Gene Detail

Contact

Missing content? – Request curation!

Request curation for specific Genes, variants, or PubMed publications.

Have questions, comments or suggestions? - Let us know!

Email us at : ckbsupport@jax.org

Gene Symbol CALR
Synonyms cC1qR | CRT | HEL-S-99n | RO | SSA
Gene Description CALR, calreticulin, is a Ca2+ binding chaperone protein that plays a role in multiple biological processes, including protein folding and quality control, calcium homeostasis, immune response, cell adhesion and migration, and cell signaling (PMID: 19940256, PMID: 28470469, PMID: 22959412). CALR frameshift mutations have been identified in myeloproliferative neoplasms, including essential thrombocytothemia and myelofibrosis (PMID: 24365789, PMID: 28470469).

Filtering

  • Case insensitive filtering will display rows where any text in any cell matches the filter term
  • Simple literal full or partial string matches
  • Separate multiple filter terms with a spaces, order doesn't matter (a b c and c b a are equivalent )
  • Filtering will only apply to rows that are already loaded on the page, filtering has no impact on query parameters
  • Use quotes to match a longer phrase which contains spaces "mtor c1483f"

Sorting

  • Generally, the default sort order for tables is set to be first column ascending, however, specific tables may set a different default sort order.
  • Click on any column header arrows to sort by that column
  • Hold down the Shift key and click multiple columns to sort by more than one column, be sure to set ascending or descending order for a given column, before moving on to the next column.

Variant Impact Protein Effect Variant Description Associated with drug Resistance
act mut unknown gain of function CALR act mut indicates that this variant results in a gain of function in the Calr protein. However, the specific amino acid change has not been identified.
D244G missense unknown CALR D244G lies within the P-domain and 4 X approximate repeat regions of the Calr protein (UniProt.org). D244G has been identified in the scientific literature (PMID: 29218307), but has not been biochemically characterized and therefore, its effect on Calr protein function is unknown (PubMed, Aug 2020).
D309Y missense unknown CALR D309Y lies within the C-domain region of the Calr protein (UniProt.org). D309Y has been identified in the scientific literature (PMID: 29218307), but has not been biochemically characterized and therefore, its effect on Calr protein function is unknown (PubMed, Aug 2020).
D335N missense unknown CALR D335N lies within the C-domain region of the Calr protein (UniProt.org). D335N has been identified in the scientific literature (PMID: 29218307), but has not been biochemically characterized and therefore, its effect on Calr protein function is unknown (PubMed, Aug 2020).
D392_D394del deletion unknown CALR D392_D394del results in the deletion of three amino acids in the C-domain region of the Calr protein from amino acids 392 to 394 (UniProt.org). D392_D394del has not been characterized in the scientific literature and therefore, its effect on Calr protein function is unknown (PubMed, Aug 2020).
D394_K401delinsE indel unknown CALR D394_K401delinsE results in a deletion of eight amino acids from amino acids 394 to 402 within the C-domain region of the Calr protein, combined with the insertion of a glutamate (E) at the same site (UniProt.org). D394_K401delinsE has not been characterized in the scientific literature and therefore, its effect on Calr protein function is unknown (PubMed, Aug 2020).
D415E missense unknown CALR D415E lies within the C-domain region of the Calr protein (UniProt.org). D415E has been identified in the scientific literature (PMID: 29218307), but has not been biochemically characterized and therefore, its effect on Calr protein function is unknown (PubMed, Aug 2020).
D45Y missense unknown CALR D45Y lies within the N-domain region of the Calr protein (UniProt.org). D45Y has been identified in the scientific literature (PMID: 29218307) but has not been biochemically characterized and therefore, its effect on Calr protein function is unknown (PubMed, Aug 2020).
E100Q missense unknown CALR E100Q lies within the N-domain region of the Calr protein (UniProt.org). E100Q has been identified in in the scientific literature (PMID: 29218307), but has not been biochemically characterized and therefore, its effect on Calr protein function is unknown (PubMed, Aug 2020).
E234K missense unknown CALR E234K lies within the P-domain and 4 X approximate repeat regions of the Calr protein (UniProt.org). E234K has been identified in the scientific literature (PMID: 29218307), but has not been biochemically characterized and therefore, its effect on Calr protein function is unknown (PubMed, Aug 2020).
E240D missense unknown CALR E240D lies within the P-domain and 4 X approximate repeat regions of the Calr protein (UniProt.org). E240D has been identified in the scientific literature (PMID: 29218307), but has not been biochemically characterized and therefore, its effect on Calr protein function is unknown (PubMed, Aug 2020).
E298* nonsense unknown CALR E298* results in a premature truncation of the Calr protein at amino acid 298 of 417 (UniProt.org). E298* has not been characterized in the scientific literature and therefore, its effect on Calr protein function is unknown (PubMed, Aug 2020).
E341G missense unknown CALR E341G lies within the C-domain region of the Calr protein (UniProt.org). E341G has been identified in the scientific literature (PMID: 29218307), but has not been biochemically characterized and therefore, its effect on Calr protein function is unknown (PubMed, Aug 2020).
E364Gfs*49 frameshift unknown CALR E364Gfs*49 indicates a shift in the reading frame starting at amino acid 364 and terminating 49 residues downstream causing a premature truncation of the 417 amino acid Calr protein (UniProt.org). E364Gfs*49 has not been characterized in the scientific literature and therefore, its effect on Calr protein function is unknown (PubMed, Jun 2020).
E380fs frameshift unknown CALR E380fs results in a change in the amino acid sequence of the Calr protein beginning at aa 380 of 417, likely resulting in premature truncation of the functional protein (UniProt.org). E380fs has been identified in the scientific literature (PMID: 30805227), but has not been biochemically characterized and therefore, its effect on Calr protein function is unknown (PubMed, Jun 2020).
E380Gfs*50 frameshift unknown CALR E380Gfs*50 indicates a shift in the reading frame starting at amino acid 380 and terminating 50 residues downstream, resulting in premature truncation of the functional protein and extension of the 417aa Calr protein length by 13 amino acids (UniProt.org). E380Gfs*50 has been identified in the scientific literature (PMID: 30805227), but has not been biochemically characterized and therefore, its effect on Calr protein function is unknown (PubMed, Jun 2020).
E381Q missense unknown CALR E381Q lies within the C-domain region of the Calr protein (UniProt.org). E381Q has not been characterized in the scientific literature and therefore, its effect on Calr protein function is unknown (PubMed, Aug 2020).
E386G missense unknown CALR E386G lies within the C-domain region of the Calr protein (UniProt.org). E386G has been identified in the scientific literature (PMID: 29218307), but has not been biochemically characterized and therefore, its effect on Calr protein function is unknown (PubMed, Aug 2020).
E389D missense unknown CALR E389D lies within the C-domain region of the Calr protein (UniProt.org). E389D has been identified in the scientific literature (PMID: 29218307), but has not been biochemically characterized and therefore, its effect on Calr protein function is unknown (PubMed, Aug 2020).
E389K missense unknown CALR E389K lies within the C-domain region of the Calr protein (UniProt.org). E389K has not been characterized in the scientific literature and therefore, its effect on Calr protein function is unknown (PubMed, Aug 2020).
E398_D400del deletion unknown CALR E398_D400del results in the deletion of three amino acids in the C-domain region of the Calr protein from amino acids 398 to 400 (UniProt.org). E398_D400del has been identified in the scientific literature (PMID: 25729726, PMID: 29306106), but has not been biochemically characterized and therefore, its effect on Calr protein function is unknown (PubMed, Aug 2020).
E403* nonsense unknown CALR E403* results in a premature truncation of the Calr protein at amino acid 403 of 417 (UniProt.org). E403* has been identified in sequencing studies (PMID: 23297126), but has not been biochemically characterized and therefore, its effect on Calr protein function is unknown (PubMed, Aug 2020).
E406Q missense unknown CALR E406Q lies within the C-domain region of the Calr protein (UniProt.org). E406Q has not been characterized in the scientific literature and therefore, its effect on Calr protein function is unknown (PubMed, Aug 2020).
F132L missense unknown CALR F132L lies within the N-domain region of the Calr protein (UniProt.org). F132L has been identified in the scientific literature (PMID: 29218307), but has not been biochemically characterized and therefore, its effect on Calr protein function is unknown (PubMed, Aug 2020).
F56L missense unknown CALR F56L lies within the N-domain region of the Calr protein (UniProt.org). F56L has been identified in the scientific literature (PMID: 29218307), but has not been biochemically characterized and therefore, its effect on Calr protein function is unknown (PubMed, Aug 2020).
G343D missense unknown CALR G343D lies within the C-domain region of the Calr protein (UniProt.org). G343D has been identified in the scientific literature (PMID: 29218307), but has not been biochemically characterized and therefore, its effect on Calr protein function is unknown (PubMed, Aug 2020).
K385fs frameshift gain of function CALR K385fs (reported as K385fs*47) results in a change in the amino acid sequence of the Calr protein beginning at aa 385 of 417, likely resulting in premature truncation of the functional protein (UniProt.org). K385fs confers a gain of function to Calr, as indicated by activation of JAK-STAT signaling and is transforming in cell culture (PMID: 26817954, PMID: 26987905, PMID: 26668133).
K385Nfs*47 frameshift gain of function CALR K385Nfs*47 indicates a shift in the reading frame starting at amino acid 385 and terminating 47 residues downstream, resulting in premature truncation of the functional protein and extension of the 417aa Calr protein length by 15 amino acids (UniProt.org). K385Nfs*47 (reported as K385fs*47) results in activation of JAK-STAT signaling and is transforming in cell culture (PMID: 26817954, PMID: 26987905, PMID: 26668133).
K414E missense unknown CALR K414E lies within the C-domain region of the Calr protein (UniProt.org). K414E has been identified in the scientific literature (PMID: 29218307), but has not been biochemically characterized and therefore, its effect on Calr protein function is unknown (PubMed, Aug 2020).
K62R missense unknown CALR K62R lies within the N-domain region of the Calr protein (UniProt.org). K62R has been identified in the scientific literature (PMID: 29218307), but has not been biochemically characterized and therefore, its effect on Calr protein function is unknown (PubMed, Aug 2020).
K64T missense unknown CALR K64T lies within the N-domain region of the Calr protein (UniProt.org). K64T has been identified in the scientific literature (PMID: 29218307), but has not been biochemically characterized and therefore, its effect on Calr protein function is unknown (PubMed, Aug 2020).
L367fs frameshift gain of function CALR L367fs (reported as L367fs*46) results in a change in the amino acid sequence of the Calr protein beginning at aa 367 of 417, likely resulting in premature truncation of the functional protein (UniProt.org). L367fs*46 results in activation of Jak-Stat signaling, is transforming in culture, and drives myeloproliferative neoplasm formation in animal models (PMID: 26951227).
L367Qfs*48 frameshift gain of function CALR L367Qfs*48 indicates a shift in the reading frame starting at amino acid 367 and terminating 48 residues downstream causing a premature truncation of the 417 amino acid Calr protein (UniProt.org). L367Qfs*48 (reported as L367fs*48) confers a gain of function to Calr as indicated by constitutive activation of JAK2 and STAT1/3/5 and cytokine-independent growth in cell culture, and induces thrombocytosis and myelofibrosis in mouse models (PMID: 30846848).
L367Tfs*46 frameshift gain of function CALR L367Tfs*46 indicates a shift in the reading frame starting at amino acid 367 and terminating 46 residues downstream causing a premature truncation of the 417 amino acid Calr protein (UniProt.org). L367Tfs*46 (reported as L367fs*46) results in activation of Jak-Stat signaling, is transforming in culture, and drives myeloproliferative neoplasm formation in animal models (PMID: 26668133, PMID: 26951227).
L51V missense unknown CALR L51V lies within the N-domain region of the Calr protein (UniProt.org). L51V has been identified in the scientific literature (PMID: 29218307), but has not been biochemically characterized and therefore, its effect on Calr protein function is unknown (PubMed, Aug 2020).
mutant unknown unknown CALR mutant indicates an unspecified mutation in the CALR gene.
N158D missense unknown CALR N158D lies within the N-domain region of the Calr protein (UniProt.org). N158D has not been characterized in the scientific literature and therefore, its effect on Calr protein function is unknown (PubMed, Aug 2020).
N188D missense unknown CALR N188D lies within the N-domain region of the Calr protein (UniProt.org). N188D has been identified in the scientific literature (PMID: 29218307), but has not been biochemically characterized and therefore, its effect on Calr protein function is unknown (PubMed, Aug 2020).
P204S missense unknown CALR P204S lies within the P-domain and 4 X approximate repeat regions of the Calr protein (UniProt.org). P204S has been identified in the scientific literature (PMID: 29218307), but has not been biochemically characterized and therefore, its effect on Calr protein function is unknown (PubMed, Aug 2020).
P410L missense unknown CALR P410L lies within the C-domain region of the Calr protein (UniProt.org). P410L has been identified in the scientific literature (PMID: 29218307), but has not been biochemically characterized and therefore, its effect on Calr protein function is unknown (PubMed, Aug 2020).
Q67H missense unknown CALR Q67H lies within the N-domain region of the Calr protein (UniProt.org). Q67H has been identified in the scientific literature (PMID: 29218307), but has not been biochemically characterized and therefore, its effect on Calr protein function is unknown (PubMed, Aug 2020).
R177W missense unknown CALR R177W lies within the N-domain region of the Calr protein (UniProt.org). R177W has not been characterized in the scientific literature and therefore, its effect on Calr protein function is unknown (PubMed, Aug 2020).
S189T missense unknown CALR S189T lies within the N-domain region of the Calr protein (UniProt.org). S189T has not been characterized in the scientific literature and therefore, its effect on Calr protein function is unknown (PubMed, Aug 2020).
S300Y missense unknown CALR S300Y lies within the P-domain region of the Calr protein (UniProt.org). S300Y has been identified in the scientific literature (PMID: 29218307), but has not been biochemically characterized and therefore, its effect on Calr protein function is unknown (PubMed, Aug 2020).
S323F missense unknown CALR S323F lies within the C-domain region of the Calr protein (UniProt.org). S323F has been identified in the scientific literature (PMID: 29218307), but has not been biochemically characterized and therefore, its effect on Calr protein function is unknown (PubMed, Aug 2020).
T173fs frameshift unknown CALR T173fs results in a change in the amino acid sequence of the Calr protein beginning at aa 173 of 417, likely resulting in a premature truncation of the functional protein (UniProt.org). T173fs has not been characterized in the scientific literature and therefore, its effect on Calr protein function is unknown (PubMed, Aug 2020).
T325I missense unknown CALR T325I lies within the C-domain region of the Calr protein (UniProt.org). T325I has been identified in sequencing studies (PMID: 26343386), but has not been biochemically characterized and therefore, its effect on Calr protein function is unknown (PubMed, Aug 2020).
wild-type none no effect Wild-type CALR indicates that no mutation has been detected within the CALR gene.
Y128C missense unknown CALR Y128C lies within the N-domain region of the Calr protein (UniProt.org). Y128C has been identified in the scientific literature (PMID: 29218307), but has not been biochemically characterized and therefore, its effect on Calr protein function is unknown (PubMed, Aug 2020).