| Predicate | Object |
|---|---|
| rdf:type | |
| http://www.biopax.org/relea... |
cpath:CPATH-LOCAL-10116,
cpath:CPATH-LOCAL-10116,
cpath:CPATH-LOCAL-10116,
cpath:CPATH-LOCAL-8967,
cpath:CPATH-LOCAL-8967,
cpath:CPATH-LOCAL-8967,
cpath:CPATH-LOCAL-8968,
cpath:CPATH-LOCAL-8968,
cpath:CPATH-LOCAL-8968,
cpath:CPATH-LOCAL-8969,
cpath:CPATH-LOCAL-8969,
cpath:CPATH-LOCAL-8969,
cpath:CPATH-LOCAL-8970,
cpath:CPATH-LOCAL-8970,
cpath:CPATH-LOCAL-8970,
cpath:CPATH-LOCAL-8971,
cpath:CPATH-LOCAL-8971,
cpath:CPATH-LOCAL-8971,
cpath:CPATH-LOCAL-8972,
cpath:CPATH-LOCAL-8972,
cpath:CPATH-LOCAL-8972
|
| http://www.biopax.org/relea... |
Calreticulin,
Calreticulin,
Calreticulin
|
| http://www.biopax.org/relea... |
CALR_HUMAN,
CALR_HUMAN,
CALR_HUMAN
|
| http://www.biopax.org/relea... | |
| http://www.biopax.org/relea... |
CRP55,
CRP55,
CRP55,
Calregulin,
Calregulin,
Calregulin,
ERp60,
ERp60,
ERp60,
Endoplasmic reticulum resident protein 60,
Endoplasmic reticulum resident protein 60,
Endoplasmic reticulum resident protein 60,
HACBP,
HACBP,
HACBP,
grp60,
grp60,
grp60
|
| http://www.biopax.org/relea... |
FUNCTION: Molecular calcium-binding chaperone promoting folding, oligomeric assembly and quality control in the 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. SUBUNIT: Monomer. Component of an EIF2 complex at least composed of CELF1/CUGBP1, CALR, CALR3, EIF2S1, EIF2S2, HSP90B1 and HSPA5. Interacts with PDIA3/ERp57 (By similarity). Interacts with NR3C1 and TRIM21. Interacts with GABARAP. SUBCELLULAR LOCATION: Endoplasmic reticulum lumen. Cytoplasm, cytosol. Secreted, extracellular space, extracellular matrix. Cell surface. Note=Also found in cell surface (T cells), cytosol and extracellular matrix. Associated with the lytic granules in the cytolytic T-lymphocytes. DOMAIN: Can be divided into a N-terminal globular domain, a proline-rich P-domain forming an elongated arm-like structure and a C-terminal acidic domain. The P-domain binds one molecule of calcium with high affinity, whereas the acidic C-domain binds multiple calcium ions with low affinity. DOMAIN: The interaction with glycans occurs through a binding site in the globular lectin domain. DOMAIN: The zinc binding sites are localized to the N-domain. DOMAIN: Associates with PDIA3 through the tip of the extended arm formed by the P-domain. MASS SPECTROMETRY: Mass=46879; Method=MALDI; Range=18-417; Source=PubMed:11149926; SIMILARITY: Belongs to the calreticulin family. CAUTION: Was originally (PubMed:2332496) thought to be the 52 kDa Ro autoantigen. WEB RESOURCE: Name=Wikipedia; Note=Calreticulin entry; URL="http://en.wikipedia.org/wiki/Calreticulin"; WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding; Note=Calreticulin; URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_other_405"; GENE SYNONYMS: CRTC. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.,
FUNCTION: Molecular calcium-binding chaperone promoting folding, oligomeric assembly and quality control in the 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. SUBUNIT: Monomer. Component of an EIF2 complex at least composed of CELF1/CUGBP1, CALR, CALR3, EIF2S1, EIF2S2, HSP90B1 and HSPA5. Interacts with PDIA3/ERp57 (By similarity). Interacts with NR3C1 and TRIM21. Interacts with GABARAP. SUBCELLULAR LOCATION: Endoplasmic reticulum lumen. Cytoplasm, cytosol. Secreted, extracellular space, extracellular matrix. Cell surface. Note=Also found in cell surface (T cells), cytosol and extracellular matrix. Associated with the lytic granules in the cytolytic T-lymphocytes. DOMAIN: Can be divided into a N-terminal globular domain, a proline-rich P-domain forming an elongated arm-like structure and a C-terminal acidic domain. The P-domain binds one molecule of calcium with high affinity, whereas the acidic C-domain binds multiple calcium ions with low affinity. DOMAIN: The interaction with glycans occurs through a binding site in the globular lectin domain. DOMAIN: The zinc binding sites are localized to the N-domain. DOMAIN: Associates with PDIA3 through the tip of the extended arm formed by the P-domain. MASS SPECTROMETRY: Mass=46879; Method=MALDI; Range=18-417; Source=PubMed:11149926; SIMILARITY: Belongs to the calreticulin family. CAUTION: Was originally (PubMed:2332496) thought to be the 52 kDa Ro autoantigen. WEB RESOURCE: Name=Wikipedia; Note=Calreticulin entry; URL="http://en.wikipedia.org/wiki/Calreticulin"; WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding; Note=Calreticulin; URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_other_405"; GENE SYNONYMS: CRTC. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.,
FUNCTION: Molecular calcium-binding chaperone promoting folding, oligomeric assembly and quality control in the 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. SUBUNIT: Monomer. Component of an EIF2 complex at least composed of CELF1/CUGBP1, CALR, CALR3, EIF2S1, EIF2S2, HSP90B1 and HSPA5. Interacts with PDIA3/ERp57 (By similarity). Interacts with NR3C1 and TRIM21. Interacts with GABARAP. SUBCELLULAR LOCATION: Endoplasmic reticulum lumen. Cytoplasm, cytosol. Secreted, extracellular space, extracellular matrix. Cell surface. Note=Also found in cell surface (T cells), cytosol and extracellular matrix. Associated with the lytic granules in the cytolytic T-lymphocytes. DOMAIN: Can be divided into a N-terminal globular domain, a proline-rich P-domain forming an elongated arm-like structure and a C-terminal acidic domain. The P-domain binds one molecule of calcium with high affinity, whereas the acidic C-domain binds multiple calcium ions with low affinity. DOMAIN: The interaction with glycans occurs through a binding site in the globular lectin domain. DOMAIN: The zinc binding sites are localized to the N-domain. DOMAIN: Associates with PDIA3 through the tip of the extended arm formed by the P-domain. MASS SPECTROMETRY: Mass=46879; Method=MALDI; Range=18-417; Source=PubMed:11149926; SIMILARITY: Belongs to the calreticulin family. CAUTION: Was originally (PubMed:2332496) thought to be the 52 kDa Ro autoantigen. WEB RESOURCE: Name=Wikipedia; Note=Calreticulin entry; URL="http://en.wikipedia.org/wiki/Calreticulin"; WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding; Note=Calreticulin; URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_other_405"; GENE SYNONYMS: CRTC. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
|
| skos:exactMatch | |
| skos:closeMatch |