| UniProt ID | ORC2_YEAST | |
|---|---|---|
| UniProt AC | P32833 | |
| Protein Name | Origin recognition complex subunit 2 | |
| Gene Name | ORC2 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 620 | |
| 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 | MLNGEDFVEHNDILSSPAKSRNVTPKRVDPHGERQLRRIHSSKKNLLERISLVGNERKNTSPDPALKPKTPSKAPRKRGRPRKIQEELTDRIKKDEKDTISSKKKRKLDKDTSGNVNEESKTSNNKQVMEKTGIKEKREREKIQVATTTYEDNVTPQTDDNFVSNSPEPPEPATPSKKSLTTNHDFTSPLKQIIMNNLKEYKDSTSPGKLTLSRNFTPTPVPKNKKLYQTSETKSASSFLDTFEGYFDQRKIVRTNAKSRHTMSMAPDVTREEFSLVSNFFNENFQKRPRQKLFEIQKKMFPQYWFELTQGFSLLFYGVGSKRNFLEEFAIDYLSPKIAYSQLAYENELQQNKPVNSIPCLILNGYNPSCNYRDVFKEITDLLVPAELTRSETKYWGNHVILQIQKMIDFYKNQPLDIKLILVVHNLDGPSIRKNTFQTMLSFLSVIRQIAIVASTDHIYAPLLWDNMKAQNYNFVFHDISNFEPSTVESTFQDVMKMGKSDTSSGAEGAKYVLQSLTVNSKKMYKLLIETQMQNMGNLSANTGPKRGTQRTGVELKLFNHLCAADFIASNEIALRSMLREFIEHKMANITKNNSGMEIIWVPYTYAELEKLLKTVLNTL | |
| 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 | VEHNDILSSPAKSRN HCCCCCCCCCCCCCC | 34.31 | 22369663 | |
| 16 | Phosphorylation | EHNDILSSPAKSRNV CCCCCCCCCCCCCCC | 25.98 | 22369663 | |
| 20 | Phosphorylation | ILSSPAKSRNVTPKR CCCCCCCCCCCCCCC | 31.06 | 21440633 | |
| 24 | Phosphorylation | PAKSRNVTPKRVDPH CCCCCCCCCCCCCCH | 27.00 | 21440633 | |
| 43 | Acetylation | LRRIHSSKKNLLERI HHHHHHHHCCHHHHH | 49.01 | 25381059 | |
| 44 | Acetylation | RRIHSSKKNLLERIS HHHHHHHCCHHHHHH | 55.57 | 25381059 | |
| 51 | Phosphorylation | KNLLERISLVGNERK CCHHHHHHHCCCCCC | 24.19 | 24961812 | |
| 60 | Phosphorylation | VGNERKNTSPDPALK CCCCCCCCCCCCCCC | 44.67 | 22369663 | |
| 61 | Phosphorylation | GNERKNTSPDPALKP CCCCCCCCCCCCCCC | 36.38 | 22369663 | |
| 70 | Phosphorylation | DPALKPKTPSKAPRK CCCCCCCCCCCCCCC | 41.12 | 21440633 | |
| 72 | Phosphorylation | ALKPKTPSKAPRKRG CCCCCCCCCCCCCCC | 46.83 | 28889911 | |
| 113 | Phosphorylation | RKLDKDTSGNVNEES CCCCCCCCCCCCHHH | 38.20 | 28889911 | |
| 147 | Phosphorylation | REKIQVATTTYEDNV HHCCEEEEEEECCCC | 22.33 | 19823750 | |
| 148 | Phosphorylation | EKIQVATTTYEDNVT HCCEEEEEEECCCCC | 20.04 | 19823750 | |
| 149 | Phosphorylation | KIQVATTTYEDNVTP CCEEEEEEECCCCCC | 22.13 | 19823750 | |
| 150 | Phosphorylation | IQVATTTYEDNVTPQ CEEEEEEECCCCCCC | 21.13 | 19779198 | |
| 155 | Phosphorylation | TTYEDNVTPQTDDNF EEECCCCCCCCCCCC | 18.88 | 19823750 | |
| 158 | Phosphorylation | EDNVTPQTDDNFVSN CCCCCCCCCCCCCCC | 46.66 | 20377248 | |
| 164 | Phosphorylation | QTDDNFVSNSPEPPE CCCCCCCCCCCCCCC | 27.70 | 20377248 | |
| 166 | Phosphorylation | DDNFVSNSPEPPEPA CCCCCCCCCCCCCCC | 24.12 | 19823750 | |
| 174 | Phosphorylation | PEPPEPATPSKKSLT CCCCCCCCCCCCCCC | 38.52 | 19823750 | |
| 176 | Phosphorylation | PPEPATPSKKSLTTN CCCCCCCCCCCCCCC | 48.65 | 20377248 | |
| 179 | Phosphorylation | PATPSKKSLTTNHDF CCCCCCCCCCCCCCC | 34.38 | 19823750 | |
| 181 | Phosphorylation | TPSKKSLTTNHDFTS CCCCCCCCCCCCCCH | 32.42 | 21440633 | |
| 182 | Phosphorylation | PSKKSLTTNHDFTSP CCCCCCCCCCCCCHH | 35.53 | 22369663 | |
| 187 | Phosphorylation | LTTNHDFTSPLKQII CCCCCCCCHHHHHHH | 35.18 | 22369663 | |
| 188 | Phosphorylation | TTNHDFTSPLKQIIM CCCCCCCHHHHHHHH | 28.38 | 22369663 | |
| 204 | Phosphorylation | NLKEYKDSTSPGKLT CHHHHCCCCCCCCEE | 27.00 | 21440633 | |
| 205 | Phosphorylation | LKEYKDSTSPGKLTL HHHHCCCCCCCCEEE | 49.42 | 21440633 | |
| 206 | Phosphorylation | KEYKDSTSPGKLTLS HHHCCCCCCCCEEEC | 35.29 | 21082442 | |
| 211 | Phosphorylation | STSPGKLTLSRNFTP CCCCCCEEECCCCCC | 26.61 | 21440633 | |
| 217 | Phosphorylation | LTLSRNFTPTPVPKN EEECCCCCCCCCCCC | 29.78 | 21082442 | |
| 219 | Phosphorylation | LSRNFTPTPVPKNKK ECCCCCCCCCCCCCC | 33.58 | 29688323 | |
| 235 | Phosphorylation | YQTSETKSASSFLDT EECCCCCCHHHHHHH | 40.58 | 22369663 | |
| 237 | Phosphorylation | TSETKSASSFLDTFE CCCCCCHHHHHHHHC | 28.81 | 22369663 | |
| 238 | Phosphorylation | SETKSASSFLDTFEG CCCCCHHHHHHHHCC | 29.55 | 21440633 | |
| 436 | Phosphorylation | GPSIRKNTFQTMLSF CHHHCHHHHHHHHHH | 21.83 | 27017623 | |
| 439 | Phosphorylation | IRKNTFQTMLSFLSV HCHHHHHHHHHHHHH | 18.85 | 27017623 | |
| 442 | Phosphorylation | NTFQTMLSFLSVIRQ HHHHHHHHHHHHHHH | 17.20 | 27017623 |
| 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 ORC2_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ORC2_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 ORC2_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-15; SER-16; THR-60;SER-61; SER-166; SER-188; THR-205; SER-206; THR-217 AND SER-235, ANDMASS 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 THR-187; SER-188 ANDSER-206, AND MASS SPECTROMETRY. | |
