| UniProt ID | CALR2_ARATH | |
|---|---|---|
| UniProt AC | Q38858 | |
| Protein Name | Calreticulin-2 | |
| Gene Name | CRT2 | |
| Organism | Arabidopsis thaliana (Mouse-ear cress). | |
| Sequence Length | 424 | |
| 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 | MAKMIPSLVSLILIGLVAIASAAVIFEERFDDGWENRWVKSEWKKDDNTAGEWKHTAGNWSGDANDKGIQTSEDYRFYAISAEFPEFSNKDKTLVFQFSVKHEQKLDCGGGYMKLLSGDVDQKKFGGDTPYSIMFGPDICGYSTKKVHAILTYNEANHLIKKDVPCETDQLTHVYTFILRPDATYSILIDNVEKQTGSLYSDWDLLPPKKIKDPSAKKPEDWDEQEYISDPEDKKPDGYDDIPKEIPDTDSKKPEDWDDEEDGEWTAPTIPNPEYMGEWKPKQIKNPNYKGKWEAPLIDNPDFKDDPELYVFPKLKYVGLELWQVKSGSLFDNVLICDDPDYAKKLADETWGKLKDAEKAAFDEAEKKNEEEESKDAPAESDAEDEPEDDEGGDDSDSESKAEETKSVDSEETSEKDATAHDEL | |
| 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 | - | |
| 117 | Phosphorylation | GGYMKLLSGDVDQKK CCEEEHHCCCCCCCH | 43.30 | 19880383 | |
| 374 | Phosphorylation | KKNEEEESKDAPAES HHCHHHHHCCCCCCC | 38.83 | 23776212 | |
| 381 | Phosphorylation | SKDAPAESDAEDEPE HCCCCCCCCCCCCCC | 44.20 | 30291188 | |
| 396 | Phosphorylation | DDEGGDDSDSESKAE CCCCCCCCCCHHHHH | 48.02 | 23776212 | |
| 398 | Phosphorylation | EGGDDSDSESKAEET CCCCCCCCHHHHHHH | 47.96 | 23776212 | |
| 400 | Phosphorylation | GDDSDSESKAEETKS CCCCCCHHHHHHHCC | 40.91 | 23776212 | |
| 405 | Phosphorylation | SESKAEETKSVDSEE CHHHHHHHCCCCCHH | 21.81 | 23776212 | |
| 407 | Phosphorylation | SKAEETKSVDSEETS HHHHHHCCCCCHHHH | 38.28 | 30407730 | |
| 410 | Phosphorylation | EETKSVDSEETSEKD HHHCCCCCHHHHHHH | 34.87 | 23776212 | |
| 413 | Phosphorylation | KSVDSEETSEKDATA CCCCCHHHHHHHCCC | 37.83 | 30407730 | |
| 414 | Phosphorylation | SVDSEETSEKDATAH CCCCHHHHHHHCCCC | 46.02 | 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 CALR2_ARATH !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CALR2_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 CALR2_ARATH !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| SUMO3_ARATH | SUMO3 | physical | 20855607 | |
| SUMO1_ARATH | SUMO1 | physical | 20855607 |
| 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 MASSSPECTROMETRY. | |
