UniProt ID | IOC2_YEAST | |
---|---|---|
UniProt AC | Q12072 | |
Protein Name | ISWI one complex protein 2 | |
Gene Name | IOC2 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 812 | |
Subcellular Localization | Nucleus . | |
Protein Description | Functions as component of the ISW1B complex, which acts in remodeling the chromatin by catalyzing an ATP-dependent alteration in the structure of nucleosomal DNA. 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 | MRTKRTRGTRNVGASMPAGAANADSEDWKEYVSEDIIAQLNKHQLPYSEILDEKIADLANHWHFQYVMAWLSNVCESYTTTTFNTDQYGGSSTKCLWKNIKFDEGVFVTDVFSKIDGKDSNYYNDEVDVDEGSQNLYDRIRLQLLHQLAGNKSGQLKDWNVIVNHHLQNSSAYSDLVTDLPFLELEIARQFDIIYSIIKLIEMKNMIFKNYLANNLHLFTFSEVILDDDNSGGEEMKSLFALPNVGVLVKKTIHRVKEGSSSQVSQTLNIPIKLQNCTIKESDPDIPDSVELIHLEYSHDIDAYLQSITIDYDVITTNWGSMLEYWSENKSSKAIDEFITNLIPVYAEHRLYSAKLLANREKERAIAELMTRRKRSSRLVAKEEENKKKDLESEWFEKLDEREQFIRHRNKLVSKEIKKIKDLLWNQLWQLYDQDYRDEKLTRRNELKDRSGSGTPFFETSLGREEDNPLNEIDIGVLDHGPNFQSSIIPVEPPIPGTVGPLQTGDVPELPSDFCITKEELDELANYGIFTPQQEPDNQDSVFQCPGEPELAPMIITEDTETDLFNNRPLICCDHCYRWQHWECQPPKIIELISSTTKSPQHTLSQRDFGVIIMGNSHGNRRSSRRPQSTLEPSTKSSRPTDKRKPLSECSTFICAWCIRDLELELRNIFVPELKIIRAKQRKQQEDRERRKKMKEEKKRLEELAKKRELTESVSPPVFNNAFANMSSSTTPSIAAYEKTNPAINPAPNVNAAHPIITYSQQTGSKTVPQAPQAPQTSQASIQPQQQQQQQQQQQPLHPKEQNFHFQFPPTN | |
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 |
---|---|---|---|---|---|
260 | Phosphorylation | IHRVKEGSSSQVSQT EEHHCCCCCCHHHHC | 28.10 | 21440633 | |
261 | Phosphorylation | HRVKEGSSSQVSQTL EHHCCCCCCHHHHCC | 35.33 | 28152593 | |
262 | Phosphorylation | RVKEGSSSQVSQTLN HHCCCCCCHHHHCCC | 35.98 | 25752575 | |
265 | Phosphorylation | EGSSSQVSQTLNIPI CCCCCHHHHCCCCCE | 15.15 | 23749301 | |
267 | Phosphorylation | SSSQVSQTLNIPIKL CCCHHHHCCCCCEEE | 17.79 | 27214570 | |
355 | Acetylation | EHRLYSAKLLANREK HHHHHHHHHHHHHHH | 37.79 | 24489116 | |
451 | Phosphorylation | RNELKDRSGSGTPFF HHHHHCCCCCCCCCC | 47.66 | 27214570 | |
453 | Phosphorylation | ELKDRSGSGTPFFET HHHCCCCCCCCCCCC | 40.51 | 27214570 | |
455 | Phosphorylation | KDRSGSGTPFFETSL HCCCCCCCCCCCCCC | 20.72 | 27214570 | |
599 | Phosphorylation | LISSTTKSPQHTLSQ HHHCCCCCCCCCCCC | 27.92 | 25752575 | |
605 | Phosphorylation | KSPQHTLSQRDFGVI CCCCCCCCCCCEEEE | 25.07 | 20190278 | |
629 | Phosphorylation | RSSRRPQSTLEPSTK CCCCCCCCCCCCCCC | 37.33 | 23749301 | |
711 | Phosphorylation | LAKKRELTESVSPPV HHHHHHCHHCCCCCC | 22.82 | 24961812 | |
713 | Phosphorylation | KKRELTESVSPPVFN HHHHCHHCCCCCCCC | 23.74 | 24961812 | |
715 | Phosphorylation | RELTESVSPPVFNNA HHCHHCCCCCCCCCC | 32.53 | 25521595 | |
737 | Phosphorylation | TTPSIAAYEKTNPAI CCCCCHHHHCCCCCC | 14.67 | 28132839 | |
760 | Phosphorylation | AHPIITYSQQTGSKT CCCEEEEECCCCCCC | 13.73 | 20190278 | |
765 | Phosphorylation | TYSQQTGSKTVPQAP EEECCCCCCCCCCCC | 28.65 | 27017623 | |
778 | Phosphorylation | APQAPQTSQASIQPQ CCCCCCCCCCCCCHH | 20.64 | 23749301 |
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 IOC2_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of IOC2_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 IOC2_YEAST !! |
Kegg Drug | ||||||
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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-260; SER-261; SER-262;SER-451; THR-455 AND SER-599, AND MASS SPECTROMETRY. |