splicing as component of the U5 snRNP and U4/U6-U5 tri-snRNP complexes. Involved in spliceosome assembly, activation and disassembly. Mediates changes in the dynamic network of RNA-RNA interactions in the spliceosome. Catalyzes the ATP-dependent unwinding of U4/U6 RNA duplices, an essential step in the assembly of a catalytically active spliceosome.. | |
| Protein Sequence | MTEHETKDKAKKIREIYRYDEMSNKVLKVDKRFMNTSQNPQRDAEISQPKSMSGRISAKDMGQGLCNNINKGLKENDVAVEKTGKSASLKKIQQHNTILNSSSDFRLHYYPKDPSNVETYEQILQWVTEVLGNDIPHDLIIGTADIFIRQLKENEENEDGNIEERKEKIQHELGINIDSLKFNELVKLMKNITDYETHPDNSNKQAVAILADDEKSDEEEVTEMSNNANVLGGEINDNEDDDEEYDYNDVEVNSKKKNKRALPNIENDIIKLSDSKTSNIESVPIYSIDEFFLQRKLRSELGYKDTSVIQDLSEKILNDIETLEHNPVALEQKLVDLLKFENISLAEFILKNRSTIFWGIRLAKSTENEIPNLIEKMVAKGLNDLVEQYKFRETTHSKRELDSGDDQPQSSEAKRTKFSNPAIPPVIDLEKIKFDESSKLMTVTKVSLPEGSFKRVKPQYDEIHIPAPSKPVIDYELKEITSLPDWCQEAFPSSETTSLNPIQSKVFHAAFEGDSNMLICAPTGSGKTNIALLTVLKALSHHYNPKTKKLNLSAFKIVYIAPLKALVQEQVREFQRRLAFLGIKVAELTGDSRLSRKQIDETQVLVSTPEKWDITTRNSNNLAIVELVRLLIIDEIHLLHDDRGPVLESIVARTFWASKYGQEYPRIIGLSATLPNYEDVGRFLRVPKEGLFYFDSSFRPCPLSQQFCGIKERNSLKKLKAMNDACYEKVLESINEGNQIIVFVHSRKETSRTATWLKNKFAEENITHKLTKNDAGSKQILKTEAANVLDPSLRKLIESGIGTHHAGLTRSDRSLSEDLFADGLLQVLVCTATLAWGVNLPAHTVIIKGTDVYSPEKGSWEQLSPQDVLQMLGRAGRPRYDTFGEGIIITDQSNVQYYLSVLNQQLPIESQFVSKLVDNLNAEVVAGNIKCRNDAVNWLAYTYLYVRMLASPMLYKVPDISSDGQLKKFRESLVHSALCILKEQELVLYDAENDVIEATDLGNIASSFYINHASMDVYNRELDEHTTQIDLFRIFSMSEEFKYVSVRYEEKRELKQLLEKAPIPIREDIDDPLAKVNVLLQSYFSQLKFEGFALNSDIVFIHQNAGRLLRAMFEICLKRGWGHPTRMLLNLCKSATTKMWPTNCPLRQFKTCPVEVIKRLEASTVPWGDYLQLETPAEVGRAIRSEKYGKQVYDLLKRFPKMSVTCNAQPITRSVMRFNIEIIADWIWDMNVHGSLEPFLLMLEDTDGDSILYYDVLFITPDIVGHEFTLSFTYELKQHNQNNLPPNFFLTLISENWWHSEFEIPVSFNGFKLPKKFPPPTPLLENISISTSELGNDDFSEVFEFKTFNKIQSQVFESLYNSNDSVFVGSGKGTGKTAMAELALLNHWRQNKGRAVYINPSGEKIDFLLSDWNKRFSHLAGGKIINKLGNDPSLNLKLLAKSHVLLATPVQFELLSRRWRQRKNIQSLELMIYDDAHEISQGVYGAVYETLISRMIFIATQLEKKIRFVCLSNCLANARDFGEWAGMTKSNIYNFSPSERIEPLEINIQSFKDVEHISFNFSMLQMAFEASAAAAGNRNSSSVFLPSRKDCMEVASAFMKFSKAIEWDMLNVEEEQIVPYIEKLTDGHLRAPLKHGVGILYKGMASNDERIVKRLYEYGAVSVLLISKDCSAFACKTDEVIILGTNLYDGAEHKYMPYTINELLEMVGLASGNDSMAGKVLILTSHNMKAYYKKFLIEPLPTESYLQYIIHDTLNNEIANSIIQSKQDCVDWFTYSYFYRRIHVNPSYYGVRDTSPHGISVFLSNLVETCLNDLVESSFIEIDDTEAEVTAEVNGGDDEATEIISTLSNGLIASHYGVSFFTIQSFVSSLSNTSTLKNMLYVLSTAVEFESVPLRKGDRALLVKLSKRLPLRFPEHTSSGSVSFKVFLLLQAYFSRLELPVDFQNDLKDILEKVVPLINVVVDILSANGYLNATTAMDLAQMLIQGVWDVDNPLRQIPHFNNKILEKCKEINVETVYDIMALEDEERDEILTLTDSQLAQVAAFVNNYPNVELTYSLNNSDSLISGVKQKITIQLTRDVEPENLQVTSEKYPFDKLESWWLVLGEVSKKELYAIKKVTLNKETQQYELEFDTPTSGKHNLTIWCVCDSYLDADKELSFEINVK | |
| 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 |
|---|---|---|---|---|---|
| 36 | Phosphorylation | VDKRFMNTSQNPQRD ECHHHCCCCCCCCCC | 21.65 | 30377154 | |
| 37 | Phosphorylation | DKRFMNTSQNPQRDA CHHHCCCCCCCCCCC | 23.97 | 30377154 | |
| 59 | Acetylation | MSGRISAKDMGQGLC CCCCCCHHHHCHHHH | 41.27 | 25381059 | |
| 88 | Phosphorylation | EKTGKSASLKKIQQH ECCCCCCCHHHHHHC | 48.05 | 28889911 | |
| 97 | Phosphorylation | KKIQQHNTILNSSSD HHHHHCCCCCCCCCC | 25.39 | 30377154 | |
| 101 | Phosphorylation | QHNTILNSSSDFRLH HCCCCCCCCCCCEEE | 27.98 | 30377154 | |
| 102 | Phosphorylation | HNTILNSSSDFRLHY CCCCCCCCCCCEEEE | 32.62 | 30377154 | |
| 103 | Phosphorylation | NTILNSSSDFRLHYY CCCCCCCCCCEEEEC | 40.36 | 30377154 | |
| 304 | Acetylation | LRSELGYKDTSVIQD HHHHCCCCCCHHHHH | 53.37 | 24489116 | |
| 403 | Phosphorylation | HSKRELDSGDDQPQS CCCCCCCCCCCCCCC | 57.66 | 25521595 | |
| 410 | Phosphorylation | SGDDQPQSSEAKRTK CCCCCCCCHHHHHHC | 36.51 | 21551504 | |
| 447 | Phosphorylation | LMTVTKVSLPEGSFK EEEEEEEECCCCCCC | 39.50 | 21551504 | |
| 597 | Acetylation | GDSRLSRKQIDETQV CCCCCCHHHCCCCEE | 48.51 | 24489116 | |
| 715 | Phosphorylation | CGIKERNSLKKLKAM CCCCCCCCHHHHHHC | 48.03 | 28889911 | |
| 795 | Acetylation | VLDPSLRKLIESGIG CCCHHHHHHHHCCCC | 60.14 | 24489116 | |
| 809 | Phosphorylation | GTHHAGLTRSDRSLS CCCCCCCCCCCCCCC | 27.49 | 30377154 | |
| 930 | Ubiquitination | EVVAGNIKCRNDAVN EEECCCCCCCCHHHH | 31.01 | 23749301 | |
| 955 | Phosphorylation | MLASPMLYKVPDISS HHHCCCCCCCCCCCC | 12.04 | 19779198 | |
| 961 | Phosphorylation | LYKVPDISSDGQLKK CCCCCCCCCCCHHHH | 29.74 | 19779198 | |
| 962 | Phosphorylation | YKVPDISSDGQLKKF CCCCCCCCCCHHHHH | 46.20 | 19779198 | |
| 1437 | Acetylation | NDPSLNLKLLAKSHV CCCCCCHHHHHHCCE | 40.14 | 24489116 | |
| 1881 | Phosphorylation | STLKNMLYVLSTAVE HHHHHHHHHHHHCEE | 6.64 | 27017623 | |
| 1884 | Phosphorylation | KNMLYVLSTAVEFES HHHHHHHHHCEEEEC | 12.32 | 27017623 | |
| 1885 | Phosphorylation | NMLYVLSTAVEFESV HHHHHHHHCEEEECC | 30.48 | 27017623 |
| 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 BRR2_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of BRR2_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 BRR2_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
loading...
| 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-403, 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 SER-403, AND MASSSPECTROMETRY. | |
