| UniProt ID | ISW2_YEAST | |
|---|---|---|
| UniProt AC | Q08773 | |
| Protein Name | ISWI chromatin-remodeling complex ATPase ISW2 | |
| Gene Name | ISW2 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 1120 | |
| Subcellular Localization | Nucleus . | |
| Protein Description | Catalytic component of the ISW2 complex, which acts in remodeling the chromatin by catalyzing an ATP-dependent alteration in the structure of nucleosomal DNA. The ISW2 complex is involved in coordinating transcriptional repression and in inheritance of telomeric silencing. It is involved in repression of MAT a-specific genes, INO1, and early meiotic genes during mitotic growth dependent upon transcription factor UME6 and in a parallel pathway to the RPD3-SIN3 histone deacetylase complex.. | |
| Protein Sequence | MTTQQEEQRSDTKNSKSESPSEVLVDTLDSKSNGSSDDDNIGQSEELSDKEIYTVEDRPPEYWAQRKKKFVLDVDPKYAKQKDKSDTYKRFKYLLGVTDLFRHFIGIKAKHDKNIQKLLKQLDSDANKLSKSHSTVSSSSRHHRKTEKEEDAELMADEEEEIVDTYQEDIFVSESPSFVKSGKLRDYQVQGLNWLISLHENKLSGILADEMGLGKTLQTISFLGYLRYVKQIEGPFLIIVPKSTLDNWRREFLKWTPNVNVLVLHGDKDTRADIVRNIILEARFDVLITSYEMVIREKNALKRLAWQYIVIDEAHRIKNEQSALSQIIRLFYSKNRLLITGTPLQNNLHELWALLNFLLPDIFGDSELFDEWFEQNNSEQDQEIVIQQLHSVLNPFLLRRVKADVEKSLLPKIETNVYVGMTDMQIQWYKSLLEKDIDAVNGAVGKREGKTRLLNIVMQLRKCCNHPYLFEGAEPGPPYTTDEHLIFNSGKMIILDKLLKRLKEKGSRVLIFSQMSRLLDILEDYCYFRDFEYCRIDGSTSHEERIEAIDEYNKPNSEKFVFLLTTRAGGLGINLVTADTVILFDSDWNPQADLQAMDRAHRIGQKKQVHVYRFVTENAIEEKVIERAAQKLRLDQLVIQQGTGKKTASLGNSKDDLLDMIQFGAKNMFEKKASKVTVDADIDDILKKGEQKTQELNAKYQSLGLDDLQKFNGIENQSAYEWNGKSFQKKSNDKVVEWINPSRRERRREQTTYSVDDYYKEIIGGGSKSASKQTPQPKAPRAPKVIHGQDFQFFPKELDALQEKEQLYFKKKVNYKVTSYDITGDIRNEGSDAEEEEGEYKNAANTEGHKGHEELKRRIEEEQEKINSAPDFTQEDELRKQELISKAFTNWNKRDFMAFINACAKYGRDDMENIKKSIDSKTPEEVEVYAKIFWERLKEINGWEKYLHNVELGEKKNEKLKFQETLLRQKIEQCKHPLHELIIQYPPNNARRTYNTLEDKFLLLAVNKYGLRADKLYEKLKQEIMMSDLFTFDWFIKTRTVHELSKRVHTLLTLIVREYEQPDANKKKRSRTSATREDTPLSQNESTRASTVPNLPTTMVTNQKDTNDHVDKRTKIDQEA | |
| 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 |
|---|---|---|---|---|---|
| 15 | Phosphorylation | QRSDTKNSKSESPSE HHHCCCCCCCCCHHH | 38.83 | 22369663 | |
| 17 | Phosphorylation | SDTKNSKSESPSEVL HCCCCCCCCCHHHHH | 43.03 | 22369663 | |
| 19 | Phosphorylation | TKNSKSESPSEVLVD CCCCCCCCHHHHHHH | 40.60 | 22369663 | |
| 21 | Phosphorylation | NSKSESPSEVLVDTL CCCCCCHHHHHHHHC | 50.01 | 25521595 | |
| 30 | Phosphorylation | VLVDTLDSKSNGSSD HHHHHCCCCCCCCCC | 40.89 | 28889911 | |
| 32 | Phosphorylation | VDTLDSKSNGSSDDD HHHCCCCCCCCCCCC | 50.83 | 21551504 | |
| 35 | Phosphorylation | LDSKSNGSSDDDNIG CCCCCCCCCCCCCCC | 34.54 | 21551504 | |
| 36 | Phosphorylation | DSKSNGSSDDDNIGQ CCCCCCCCCCCCCCC | 46.59 | 21551504 | |
| 48 | Phosphorylation | IGQSEELSDKEIYTV CCCCCCCCCCCEEEC | 50.33 | 28889911 | |
| 134 | Phosphorylation | NKLSKSHSTVSSSSR HHHHHHHCCCCCCCC | 37.28 | 17563356 | |
| 497 | Acetylation | GKMIILDKLLKRLKE CCCHHHHHHHHHHHH | 52.88 | 25381059 | |
| 500 | Acetylation | IILDKLLKRLKEKGS HHHHHHHHHHHHCCC | 67.15 | 25381059 | |
| 699 | Acetylation | KTQELNAKYQSLGLD HHHHHHHHHHHCCHH | 42.63 | 24489116 | |
| 718 | Phosphorylation | FNGIENQSAYEWNGK HCCCCCCCCCEECCC | 44.38 | 21551504 | |
| 823 | Phosphorylation | KVTSYDITGDIRNEG EEEEEECCCCCCCCC | 26.38 | 21551504 | |
| 831 | Phosphorylation | GDIRNEGSDAEEEEG CCCCCCCCCHHHHHC | 27.71 | 22369663 | |
| 840 | Phosphorylation | AEEEEGEYKNAANTE HHHHHCCCCCHHCCC | 22.02 | 26447709 | |
| 946 | Phosphorylation | EINGWEKYLHNVELG HHCCHHHHHHHCCCC | 11.15 | 30377154 | |
| 961 | Acetylation | EKKNEKLKFQETLLR CHHCHHHHHHHHHHH | 56.95 | 24489116 | |
| 1072 | Phosphorylation | NKKKRSRTSATREDT CCCCCCCCCCCCCCC | 24.78 | 22369663 | |
| 1073 | Phosphorylation | KKKRSRTSATREDTP CCCCCCCCCCCCCCC | 26.91 | 23749301 | |
| 1075 | Phosphorylation | KRSRTSATREDTPLS CCCCCCCCCCCCCCC | 34.07 | 22369663 | |
| 1079 | Phosphorylation | TSATREDTPLSQNES CCCCCCCCCCCCCCC | 22.75 | 22369663 | |
| 1082 | Phosphorylation | TREDTPLSQNESTRA CCCCCCCCCCCCCCC | 31.96 | 22369663 | |
| 1090 | Phosphorylation | QNESTRASTVPNLPT CCCCCCCCCCCCCCC | 27.01 | 21551504 |
| 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 ISW2_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ISW2_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 ISW2_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-19; SER-21; SER-831;THR-1079 AND SER-1082, 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-134; SER-831; THR-1079AND SER-1082, AND MASS SPECTROMETRY. | |
| "Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae."; Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.; J. Proteome Res. 6:1190-1197(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-831, AND MASSSPECTROMETRY. | |
