GRC10_ARATH - dbPTM
GRC10_ARATH - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GRC10_ARATH
UniProt AC Q29PZ1
Protein Name Glutaredoxin-C10
Gene Name GRXC10
Organism Arabidopsis thaliana (Mouse-ear cress).
Sequence Length 148
Subcellular Localization Cytoplasm.
Protein Description Has a glutathione-disulfide oxidoreductase activity in the presence of NADPH and glutathione reductase. Reduces low molecular weight disulfides and proteins (By similarity)..
Protein Sequence MKTMRGLRNCSNDAVTLDLTVHPPPPPPLPPPAPSTVSSSTASTSLSFDEEETSESKIGRLISEHPVIIFTRFSSCCMCHVMKKLLSTVGVHPTVIEIDDGEIAYLAVEAAPVLFIGGTCVGGFESLVALHLSGQLIPRLVEVGALWA
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 GRC10_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 GRC10_ARATH !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GRC10_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 GRC10_ARATH !!

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

Oops, there are no PPI records of GRC10_ARATH !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of GRC10_ARATH

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Related Literatures of Post-Translational Modification

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