UBC9_ARATH - dbPTM
UBC9_ARATH - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UBC9_ARATH
UniProt AC P35132
Protein Name SUMO-conjugating enzyme UBC9
Gene Name UBC9
Organism Arabidopsis thaliana (Mouse-ear cress).
Sequence Length 148
Subcellular Localization
Protein Description Accepts the ubiquitin-like protein SUMO/SMT3 from the E1 complex and catalyzes its covalent attachment to other proteins. Mediates the selective degradation of short-lived and abnormal proteins..
Protein Sequence MASKRILKELKDLQKDPPTSCSAGPVAEDMFHWQATIMGPSDSPYSGGVFLVTIHFPPDYPFKPPKVAFRTKVFHPNINSNGSICLDILKEQWSPALTISKVLLSICSLLTDPNPDDPLVPEIAHMYKTDKNKYESTARTWTQKYAMG
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

Oops, there are no PTM records of UBC9_ARATH !!

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 UBC9_ARATH !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of UBC9_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 UBC9_ARATH !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UBQ3_ARATHUBQ3physical
16339806

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of UBC9_ARATH

loading...

Related Literatures of Post-Translational Modification

TOP