UniProt ID | CLPP3_ARATH | |
---|---|---|
UniProt AC | Q9SXJ6 | |
Protein Name | ATP-dependent Clp protease proteolytic subunit 3, chloroplastic {ECO:0000303|PubMed:11299370} | |
Gene Name | CLPP3 {ECO:0000303|PubMed:11299370} | |
Organism | Arabidopsis thaliana (Mouse-ear cress). | |
Sequence Length | 309 | |
Subcellular Localization | Plastid, chloroplast stroma . | |
Protein Description | Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins (By similarity). In the absence of CLPP3, modified ClpPR core(s) could be formed, albeit at strongly reduced levels. [PubMed: 23548781] | |
Protein Sequence | MEMSLRLASSSTSNPICLLNPGKNLNFPIRNHRIPKTSKPFCVRSSMSLSKPPRQTLSSNWDVSSFSIDSVAQSPSRLPSFEELDTTNMLLRQRIVFLGSQVDDMTADLVISQLLLLDAEDSERDITLFINSPGGSITAGMGIYDAMKQCKADVSTVCLGLAASMGAFLLASGSKGKRYCMPNSKVMIHQPLGTAGGKATEMSIRIREMMYHKIKLNKIFSRITGKPESEIESDTDRDNFLNPWEAKEYGLIDAVIDDGKPGLIAPIGDGTPPPKTKVWDLWKVEGTKKDNTNLPSERSMTQNGYAAIE | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
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 CLPP3_ARATH !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CLPP3_ARATH !! |
* 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 CLPP3_ARATH !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
CLPP4_ARATH | CLPP4 | physical | 21712416 | |
CLPP5_ARATH | CLPP5 | physical | 21712416 | |
CLPP6_ARATH | CLPP6 | physical | 21712416 |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"Large-scale Arabidopsis phosphoproteome profiling reveals novelchloroplast kinase substrates and phosphorylation networks."; Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,Grossmann J., Gruissem W., Baginsky S.; Plant Physiol. 150:889-903(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-194, AND MASSSPECTROMETRY. |