| UniProt ID | HMGB4_ARATH | |
|---|---|---|
| UniProt AC | Q42344 | |
| Protein Name | High mobility group B protein 4 | |
| Gene Name | HMGB4 | |
| Organism | Arabidopsis thaliana (Mouse-ear cress). | |
| Sequence Length | 138 | |
| Subcellular Localization | Nucleus . Cytoplasm, cytosol . | |
| Protein Description | Binds preferentially double-stranded DNA.. | |
| Protein Sequence | MKGGESKAEATSTDQRLKTRGRKAGKKTKKDPNQPKRPPSAFFVFLEDFRKEFNLANPNNKSVATVGKAAGARWKAMTDEDKAPYVAKAESRKTEYIKNVQQYNLKLASGTNREEDDSDKSKSEVDEAVSEEEAEDDD | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 118 | Phosphorylation | TNREEDDSDKSKSEV CCCCCCCCCHHHHHH | 60.30 | 23776212 | |
| 121 | Phosphorylation | EEDDSDKSKSEVDEA CCCCCCHHHHHHHHH | 46.54 | 23776212 | |
| 123 | Phosphorylation | DDSDKSKSEVDEAVS CCCCHHHHHHHHHHC | 50.36 | 23776212 | |
| 130 | Phosphorylation | SEVDEAVSEEEAEDD HHHHHHHCHHHHHCC | 46.46 | 30291188 |
| 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 HMGB4_ARATH !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of HMGB4_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 HMGB4_ARATH !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of HMGB4_ARATH !! | ||||
| 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-130, AND MASSSPECTROMETRY. | |
| "Phosphoproteomic analysis of nuclei-enriched fractions fromArabidopsis thaliana."; Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A.,Andreasson E., Rathjen J.P., Peck S.C.; J. Proteomics 72:439-451(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130, AND MASSSPECTROMETRY. | |