UniProt ID | NACA1_ARATH | |
---|---|---|
UniProt AC | Q9LHG9 | |
Protein Name | Nascent polypeptide-associated complex subunit alpha-like protein 1 | |
Gene Name | At3g12390 | |
Organism | Arabidopsis thaliana (Mouse-ear cress). | |
Sequence Length | 203 | |
Subcellular Localization | ||
Protein Description | May promote appropriate targeting of ribosome-nascent polypeptide complexes.. | |
Protein Sequence | MTTEEKEILAAKLEEQKIDLDKPEVEDDDDNEDDDSDDDDKDDDEADGLDGEAGGKSKQSRSEKKSRKAMLKLGMKPITGVSRVTVKKSKNILFVISKPDVFKSPASDTYVIFGEAKIEDLSSQIQSQAAEQFKAPDLSNVISKGESSSAAVVQDDEEVDEEGVEPKDIELVMTQAGVSRPNAVKALKAADGDIVSAIMELTT | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
36 | Phosphorylation | DDNEDDDSDDDDKDD CCCCCCCCCCCCCCC | 50.35 | 30291188 | |
57 | Phosphorylation | DGEAGGKSKQSRSEK CCCCCCCCCCCHHHH | 38.92 | 19376835 | |
75 | Sulfoxidation | KAMLKLGMKPITGVS HHHHHHCCCCCCCCE | 7.27 | 23289948 | |
139 | Phosphorylation | QFKAPDLSNVISKGE HHCCCCHHHHHCCCC | 36.11 | 27288362 | |
143 | Phosphorylation | PDLSNVISKGESSSA CCHHHHHCCCCCCCC | 30.26 | 27288362 |
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 NACA1_ARATH !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of NACA1_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 NACA1_ARATH !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|
Kegg Drug | ||||||
---|---|---|---|---|---|---|
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 SER-36, AND MASSSPECTROMETRY. |