TOP1A_ARATH - dbPTM
TOP1A_ARATH - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TOP1A_ARATH
UniProt AC P30181
Protein Name DNA topoisomerase 1 alpha {ECO:0000305}
Gene Name TOP1A {ECO:0000305}
Organism Arabidopsis thaliana (Mouse-ear cress).
Sequence Length 916
Subcellular Localization Nucleus .
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. 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). Can complement a TOP1-deficient yeast mutant. [PubMed: 16669064 Plays a critical role in the maintenance of a regular pattern of organ initiation. Topoisomerases I enzymes (TOP1A and TOP1B) are essential for plant survival]
Protein Sequence MGTETVSKPVMDNGSGDSDDDKPLAFKRNNTVASNSNQSKSNSQRSKAVPTTKVSPMRSPVTSPNGTTPSNKTSIVKSSMPSSSSKASPAKSPLRNDMPSTVKDRSQLQKDQSECKIEHEDSEDDRPLSSILSGNKGPTSSRQVSSPQPEKKNNGDRPLDRASRIIKDESDDETPISSMFRKKIDSGMSGGNQLSNDEKKPLVQKLHQNGSTVKNEVPNGKVLGKRPLEKNSSADQSSLKKAKISASPTSVKMKQDSVKKEIDDKGRVLVSPKMKAKQLSTREDGTDDDDDDDVPISKRFKSDSSNSNTSSAKPKAVKLNSTSSAAKPKARNVVSPRSRAMTKNTKKVTKDSKYSTSSKSSPSSGDGQKKWTTLVHNGVIFPPPYKPHGIKILYKGKPVDLTIEQEEVATMFAVMRETDYYTKPQFRENFWNDWRRLLGKKHVIQKLDDCDFTPIYEWHLEEKEKKKQMSTEEKKALKEEKMKQEEKYMWAVVDGVKEKIGNFRVEPPGLFRGRGEHPKMGKLKKRIHPCEITLNIGKGAPIPECPIAGERWKEVKHDNTVTWLAFWADPINPKEFKYVFLGAGSSLKGLSDKEKYEKARNLTDHIDNIRTTYTKNFTAKDVKMRQIAVATYLIDKLALRAGNEKDDDEADTVGCCTLKVGNVECIPPNKIKFDFLGKDSIQYVNTVEVEPLVYKAIGQFQAGKSKTDDLFDELDTSKLNAHLKELVPGLTAKVFRTYNASITLDEMLSQETKDGDVTQKIVVYQKANKEVAIICNHQRTVSKTHGAQIEKLTARIEELKEVLKELKTNLDRAKKGKPPLEGSDGKKIRSLEPNAWEKKIAQQSAKIEKMERDMHTKEDLKTVALGTSKINYLDPRITVAWCKRHEVPIEKIFTKSLLEKFAWAMDVEPEYRFSRR
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
15PhosphorylationKPVMDNGSGDSDDDK
CCCCCCCCCCCCCCC
27531888
18PhosphorylationMDNGSGDSDDDKPLA
CCCCCCCCCCCCCCC
27531888
55PhosphorylationAVPTTKVSPMRSPVT
CCCCCCCCCCCCCCC
30589143
88PhosphorylationPSSSSKASPAKSPLR
CCCCCCCCCCCCCCC
25561503
92PhosphorylationSKASPAKSPLRNDMP
CCCCCCCCCCCCCCC
30589143
113PhosphorylationSQLQKDQSECKIEHE
HHHHHCHHHCCCCCC
23776212
122PhosphorylationCKIEHEDSEDDRPLS
CCCCCCCCCCCCCHH
23776212
129PhosphorylationSEDDRPLSSILSGNK
CCCCCCHHHHHCCCC
23776212
130PhosphorylationEDDRPLSSILSGNKG
CCCCCHHHHHCCCCC
23776212
133PhosphorylationRPLSSILSGNKGPTS
CCHHHHHCCCCCCCC
23776212
145PhosphorylationPTSSRQVSSPQPEKK
CCCCCCCCCCCCCCC
25561503
146PhosphorylationTSSRQVSSPQPEKKN
CCCCCCCCCCCCCCC
25561503
170PhosphorylationSRIIKDESDDETPIS
HHHHCCCCCCCCCCH
30291188
174PhosphorylationKDESDDETPISSMFR
CCCCCCCCCCHHHHH
23776212
177PhosphorylationSDDETPISSMFRKKI
CCCCCCCHHHHHHHH
23776212
178PhosphorylationDDETPISSMFRKKID
CCCCCCHHHHHHHHC
23776212
247PhosphorylationKKAKISASPTSVKMK
HHHCCCCCCCCCCCC
23111157
249PhosphorylationAKISASPTSVKMKQD
HCCCCCCCCCCCCHH
19880383
250PhosphorylationKISASPTSVKMKQDS
CCCCCCCCCCCCHHH
19880383
280PhosphorylationKMKAKQLSTREDGTD
CCCHHHCCCCCCCCC
23776212
281PhosphorylationMKAKQLSTREDGTDD
CCHHHCCCCCCCCCC
23776212
286PhosphorylationLSTREDGTDDDDDDD
CCCCCCCCCCCCCCC
30291188
297PhosphorylationDDDDVPISKRFKSDS
CCCCCCHHHHHCCCC
19376835
823PhosphorylationGKPPLEGSDGKKIRS
CCCCCCCCCCCEEEC
25561503

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 TOP1A_ARATH !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TOP1A_ARATH !!

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 TOP1A_ARATH !!

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

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TOP1A_ARATH

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Related Literatures of Post-Translational Modification

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