| UniProt ID | BNR1_YEAST | |
|---|---|---|
| UniProt AC | P40450 | |
| Protein Name | BNI1-related protein 1 | |
| Gene Name | BNR1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 1375 | |
| Subcellular Localization | ||
| Protein Description | May organize microtubules by mediating spindle positioning and movement in the budding process. Potential target of the RHO family members (By similarity).. | |
| Protein Sequence | MDSSPNKKTYRYPRRSLSLHARDRVSEARKLEELNLNDGLVAAGLQLVGVALEKQGTGSHIYMKQKNFSANDVSSSPMVSEEVNGSEMDFNPKCMPQDASLVERMFDELLKDGTFFWGAAYKNLQNISLRRKWLLICKIRSSNHWGKKKVTSSTTYSTHLATNELAENAHFLDGLVRNLSTGGMKLSKALYKLEKFLRKQSFLQLFLKDEIYLTTLIEKTLPLISKELQFVYLRCFKILMNNPLARIRALHSEPLIRWFTELLTDQNSNLKCQLLSMELLLLLTYVEGSTGCELIWDQLSILFTDWLEWFDKILADDIAIHSSLYLNWNQLKIDYSTTFLLLINSILQGFNNKTALEILNFLKKNNIHNTITFLELAYKDDPNSVVIMEQIKQFKSKESAIFDSMIKTTNDTNSLHPTKDIARIESEPLCLENCLLLKAKDSPVEAPINEIIQSLWKILDSQKPYSESIKLLKLINSLLFYLIDSFQVSTNPSFDETLESAENVDYVFQDSVNKLLDSLQSDEIARRAVTEIDDLNAKISHLNEKLNLVENHDKDHLIAKLDESESLISLKTKEIENLKLQLKATKKRLDQITTHQRLYDQPPSLASSNLSIAGSIIKNNSHGNIIFQNLAKKQQQQQKISLPKRSTSLLKSKRVTSLSSYLTDANNENESQNESEDKSKDSLFQRSTSTINFNIPSMKNITNMQNVSLNSILSELEFSNSLGTQPNYQSSPVLSSVSSSPKLFPRLSSDSLDNGIQLVPEVVKLPQLPPPPPPPPPPPLPQSLLTEAEAKPDGVSCIAAPAPPPLPDLFKTKTCGAVPPPPPPPPLPESLSMNKGPSNHDLVTPPAPPLPNGLLSSSSVSINPTTTDLKPPPTEKRLKQIHWDKVEDIKDTLWEDTFQRQETIKELQTDGIFSQIEDIFKMKSPTKIANKRNAESSIALSSNNGKSSNELKKISFLSRDLAQQFGINLHMFSQLSDMEFVMKVLNCDNDIVQNVNILKFFCKEELVNIPKSMLNKYEPYSQGKDGKAVSDLQRADRIFLELCINLRFYWNARSKSLLTLSTYERDYYDLIFKLQKIDDAISHLNRSPKFKSLMFIITEIGNHMNKRIVKGIKLKSLTKLAFVRSSIDQNVSFLHFIEKVIRIKYPDIYGFVDDLKNIEDLGKISLEHVESECHEFHKKIEDLVTQFQVGKLSKEENLDPRDQIIKKVKFKINRAKTKSELLIGQCKLTLIDLNKLMKYYGEDPKDKESKNEFFQPFIEFLAMFKKCAKENIEKEEMERVYEQRKSLLDMRTSSNKKSNGSDENDGEKVNRDAVDLLISKLREVKKDPEPLRRRKSTKLNEIAINVHEGDVKTRKDEDHVLLERTHAMLNDIQNI | |
| 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 |
|---|---|---|---|---|---|
| 3 | Phosphorylation | -----MDSSPNKKTY -----CCCCCCCCCC | 60.60 | 30377154 | |
| 4 | Phosphorylation | ----MDSSPNKKTYR ----CCCCCCCCCCC | 44.84 | 27717283 | |
| 18 | Phosphorylation | RYPRRSLSLHARDRV CCCCHHHHHHHHHHH | 21.25 | 25533186 | |
| 69 | Phosphorylation | YMKQKNFSANDVSSS EEEECCCCCCCCCCC | 35.24 | 21440633 | |
| 74 | Phosphorylation | NFSANDVSSSPMVSE CCCCCCCCCCCCCCC | 28.14 | 21551504 | |
| 76 | Phosphorylation | SANDVSSSPMVSEEV CCCCCCCCCCCCCCC | 14.98 | 27738172 | |
| 414 | Phosphorylation | KTTNDTNSLHPTKDI CCCCCCCCCCCCCCC | 30.10 | 23749301 | |
| 569 | Phosphorylation | DESESLISLKTKEIE CCCCCCEECCHHHHH | 29.16 | 28889911 | |
| 572 | Phosphorylation | ESLISLKTKEIENLK CCCEECCHHHHHHHH | 38.92 | 28889911 | |
| 607 | Phosphorylation | DQPPSLASSNLSIAG CCCCCHHCCCCEEEC | 25.67 | 30377154 | |
| 608 | Phosphorylation | QPPSLASSNLSIAGS CCCCHHCCCCEEECC | 35.86 | 29734811 | |
| 611 | Phosphorylation | SLASSNLSIAGSIIK CHHCCCCEEECCHHC | 18.03 | 30377154 | |
| 621 | Phosphorylation | GSIIKNNSHGNIIFQ CCHHCCCCCCCHHHH | 42.01 | 22369663 | |
| 646 | Phosphorylation | KISLPKRSTSLLKSK CCCCCHHHHHHHHHC | 28.60 | 21440633 | |
| 647 | Phosphorylation | ISLPKRSTSLLKSKR CCCCHHHHHHHHHCC | 27.68 | 21440633 | |
| 648 | Phosphorylation | SLPKRSTSLLKSKRV CCCHHHHHHHHHCCC | 32.71 | 21440633 | |
| 656 | Phosphorylation | LLKSKRVTSLSSYLT HHHHCCCCCHHHHHH | 28.16 | 23749301 | |
| 657 | Phosphorylation | LKSKRVTSLSSYLTD HHHCCCCCHHHHHHH | 24.32 | 21551504 | |
| 659 | Phosphorylation | SKRVTSLSSYLTDAN HCCCCCHHHHHHHCC | 19.39 | 28889911 | |
| 663 | Phosphorylation | TSLSSYLTDANNENE CCHHHHHHHCCCCCC | 25.49 | 27017623 | |
| 671 | Phosphorylation | DANNENESQNESEDK HCCCCCCCCCCCCCC | 50.30 | 21440633 | |
| 675 | Phosphorylation | ENESQNESEDKSKDS CCCCCCCCCCCCHHH | 59.66 | 24961812 | |
| 682 | Phosphorylation | SEDKSKDSLFQRSTS CCCCCHHHHHHHHHC | 34.52 | 24961812 | |
| 687 | Phosphorylation | KDSLFQRSTSTINFN HHHHHHHHHCEEECC | 18.87 | 21440633 | |
| 688 | Phosphorylation | DSLFQRSTSTINFNI HHHHHHHHCEEECCC | 31.88 | 20377248 | |
| 689 | Phosphorylation | SLFQRSTSTINFNIP HHHHHHHCEEECCCC | 28.65 | 28152593 | |
| 690 | Phosphorylation | LFQRSTSTINFNIPS HHHHHHCEEECCCCC | 21.74 | 25752575 | |
| 748 | Phosphorylation | PKLFPRLSSDSLDNG CCCCCCCCCCCCCCC | 33.12 | 21440633 | |
| 749 | Phosphorylation | KLFPRLSSDSLDNGI CCCCCCCCCCCCCCC | 35.49 | 21440633 | |
| 751 | Phosphorylation | FPRLSSDSLDNGIQL CCCCCCCCCCCCCCC | 39.30 | 28889911 | |
| 838 | Phosphorylation | LSMNKGPSNHDLVTP HCCCCCCCCCCCCCC | 56.30 | 20377248 | |
| 844 | Phosphorylation | PSNHDLVTPPAPPLP CCCCCCCCCCCCCCC | 30.74 | 24961812 | |
| 936 | Phosphorylation | ANKRNAESSIALSSN CCCCCCCCCEECCCC | 25.32 | 21440633 | |
| 937 | Phosphorylation | NKRNAESSIALSSNN CCCCCCCCEECCCCC | 11.91 | 27017623 | |
| 1294 | Phosphorylation | LLDMRTSSNKKSNGS HHHHCCCCCCCCCCC | 52.64 | 21440633 |
| 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 BNR1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of BNR1_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 BNR1_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-18; SER-687 AND SER-936,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-621, AND MASSSPECTROMETRY. | |