TOP1M_HUMAN - dbPTM
TOP1M_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TOP1M_HUMAN
UniProt AC Q969P6
Protein Name DNA topoisomerase I, mitochondrial
Gene Name TOP1MT
Organism Homo sapiens (Human).
Sequence Length 601
Subcellular Localization Mitochondrion .
Protein Description Releases the supercoiling and torsional tension of DNA introduced during duplication of mitochondrial DNA 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. The 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 MRVVRLLRLRAALTLLGEVPRRPASRGVPGSRRTQKGSGARWEKEKHEDGVKWRQLEHKGPYFAPPYEPLPDGVRFFYEGRPVRLSVAAEEVATFYGRMLDHEYTTKEVFRKNFFNDWRKEMAVEEREVIKSLDKCDFTEIHRYFVDKAAARKVLSREEKQKLKEEAEKLQQEFGYCILDGHQEKIGNFKIEPPGLFRGRGDHPKMGMLKRRITPEDVVINCSRDSKIPEPPAGHQWKEVRSDNTVTWLAAWTESVQNSIKYIMLNPCSKLKGETAWQKFETARRLRGFVDEIRSQYRADWKSREMKTRQRAVALYFIDKLALRAGNEKEDGEAADTVGCCSLRVEHVQLHPEADGCQHVVEFDFLGKDCIRYYNRVPVEKPVYKNLQLFMENKDPRDDLFDRLTTTSLNKHLQELMDGLTAKVFRTYNASITLQEQLRALTRAEDSIAAKILSYNRANRVVAILCNHQRATPSTFEKSMQNLQTKIQAKKEQVAEARAELRRARAEHKAQGDGKSRSVLEKKRRLLEKLQEQLAQLSVQATDKEENKQVALGTSKLNYLDPRISIAWCKRFRVPVEKIYSKTQRERFAWALAMAGEDFEF
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
31PhosphorylationASRGVPGSRRTQKGS
HHCCCCCCCCCCCCC
16.7223312004
34O-linked_GlycosylationGVPGSRRTQKGSGAR
CCCCCCCCCCCCCCC
33.2630379171
46AcetylationGARWEKEKHEDGVKW
CCCCCHHCCCCCCCC
64.4619823717
52AcetylationEKHEDGVKWRQLEHK
HCCCCCCCCCCCCCC
42.0319823725
96PhosphorylationAEEVATFYGRMLDHE
HHHHHHHHHHHHCCC
10.24-
104PhosphorylationGRMLDHEYTTKEVFR
HHHHCCCCCHHHHHH
19.11-
112AcetylationTTKEVFRKNFFNDWR
CHHHHHHHHCCHHHH
46.7912432645
210MethylationHPKMGMLKRRITPED
CCCCCCEECCCCHHH
30.64-
214PhosphorylationGMLKRRITPEDVVIN
CCEECCCCHHHEEEE
20.8625599653
226PhosphorylationVINCSRDSKIPEPPA
EEECCCCCCCCCCCC
31.2325599653
242PhosphorylationHQWKEVRSDNTVTWL
CCCEEECCCCCCHHH
40.1520068231
245PhosphorylationKEVRSDNTVTWLAAW
EEECCCCCCHHHHHH
25.0520068231
247PhosphorylationVRSDNTVTWLAAWTE
ECCCCCCHHHHHHHH
16.8420068231
253PhosphorylationVTWLAAWTESVQNSI
CHHHHHHHHHHHHHH
17.4120068231
255PhosphorylationWLAAWTESVQNSIKY
HHHHHHHHHHHHHHH
22.9420068231
259PhosphorylationWTESVQNSIKYIMLN
HHHHHHHHHHHHEEC
11.9020068231
262PhosphorylationSVQNSIKYIMLNPCS
HHHHHHHHHEECCHH
7.0119835603
269PhosphorylationYIMLNPCSKLKGETA
HHEECCHHHCCCCHH
42.1324114839
282PhosphorylationTAWQKFETARRLRGF
HHHHHHHHHHHHHHH
28.7024719451
295PhosphorylationGFVDEIRSQYRADWK
HHHHHHHHHHHHHHH
36.9119369195
316PhosphorylationRQRAVALYFIDKLAL
HHHHHHHHHHHHHHH
6.6928152594
320UbiquitinationVALYFIDKLALRAGN
HHHHHHHHHHHHCCC
30.73-
329UbiquitinationALRAGNEKEDGEAAD
HHHCCCCCCCCCCCC
66.17-
384PhosphorylationVPVEKPVYKNLQLFM
CCCCCHHHHCHHHHH
11.59-
405PhosphorylationDDLFDRLTTTSLNKH
CCHHHHHHHHHHHHH
28.99-
408PhosphorylationFDRLTTTSLNKHLQE
HHHHHHHHHHHHHHH
28.0524719451
421PhosphorylationQELMDGLTAKVFRTY
HHHHHHHHHHHHHHH
29.9324719451
427PhosphorylationLTAKVFRTYNASITL
HHHHHHHHHCCCCCH
15.06-
428PhosphorylationTAKVFRTYNASITLQ
HHHHHHHHCCCCCHH
12.41-
479PhosphorylationTPSTFEKSMQNLQTK
CHHHHHHHHHHHHHH
20.5728842319
485PhosphorylationKSMQNLQTKIQAKKE
HHHHHHHHHHHHHHH
33.0329888752
515AcetylationHKAQGDGKSRSVLEK
HHHCCCCCCHHHHHH
47.657710503
559PhosphorylationLGTSKLNYLDPRISI
EECCCCCCCCCCCEE
23.9528152594

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 TOP1M_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TOP1M_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 TOP1M_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of TOP1M_HUMAN !!

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
DB00762Irinotecan
DB01030Topotecan
Regulatory Network of TOP1M_HUMAN

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Related Literatures of Post-Translational Modification

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