| UniProt ID | ITC1_YEAST | |
|---|---|---|
| UniProt AC | P53125 | |
| Protein Name | Imitation switch two complex protein 1 | |
| Gene Name | ITC1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 1264 | |
| Subcellular Localization | Nucleus . | |
| Protein Description | Functions as 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. ITC1 is required for nucleosome-stimulated ATPase activity and chromatin-remodeling activity of the complex. Required for the repression of MATa a-specific genes.. | |
| Protein Sequence | MVLYKRKPILLPDPKPLPLDLNVQVWHIEETGEWFSSYEEFLERFDFYTRHHFTCEITGTSCLTFFQALDSEETQFKYVEDRFPLKLREPVARFLHFNGIRRLDALVEKVYARFKNDFFPGEVVYLRKQKDSSTTSSNSQQSTPQPDDMVEINSVGNPGLPQYQYQRRYVIKEKVQFNATINPESREIVMPAHTKYMLIEEAASSNKSFIVDQGQIYRDRSTFTKHLIKCFFKITLQRASSKMGAPWCVKPEYLAMYGLTMEWPKDMLKYKEDEPVVARRSNSANVSSPESEKNKRQSKSSGKSNTSNDASNKKETKKKRKPTEVNDSENNSSEEDKKKGQNVTSETHSKKRKKEANEEPNTENVESVPTPANAEPQAVTITSIMDDLALPYQHPPNIFPNLTYYNEKLECISLGSTKLSRPFDSFGKLLQAYQFLNTFGSKICLSHFSLDQFITSLKCTDPYELKGEVVLVNIRTQTSKEQEIENNGLPMKNKAETTTEEDSENPSDWQRNSFIRDMIMKRNSDKVEYKIVHDDPASDDILDNINHNGSALLIEVFTALLRLFINEEGDWSCIVVENWIIDDKGVLMERKDERGEGEAKQKRNAHGYFLQDKEKIDNLKDTLKENATEVQKESDAKNETNSESDSKSDSDSEERDPKLEKCLNYRNVNWIERLTKRQFNNSYWLIILLGVLEDCRHLPMYTEFIDSFIEKIIPKDISATQLPKQLWRNFCRKLSFSDKVNALWILVDLVSHFSPDIKAAVDDSMELCGQIRSERFKVARELKTEAAVLSNLQGDLQAIQEKLNKTDENTPSADGADKKDDSESNSEPIDLIIIEKKQKLIEEQDKKVQALQSDKNFLDNCLFENDLQRLKPLGLDRYGNRYFWLDHNGVPFPQYPAGMNETPKSNNSLSYHSGRLLIQGPKASSAKFFLNVSDEQLSNWQKIRNSEGISEATREVFGISKTSSGSYNYVENGIEVELLDSNDRVNPLIELTPIQKKIMDETPSRLLLSPDQWYCIDKLEDLSRIMDWLDNWGRKEHDLLRQIRPIMERIKSSLSLRDHALSLTAFTKNEEKLLKELENNEFTENELNVDSMDVDDKNSGVKSEVDVQVDAEEKREAVIDEKLEVIADELMKLDDSSKTRNVLNRIQELEDQRDELLEQKKSIINSQRPGARILARSERKRTKISRGNKVNKQIEILTDLVNYRHFKAMEDVIAWKNVLANSIWGSSLRKNASGNKRSGVIETVDDKLKDIVGQTSRTVTPAPN | |
| 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 |
|---|---|---|---|---|---|
| 136 | Phosphorylation | QKDSSTTSSNSQQST CCCCCCCCCCCCCCC | 27.84 | 19779198 | |
| 137 | Phosphorylation | KDSSTTSSNSQQSTP CCCCCCCCCCCCCCC | 38.11 | 21440633 | |
| 139 | Phosphorylation | SSTTSSNSQQSTPQP CCCCCCCCCCCCCCC | 31.38 | 19779198 | |
| 142 | Phosphorylation | TSSNSQQSTPQPDDM CCCCCCCCCCCCCCC | 34.12 | 20377248 | |
| 143 | Phosphorylation | SSNSQQSTPQPDDMV CCCCCCCCCCCCCCE | 22.93 | 21440633 | |
| 196 | Phosphorylation | VMPAHTKYMLIEEAA EECCCCCCHHHHHHH | 9.79 | 28889911 | |
| 207 | Ubiquitination | EEAASSNKSFIVDQG HHHHHCCCCEEEECC | 49.00 | 23749301 | |
| 270 | Phosphorylation | WPKDMLKYKEDEPVV CCHHHHCCCCCCCCE | 18.69 | 19823750 | |
| 281 | Phosphorylation | EPVVARRSNSANVSS CCCEEECCCCCCCCC | 29.59 | 17287358 | |
| 283 | Phosphorylation | VVARRSNSANVSSPE CEEECCCCCCCCCCH | 23.59 | 19823750 | |
| 287 | Phosphorylation | RSNSANVSSPESEKN CCCCCCCCCCHHHHH | 39.73 | 17563356 | |
| 288 | Phosphorylation | SNSANVSSPESEKNK CCCCCCCCCHHHHHH | 28.53 | 19823750 | |
| 291 | Phosphorylation | ANVSSPESEKNKRQS CCCCCCHHHHHHHHC | 58.20 | 23749301 | |
| 317 | Acetylation | ASNKKETKKKRKPTE CCCCHHCCCCCCCCC | 58.34 | 23572591 | |
| 319 | Acetylation | NKKETKKKRKPTEVN CCHHCCCCCCCCCCC | 68.18 | 23572591 | |
| 323 | Phosphorylation | TKKKRKPTEVNDSEN CCCCCCCCCCCCCCC | 56.45 | 19795423 | |
| 328 | Phosphorylation | KPTEVNDSENNSSEE CCCCCCCCCCCCCHH | 36.70 | 19795423 | |
| 332 | Phosphorylation | VNDSENNSSEEDKKK CCCCCCCCCHHHHHH | 51.19 | 25521595 | |
| 333 | Phosphorylation | NDSENNSSEEDKKKG CCCCCCCCHHHHHHC | 47.32 | 21440633 | |
| 344 | Phosphorylation | KKKGQNVTSETHSKK HHHCCCCHHHHHHHH | 28.53 | 30377154 | |
| 345 | Phosphorylation | KKGQNVTSETHSKKR HHCCCCHHHHHHHHH | 35.89 | 30377154 | |
| 478 | Phosphorylation | LVNIRTQTSKEQEIE EEEEECCCCCHHHHH | 40.95 | 28889911 | |
| 499 | Phosphorylation | KNKAETTTEEDSENP CCCCCCCCHHHCCCC | 44.81 | 23749301 | |
| 634 | Phosphorylation | ATEVQKESDAKNETN HHHHHHHHHHCCCCC | 50.32 | 27017623 | |
| 640 | Phosphorylation | ESDAKNETNSESDSK HHHHCCCCCCCCCCC | 54.13 | 24961812 | |
| 642 | Phosphorylation | DAKNETNSESDSKSD HHCCCCCCCCCCCCC | 45.99 | 28889911 | |
| 644 | Phosphorylation | KNETNSESDSKSDSD CCCCCCCCCCCCCCC | 47.18 | 28889911 | |
| 646 | Phosphorylation | ETNSESDSKSDSDSE CCCCCCCCCCCCCCC | 43.25 | 24961812 | |
| 648 | Phosphorylation | NSESDSKSDSDSEER CCCCCCCCCCCCCCC | 46.42 | 28889911 | |
| 650 | Phosphorylation | ESDSKSDSDSEERDP CCCCCCCCCCCCCCH | 50.56 | 28889911 | |
| 652 | Phosphorylation | DSKSDSDSEERDPKL CCCCCCCCCCCCHHH | 45.36 | 21551504 | |
| 806 | Phosphorylation | IQEKLNKTDENTPSA HHHHHCCCCCCCCCC | 47.69 | 29136822 | |
| 810 | Phosphorylation | LNKTDENTPSADGAD HCCCCCCCCCCCCCC | 19.30 | 29136822 | |
| 812 | Phosphorylation | KTDENTPSADGADKK CCCCCCCCCCCCCCC | 36.63 | 28889911 | |
| 822 | Phosphorylation | GADKKDDSESNSEPI CCCCCCCCCCCCCCC | 53.72 | 21551504 | |
| 855 | Ubiquitination | VQALQSDKNFLDNCL HHHHHCCCCHHHHCC | 55.64 | 23749301 | |
| 1052 | Phosphorylation | PIMERIKSSLSLRDH HHHHHHHHHCCHHHH | 33.85 | 19779198 | |
| 1053 | Phosphorylation | IMERIKSSLSLRDHA HHHHHHHHCCHHHHH | 19.58 | 22369663 | |
| 1055 | Phosphorylation | ERIKSSLSLRDHALS HHHHHHCCHHHHHHH | 24.25 | 22369663 | |
| 1222 | Phosphorylation | WKNVLANSIWGSSLR HHHHHHHHHHCHHHH | 17.70 | 28889911 | |
| 1255 | Phosphorylation | LKDIVGQTSRTVTPA HHHHCCCCCCCCCCC | 17.78 | 20377248 | |
| 1256 | Phosphorylation | KDIVGQTSRTVTPAP HHHCCCCCCCCCCCC | 20.33 | 22369663 | |
| 1258 | Phosphorylation | IVGQTSRTVTPAPN- HCCCCCCCCCCCCC- | 28.62 | 22369663 | |
| 1260 | Phosphorylation | GQTSRTVTPAPN--- CCCCCCCCCCCC--- | 17.08 | 22369663 |
| 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 ITC1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ITC1_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 ITC1_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-281; SER-283; SER-288AND THR-478, 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-281; SER-283; SER-287AND SER-288, AND MASS SPECTROMETRY. | |
