| UniProt ID | TOP2_YEAST | |
|---|---|---|
| UniProt AC | P06786 | |
| Protein Name | DNA topoisomerase 2 | |
| Gene Name | TOP2 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 1428 | |
| Subcellular Localization | Nucleus. | |
| Protein Description | Control of topological states of DNA by transient breakage and subsequent rejoining of DNA strands. Topoisomerase II makes double-strand breaks. Essential during mitosis and meiosis for proper segregation of daughter chromosomes.. | |
| Protein Sequence | MSTEPVSASDKYQKISQLEHILKRPDTYIGSVETQEQLQWIYDEETDCMIEKNVTIVPGLFKIFDEILVNAADNKVRDPSMKRIDVNIHAEEHTIEVKNDGKGIPIEIHNKENIYIPEMIFGHLLTSSNYDDDEKKVTGGRNGYGAKLCNIFSTEFILETADLNVGQKYVQKWENNMSICHPPKITSYKKGPSYTKVTFKPDLTRFGMKELDNDILGVMRRRVYDINGSVRDINVYLNGKSLKIRNFKNYVELYLKSLEKKRQLDNGEDGAAKSDIPTILYERINNRWEVAFAVSDISFQQISFVNSIATTMGGTHVNYITDQIVKKISEILKKKKKKSVKSFQIKNNMFIFINCLIENPAFTSQTKEQLTTRVKDFGSRCEIPLEYINKIMKTDLATRMFEIADANEENALKKSDGTRKSRITNYPKLEDANKAGTKEGYKCTLVLTEGDSALSLAVAGLAVVGRDYYGCYPLRGKMLNVREASADQILKNAEIQAIKKIMGLQHRKKYEDTKSLRYGHLMIMTDQDHDGSHIKGLIINFLESSFPGLLDIQGFLLEFITPIIKVSITKPTKNTIAFYNMPDYEKWREEESHKFTWKQKYYKGLGTSLAQEVREYFSNLDRHLKIFHSLQGNDKDYIDLAFSKKKADDRKEWLRQYEPGTVLDPTLKEIPISDFINKELILFSLADNIRSIPNVLDGFKPGQRKVLYGCFKKNLKSELKVAQLAPYVSECTAYHHGEQSLAQTIIGLAQNFVGSNNIYLLLPNGAFGTRATGGKDAAAARYIYTELNKLTRKIFHPADDPLYKYIQEDEKTVEPEWYLPILPMILVNGAEGIGTGWSTYIPPFNPLEIIKNIRHLMNDEELEQMHPWFRGWTGTIEEIEPLRYRMYGRIEQIGDNVLEITELPARTWTSTIKEYLLLGLSGNDKIKPWIKDMEEQHDDNIKFIITLSPEEMAKTRKIGFYERFKLISPISLMNMVAFDPHGKIKKYNSVNEILSEFYYVRLEYYQKRKDHMSERLQWEVEKYSFQVKFIKMIIEKELTVTNKPRNAIIQELENLGFPRFNKEGKPYYGSPNDEIAEQINDVKGATSDEEDEESSHEDTENVINGPEELYGTYEYLLGMRIWSLTKERYQKLLKQKQEKETELENLLKLSAKDIWNTDLKAFEVGYQEFLQRDAEARGGNVPNKGSKTKGKGKRKLVDDEDYDPSKKNKKSTARKGKKIKLEDKNFERILLEQKLVTKSKAPTKIKKEKTPSVSETKTEEEENAPSSTSSSSIFDIKKEDKDEGELSKISNKFKKISTIFDKMGSTSATSKENTPEQDDVATKKNQTTAKKTAVKPKLAKKPVRKQQKVVELSGESDLEILDSYTDREDSNKDEDDAIPQRSRRQRSSRAASVPKKSYVETLELSDDSFIEDDEEENQGSDVSFNEED | |
| 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 |
|---|---|---|---|---|---|
| 2 | Phosphorylation | ------MSTEPVSAS ------CCCCCCCHH | 53.43 | 28152593 | |
| 3 | Phosphorylation | -----MSTEPVSASD -----CCCCCCCHHH | 57.05 | 28889911 | |
| 7 | Phosphorylation | -MSTEPVSASDKYQK -CCCCCCCHHHHHHH | 32.54 | 30377154 | |
| 9 | Phosphorylation | STEPVSASDKYQKIS CCCCCCHHHHHHHHH | 27.42 | 30377154 | |
| 11 | Acetylation | EPVSASDKYQKISQL CCCCHHHHHHHHHHH | 47.27 | 22865919 | |
| 128 | Phosphorylation | FGHLLTSSNYDDDEK HHHHHCCCCCCCCCC | 33.89 | 19779198 | |
| 130 | Phosphorylation | HLLTSSNYDDDEKKV HHHCCCCCCCCCCCC | 23.77 | 19779198 | |
| 592 | Phosphorylation | EKWREEESHKFTWKQ HHHHHHHHCCCCCCH | 34.94 | 19823750 | |
| 596 | Phosphorylation | EEESHKFTWKQKYYK HHHHCCCCCCHHHHC | 36.23 | 19823750 | |
| 629 | Phosphorylation | RHLKIFHSLQGNDKD HHHHHHHHHCCCCCC | 16.19 | 28889911 | |
| 700 | Ubiquitination | PNVLDGFKPGQRKVL CCCCCCCCCCHHHHH | 54.49 | 24961812 | |
| 716 | Acetylation | GCFKKNLKSELKVAQ HHHHCCHHHHHHHHH | 51.80 | 25381059 | |
| 789 | Acetylation | YIYTELNKLTRKIFH HHHHHHHHHHHHHCC | 64.95 | 24489116 | |
| 791 | Phosphorylation | YTELNKLTRKIFHPA HHHHHHHHHHHCCCC | 31.37 | 27017623 | |
| 987 | Phosphorylation | PHGKIKKYNSVNEIL CCCCCCCCCCHHHHH | 13.99 | 30377154 | |
| 989 | Phosphorylation | GKIKKYNSVNEILSE CCCCCCCCHHHHHHH | 24.19 | 30377154 | |
| 995 | Phosphorylation | NSVNEILSEFYYVRL CCHHHHHHHHHHHHH | 31.18 | 30377154 | |
| 999 | Phosphorylation | EILSEFYYVRLEYYQ HHHHHHHHHHHHHHH | 5.61 | 30377154 | |
| 1086 | Phosphorylation | INDVKGATSDEEDEE HHHCCCCCCCCCCHH | 45.43 | 1316274 | |
| 1087 | Phosphorylation | NDVKGATSDEEDEES HHCCCCCCCCCCHHC | 42.35 | 1316274 | |
| 1094 | Phosphorylation | SDEEDEESSHEDTEN CCCCCHHCCCCCCCC | 34.64 | 28889911 | |
| 1095 | Phosphorylation | DEEDEESSHEDTENV CCCCHHCCCCCCCCC | 33.89 | 19779198 | |
| 1099 | Phosphorylation | EESSHEDTENVINGP HHCCCCCCCCCCCCH | 26.86 | 19779198 | |
| 1202 | Phosphorylation | KLVDDEDYDPSKKNK CCCCCCCCCCCCCCC | 27.92 | 27017623 | |
| 1206 | Acetylation | DEDYDPSKKNKKSTA CCCCCCCCCCCCCCC | 66.80 | 24489116 | |
| 1220 | Sumoylation | ARKGKKIKLEDKNFE CCCCCCCCCCCCCHH | 55.49 | - | |
| 1234 | Acetylation | ERILLEQKLVTKSKA HHHHHHHHHHHCCCC | 35.23 | 24489116 | |
| 1246 | Sumoylation | SKAPTKIKKEKTPSV CCCCCCCCCCCCCCC | 57.33 | - | |
| 1250 | Phosphorylation | TKIKKEKTPSVSETK CCCCCCCCCCCCCCC | 23.14 | 21551504 | |
| 1252 | Phosphorylation | IKKEKTPSVSETKTE CCCCCCCCCCCCCCC | 43.43 | 28889911 | |
| 1254 | Phosphorylation | KEKTPSVSETKTEEE CCCCCCCCCCCCCCH | 43.84 | 25521595 | |
| 1256 | Phosphorylation | KTPSVSETKTEEEEN CCCCCCCCCCCCHHC | 35.44 | 20377248 | |
| 1258 | Phosphorylation | PSVSETKTEEEENAP CCCCCCCCCCHHCCC | 56.92 | 1316274 | |
| 1266 | Phosphorylation | EEEENAPSSTSSSSI CCHHCCCCCCCCCCC | 43.78 | 1316274 | |
| 1267 | Phosphorylation | EEENAPSSTSSSSIF CHHCCCCCCCCCCCE | 31.11 | 23749301 | |
| 1268 | Phosphorylation | EENAPSSTSSSSIFD HHCCCCCCCCCCCEE | 36.64 | 27214570 | |
| 1269 | Phosphorylation | ENAPSSTSSSSIFDI HCCCCCCCCCCCEEE | 30.12 | 1316274 | |
| 1270 | Phosphorylation | NAPSSTSSSSIFDIK CCCCCCCCCCCEEEE | 28.35 | 23749301 | |
| 1271 | Phosphorylation | APSSTSSSSIFDIKK CCCCCCCCCCEEEEH | 27.50 | 27214570 | |
| 1272 | Phosphorylation | PSSTSSSSIFDIKKE CCCCCCCCCEEEEHH | 29.26 | 1316274 | |
| 1277 | Sumoylation | SSSIFDIKKEDKDEG CCCCEEEEHHHCCCC | 52.54 | - | |
| 1290 | Phosphorylation | EGELSKISNKFKKIS CCHHHHHHHHHHHHH | 37.39 | 19795423 | |
| 1292 | Acetylation | ELSKISNKFKKISTI HHHHHHHHHHHHHHH | 52.34 | 25381059 | |
| 1294 | Acetylation | SKISNKFKKISTIFD HHHHHHHHHHHHHHH | 51.29 | 25381059 | |
| 1297 | Phosphorylation | SNKFKKISTIFDKMG HHHHHHHHHHHHHHC | 25.08 | 21440633 | |
| 1302 | Acetylation | KISTIFDKMGSTSAT HHHHHHHHHCCCCCC | 34.12 | 24489116 | |
| 1305 | Phosphorylation | TIFDKMGSTSATSKE HHHHHHCCCCCCCCC | 18.72 | 29136822 | |
| 1306 | Phosphorylation | IFDKMGSTSATSKEN HHHHHCCCCCCCCCC | 19.36 | 17330950 | |
| 1307 | Phosphorylation | FDKMGSTSATSKENT HHHHCCCCCCCCCCC | 31.11 | 19823750 | |
| 1309 | Phosphorylation | KMGSTSATSKENTPE HHCCCCCCCCCCCCC | 39.85 | 19823750 | |
| 1310 | Phosphorylation | MGSTSATSKENTPEQ HCCCCCCCCCCCCCC | 37.37 | 19823750 | |
| 1314 | Phosphorylation | SATSKENTPEQDDVA CCCCCCCCCCCCCCC | 29.33 | 22369663 | |
| 1322 | Phosphorylation | PEQDDVATKKNQTTA CCCCCCCCHHCCHHH | 42.26 | 22369663 | |
| 1323 | Acetylation | EQDDVATKKNQTTAK CCCCCCCHHCCHHHC | 39.73 | 25381059 | |
| 1331 | Acetylation | KNQTTAKKTAVKPKL HCCHHHCHHCCCHHH | 38.97 | 25381059 | |
| 1335 | Acetylation | TAKKTAVKPKLAKKP HHCHHCCCHHHCCCC | 33.69 | 25381059 | |
| 1353 | Phosphorylation | QQKVVELSGESDLEI CCEEEEECCCCCHHH | 27.32 | 1316274 | |
| 1356 | Phosphorylation | VVELSGESDLEILDS EEEECCCCCHHHHHH | 51.53 | 1316274 | |
| 1363 | Phosphorylation | SDLEILDSYTDREDS CCHHHHHHCCCCCCC | 26.87 | 19795423 | |
| 1364 | Phosphorylation | DLEILDSYTDREDSN CHHHHHHCCCCCCCC | 16.60 | 19795423 | |
| 1365 | Phosphorylation | LEILDSYTDREDSNK HHHHHHCCCCCCCCC | 32.31 | 21440633 | |
| 1370 | Phosphorylation | SYTDREDSNKDEDDA HCCCCCCCCCCCCCC | 40.81 | 25704821 | |
| 1392 | Phosphorylation | QRSSRAASVPKKSYV HHHHHCCCCCCHHHE | 37.66 | 30377154 | |
| 1408 | Phosphorylation | TLELSDDSFIEDDEE EEECCCCCCCCCCCC | 32.87 | 1316274 | |
| 1423 | Phosphorylation | ENQGSDVSFNEED-- CCCCCCCCCCCCC-- | 27.61 | 1316274 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
| 1086 | T | Phosphorylation | Kinase | CK2_GROUP | - | PhosphoELM |
| 1086 | T | Phosphorylation | Kinase | CK2-FAMILY | - | GPS |
| 1086 | T | Phosphorylation | Kinase | CK2 | - | Uniprot |
| 1087 | S | Phosphorylation | Kinase | CK2_GROUP | - | PhosphoELM |
| 1087 | S | Phosphorylation | Kinase | CK2-FAMILY | - | GPS |
| 1087 | S | Phosphorylation | Kinase | CK2 | - | Uniprot |
| 1258 | T | Phosphorylation | Kinase | CK2 | - | Uniprot |
| 1258 | T | Phosphorylation | Kinase | CK2-FAMILY | - | GPS |
| 1258 | T | Phosphorylation | Kinase | CK2_GROUP | - | PhosphoELM |
| 1266 | S | Phosphorylation | Kinase | CK2_GROUP | - | PhosphoELM |
| 1266 | S | Phosphorylation | Kinase | CK2 | - | Uniprot |
| 1266 | S | Phosphorylation | Kinase | CK2-FAMILY | - | GPS |
| 1269 | S | Phosphorylation | Kinase | CK2-FAMILY | - | GPS |
| 1269 | S | Phosphorylation | Kinase | CK2_GROUP | - | PhosphoELM |
| 1269 | S | Phosphorylation | Kinase | CK2 | - | Uniprot |
| 1272 | S | Phosphorylation | Kinase | CK2 | - | Uniprot |
| 1272 | S | Phosphorylation | Kinase | CK2_GROUP | - | PhosphoELM |
| 1272 | S | Phosphorylation | Kinase | CK2-FAMILY | - | GPS |
| 1353 | S | Phosphorylation | Kinase | CK2 | - | Uniprot |
| 1353 | S | Phosphorylation | Kinase | CK2_GROUP | - | PhosphoELM |
| 1353 | S | Phosphorylation | Kinase | CK2-FAMILY | - | GPS |
| 1356 | S | Phosphorylation | Kinase | CK2 | - | Uniprot |
| 1356 | S | Phosphorylation | Kinase | CK2-FAMILY | - | GPS |
| 1356 | S | Phosphorylation | Kinase | CK2_GROUP | - | PhosphoELM |
| 1408 | S | Phosphorylation | Kinase | CK2 | - | Uniprot |
| 1408 | S | Phosphorylation | Kinase | CK2_GROUP | - | PhosphoELM |
| 1408 | S | Phosphorylation | Kinase | CK2-FAMILY | - | GPS |
| 1423 | S | Phosphorylation | Kinase | CK2 | - | Uniprot |
| 1423 | S | Phosphorylation | Kinase | CK2_GROUP | - | PhosphoELM |
| 1423 | S | Phosphorylation | Kinase | CK2-FAMILY | - | GPS |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of TOP2_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 TOP2_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 THR-1268 AND SER-1269, 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-1250; THR-1306;THR-1309; SER-1310 AND THR-1314, AND MASS SPECTROMETRY. | |
