TOP3A_HUMAN - dbPTM
TOP3A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TOP3A_HUMAN
UniProt AC Q13472
Protein Name DNA topoisomerase 3-alpha
Gene Name TOP3A
Organism Homo sapiens (Human).
Sequence Length 1001
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-(5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand thus removing DNA supercoils. Finally, in the religation step, the DNA 3'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone. Essential component of the RMI complex, a complex that plays an important role in the processing of homologous recombination intermediates to limit DNA crossover formation in cells. Has DNA decatenation activity..
Protein Sequence MIFPVARYALRWLRRPEDRAFSRAAMEMALRGVRKVLCVAEKNDAAKGIADLLSNGRMRRREGLSKFNKIYEFDYHLYGQNVTMVMTSVSGHLLAHDFQMQFRKWQSCNPLVLFEAEIEKYCPENFVDIKKTLERETRQCQALVIWTDCDREGENIGFEIIHVCKAVKPNLQVLRARFSEITPHAVRTACENLTEPDQRVSDAVDVRQELDLRIGAAFTRFQTLRLQRIFPEVLAEQLISYGSCQFPTLGFVVERFKAIQAFVPEIFHRIKVTHDHKDGIVEFNWKRHRLFNHTACLVLYQLCVEDPMATVVEVRSKPKSKWRPQALDTVELEKLASRKLRINAKETMRIAEKLYTQGYISYPRTETNIFPRDLNLTVLVEQQTPDPRWGAFAQSILERGGPTPRNGNKSDQAHPPIHPTKYTNNLQGDEQRLYEFIVRHFLACCSQDAQGQETTVEIDIAQERFVAHGLMILARNYLDVYPYDHWSDKILPVYEQGSHFQPSTVEMVDGETSPPKLLTEADLIALMEKHGIGTDATHAEHIETIKARMYVGLTPDKRFLPGHLGMGLVEGYDSMGYEMSKPDLRAELEADLKLICDGKKDKFVVLRQQVQKYKQVFIEAVAKAKKLDEALAQYFGNGTELAQQEDIYPAMPEPIRKCPQCNKDMVLKTKKNGGFYLSCMGFPECRSAVWLPDSVLEASRDSSVCPVCQPHPVYRLKLKFKRGSLPPTMPLEFVCCIGGCDDTLREILDLRFSGGPPRASQPSGRLQANQSLNRMDNSQHPQPADSRQTGSSKALAQTLPPPTAAGESNSVTCNCGQEAVLLTVRKEGPNRGRQFFKCNGGSCNFFLWADSPNPGAGGPPALAYRPLGASLGCPPGPGIHLGGFGNPGDGSGSGTSCLCSQPSVTRTVQKDGPNKGRQFHTCAKPREQQCGFFQWVDENTAPGTSGAPSWTGDRGRTLESEARSKRPRASSSDMGSTAKKPRKCSLCHQPGHTRPFCPQNR
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
22PhosphorylationRPEDRAFSRAAMEMA
CHHHHHHHHHHHHHH		21.74-
35UbiquitinationMALRGVRKVLCVAEK
HHHHHHCCEEEEECC		36.83-
42UbiquitinationKVLCVAEKNDAAKGI
CEEEEECCCHHHHHH		50.84-
47UbiquitinationAEKNDAAKGIADLLS
ECCCHHHHHHHHHHH		53.20-
54PhosphorylationKGIADLLSNGRMRRR
HHHHHHHHCCHHHHH		44.5318669648
66UbiquitinationRRREGLSKFNKIYEF
HHHHHHHHHHHHEEE		58.98-
73UbiquitinationKFNKIYEFDYHLYGQ
HHHHHEEEEEEECCC		6.75-
130UbiquitinationPENFVDIKKTLERET
CCCCCCHHHHHHHHH		34.93-
162UbiquitinationNIGFEIIHVCKAVKP
CCCHHHHHHHHHCCC		25.28-
168UbiquitinationIHVCKAVKPNLQVLR
HHHHHHCCCCHHHHH		32.80-
226UbiquitinationTRFQTLRLQRIFPEV
HHHHHHHHHHHCHHH		4.51-
232 (in isoform 2)Ubiquitination-39.1421890473
239UbiquitinationEVLAEQLISYGSCQF
HHHHHHHHHCCCCCC		2.73-
250UbiquitinationSCQFPTLGFVVERFK
CCCCCCHHHHHHHHH		18.77-
257UbiquitinationGFVVERFKAIQAFVP
HHHHHHHHHHHHHHH		51.2921890473
257 (in isoform 1)Ubiquitination-51.2921890473
257UbiquitinationGFVVERFKAIQAFVP
HHHHHHHHHHHHHHH		51.2921890473
258UbiquitinationFVVERFKAIQAFVPE
HHHHHHHHHHHHHHH		9.09-
321AcetylationVRSKPKSKWRPQALD
EECCCCCCCCCCCCC		54.0425953088
321UbiquitinationVRSKPKSKWRPQALD
EECCCCCCCCCCCCC		54.04-
326UbiquitinationKSKWRPQALDTVELE
CCCCCCCCCCHHHHH		15.30-
334UbiquitinationLDTVELEKLASRKLR
CCHHHHHHHHHCCCC		63.08-
345UbiquitinationRKLRINAKETMRIAE
CCCCCCHHHHHHHHH		49.59-
353UbiquitinationETMRIAEKLYTQGYI
HHHHHHHHHHHCCCC		37.46-
355PhosphorylationMRIAEKLYTQGYISY
HHHHHHHHHCCCCCC		14.2123663014
356PhosphorylationRIAEKLYTQGYISYP
HHHHHHHHCCCCCCC		26.4223663014
359PhosphorylationEKLYTQGYISYPRTE
HHHHHCCCCCCCCCC		4.1123663014
361PhosphorylationLYTQGYISYPRTETN
HHHCCCCCCCCCCCC		22.1723663014
362PhosphorylationYTQGYISYPRTETNI
HHCCCCCCCCCCCCC		6.2823663014
421UbiquitinationHPPIHPTKYTNNLQG
CCCCCCCCCCCCCCC		55.30-
451UbiquitinationCCSQDAQGQETTVEI
HHCCCCCCCEEEEEE		29.07-
462UbiquitinationTVEIDIAQERFVAHG
EEEEEHHHHHHHHHH		42.61-
498PhosphorylationLPVYEQGSHFQPSTV
ECCCCCCCCCCCCCE		22.3329116813
503PhosphorylationQGSHFQPSTVEMVDG
CCCCCCCCCEEEECC		34.0129116813
504PhosphorylationGSHFQPSTVEMVDGE
CCCCCCCCEEEECCC		27.4529116813
507UbiquitinationFQPSTVEMVDGETSP
CCCCCEEEECCCCCC		2.64-
513PhosphorylationEMVDGETSPPKLLTE
EEECCCCCCCCCCCH		34.6029116813
529UbiquitinationDLIALMEKHGIGTDA
HHHHHHHHCCCCCCC		32.92-
546UbiquitinationAEHIETIKARMYVGL
HHHHHHHHHHHCCCC		37.04-
554PhosphorylationARMYVGLTPDKRFLP
HHHCCCCCCCCCCCC		24.42-
557UbiquitinationYVGLTPDKRFLPGHL
CCCCCCCCCCCCCCC		46.37-
576UbiquitinationVEGYDSMGYEMSKPD
CCCCHHCCCCCCCCH		21.14-
602UbiquitinationICDGKKDKFVVLRQQ
EECCCCCEEEEEHHH		49.27-
668AcetylationCNKDMVLKTKKNGGF
CCCCEEEEEEECCCE		47.0619826825
669PhosphorylationNKDMVLKTKKNGGFY
CCCEEEEEEECCCEE		42.9920166139
670AcetylationKDMVLKTKKNGGFYL
CCEEEEEEECCCEEE		42.5319826833
671UbiquitinationDMVLKTKKNGGFYLS
CEEEEEEECCCEEEE		67.09-
694PhosphorylationSAVWLPDSVLEASRD
CCEECCHHHHHHCCC		27.02-
703PhosphorylationLEASRDSSVCPVCQP
HHHCCCCCCCCCCCC		31.84-
760PhosphorylationSGGPPRASQPSGRLQ
CCCCCCCCCCCCCCC		43.8526714015
771PhosphorylationGRLQANQSLNRMDNS
CCCCCCHHHHCCCCC		27.6725159151
778PhosphorylationSLNRMDNSQHPQPAD
HHHCCCCCCCCCCCC		26.12-
964PhosphorylationTLESEARSKRPRASS
CHHHHHHHCCCCCCC		39.81-
970PhosphorylationRSKRPRASSSDMGST
HHCCCCCCCCCCCCC		31.4928176443
971PhosphorylationSKRPRASSSDMGSTA
HCCCCCCCCCCCCCC		29.4028985074
972PhosphorylationKRPRASSSDMGSTAK
CCCCCCCCCCCCCCC		29.1728176443
976PhosphorylationASSSDMGSTAKKPRK
CCCCCCCCCCCCCCC		20.6729083192
977PhosphorylationSSSDMGSTAKKPRKC
CCCCCCCCCCCCCCC		36.4529083192
985PhosphorylationAKKPRKCSLCHQPGH
CCCCCCCCCCCCCCC		36.7528152594
993PhosphorylationLCHQPGHTRPFCPQN
CCCCCCCCCCCCCCC		46.0528152594
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 TOP3A_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TOP3A_HUMAN !!
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 TOP3A_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BLM_HUMANBLMphysical
11470874
BLM_HUMANBLMphysical
11406610
RFA1_HUMANRPA1physical
12724401
FANCA_HUMANFANCAphysical
12724401
BLM_HUMANBLMphysical
12724401
TERF2_HUMANTERF2physical
18418389
RMI1_HUMANRMI1physical
24509834
CHK1_HUMANCHEK1genetic
27453043
BRCA2_HUMANBRCA2genetic
27453043
WEE1_HUMANWEE1genetic
27453043
PALB2_HUMANPALB2genetic
27453043
RAD17_HUMANRAD17genetic
27453043
L2GL1_HUMANLLGL1genetic
27453043
MSH2_HUMANMSH2genetic
27453043
NF1_HUMANNF1genetic
27453043
RS11_HUMANRPS11genetic
27453043
CDC73_HUMANCDC73genetic
27453043
CDC6_HUMANCDC6genetic
27453043
M3K4_HUMANMAP3K4genetic
27453043
TITIN_HUMANTTNgenetic
27453043
FUMH_HUMANFHgenetic
27453043
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TOP3A_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-54 AND SER-771, AND MASSSPECTROMETRY.

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