UniProt ID | CALR_HUMAN | |
---|---|---|
UniProt AC | P27797 | |
Protein Name | Calreticulin | |
Gene Name | CALR | |
Organism | Homo sapiens (Human). | |
Sequence Length | 417 | |
Subcellular Localization | Endoplasmic reticulum lumen . Cytoplasm, cytosol . Secreted, extracellular space, extracellular matrix . Cell surface . Sarcoplasmic reticulum lumen . Also found in cell surface (T cells), cytosol and extracellular matrix (PubMed:10358038). Associate | |
Protein Description | Calcium-binding chaperone that promotes folding, oligomeric assembly and quality control in the endoplasmic reticulum (ER) via the calreticulin/calnexin cycle. This lectin interacts transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER. Interacts with the DNA-binding domain of NR3C1 and mediates its nuclear export. Involved in maternal gene expression regulation. May participate in oocyte maturation via the regulation of calcium homeostasis (By similarity).. | |
Protein Sequence | MLLSVPLLLGLLGLAVAEPAVYFKEQFLDGDGWTSRWIESKHKSDFGKFVLSSGKFYGDEEKDKGLQTSQDARFYALSASFEPFSNKGQTLVVQFTVKHEQNIDCGGGYVKLFPNSLDQTDMHGDSEYNIMFGPDICGPGTKKVHVIFNYKGKNVLINKDIRCKDDEFTHLYTLIVRPDNTYEVKIDNSQVESGSLEDDWDFLPPKKIKDPDASKPEDWDERAKIDDPTDSKPEDWDKPEHIPDPDAKKPEDWDEEMDGEWEPPVIQNPEYKGEWKPRQIDNPDYKGTWIHPEIDNPEYSPDPSIYAYDNFGVLGLDLWQVKSGTIFDNFLITNDEAYAEEFGNETWGVTKAAEKQMKDKQDEEQRLKEEEEDKKRKEEEEAEDKEDDEDKDEDEEDEEDKEEDEEEDVPGQAKDEL | |
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 |
---|---|---|---|---|---|
7 | Ubiquitination | -MLLSVPLLLGLLGL -CCCHHHHHHHHHHH | 6.05 | 21890473 | |
22 | Phosphorylation | AVAEPAVYFKEQFLD HHHCCCCCCCCCCCC | 15.84 | - | |
24 | Ubiquitination | AEPAVYFKEQFLDGD HCCCCCCCCCCCCCC | 32.68 | 21890473 | |
24 | Sumoylation | AEPAVYFKEQFLDGD HCCCCCCCCCCCCCC | 32.68 | - | |
34 | Phosphorylation | FLDGDGWTSRWIESK CCCCCCHHHHHHHHC | 17.59 | 21712546 | |
35 | Phosphorylation | LDGDGWTSRWIESKH CCCCCHHHHHHHHCC | 21.07 | 21712546 | |
41 | Acetylation | TSRWIESKHKSDFGK HHHHHHHCCHHHCCE | 42.11 | 25953088 | |
41 | 2-Hydroxyisobutyrylation | TSRWIESKHKSDFGK HHHHHHHCCHHHCCE | 42.11 | - | |
41 | Ubiquitination | TSRWIESKHKSDFGK HHHHHHHCCHHHCCE | 42.11 | - | |
43 | Succinylation | RWIESKHKSDFGKFV HHHHHCCHHHCCEEE | 56.29 | 23954790 | |
43 | 2-Hydroxyisobutyrylation | RWIESKHKSDFGKFV HHHHHCCHHHCCEEE | 56.29 | - | |
44 | Phosphorylation | WIESKHKSDFGKFVL HHHHCCHHHCCEEEE | 37.58 | 24719451 | |
48 | Acetylation | KHKSDFGKFVLSSGK CCHHHCCEEEECCCC | 32.09 | 19608861 | |
48 | Ubiquitination | KHKSDFGKFVLSSGK CCHHHCCEEEECCCC | 32.09 | 21890473 | |
48 | Succinylation | KHKSDFGKFVLSSGK CCHHHCCEEEECCCC | 32.09 | 23954790 | |
48 | 2-Hydroxyisobutyrylation | KHKSDFGKFVLSSGK CCHHHCCEEEECCCC | 32.09 | - | |
48 | Ubiquitination | KHKSDFGKFVLSSGK CCHHHCCEEEECCCC | 32.09 | 21890473 | |
52 | Phosphorylation | DFGKFVLSSGKFYGD HCCEEEECCCCCCCC | 31.57 | 23911959 | |
53 | Phosphorylation | FGKFVLSSGKFYGDE CCEEEECCCCCCCCC | 41.67 | 23911959 | |
55 | Ubiquitination | KFVLSSGKFYGDEEK EEEECCCCCCCCCHH | 37.04 | 21890473 | |
55 | Acetylation | KFVLSSGKFYGDEEK EEEECCCCCCCCCHH | 37.04 | 26822725 | |
55 | Ubiquitination | KFVLSSGKFYGDEEK EEEECCCCCCCCCHH | 37.04 | 21890473 | |
57 | Phosphorylation | VLSSGKFYGDEEKDK EECCCCCCCCCHHCC | 27.44 | 28152594 | |
62 | Malonylation | KFYGDEEKDKGLQTS CCCCCCHHCCCCCCC | 63.79 | 26320211 | |
62 | 2-Hydroxyisobutyrylation | KFYGDEEKDKGLQTS CCCCCCHHCCCCCCC | 63.79 | - | |
62 | Acetylation | KFYGDEEKDKGLQTS CCCCCCHHCCCCCCC | 63.79 | 27178108 | |
62 | Ubiquitination | KFYGDEEKDKGLQTS CCCCCCHHCCCCCCC | 63.79 | - | |
64 | Acetylation | YGDEEKDKGLQTSQD CCCCHHCCCCCCCHH | 73.00 | 26822725 | |
64 | Ubiquitination | YGDEEKDKGLQTSQD CCCCHHCCCCCCCHH | 73.00 | - | |
73 | Methylation | LQTSQDARFYALSAS CCCCHHHHHEEEEEE | 33.14 | - | |
75 | Phosphorylation | TSQDARFYALSASFE CCHHHHHEEEEEEEE | 10.90 | 28152594 | |
78 | Phosphorylation | DARFYALSASFEPFS HHHHEEEEEEEECCC | 17.44 | 28152594 | |
80 | Phosphorylation | RFYALSASFEPFSNK HHEEEEEEEECCCCC | 27.11 | 21712546 | |
85 | Phosphorylation | SASFEPFSNKGQTLV EEEEECCCCCCCEEE | 48.63 | 21712546 | |
105 | S-nitrosylation | KHEQNIDCGGGYVKL ECCCCCCCCCCEEEE | 4.90 | 25040305 | |
105 | Glutathionylation | KHEQNIDCGGGYVKL ECCCCCCCCCCEEEE | 4.90 | 22555962 | |
109 | Phosphorylation | NIDCGGGYVKLFPNS CCCCCCCEEEECCCC | 9.55 | 28152594 | |
111 | Methylation | DCGGGYVKLFPNSLD CCCCCEEEECCCCCC | 35.61 | - | |
122 | Sulfoxidation | NSLDQTDMHGDSEYN CCCCCCCCCCCCCEE | 4.29 | 30846556 | |
131 | Sulfoxidation | GDSEYNIMFGPDICG CCCCEEEEECCCCCC | 2.57 | 30846556 | |
142 | Ubiquitination | DICGPGTKKVHVIFN CCCCCCCCEEEEEEE | 59.73 | - | |
142 | Acetylation | DICGPGTKKVHVIFN CCCCCCCCEEEEEEE | 59.73 | 2374799 | |
143 | Acetylation | ICGPGTKKVHVIFNY CCCCCCCEEEEEEEE | 37.09 | 26051181 | |
143 | Ubiquitination | ICGPGTKKVHVIFNY CCCCCCCEEEEEEEE | 37.09 | 21906983 | |
143 | Malonylation | ICGPGTKKVHVIFNY CCCCCCCEEEEEEEE | 37.09 | 26320211 | |
150 | Phosphorylation | KVHVIFNYKGKNVLI EEEEEEEECCCEEEE | 15.46 | - | |
151 | Ubiquitination | VHVIFNYKGKNVLIN EEEEEEECCCEEEEC | 65.59 | - | |
151 | Acetylation | VHVIFNYKGKNVLIN EEEEEEECCCEEEEC | 65.59 | 21466224 | |
151 | Succinylation | VHVIFNYKGKNVLIN EEEEEEECCCEEEEC | 65.59 | 23954790 | |
153 | Acetylation | VIFNYKGKNVLINKD EEEEECCCEEEECCC | 39.47 | 18795239 | |
153 | Ubiquitination | VIFNYKGKNVLINKD EEEEECCCEEEECCC | 39.47 | 21890473 | |
153 | 2-Hydroxyisobutyrylation | VIFNYKGKNVLINKD EEEEECCCEEEECCC | 39.47 | - | |
153 | Ubiquitination | VIFNYKGKNVLINKD EEEEECCCEEEECCC | 39.47 | 21890473 | |
159 | Malonylation | GKNVLINKDIRCKDD CCEEEECCCCCCCCC | 47.76 | 26320211 | |
159 | Acetylation | GKNVLINKDIRCKDD CCEEEECCCCCCCCC | 47.76 | 19608861 | |
159 | Ubiquitination | GKNVLINKDIRCKDD CCEEEECCCCCCCCC | 47.76 | 21890473 | |
159 | 2-Hydroxyisobutyrylation | GKNVLINKDIRCKDD CCEEEECCCCCCCCC | 47.76 | - | |
159 | Ubiquitination | GKNVLINKDIRCKDD CCEEEECCCCCCCCC | 47.76 | 21890473 | |
164 | Acetylation | INKDIRCKDDEFTHL ECCCCCCCCCCCEEE | 59.36 | 26051181 | |
169 | Phosphorylation | RCKDDEFTHLYTLIV CCCCCCCEEEEEEEE | 14.66 | - | |
172 | Phosphorylation | DDEFTHLYTLIVRPD CCCCEEEEEEEECCC | 7.59 | 28152594 | |
173 | Phosphorylation | DEFTHLYTLIVRPDN CCCEEEEEEEECCCC | 19.17 | 28152594 | |
181 | Phosphorylation | LIVRPDNTYEVKIDN EEECCCCEEEEEECC | 28.56 | 28152594 | |
182 | Phosphorylation | IVRPDNTYEVKIDNS EECCCCEEEEEECCC | 25.61 | 28152594 | |
189 | Phosphorylation | YEVKIDNSQVESGSL EEEEECCCCCCCCCC | 31.67 | 28450419 | |
193 | Phosphorylation | IDNSQVESGSLEDDW ECCCCCCCCCCCCCC | 34.52 | 29507054 | |
195 | Phosphorylation | NSQVESGSLEDDWDF CCCCCCCCCCCCCCC | 37.55 | 29507054 | |
206 | 2-Hydroxyisobutyrylation | DWDFLPPKKIKDPDA CCCCCCCCCCCCCCC | 66.25 | - | |
206 | Acetylation | DWDFLPPKKIKDPDA CCCCCCCCCCCCCCC | 66.25 | 26051181 | |
206 | Ubiquitination | DWDFLPPKKIKDPDA CCCCCCCCCCCCCCC | 66.25 | 21890473 | |
207 | Ubiquitination | WDFLPPKKIKDPDAS CCCCCCCCCCCCCCC | 61.84 | - | |
207 | Acetylation | WDFLPPKKIKDPDAS CCCCCCCCCCCCCCC | 61.84 | 18795239 | |
209 | Ubiquitination | FLPPKKIKDPDASKP CCCCCCCCCCCCCCC | 72.58 | 19608861 | |
209 | Acetylation | FLPPKKIKDPDASKP CCCCCCCCCCCCCCC | 72.58 | 19608861 | |
214 | Phosphorylation | KIKDPDASKPEDWDE CCCCCCCCCCCCHHH | 57.00 | 23401153 | |
215 | Acetylation | IKDPDASKPEDWDER CCCCCCCCCCCHHHH | 54.89 | 25038526 | |
222 | Methylation | KPEDWDERAKIDDPT CCCCHHHHHCCCCCC | 38.41 | - | |
229 | Phosphorylation | RAKIDDPTDSKPEDW HHCCCCCCCCCCCCC | 60.96 | 26471730 | |
231 | Phosphorylation | KIDDPTDSKPEDWDK CCCCCCCCCCCCCCC | 53.22 | 26657352 | |
238 | Acetylation | SKPEDWDKPEHIPDP CCCCCCCCCCCCCCC | 48.31 | 27178108 | |
238 | Methylation | SKPEDWDKPEHIPDP CCCCCCCCCCCCCCC | 48.31 | - | |
249 | Acetylation | IPDPDAKKPEDWDEE CCCCCCCCCCCCCHH | 56.19 | 26051181 | |
257 | Sulfoxidation | PEDWDEEMDGEWEPP CCCCCHHCCCCCCCC | 8.25 | 30846556 | |
271 | Phosphorylation | PVIQNPEYKGEWKPR CCCCCCCCCCCCCCC | 26.08 | - | |
272 | 2-Hydroxyisobutyrylation | VIQNPEYKGEWKPRQ CCCCCCCCCCCCCCC | 49.01 | - | |
285 | Phosphorylation | RQIDNPDYKGTWIHP CCCCCCCCCCCEECC | 16.75 | 25884760 | |
285 | Nitration | RQIDNPDYKGTWIHP CCCCCCCCCCCEECC | 16.75 | - | |
299 | Phosphorylation | PEIDNPEYSPDPSIY CCCCCCCCCCCCCEE | 27.10 | - | |
300 | Phosphorylation | EIDNPEYSPDPSIYA CCCCCCCCCCCCEEE | 22.59 | - | |
325 | O-linked_Glycosylation | LWQVKSGTIFDNFLI EEEEECCEEEECEEE | 26.09 | 32119511 | |
333 | Phosphorylation | IFDNFLITNDEAYAE EEECEEECCCHHHHH | 38.47 | - | |
344 | N-linked_Glycosylation | AYAEEFGNETWGVTK HHHHHHCCCCHHHHH | 49.17 | 19159218 | |
351 | Ubiquitination | NETWGVTKAAEKQMK CCCHHHHHHHHHHHC | 43.10 | - | |
357 | Sulfoxidation | TKAAEKQMKDKQDEE HHHHHHHHCCHHHHH | 10.06 | 30846556 | |
366 | Methylation | DKQDEEQRLKEEEED CHHHHHHHHHHHHHH | 51.51 | - |
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 CALR_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CALR_HUMAN !! |
* 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 CALR_HUMAN !! |
Kegg Disease | ||||||
---|---|---|---|---|---|---|
There are no disease associations of PTM sites. | ||||||
OMIM Disease | ||||||
There are no disease associations of PTM sites. | ||||||
Kegg Drug | ||||||
There are no disease associations of PTM sites. | ||||||
DrugBank | ||||||
There are no disease associations of PTM sites. |
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Acetylation | |
Reference | PubMed |
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-48; LYS-159 AND LYS-209, ANDMASS SPECTROMETRY. | |
N-linked Glycosylation | |
Reference | PubMed |
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry."; Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; J. Proteome Res. 8:651-661(2009). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-344, AND MASSSPECTROMETRY. |