TOP3B_HUMAN - dbPTM
TOP3B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TOP3B_HUMAN
UniProt AC O95985
Protein Name DNA topoisomerase 3-beta-1
Gene Name TOP3B
Organism Homo sapiens (Human).
Sequence Length 862
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 than 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 (By similarity). Possesses negatively supercoiled DNA relaxing activity..
Protein Sequence MKTVLMVAEKPSLAQSIAKILSRGSLSSHKGLNGACSVHEYTGTFAGQPVRFKMTSVCGHVMTLDFLGKYNKWDKVDPAELFSQAPTEKKEANPKLNMVKFLQVEGRGCDYIVLWLDCDKEGENICFEVLDAVLPVMNKAHGGEKTVFRARFSSITDTDICNAMACLGEPDHNEALSVDARQELDLRIGCAFTRFQTKYFQGKYGDLDSSLISFGPCQTPTLGFCVERHDKIQSFKPETYWVLQAKVNTDKDRSLLLDWDRVRVFDREIAQMFLNMTKLEKEAQVEATSRKEKAKQRPLALNTVEMLRVASSSLGMGPQHAMQTAERLYTQGYISYPRTETTHYPENFDLKGSLRQQANHPYWADTVKRLLAEGINRPRKGHDAGDHPPITPMKSATEAELGGDAWRLYEYITRHFIATVSHDCKYLQSTISFRIGPELFTCSGKTVLSPGFTEVMPWQSVPLEESLPTCQRGDAFPVGEVKMLEKQTNPPDYLTEAELITLMEKHGIGTDASIPVHINNICQRNYVTVESGRRLKPTNLGIVLVHGYYKIDAELVLPTIRSAVEKQLNLIAQGKADYRQVLGHTLDVFKRKFHYFVDSIAGMDELMEVSFSPLAATGKPLSRCGKCHRFMKYIQAKPSRLHCSHCDETYTLPQNGTIKLYKELRCPLDDFELVLWSSGSRGKSYPLCPYCYNHPPFRDMKKGMGCNECTHPSCQHSLSMLGIGQCVECESGVLVLDPTSGPKWKVACNKCNVVAHCFENAHRVRVSADTCSVCEAALLDVDFNKAKSPLPGDETQHMGCVFCDPVFQELVELKHAASCHPMHRGGPGRRQGRGRGRARRPPGKPNPRRPKDKMSALAAYFV
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
3Phosphorylation-----MKTVLMVAEK
-----CCEEEEEECC
19.9929083192
12PhosphorylationLMVAEKPSLAQSIAK
EEEECCHHHHHHHHH
47.6129083192
16PhosphorylationEKPSLAQSIAKILSR
CCHHHHHHHHHHHHC
20.9329083192
19UbiquitinationSLAQSIAKILSRGSL
HHHHHHHHHHHCCCC
42.3721890473
19 (in isoform 3)Ubiquitination-42.3721890473
19 (in isoform 1)Ubiquitination-42.3721890473
19 (in isoform 2)Ubiquitination-42.3721890473
70PhosphorylationTLDFLGKYNKWDKVD
EHHHHCCCCCCCCCC
21.85-
75UbiquitinationGKYNKWDKVDPAELF
CCCCCCCCCCHHHHH
47.63-
83PhosphorylationVDPAELFSQAPTEKK
CCHHHHHHCCCCCCC
37.7529083192
87PhosphorylationELFSQAPTEKKEANP
HHHHCCCCCCCCCCC
64.5529083192
89UbiquitinationFSQAPTEKKEANPKL
HHCCCCCCCCCCCCC
59.39-
95AcetylationEKKEANPKLNMVKFL
CCCCCCCCCCEEEEE
52.9125953088
100 (in isoform 2)Ubiquitination-29.5921890473
100 (in isoform 1)Ubiquitination-29.5921890473
100AcetylationNPKLNMVKFLQVEGR
CCCCCEEEEEEECCC
29.5926051181
100 (in isoform 3)Ubiquitination-29.5921890473
100UbiquitinationNPKLNMVKFLQVEGR
CCCCCEEEEEEECCC
29.5921890473
139UbiquitinationAVLPVMNKAHGGEKT
HHHHHHHHHCCCCCE
24.54-
198UbiquitinationAFTRFQTKYFQGKYG
CHHHHHHHHHCCCCC
33.03-
236AcetylationHDKIQSFKPETYWVL
CHHHHHCCCEEEEEE
47.3826051181
254PhosphorylationVNTDKDRSLLLDWDR
ECCCCCCCCEECHHH
33.2429523821
281AcetylationLNMTKLEKEAQVEAT
HHHHHHHHHHHHHHH
69.64156179
281UbiquitinationLNMTKLEKEAQVEAT
HHHHHHHHHHHHHHH
69.64-
330PhosphorylationQTAERLYTQGYISYP
HHHHHHHHCCCCCCC
21.8028152594
333PhosphorylationERLYTQGYISYPRTE
HHHHHCCCCCCCCCC
4.1123663014
335PhosphorylationLYTQGYISYPRTETT
HHHCCCCCCCCCCCC
22.1728152594
336PhosphorylationYTQGYISYPRTETTH
HHCCCCCCCCCCCCC
6.2828152594
351 (in isoform 2)Ubiquitination-48.5821890473
351 (in isoform 1)Ubiquitination-48.5821890473
351 (in isoform 3)Ubiquitination-48.5821890473
351UbiquitinationYPENFDLKGSLRQQA
CCCCCCCCCHHHHHC
48.582190698
430PhosphorylationDCKYLQSTISFRIGP
CCCHHCCEEEEEECC
14.0023927012
432PhosphorylationKYLQSTISFRIGPEL
CHHCCEEEEEECCCC
14.4629496963
501PhosphorylationLTEAELITLMEKHGI
CCHHHHHHHHHHCCC
32.45-
526PhosphorylationNNICQRNYVTVESGR
HCCCCCCCEEECCCC
10.3329496907
566UbiquitinationTIRSAVEKQLNLIAQ
HHHHHHHHHHHHHHH
54.19-
590AcetylationGHTLDVFKRKFHYFV
HHHHHHHHHHHHHHH
55.3025953088
633PhosphorylationKCHRFMKYIQAKPSR
HHHHHHHHHHCCCCC
6.1028634120
637UbiquitinationFMKYIQAKPSRLHCS
HHHHHHCCCCCEEEC
27.44-
639PhosphorylationKYIQAKPSRLHCSHC
HHHHCCCCCEEECCC
46.9328634120
644PhosphorylationKPSRLHCSHCDETYT
CCCCEEECCCCCEEE
19.1928634120
657PhosphorylationYTLPQNGTIKLYKEL
EECCCCCEEEEEEEE
23.6128634120
662AcetylationNGTIKLYKELRCPLD
CCEEEEEEEECCCCC
61.7926051181
677PhosphorylationDFELVLWSSGSRGKS
CCEEEEEECCCCCCC
22.2127174698
678PhosphorylationFELVLWSSGSRGKSY
CEEEEEECCCCCCCC
29.2527174698
680PhosphorylationLVLWSSGSRGKSYPL
EEEEECCCCCCCCCC
39.5527174698
772PhosphorylationRVSADTCSVCEAALL
EECCCCCHHHHHHHC
31.7127251275
788PhosphorylationVDFNKAKSPLPGDET
CCCCCCCCCCCCCCC
36.2125159151
824MethylationASCHPMHRGGPGRRQ
HHCCCCCCCCCCCCC
45.58115384017
829MethylationMHRGGPGRRQGRGRG
CCCCCCCCCCCCCCC
30.77115918741
853UbiquitinationNPRRPKDKMSALAAY
CCCCCHHHHHHHHHH
40.66-

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 TOP3B_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TOP3B_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 TOP3B_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RSMB_HUMANSNRPBphysical
11549288
CENPF_HUMANCENPFphysical
11549288
CHD8_HUMANCHD8physical
11549288
CHIC2_HUMANCHIC2physical
16189514
KR412_HUMANKRTAP4-12physical
16189514
FBLN5_HUMANFBLN5physical
11549288
GRN_HUMANGRNphysical
11549288
PNMA2_HUMANPNMA2physical
25416956
TRIM1_HUMANMID2physical
25416956
ATL4_HUMANADAMTSL4physical
25416956
TRI41_HUMANTRIM41physical
25416956
ADIP_HUMANSSX2IPphysical
25416956
SPRE2_HUMANSPRED2physical
25416956
TDRD3_HUMANTDRD3physical
26344197
TDRD3_HUMANTDRD3physical
28101374

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 TOP3B_HUMAN

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Related Literatures of Post-Translational Modification

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