TOP2_SCHPO - dbPTM
TOP2_SCHPO - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TOP2_SCHPO
UniProt AC P08096
Protein Name DNA topoisomerase 2
Gene Name top2
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length 1485
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..
Protein Sequence MSIDADFSDYEDEASGDENVLPNTTTKRKASTTSSKSRAKKASTPDLRQTSLTSMTASEQIPLVTNNGNGNSNVSTQYQRLTPREHVLRRPDTYIGSIEPTTSEMWVFDSEKNKLDYKAVTYVPGLYKIFDEIIVNAADNKVRDPNMNTLKVTLDPEANVISIYNNGKGIPIEIHDKEKIYIPELIFGNLLTSSNYDDNQKKVTGGRNGYGAKLCNIFSTEFVVETADKERMKKYKQTWYDNMSRKSEPVITSLKKPDEYTKITFKPDLAKFGMDKIDDDMVSIIKRRIYDMAGTVRETKVYLNNERISISGFKKYVEMYLASDTKPDEEPPRVIYEHVNDRWDVAFAVSDGQFKQVSFVNNISTIRGGTHVNYVANKIVDAIDEVVKKENKKAPVKAFQIKNYVQVFVNCQIENPSFDSQTKETLTTKVSAFGSQCTLSDKFLKAIKKSSVVEEVLKFATAKADQQLSKGDGGLRSRITGLTKLEDANKAGTKESHKCVLILTEGDSAKSLAVSGLSVVGRDYYGVFPLRGKLLNVREASHSQILNNKEIQAIKKIMGFTHKKTYTDVKGLRYGHLMIMTDQDHDGSHIKGLIINYLESSYPSLLQIPGFLIQFITPIIKCTRGNQVQAFYTLPEYEYWKEANNNGRGWKIKYYKGLGTSDHDDMKSYFSDLDRHMKYFHAMQEKDAELIEMAFAKKKADVRKEWLRTYRPGIYMDYTQPQIPIDDFINRELIQFSMADNIRSIPSVVDGLKPGQRKVVYYCFKRNLVHETKVSRLAGYVASETAYHHGEVSMEQTIVNLAQNFVGSNNINLLMPNGQFGTRSEGGKNASASRYLNTALSPLARVLFNSNDDQLLNYQNDEGQWIEPEYYVPILPMVLVNGAEGIGTGWSTFIPNYNPKDITANLRHMLNGEPLEIMTPWYRGFRGSITKVAPDRYKISGIINQIGENKVEITELPIRFWTQDMKEYLEAGLVGTEKIRKFIVDYESHHGEGNVHFNVTLTEAGMKEALNESLEVKFKLSRTQATSNMIAFDASGRIKKYDSVEDILTEFYEVRLRTYQRRKEHMVNELEKRFDRFSNQARFIHMIIEGELVVSKKKKKDLIVELKEKKFQPISKPKKGHLVDLEVENALAEEEQSGDVSQDEDSDAYNYLLSMPLWSLTYERYVELLKKKDEVMAELDALIKKTPKELWLHDLDAFEHAWNKVMDDIQREMLEEEQSSRDFVNRTKKKPRGKSTGTRKPRAIAGSSSSTAVKKEASSESKPSTTNRKQQTLLEFAASKEPEKSSDINIVKTEDNSHGLSVEENRISKSPGLDSSDSGKSRKRSQSVDSEDAGSKKPVKKIAASASGRGRKTNKPVATTIFSSDDEDDLLPSSLKPSTITSTKASAKNKGKKASSVKKQSPEDDDDDFIIPGSSSTPKASSTNAEPPEDSDSPIRKRPTRRAAATVKTPIYVDPSFDSMDEPSMQDDSFIVDNDEDVDDYDESD
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
2Phosphorylation------MSIDADFSD
------CCCCCCCCC		40.2424763107
8PhosphorylationMSIDADFSDYEDEAS
CCCCCCCCCCCCCCC		39.5728889911
15PhosphorylationSDYEDEASGDENVLP
CCCCCCCCCCCCCCC		44.7424763107
43PhosphorylationKSRAKKASTPDLRQT
HHHHHHCCCCCHHHH		49.7229996109
44PhosphorylationSRAKKASTPDLRQTS
HHHHHCCCCCHHHHH		26.1929996109
1308PhosphorylationSVEENRISKSPGLDS
CCCCCCCCCCCCCCC		24.6825720772
1310PhosphorylationEENRISKSPGLDSSD
CCCCCCCCCCCCCCC		19.8728889911
1315PhosphorylationSKSPGLDSSDSGKSR
CCCCCCCCCCCCCCC		40.8829996109
1316PhosphorylationKSPGLDSSDSGKSRK
CCCCCCCCCCCCCCC		35.1525720772
1325PhosphorylationSGKSRKRSQSVDSED
CCCCCCCCCCCCCCC		29.8221712547
1327PhosphorylationKSRKRSQSVDSEDAG
CCCCCCCCCCCCCCC		29.1924763107
1330PhosphorylationKRSQSVDSEDAGSKK
CCCCCCCCCCCCCCC		34.9124763107
1335PhosphorylationVDSEDAGSKKPVKKI
CCCCCCCCCCCHHHH		38.9521712547
1345PhosphorylationPVKKIAASASGRGRK
CHHHHHHCCCCCCCC		17.5928889911
1353PhosphorylationASGRGRKTNKPVATT
CCCCCCCCCCCEEEE		47.3021712547
1359PhosphorylationKTNKPVATTIFSSDD
CCCCCEEEEEECCCC		22.2121712547
1360PhosphorylationTNKPVATTIFSSDDE
CCCCEEEEEECCCCC		15.4129996109
1363PhosphorylationPVATTIFSSDDEDDL
CEEEEEECCCCCCCC		29.0724763107
1364PhosphorylationVATTIFSSDDEDDLL
EEEEEECCCCCCCCC		38.0328889911
1401PhosphorylationASSVKKQSPEDDDDD
CCCCCCCCCCCCCCC		38.8528889911
1414PhosphorylationDDFIIPGSSSTPKAS
CCCCCCCCCCCCCCC		18.7624763107
1415PhosphorylationDFIIPGSSSTPKASS
CCCCCCCCCCCCCCC		44.1125720772
1416PhosphorylationFIIPGSSSTPKASST
CCCCCCCCCCCCCCC		50.8829996109
1417PhosphorylationIIPGSSSTPKASSTN
CCCCCCCCCCCCCCC		30.6521712547
1421PhosphorylationSSSTPKASSTNAEPP
CCCCCCCCCCCCCCC		43.7721712547
1422PhosphorylationSSTPKASSTNAEPPE
CCCCCCCCCCCCCCC		30.4629996109
1423PhosphorylationSTPKASSTNAEPPED
CCCCCCCCCCCCCCC		35.6329996109
1431PhosphorylationNAEPPEDSDSPIRKR
CCCCCCCCCCCCCCC		38.0221712547
1433PhosphorylationEPPEDSDSPIRKRPT
CCCCCCCCCCCCCCC		26.6128889911
1484PhosphorylationDVDDYDESD------
CCCCCCCCC------		45.8027738172
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
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 TOP2_SCHPO !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TOP2_SCHPO !!
Disease-associated PTM Sites based on SAP

* 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_SCHPO !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
REC7_SCHPOrec7genetic
9763441
FIN1_SCHPOfin1genetic
9490640
CUT1_SCHPOcut1genetic
19528228
CHK1_SCHPOchk1genetic
21767457
CUT1_SCHPOcut1genetic
24687850
H2AZ_SCHPOpht1genetic
24687850
ADA2_SCHPOada2genetic
25669599
GCN5_SCHPOgcn5genetic
25669599
NGG1_SCHPOngg1genetic
25669599
IEC1_SCHPOiec1genetic
25669599
YF98_SCHPOnht10genetic
25669599
ARP42_SCHPOarp42genetic
25669599
RSC1_SCHPOrsc1genetic
25669599
RSC4_SCHPOrsc4genetic
25669599
RAD54_SCHPOrad54genetic
25669599
RAD55_SCHPOrad55genetic
25669599
YCGK_SCHPOSPCC16C4.20cgenetic
25669599
DAD2_SCHPOdad2genetic
25669599
DAD3_SCHPOdad3genetic
25669599
HOS3_SCHPOdad5genetic
25669599
SPC19_SCHPOspc19genetic
25669599
AMPD_SCHPOada1genetic
25669599
CCR4_SCHPOccr4genetic
25669599
CSN1_SCHPOcsn1genetic
25669599
CSN2_SCHPOcsn2genetic
25669599
PPX1_SCHPOSPAC2F3.11genetic
25669599
COQ2_SCHPOppt1genetic
25669599
COQ4_SCHPOcoq4genetic
25669599
COQ6_SCHPOcoq6genetic
25669599
DPS1_SCHPOdps1genetic
25669599
S2538_SCHPOSPAC823.10cgenetic
25669599
PPR1_SCHPOppr1genetic
25669599
CBP6_SCHPOcbp6genetic
25669599
COX19_SCHPOSPCC1672.04cgenetic
25669599
YQJ9_SCHPOSPCC1840.09genetic
25669599
ATPJ_SCHPOtim11genetic
25669599
AP3B_SCHPOapl6genetic
25669599
NP106_SCHPOnpp106genetic
25669599
PMD1_SCHPOpmd1genetic
25669599
YQ92_SCHPOSPCC18.02genetic
25669599
VPH2_SCHPOvph2genetic
25669599
VPS35_SCHPOvps35genetic
25669599
GBB_SCHPOgit5genetic
25669599
NRM1_SCHPOnrm1genetic
25669599
RPA12_SCHPOrpa12genetic
25669599
RFA3_SCHPOssb3genetic
25669599
YEJJ_SCHPOabo1genetic
25669599
PTPA1_SCHPOypa1genetic
25669599
YOX1_SCHPOyox1genetic
25669599
TUP12_SCHPOtup12genetic
25669599
AF9_SCHPOyaf9genetic
25669599
NDUV2_SCHPOSPAC11E3.12genetic
25669599
YDHE_SCHPOSPAC6G9.14genetic
25669599
ASE1_SCHPOase1genetic
25669599
SCE3_SCHPOsce3genetic
25669599
YEM8_SCHPOclr5genetic
25669599
GCN5_SCHPOgcn5genetic
27266525
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TOP2_SCHPO

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Phosphoproteome analysis of fission yeast.";
Wilson-Grady J.T., Villen J., Gygi S.P.;
J. Proteome Res. 7:1088-1097(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1310; SER-1345 ANDSER-1433, AND MASS SPECTROMETRY.

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