| UniProt ID | ORC6_YEAST | |
|---|---|---|
| UniProt AC | P38826 | |
| Protein Name | Origin recognition complex subunit 6 | |
| Gene Name | ORC6 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 435 | |
| Subcellular Localization | Nucleus. | |
| Protein Description | Component of the origin recognition complex (ORC) that binds origins of replication. It has a role in both chromosomal replication and mating type transcriptional silencing. Binds to the ARS consensus sequence (ACS) of origins of replication.. | |
| Protein Sequence | MSMQQVQHCVAEVLRLDPQEKPDWSSGYLKKLTNATSILYNTSLNKVMLKQDEEVARCHICAYIASQKMNEKHMPDLCYYIDSIPLEPKKAKHLMNLFRQSLSNSSPMKQFAWTPSPKKNKRSPVKNGGRFTSSDPKELRNQLFGTPTKVRKSQNNDSFVIPELPPMQTNESPSITRRKLAFEEDEDEDEEEPGNDGLSLKSHSNKSITGTRNVDSDEYENHESDPTSEEEPLGVQESRSGRTKQNKAVGKPQSELKTAKALRKRGRIPNSLLVKKYCKMTTEEIIRLCNDFELPREVAYKIVDEYNINASRLVCPWQLVCGLVLNCTFIVFNERRRKDPRIDHFIVSKMCSLMLTSKVDDVIECVKLVKELIIGEKWFRDLQIRYDDFDGIRYDEIIFRKLGSMLQTTNILVTDDQYNIWKKRIEMDLALTEPL | |
| 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 |
|---|---|---|---|---|---|
| 101 | Phosphorylation | LMNLFRQSLSNSSPM HHHHHHHHHCCCCCC | 29.52 | 22369663 | |
| 103 | Phosphorylation | NLFRQSLSNSSPMKQ HHHHHHHCCCCCCCC | 39.65 | 22369663 | |
| 105 | Phosphorylation | FRQSLSNSSPMKQFA HHHHHCCCCCCCCCC | 32.23 | 22369663 | |
| 106 | Phosphorylation | RQSLSNSSPMKQFAW HHHHCCCCCCCCCCC | 33.01 | 22369663 | |
| 114 | Phosphorylation | PMKQFAWTPSPKKNK CCCCCCCCCCCCCCC | 15.51 | 25752575 | |
| 116 | Phosphorylation | KQFAWTPSPKKNKRS CCCCCCCCCCCCCCC | 41.81 | 28152593 | |
| 123 | Phosphorylation | SPKKNKRSPVKNGGR CCCCCCCCCCCCCCC | 35.34 | 21289063 | |
| 132 | Phosphorylation | VKNGGRFTSSDPKEL CCCCCCCCCCCHHHH | 26.43 | 23749301 | |
| 133 | Phosphorylation | KNGGRFTSSDPKELR CCCCCCCCCCHHHHH | 29.99 | 30377154 | |
| 134 | Phosphorylation | NGGRFTSSDPKELRN CCCCCCCCCHHHHHH | 55.67 | 23749301 | |
| 146 | Phosphorylation | LRNQLFGTPTKVRKS HHHHHHCCCCEEECC | 22.05 | 25521595 | |
| 148 | Phosphorylation | NQLFGTPTKVRKSQN HHHHCCCCEEECCCC | 41.85 | 19823750 | |
| 153 | Phosphorylation | TPTKVRKSQNNDSFV CCCEEECCCCCCCCC | 27.81 | 29136822 | |
| 158 | Phosphorylation | RKSQNNDSFVIPELP ECCCCCCCCCCCCCC | 24.44 | 29136822 | |
| 169 | Phosphorylation | PELPPMQTNESPSIT CCCCCCCCCCCCCCC | 34.40 | 25521595 | |
| 172 | Phosphorylation | PPMQTNESPSITRRK CCCCCCCCCCCCHHH | 26.47 | 29136822 | |
| 174 | Phosphorylation | MQTNESPSITRRKLA CCCCCCCCCCHHHCC | 45.96 | 21440633 | |
| 176 | Phosphorylation | TNESPSITRRKLAFE CCCCCCCCHHHCCEE | 28.85 | 19795423 | |
| 206 | Acetylation | SLKSHSNKSITGTRN CCCCCCCCCCCCCCC | 46.37 | 25381059 | |
| 207 | Phosphorylation | LKSHSNKSITGTRNV CCCCCCCCCCCCCCC | 29.63 | 23749301 | |
| 209 | Phosphorylation | SHSNKSITGTRNVDS CCCCCCCCCCCCCCH | 39.32 | 24961812 | |
| 211 | Phosphorylation | SNKSITGTRNVDSDE CCCCCCCCCCCCHHH | 15.49 | 19823750 | |
| 216 | Phosphorylation | TGTRNVDSDEYENHE CCCCCCCHHHHCCCC | 28.23 | 17563356 | |
| 219 | Phosphorylation | RNVDSDEYENHESDP CCCCHHHHCCCCCCC | 27.33 | 28152593 | |
| 224 | Phosphorylation | DEYENHESDPTSEEE HHHCCCCCCCCCCCC | 41.14 | 28152593 | |
| 227 | Phosphorylation | ENHESDPTSEEEPLG CCCCCCCCCCCCCCC | 54.48 | 28152593 | |
| 228 | Phosphorylation | NHESDPTSEEEPLGV CCCCCCCCCCCCCCC | 48.69 | 28152593 | |
| 238 | Phosphorylation | EPLGVQESRSGRTKQ CCCCCCCCCCCCCCC | 18.04 | 19795423 | |
| 240 | Phosphorylation | LGVQESRSGRTKQNK CCCCCCCCCCCCCCC | 41.74 | 19823750 | |
| 243 | Phosphorylation | QESRSGRTKQNKAVG CCCCCCCCCCCCCCC | 40.27 | 19823750 | |
| 254 | Phosphorylation | KAVGKPQSELKTAKA CCCCCCHHHHHHHHH | 54.12 | 21551504 | |
| 271 | Phosphorylation | KRGRIPNSLLVKKYC HCCCCCCHHHHHHHC | 20.09 | 21551504 | |
| 404 | Phosphorylation | IIFRKLGSMLQTTNI HHHHHHHHHHHHCCE | 27.10 | 19779198 | |
| 408 | Phosphorylation | KLGSMLQTTNILVTD HHHHHHHHCCEEECC | 20.18 | 19779198 |
| 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 ORC6_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ORC6_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 ORC6_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "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-216, 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-106, AND MASSSPECTROMETRY. | |
| "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-146, 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 THR-146, AND MASSSPECTROMETRY. | |
