TOP1_SCHPO - dbPTM
TOP1_SCHPO - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TOP1_SCHPO
UniProt AC P07799
Protein Name DNA topoisomerase 1
Gene Name top1
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length 814
Subcellular Localization
Protein Description Releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(3'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 5'-OH DNA strand. TThe free DNA strand then rotates around the intact phosphodiester bond on the opposing strand, thus removing DNA supercoils. Finally, in the religation step, the DNA 5'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone (By similarity)..
Protein Sequence MSSSDSDSVSLSIRRRQRRGSSKRISMKESDEESDSSENHPLSESLNKKSKSESDEDDIPIRKRRASSKKNMSNSSSKKRAKVMGNGGLKNGKKTAVVKEEEDFNEIAKPSPKHKRVSKANGSKNGAKSAVKKEESDTDDSVPLRAVSTVSLTPYKSELPSGASTTQNRSPNDEEDEDEDYKWWTSENIDDTQKWTTLEHNGVIFAPPYEPLPKNVKLIYDGNPVNLPPEAEEVAGFYAAMLETDHAKNPVFQDNFFRDFLKVCDECNFNHNIKEFSKCDFTQMFHHFEQKREEKKSMPKEQKKAIKQKKDEEEEKYKWCILDGRKEKVGNFRIEPPGLFRGRGSHPKTGSLKRRVYPEQITINIGEGVPVPEPLPGHQWAEVKHDNTVTWLATWHENINNNVKYVFLAAGSSLKGQSDLKKYEKSRKLKDYIDDIRKGYRKDLKSELTVERQRGTAMYLIDVFALRAGNEKGEDEADTVGCCSLRYEHVTLKPPRTVVFDFLGKDSIRYYNEVEVDPQVFKNLKIFKRPPKKEGDLIFDRLSTNSLNKYLTSLMDGLSAKVFRTYNASYTMAEELKKMPKNLTLADKILFYNRANRTVAILCNHQRSVTKNHDVQMERFAERIKALQYQRMRLRKMMLNLEPKLAKSKPELLAKEEGITDSWIVKHHETLYELEKEKIKKKFDRENEKLAAEDPKSVLPESELEVRLKAADELKKALDAELKSKKVDPGRSSMEQLEKRLNKLNERINVMRTQMIDKDENKTTALGTSKINYIDPRLTYSFSKREDVPIEKLFSKTIRDKFNWAADTPPDWKW
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
26PhosphorylationRGSSKRISMKESDEE
CCCCCCCCCCCCCCC		28.0321712547
30PhosphorylationKRISMKESDEESDSS
CCCCCCCCCCCCCCC		44.8224763107
34PhosphorylationMKESDEESDSSENHP
CCCCCCCCCCCCCCC		40.5224763107
36PhosphorylationESDEESDSSENHPLS
CCCCCCCCCCCCCCH		49.1624763107
37PhosphorylationSDEESDSSENHPLSE
CCCCCCCCCCCCCHH		47.6224763107
50PhosphorylationSESLNKKSKSESDED
HHHHCHHCCCCCCCC		42.9224763107
52PhosphorylationSLNKKSKSESDEDDI
HHCHHCCCCCCCCCC		49.8028889911
54PhosphorylationNKKSKSESDEDDIPI
CHHCCCCCCCCCCCH		54.0828889911
111PhosphorylationFNEIAKPSPKHKRVS
HHHHCCCCCCCCCHH		45.9628889911
136PhosphorylationSAVKKEESDTDDSVP
HHHCHHHCCCCCCCE		47.0728889911
138PhosphorylationVKKEESDTDDSVPLR
HCHHHCCCCCCCEEE		51.4928889911
141PhosphorylationEESDTDDSVPLRAVS
HHCCCCCCCEEEEEE		28.5724763107
148PhosphorylationSVPLRAVSTVSLTPY
CCEEEEEEEEEECCC		23.3121712547
149PhosphorylationVPLRAVSTVSLTPYK
CEEEEEEEEEECCCC		13.9121712547
151PhosphorylationLRAVSTVSLTPYKSE
EEEEEEEEECCCCCC		26.9821712547
161PhosphorylationPYKSELPSGASTTQN
CCCCCCCCCCCCCCC		60.6629996109
164PhosphorylationSELPSGASTTQNRSP
CCCCCCCCCCCCCCC		35.2029996109
165PhosphorylationELPSGASTTQNRSPN
CCCCCCCCCCCCCCC		31.6929996109
166PhosphorylationLPSGASTTQNRSPND
CCCCCCCCCCCCCCC		22.7329996109
170PhosphorylationASTTQNRSPNDEEDE
CCCCCCCCCCCCCCC		35.2929996109
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 TOP1_SCHPO !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TOP1_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 TOP1_SCHPO !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TOP2_SCHPOtop2genetic
6090122
TOP2_SCHPOtop2genetic
2839305
TOP2_SCHPOtop2genetic
2827111
TOP2_SCHPOtop2genetic
10712506
TOP2_SCHPOtop2genetic
2436053
HOP1_SCHPOhop1genetic
18818364
CSN1_SCHPOcsn1genetic
18818364
YO48_SCHPOSPBC36B7.08cgenetic
18818364
SDC1_SCHPOsdc1genetic
18818364
CCR4_SCHPOccr4genetic
18818364
MU154_SCHPOmug154genetic
18818364
TAS3_SCHPOtas3genetic
18818364
YE7A_SCHPOSPAC4A8.10genetic
22681890
MUG66_SCHPOatg101genetic
22681890
YAS2_SCHPOcsr102genetic
22681890
SCE3_SCHPOsce3genetic
22681890
ALG12_SCHPOalg12genetic
22681890
SWI6_SCHPOswi6genetic
22681890
YBD3_SCHPOSPBC16C6.03cgenetic
22681890
6PGL_SCHPOSPCC16C4.10genetic
22681890
YNU4_SCHPOSPBC28E12.04genetic
22681890
ATP10_SCHPOatp10genetic
22681890
VPS1_SCHPOvps1genetic
22681890
YDG8_SCHPOSPAC26F1.08cgenetic
22681890
YJ52_SCHPOSPCP20C8.02cgenetic
22681890
APT_SCHPOapt1genetic
22681890
DEP1_SCHPOdep1genetic
22681890
ALG9_SCHPOalg9genetic
22681890
CHP1_SCHPOchp1genetic
22681890
PPR2_SCHPOppr2genetic
22681890
GCN5_SCHPOgcn5genetic
22681890
MU113_SCHPOmug113genetic
22681890
TEA2_SCHPOtea2genetic
22681890
RAD57_SCHPOrad57genetic
22681890
GBB_SCHPOgit5genetic
22681890
GPA2_SCHPOgpa2genetic
22681890
YOOH_SCHPOSPBC887.17genetic
22681890
ING2_SCHPOpng2genetic
22681890
PEX6_SCHPOpex6genetic
22681890
YE98_SCHPOerp2genetic
22681890
PPZ_SCHPOpzh1genetic
22681890
PYRD_SCHPOura3genetic
22681890
YGVA_SCHPOdef1genetic
22681890
MU150_SCHPOmug150genetic
22681890
YBAC_SCHPOrud3genetic
22681890
ERD11_SCHPOerd1genetic
22681890
MU170_SCHPOmug170genetic
22681890
YORS_SCHPOstc1genetic
22681890
KTI12_SCHPOSPAC30.02cgenetic
22681890
FFT3_SCHPOfft3genetic
22681890
SUM2_SCHPOsum2genetic
22681890
DAD2_SCHPOdad2genetic
22681890
BHD1_SCHPObhd1genetic
22681890
YJ61_SCHPOSPCC1884.01genetic
22681890
TCP4_SCHPOsub1genetic
22681890
YN53_SCHPOSPBC713.03genetic
22681890
YFE6_SCHPOgmh5genetic
22681890
FYV10_SCHPOSPBC106.13genetic
22681890
ARC1_SCHPOSPAC30C2.04genetic
22681890
ATCZ_SCHPOSPAC4F10.16cgenetic
22681890
MET8_SCHPOSPAC4D7.06cgenetic
22681890
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TOP1_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-52; SER-54; SER-136 ANDTHR-138, AND MASS SPECTROMETRY.

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