| UniProt ID | SWI1_YEAST | |
|---|---|---|
| UniProt AC | P09547 | |
| Protein Name | SWI/SNF chromatin-remodeling complex subunit SWI1 | |
| Gene Name | SWI1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 1314 | |
| Subcellular Localization | Nucleus . While the soluble protein is nuclear, [SWI+] aggregates appear to be cytoplasmic. | |
| Protein Description | Involved in transcriptional activation. Component of the SWI/SNF complex, an ATP-dependent chromatin remodeling complex, which is required for the positive and negative regulation of gene expression of a large number of genes. It changes chromatin structure by altering DNA-histone contacts within a nucleosome, leading eventually to a change in nucleosome position, thus facilitating or repressing binding of gene-specific transcription factors.. | |
| Protein Sequence | MDFFNLNNNNNNNNTTTTTTTTNNNNTNNNNTNNNNNPANNTNNNNSTGHSSNTNNNTNNNNTNTGASGVDDFQNFFDPKPFDQNLDSNNNNSNSNNNDNNNSNTVASSTNFTSPTAVVNNAAPANVTGGKAANFIQNQSPQFNSPYDSNNSNTNLNSLSPQAILAKNSIIDSSNLPLQAQQQLYGGNNNNNSTGIANDNVITPHFITNVQSISQNSSSSTPNTNSNSTPNANQQFLPFNNSASNNGNLTSNQLISNYAASNSMDRSSSASNEFVPNTSDNNNNSNNHNMRNNSNNKTSNNNNVTAVPAATPANTNNSTSNANTVFSERAAMFAALQQKQQQRFQALQQQQQQQQNQQQQNQQPQQQQQQQQNPKFLQSQRQQQQRSILQSLNPALQEKISTELNNKQYELFMKSLIENCKKRNMPLQSIPEIGNRKINLFYLYMLVQKFGGADQVTRTQQWSMVAQRLQISDYQQLESIYFRILLPYERHMISQEGIKETQAKRIFLQQFLQELLKKVQQQQQAAALANANNNINSASSAPTPAAPGASVPATAAPGTEAGIVPVSANTPKSLNSNININVNNNNIGQQQVKKPRKQRVKKKTKKELELERKEREDFQKRQQKLLEDQQRQQKLLLETKLRQQYEIELKKLPKVYKRSIVRNYKPLINRLKHYNGYDINYISKIGEKIDSNKPIFLFAPELGAINLHALSMSLQSKNLGEINTALNTLLVTSADSNLKISLVKYPELLDSLAILGMNLLSNLSQNVVPYHRNTSDYYYEDAGSNQYYVTQHDKMVDKIFEKVNNNATLTPNDSNDEKVTILVDSLTGNQLPTPTPTEMEPDLDTECFISMQSTSPAVKQWDLLPEPIRFLPNQFPLKIHRTPYLTSLKKIKDEIDDPFTKINTRGAEDPKVLINDQLSTISMILRNISFSDNNSRIMSRNFYLKRFISDLLWLVLIHPENFTCNRKILNFKKDLVIVLSNISHLLEIASSIDCLLILILVISFGQPKLNPMASSSSFGSESLTFNEFQLQWGKYQTFGVDILAKLFSLEKPNLNYFKSILLNKNTGNNLYDRNSNNNHKDKKLLRRLLNLYNDNNKNNNNRHNLLNDVVSFLFSAIPLQQVLSQSADPSLLIDQFSPVISQSLTSILVIVQKILPLSNEVFEISENNSDSNSNNNGNKDSSFNFNKNLPFVWLSSEENIGSGLLKLSEIILNINNSTSKNTLLQQQNYSKVLLPSINISCVQLIKCLVEKSICFENCLNNDPEILKKIASIPNLFPTDLEIFQLFTNPSVDIQIINQYQLLYNLKNDILTNLE | |
| 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 |
|---|---|---|---|---|---|
| 140 | Phosphorylation | ANFIQNQSPQFNSPY HHHHCCCCCCCCCCC | 28.37 | 21440633 | |
| 145 | Phosphorylation | NQSPQFNSPYDSNNS CCCCCCCCCCCCCCC | 26.56 | 21440633 | |
| 147 | Phosphorylation | SPQFNSPYDSNNSNT CCCCCCCCCCCCCCC | 31.65 | 21440633 | |
| 149 | Phosphorylation | QFNSPYDSNNSNTNL CCCCCCCCCCCCCCC | 31.87 | 21440633 | |
| 152 | Phosphorylation | SPYDSNNSNTNLNSL CCCCCCCCCCCCCCC | 49.64 | 21440633 | |
| 154 | Phosphorylation | YDSNNSNTNLNSLSP CCCCCCCCCCCCCCH | 40.69 | 28889911 | |
| 158 | Phosphorylation | NSNTNLNSLSPQAIL CCCCCCCCCCHHHHH | 33.13 | 21440633 | |
| 160 | Phosphorylation | NTNLNSLSPQAILAK CCCCCCCCHHHHHHC | 18.13 | 28152593 | |
| 267 | Phosphorylation | ASNSMDRSSSASNEF HHCCCCCCCCCCCCC | 25.12 | 22369663 | |
| 268 | Phosphorylation | SNSMDRSSSASNEFV HCCCCCCCCCCCCCC | 30.71 | 22369663 | |
| 269 | Phosphorylation | NSMDRSSSASNEFVP CCCCCCCCCCCCCCC | 36.64 | 22369663 | |
| 271 | Phosphorylation | MDRSSSASNEFVPNT CCCCCCCCCCCCCCC | 38.55 | 23749301 | |
| 278 | Phosphorylation | SNEFVPNTSDNNNNS CCCCCCCCCCCCCCC | 31.24 | 22369663 | |
| 279 | Phosphorylation | NEFVPNTSDNNNNSN CCCCCCCCCCCCCCC | 45.01 | 22369663 | |
| 399 | Ubiquitination | LNPALQEKISTELNN HCHHHHHHHHHHHCH | 29.06 | 24961812 | |
| 567 | Phosphorylation | EAGIVPVSANTPKSL CCEEEEECCCCCCCC | 15.10 | 27738172 | |
| 570 | Phosphorylation | IVPVSANTPKSLNSN EEEECCCCCCCCCCC | 31.63 | 27738172 | |
| 573 | Phosphorylation | VSANTPKSLNSNINI ECCCCCCCCCCCEEE | 33.71 | 24961812 | |
| 576 | Phosphorylation | NTPKSLNSNININVN CCCCCCCCCEEEECC | 44.36 | 24961812 | |
| 656 | Phosphorylation | LKKLPKVYKRSIVRN HHHCCHHHHHHHHHH | 13.55 | 21126336 | |
| 674 | Phosphorylation | LINRLKHYNGYDINY HHHHHHHCCCCCHHH | 14.54 | 19684113 | |
| 677 | Phosphorylation | RLKHYNGYDINYISK HHHHCCCCCHHHHHH | 15.26 | 19684113 | |
| 684 | Acetylation | YDINYISKIGEKIDS CCHHHHHHCCCCCCC | 45.21 | 22865919 | |
| 808 | Phosphorylation | EKVNNNATLTPNDSN HHHCCCCCCCCCCCC | 33.03 | 22369663 | |
| 810 | Phosphorylation | VNNNATLTPNDSNDE HCCCCCCCCCCCCCC | 18.72 | 22369663 | |
| 814 | Phosphorylation | ATLTPNDSNDEKVTI CCCCCCCCCCCEEEE | 53.47 | 22369663 | |
| 878 | Acetylation | LPNQFPLKIHRTPYL CCCCCCCEECCCCCH | 36.38 | 24489116 | |
| 1092 | Phosphorylation | LRRLLNLYNDNNKNN HHHHHHHHCCCCCCC | 21.28 | 27017623 | |
| 1165 | Phosphorylation | SNEVFEISENNSDSN CCCCEECCCCCCCCC | 27.37 | 30377154 | |
| 1169 | Phosphorylation | FEISENNSDSNSNNN EECCCCCCCCCCCCC | 54.73 | 21440633 | |
| 1171 | Phosphorylation | ISENNSDSNSNNNGN CCCCCCCCCCCCCCC | 41.81 | 21551504 | |
| 1173 | Phosphorylation | ENNSDSNSNNNGNKD CCCCCCCCCCCCCCC | 44.90 | 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 SWI1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SWI1_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 SWI1_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-152; THR-154 ANDSER-160, AND MASS SPECTROMETRY. | |
