| UniProt ID | STH1_YEAST | |
|---|---|---|
| UniProt AC | P32597 | |
| Protein Name | Nuclear protein STH1/NPS1 | |
| Gene Name | STH1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 1359 | |
| Subcellular Localization | Nucleus . Localizes to centromeric and flanking chromatin. Association of the RSC complex with these loci is dependent on this subunit. | |
| Protein Description | Catalytic component of the chromatin structure-remodeling complex (RSC), which is involved in transcription regulation and nucleosome positioning. RSC is responsible for the transfer of a histone octamer from a nucleosome core particle to naked DNA. The reaction requires ATP and involves an activated RSC-nucleosome intermediate. Remodeling reaction also involves DNA translocation, DNA twist and conformational change. As a reconfigurer of centromeric and flanking nucleosomes, RSC complex is required both for proper kinetochore function in chromosome segregation and, via a PKC1-dependent signaling pathway, for organization of the cellular cytoskeleton. This subunit is the essential ATPase of the complex. It is a DNA translocase capable of nucleosome remodeling. Required for full expression of early meiotic genes. Essential for mitotic growth and repression of CHA1 expression. Also involved in G2 phase control.. | |
| Protein Sequence | MLQEQSELMSTVMNNTPTTVAALAAVAAASETNGKLGSEEQPEITIPKPRSSAQLEQLLYRYRAIQNHPKENKLEIKAIEDTFRNISRDQDIYETKLDTLRKSIDKGFQYDEDLLNKHLVALQLLEKDTDVPDYFLDLPDTKNDNTTAIEVDYSEKKPIKISADFNAKAKSLGLESKFSNATKTALGDPDTEIRISARISNRINELERLPANLGTYSLDDCLEFITKDDLSSRMDTFKIKALVELKSLKLLTKQKSIRQKLINNVASQAHHNIPYLRDSPFTAAAQRSVQIRSKVIVPQTVRLAEELERQQLLEKRKKERNLHLQKINSIIDFIKERQSEQWSRQERCFQFGRLGASLHNQMEKDEQKRIERTAKQRLAALKSNDEEAYLKLLDQTKDTRITQLLRQTNSFLDSLSEAVRAQQNEAKILHGEEVQPITDEEREKTDYYEVAHRIKEKIDKQPSILVGGTLKEYQLRGLEWMVSLYNNHLNGILADEMGLGKTIQSISLITYLYEVKKDIGPFLVIVPLSTITNWTLEFEKWAPSLNTIIYKGTPNQRHSLQHQIRVGNFDVLLTTYEYIIKDKSLLSKHDWAHMIIDEGHRMKNAQSKLSFTISHYYRTRNRLILTGTPLQNNLPELWALLNFVLPKIFNSAKTFEDWFNTPFANTGTQEKLELTEEETLLIIRRLHKVLRPFLLRRLKKEVEKDLPDKVEKVIKCKLSGLQQQLYQQMLKHNALFVGAGTEGATKGGIKGLNNKIMQLRKICNHPFVFDEVEGVVNPSRGNSDLLFRVAGKFELLDRVLPKFKASGHRVLMFFQMTQVMDIMEDFLRMKDLKYMRLDGSTKTEERTEMLNAFNAPDSDYFCFLLSTRAGGLGLNLQTADTVIIFDTDWNPHQDLQAQDRAHRIGQKNEVRILRLITTDSVEEVILERAMQKLDIDGKVIQAGKFDNKSTAEEQEAFLRRLIESETNRDDDDKAELDDDELNDTLARSADEKILFDKIDKERMNQERADAKAQGLRVPPPRLIQLDELPKVFREDIEEHFKKEDSEPLGRIRQKKRVYYDDGLTEEQFLEAVEDDNMSLEDAIKKRREARERRRLRQNGTKENEIETLENTPEASETSLIENNSFTAAVDEETNADKETTASRSKRRSSRKKRTISIVTAEDKENTQEESTSQENGGAKVEEEVKSSSVEIINGSESKKKKPKLTVKIKLNKTTVLENNDGKRAEEKPESKSPAKKTAAKKTKTKSKSLGIFPTVEKLVEEMREQLDEVDSHPRTSIFEKLPSKRDYPDYFKVIEKPMAIDIILKNCKNGTYKTLEEVRQALQTMFENARFYNEEGSWVYVDADKLNEFTDEWFKEHSS | |
| 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 |
|---|---|---|---|---|---|
| 38 | Phosphorylation | ETNGKLGSEEQPEIT HHCCCCCCCCCCCCC | 48.69 | 29136822 | |
| 45 | Phosphorylation | SEEQPEITIPKPRSS CCCCCCCCCCCCCCH | 29.57 | 29136822 | |
| 51 | Phosphorylation | ITIPKPRSSAQLEQL CCCCCCCCHHHHHHH | 38.25 | 22369663 | |
| 52 | Phosphorylation | TIPKPRSSAQLEQLL CCCCCCCHHHHHHHH | 22.70 | 22369663 | |
| 60 | Phosphorylation | AQLEQLLYRYRAIQN HHHHHHHHHHHHHHH | 17.75 | 21440633 | |
| 99 | Phosphorylation | IYETKLDTLRKSIDK HHHHHHHHHHHHHHC | 38.61 | 19823750 | |
| 103 | Phosphorylation | KLDTLRKSIDKGFQY HHHHHHHHHHCCCCC | 29.59 | 19795423 | |
| 156 | Acetylation | IEVDYSEKKPIKISA EEEECCCCCCEEEEE | 58.89 | 24489116 | |
| 157 | Acetylation | EVDYSEKKPIKISAD EEECCCCCCEEEEEC | 48.17 | 24489116 | |
| 177 | Acetylation | KSLGLESKFSNATKT HHHCCHHHCCCCCCC | 43.36 | 24489116 | |
| 183 | Ubiquitination | SKFSNATKTALGDPD HHCCCCCCCCCCCCC | 29.41 | 23749301 | |
| 232 | Phosphorylation | ITKDDLSSRMDTFKI HCCCCHHHCCCHHHH | 38.63 | 21440633 | |
| 236 | Phosphorylation | DLSSRMDTFKIKALV CHHHCCCHHHHHHHH | 19.93 | 21440633 | |
| 326 | Acetylation | ERNLHLQKINSIIDF HHHHHHHHHHHHHHH | 50.65 | 24489116 | |
| 329 | Phosphorylation | LHLQKINSIIDFIKE HHHHHHHHHHHHHHH | 25.13 | 22369663 | |
| 382 | Acetylation | KQRLAALKSNDEEAY HHHHHHHHCCCHHHH | 42.35 | 25381059 | |
| 383 | Phosphorylation | QRLAALKSNDEEAYL HHHHHHHCCCHHHHH | 50.82 | 30377154 | |
| 397 | Ubiquitination | LKLLDQTKDTRITQL HHHHHHCCHHHHHHH | 52.01 | 23749301 | |
| 408 | Phosphorylation | ITQLLRQTNSFLDSL HHHHHHHHHHHHHHH | 26.79 | 30377154 | |
| 410 | Phosphorylation | QLLRQTNSFLDSLSE HHHHHHHHHHHHHHH | 30.49 | 30377154 | |
| 414 | Phosphorylation | QTNSFLDSLSEAVRA HHHHHHHHHHHHHHH | 35.62 | 30377154 | |
| 438 | Phosphorylation | GEEVQPITDEEREKT CCCCCCCCHHHHHHC | 44.00 | 21440633 | |
| 444 | Acetylation | ITDEEREKTDYYEVA CCHHHHHHCCHHHHH | 53.57 | 24489116 | |
| 460 | Ubiquitination | RIKEKIDKQPSILVG HHHHHHHCCCCEEEC | 68.53 | 24961812 | |
| 712 | Acetylation | DLPDKVEKVIKCKLS HCCHHHHHHHHHHHH | 52.85 | 24489116 | |
| 741 | Phosphorylation | ALFVGAGTEGATKGG CEEECCCCCCHHCCC | 30.61 | 19823750 | |
| 745 | Phosphorylation | GAGTEGATKGGIKGL CCCCCCHHCCCHHCH | 40.87 | 19823750 | |
| 842 | Ubiquitination | MRLDGSTKTEERTEM EECCCCCCHHHHHHH | 56.49 | 23749301 | |
| 964 | Phosphorylation | FLRRLIESETNRDDD HHHHHHHHHCCCCCC | 42.60 | 28889911 | |
| 997 | Acetylation | DEKILFDKIDKERMN CHHHHHHHHCHHHHH | 45.53 | 24489116 | |
| 1000 | Acetylation | ILFDKIDKERMNQER HHHHHHCHHHHHHHH | 51.17 | 24489116 | |
| 1045 | Phosphorylation | EHFKKEDSEPLGRIR HHHCCCCCCCCHHHC | 42.05 | 29136822 | |
| 1111 | Phosphorylation | EIETLENTPEASETS HHCHHHCCCCCCCCE | 17.09 | 21440633 | |
| 1115 | Phosphorylation | LENTPEASETSLIEN HHCCCCCCCCEEEEC | 39.48 | 19779198 | |
| 1117 | Phosphorylation | NTPEASETSLIENNS CCCCCCCCEEEECCC | 26.74 | 19779198 | |
| 1154 | Phosphorylation | RSSRKKRTISIVTAE HHCCCCCEEEEEECC | 28.14 | 22890988 | |
| 1156 | Phosphorylation | SRKKRTISIVTAEDK CCCCCEEEEEECCHH | 15.47 | 19823750 | |
| 1159 | Phosphorylation | KRTISIVTAEDKENT CCEEEEEECCHHCCC | 23.74 | 22890988 | |
| 1166 | Phosphorylation | TAEDKENTQEESTSQ ECCHHCCCCCCCCCC | 38.15 | 20190278 | |
| 1170 | Phosphorylation | KENTQEESTSQENGG HCCCCCCCCCCCCCC | 32.38 | 24961812 | |
| 1171 | Phosphorylation | ENTQEESTSQENGGA CCCCCCCCCCCCCCC | 37.40 | 28889911 | |
| 1172 | Phosphorylation | NTQEESTSQENGGAK CCCCCCCCCCCCCCC | 44.79 | 20190278 | |
| 1179 | Acetylation | SQENGGAKVEEEVKS CCCCCCCCCHHHHHH | 54.15 | 24489116 | |
| 1186 | Phosphorylation | KVEEEVKSSSVEIIN CCHHHHHHCCEEEEC | 32.78 | 22369663 | |
| 1187 | Phosphorylation | VEEEVKSSSVEIING CHHHHHHCCEEEECC | 32.46 | 22369663 | |
| 1188 | Phosphorylation | EEEVKSSSVEIINGS HHHHHHCCEEEECCC | 30.75 | 22369663 | |
| 1222 | Acetylation | VLENNDGKRAEEKPE EEECCCCCCCCCCCC | 51.83 | 25381059 | |
| 1230 | Phosphorylation | RAEEKPESKSPAKKT CCCCCCCCCCHHHHH | 47.13 | 19823750 | |
| 1231 | Acetylation | AEEKPESKSPAKKTA CCCCCCCCCHHHHHH | 59.81 | 25381059 | |
| 1232 | Phosphorylation | EEKPESKSPAKKTAA CCCCCCCCHHHHHHC | 39.09 | 17287358 | |
| 1247 | Acetylation | KKTKTKSKSLGIFPT CCCCCCCHHCCCCHH | 51.78 | 24489116 |
| 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 STH1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of STH1_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 STH1_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-38; SER-51; SER-52;SER-964; SER-1156; THR-1166; SER-1187 AND SER-1188, AND MASSSPECTROMETRY. | |
| "Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry."; Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.; Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1232, AND MASSSPECTROMETRY. | |
| "Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway."; Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.; Mol. Cell. Proteomics 4:310-327(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51, AND MASSSPECTROMETRY. | |
