Search results for SEC23A

Showing 11 results out of 11

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Species

Types

Compartments

Reaction types

Search properties

Protein (4 results from a total of 4)

Identifier: R-HSA-203976
Species: Homo sapiens
Compartment: endoplasmic reticulum membrane
Primary external reference: UniProt: SEC23A: Q15436
Identifier: R-HSA-203972
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: SEC23A: Q15436
Identifier: R-HSA-204024
Species: Homo sapiens
Compartment: ER to Golgi transport vesicle membrane
Primary external reference: UniProt: SEC23A: Q15436
Identifier: R-HSA-5685740
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: SEC23A: Q15436

Complex (3 results from a total of 3)

Identifier: R-HSA-5694245
Species: Homo sapiens
Compartment: endoplasmic reticulum membrane
Identifier: R-HSA-5694270
Species: Homo sapiens
Compartment: ER to Golgi transport vesicle membrane
Identifier: R-HSA-5694252
Species: Homo sapiens
Compartment: endoplasmic reticulum-Golgi intermediate compartment membrane

Reaction (4 results from a total of 4)

Identifier: R-HSA-5694413
Species: Homo sapiens
Compartment: endoplasmic reticulum membrane
SEC24 isoforms C and D are required in conjunction with SEC23A for packaging the t-SNARES STX5 and GOSR2 into COPII vesicles for transport to the Golgi (Mancias and Goldberg, 2008).
Identifier: R-HSA-8874191
Species: Homo sapiens
Compartment: nucleoplasm, cytosol
After cleavage by MBTPS2 the N-terminal cytoplasmic domain of CREB3L2 is released into the cytosol and traffics to the nucleus where it binds CRE-like elements in promoters of genes such as Sec23a (inferred from mouse).
Identifier: R-HSA-5694415
Species: Homo sapiens
Compartment: endoplasmic reticulum membrane
Of the four human SEC24 isoforms, SEC24A and B are required for packaging the v-SNARE SEC22 into COPII vesicles. Recognition of the ER packaging epitope on SEC22 also depends on SEC23A (Mancias and Goldberg, 2007).
Identifier: R-HSA-5694435
Species: Homo sapiens
Compartment: endoplasmic reticulum membrane
MIA2 (also known as CTAGE5) and MIA3 form heterodimers through their second coiled coil domains and interact with inner coat proteins SEC24C and SEC23A through their proline-rich domains. In this way, the MIA3 and MIA2 concentrate procollagen VII at ER exit sites (Saito et al, 2011; reviewed in Malhotra and Erlmann, 2011; Malhotra et al, 2015).
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