| UniProt ID | CALR1_ARATH | |
|---|---|---|
| UniProt AC | O04151 | |
| Protein Name | Calreticulin-1 | |
| Gene Name | CRT1 | |
| Organism | Arabidopsis thaliana (Mouse-ear cress). | |
| Sequence Length | 425 | |
| Subcellular Localization | Endoplasmic reticulum lumen . | |
| Protein Description | Molecular calcium-binding chaperone promoting folding, oligomeric assembly and quality control in the ER via the calreticulin/calnexin cycle. This lectin may interact transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER (By similarity).. | |
| Protein Sequence | MAKLNPKFISLILFALVVIVSAEVIFEEKFEDGWEKRWVKSDWKKDDNTAGEWKHTAGNWSGDANDKGIQTSEDYRFYAISAEFPEFSNKDKTLVFQFSVKHEQKLDCGGGYMKLLSDDVDQTKFGGDTPYSIMFGPDICGYSTKKVHAILTYNGTNHLIKKEVPCETDQLTHVYTFVLRPDATYSILIDNVEKQTGSLYSDWDLLPAKKIKDPSAKKPEDWDDKEYIPDPEDTKPAGYDDIPKEIPDTDAKKPEDWDDEEDGEWTAPTIPNPEYNGEWKPKKIKNPAYKGKWKAPMIDNPEFKDDPELYVFPKLKYVGVELWQVKSGSLFDNVLVSDDPEYAKKLAEETWGKHKDAEKAAFDEAEKKREEEESKDAPAESDAEEEAEDDDNEGDDSDNESKSEETKEAEETKEAEETDAAHDEL | |
| 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 |
|---|---|---|---|---|---|
| 59 | N-linked_Glycosylation | EWKHTAGNWSGDAND CCEECCCCCCCCCCC | 27.55 | - | |
| 154 | N-linked_Glycosylation | VHAILTYNGTNHLIK EEEEEEECCCCCEEE | 45.65 | - | |
| 337 | Phosphorylation | LFDNVLVSDDPEYAK CCCCEEECCCHHHHH | 31.94 | 19880383 | |
| 374 | Phosphorylation | KKREEEESKDAPAES HHHHHHHHCCCCCCC | 38.83 | 23776212 | |
| 381 | Phosphorylation | SKDAPAESDAEEEAE HCCCCCCCCHHHHHC | 44.20 | 24601666 | |
| 397 | Phosphorylation | DDNEGDDSDNESKSE CCCCCCCCCCCCHHH | 47.26 | 19880383 | |
| 399 | N-linked_Glycosylation | NEGDDSDNESKSEET CCCCCCCCCCHHHHH | 60.43 | - | |
| 401 | Phosphorylation | GDDSDNESKSEETKE CCCCCCCCHHHHHHH | 47.97 | 23776212 | |
| 403 | Phosphorylation | DSDNESKSEETKEAE CCCCCCHHHHHHHHH | 50.36 | 23776212 | |
| 406 | Phosphorylation | NESKSEETKEAEETK CCCHHHHHHHHHHHH | 30.08 | 23776212 | |
| 412 | Phosphorylation | ETKEAEETKEAEETD HHHHHHHHHHHHHHH | 26.20 | 23660473 | |
| 418 | Phosphorylation | ETKEAEETDAAHDEL HHHHHHHHHHHHHCC | 23.57 | 30407730 |
| 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 CALR1_ARATH !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CALR1_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 CALR1_ARATH !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of CALR1_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-381 AND SER-397, ANDMASS SPECTROMETRY. | |
| "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-381, AND MASSSPECTROMETRY. | |