| UniProt ID | ISW1_YEAST | |
|---|---|---|
| UniProt AC | P38144 | |
| Protein Name | ISWI chromatin-remodeling complex ATPase ISW1 | |
| Gene Name | ISW1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 1129 | |
| Subcellular Localization | Nucleus . | |
| Protein Description | Catalytic component of ISW1-type complexes, which act by remodeling the chromatin by catalyzing an ATP-dependent alteration in the structure of nucleosomal DNA. They are involved in coordinating transcriptional repression, activation and elongation phases. The ISW1A complex represses gene expression at initiation through specific positioning of a promoter proximal dinucleosome. The ISW1B complex acts within coding regions to control the amount of RNA polymerase II released into productive elongation and to coordinate elongation with termination and pre-mRNA processing.. | |
| Protein Sequence | MAYMLAIANFHFFKFYTRMRKKHENNSCNEKDKDENLFKIILAIFLQEKKKYDCISSGSIMTASEEYLENLKPFQVGLPPHDPESNKKRYLLKDANGKKFDLEGTTKRFEHLLSLSGLFKHFIESKAAKDPKFRQVLDVLEENKANGKGKGKHQDVRRRKTEHEEDAELLKEEDSDDDESIEFQFRESPAYVNGQLRPYQIQGVNWLVSLHKNKIAGILADEMGLGKTLQTISFLGYLRYIEKIPGPFLVIAPKSTLNNWLREINRWTPDVNAFILQGDKEERAELIQKKLLGCDFDVVIASYEIIIREKSPLKKINWEYIIIDEAHRIKNEESMLSQVLREFTSRNRLLITGTPLQNNLHELWALLNFLLPDIFSDAQDFDDWFSSESTEEDQDKIVKQLHTVLQPFLLRRIKSDVETSLLPKKELNLYVGMSSMQKKWYKKILEKDLDAVNGSNGSKESKTRLLNIMMQLRKCCNHPYLFDGAEPGPPYTTDEHLVYNAAKLQVLDKLLKKLKEEGSRVLIFSQMSRLLDILEDYCYFRNYEYCRIDGSTAHEDRIQAIDDYNAPDSKKFVFLLTTRAGGLGINLTSADVVVLYDSDWNPQADLQAMDRAHRIGQKKQVKVFRLVTDNSVEEKILERATQKLRLDQLVIQQNRTSLKKKENKADSKDALLSMIQHGAADVFKSGTSTGSAGTPEPGSGEKGDDIDLDELLLKSENKTKSLNAKYETLGLDDLQKFNQDSAYEWNGQDFKKKIQRDIISPLLLNPTKRERKENYSIDNYYKDVLNTGRSSTPSHPRMPKPHVFHSHQLQPPQLKVLYEKERMWTAKKTGYVPTMDDVKAAYGDISDEEEKKQKLELLKLSVNNSQPLTEEEEKMKADWESEGFTNWNKLEFRKFITVSGKYGRNSIQAIARELAPGKTLEEVRAYAKAFWSNIERIEDYEKYLKIIENEEEKIKRVKMQQEALRRKLSEYKNPFFDLKLKHPPSSNNKRTYSEEEDRFILLMLFKYGLDRDDVYELVRDEIRDCPLFELDFYFRSRTPVELARRGNTLLQCLEKEFNAGIVLDDATKDRMKKEDENGKRIREEFADQTANEKENVDGVESKKAKIEDTSNVGTEQLVAEKIPENETTH | |
| 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 |
|---|---|---|---|---|---|
| 14 | Methylation | IANFHFFKFYTRMRK HHHHHHHHHHHHHHH | 36.20 | 20137074 | |
| 14 | Acetylation | IANFHFFKFYTRMRK HHHHHHHHHHHHHHH | 36.20 | 25381059 | |
| 150 | Acetylation | NKANGKGKGKHQDVR HHHCCCCCCCHHHHH | 69.17 | 25381059 | |
| 152 | Acetylation | ANGKGKGKHQDVRRR HCCCCCCCHHHHHHH | 41.39 | 25381059 | |
| 161 | Phosphorylation | QDVRRRKTEHEEDAE HHHHHHHCCCHHHHH | 40.54 | 28889911 | |
| 175 | Phosphorylation | ELLKEEDSDDDESIE HHHHHCCCCCCCCCE | 46.34 | 22369663 | |
| 180 | Phosphorylation | EDSDDDESIEFQFRE CCCCCCCCCEEEEEC | 34.12 | 29734811 | |
| 280 | Acetylation | AFILQGDKEERAELI EEHHCCCHHHHHHHH | 69.19 | 24489116 | |
| 330 | Acetylation | IDEAHRIKNEESMLS EECHHHHCCHHHHHH | 59.26 | 24489116 | |
| 415 | Phosphorylation | FLLRRIKSDVETSLL HHHHHHHCCCCHHCC | 44.51 | 28889911 | |
| 430 | Phosphorylation | PKKELNLYVGMSSMQ CHHHHHHEECCHHHH | 8.22 | 19779198 | |
| 434 | Phosphorylation | LNLYVGMSSMQKKWY HHHEECCHHHHHHHH | 19.41 | 19779198 | |
| 447 | Acetylation | WYKKILEKDLDAVNG HHHHHHHHHHHHHCC | 61.21 | 24489116 | |
| 455 | Phosphorylation | DLDAVNGSNGSKESK HHHHHCCCCCCHHHH | 32.58 | 30377154 | |
| 635 | Acetylation | TDNSVEEKILERATQ CCCCHHHHHHHHHHH | 38.80 | 24489116 | |
| 667 | Phosphorylation | KKENKADSKDALLSM HHCCCCCHHHHHHHH | 36.98 | 28889911 | |
| 668 | Acetylation | KENKADSKDALLSMI HCCCCCHHHHHHHHH | 47.79 | 24489116 | |
| 673 | Phosphorylation | DSKDALLSMIQHGAA CHHHHHHHHHHHCCH | 18.06 | 17563356 | |
| 685 | Phosphorylation | GAADVFKSGTSTGSA CCHHHHCCCCCCCCC | 35.52 | 22890988 | |
| 687 | Phosphorylation | ADVFKSGTSTGSAGT HHHHCCCCCCCCCCC | 30.15 | 22890988 | |
| 688 | Phosphorylation | DVFKSGTSTGSAGTP HHHCCCCCCCCCCCC | 34.01 | 22890988 | |
| 689 | Phosphorylation | VFKSGTSTGSAGTPE HHCCCCCCCCCCCCC | 34.69 | 22890988 | |
| 691 | Phosphorylation | KSGTSTGSAGTPEPG CCCCCCCCCCCCCCC | 24.50 | 22890988 | |
| 694 | Phosphorylation | TSTGSAGTPEPGSGE CCCCCCCCCCCCCCC | 24.97 | 22369663 | |
| 699 | Phosphorylation | AGTPEPGSGEKGDDI CCCCCCCCCCCCCCC | 55.27 | 22890988 | |
| 702 | Acetylation | PEPGSGEKGDDIDLD CCCCCCCCCCCCCHH | 71.77 | 24489116 | |
| 725 | Acetylation | KTKSLNAKYETLGLD CCCCCHHHHHHCCHH | 42.41 | 24489116 | |
| 752 | Acetylation | WNGQDFKKKIQRDII CCCHHHHHHHHHHCH | 55.92 | 24489116 | |
| 760 | Phosphorylation | KIQRDIISPLLLNPT HHHHHCHHHHHCCCC | 15.16 | 20377248 | |
| 768 | Acetylation | PLLLNPTKRERKENY HHHCCCCHHHHHHCC | 54.22 | 22865919 | |
| 776 | Phosphorylation | RERKENYSIDNYYKD HHHHHCCCCCHHHHH | 34.74 | 27214570 | |
| 782 | Acetylation | YSIDNYYKDVLNTGR CCCCHHHHHHHHCCC | 30.88 | 24489116 | |
| 790 | Phosphorylation | DVLNTGRSSTPSHPR HHHHCCCCCCCCCCC | 39.65 | 21440633 | |
| 791 | Phosphorylation | VLNTGRSSTPSHPRM HHHCCCCCCCCCCCC | 42.87 | 27214570 | |
| 792 | Phosphorylation | LNTGRSSTPSHPRMP HHCCCCCCCCCCCCC | 30.01 | 21440633 | |
| 794 | Phosphorylation | TGRSSTPSHPRMPKP CCCCCCCCCCCCCCC | 46.33 | 21551504 | |
| 831 | Phosphorylation | WTAKKTGYVPTMDDV HHCHHHCCCCCHHHH | 14.42 | 28889911 | |
| 846 | Phosphorylation | KAAYGDISDEEEKKQ HHHHCCCCCHHHHHH | 43.65 | 25521595 | |
| 901 | Acetylation | KFITVSGKYGRNSIQ EEEEECCCCCHHHHH | 36.71 | 25381059 | |
| 928 | Acetylation | EEVRAYAKAFWSNIE HHHHHHHHHHHHCHH | 31.29 | 24489116 | |
| 972 | Acetylation | RRKLSEYKNPFFDLK HHHHHHCCCCCCCCC | 54.84 | 24489116 | |
| 979 | Acetylation | KNPFFDLKLKHPPSS CCCCCCCCCCCCCCC | 58.28 | 24489116 | |
| 1038 | Phosphorylation | DFYFRSRTPVELARR EEEECCCCHHHHHHC | 32.69 | 27214570 | |
| 1089 | Phosphorylation | REEFADQTANEKENV HHHHHHHCCCCCCCC | 31.81 | 27214570 | |
| 1093 | Acetylation | ADQTANEKENVDGVE HHHCCCCCCCCCCCH | 55.16 | 24489116 | |
| 1105 | Acetylation | GVESKKAKIEDTSNV CCHHCCCEEECCCCC | 56.35 | 24489116 | |
| 1109 | Phosphorylation | KKAKIEDTSNVGTEQ CCCEEECCCCCCHHH | 14.92 | 21440633 | |
| 1110 | Phosphorylation | KAKIEDTSNVGTEQL CCEEECCCCCCHHHH | 41.67 | 21551504 | |
| 1114 | Phosphorylation | EDTSNVGTEQLVAEK ECCCCCCHHHHHHHC | 19.10 | 27214570 | |
| 1121 | Acetylation | TEQLVAEKIPENETT HHHHHHHCCCCCCCC | 54.55 | 24489116 | |
| 1127 | Phosphorylation | EKIPENETTH----- HCCCCCCCCC----- | 41.57 | 17563356 | |
| 1128 | Phosphorylation | KIPENETTH------ CCCCCCCCC------ | 21.29 | 25521595 |
| 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 ISW1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ISW1_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 ISW1_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 THR-694; SER-699; SER-846AND SER-1110, 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-673; THR-694; SER-760;SER-846; SER-1110 AND THR-1127, AND MASS SPECTROMETRY. | |
