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Details on Person Unknown:Q14444-3 CAPRIN1
| Class:Id | ReferenceIsoform:9948491 |
|---|---|
| _chainChangeLog | initiator methionine: for 9948491 added on Wed May 21 2025;chain:2-709 for 9948491 added on Wed May 21 2025;initiator methionine: for 9948491 added on Wed May 21 2025;initiator methionine: for 9948491 removed on Fri Aug 15 2025;initiator methionine: for 9948491 removed on Fri Aug 15 2025;initiator methionine:1 for 9948491 added on Fri Aug 15 2025;initiator methionine:1 for 9948491 added on Fri Aug 15 2025 |
| _displayName | Unknown:Q14444-3 CAPRIN1 |
| _timestamp | 2025-08-15 21:05:46 |
| chain | initiator methionine:1 chain:2-709 initiator methionine:1 |
| checksum | 56F5BC188CA3A2D4 |
| comment | FUNCTION mRNA-binding protein that acts as a regulator of mRNAs transport, translation and/or stability, and which is involved in neurogenesis, synaptic plasticity in neurons and cell proliferation and migration in multiple cell types (PubMed:17210633, PubMed:31439799, PubMed:35979925). Plays an essential role in cytoplasmic stress granule formation (PubMed:35977029). Acts as an mRNA regulator by mediating formation of some phase-separated membraneless compartment: undergoes liquid-liquid phase separation upon binding to target mRNAs, leading to assemble mRNAs into cytoplasmic ribonucleoprotein granules that concentrate mRNAs with associated regulatory factors (PubMed:31439799, PubMed:32302570, PubMed:32302571, PubMed:32302572, PubMed:34074792, PubMed:36040869, PubMed:36279435). Undergoes liquid-liquid phase separation following phosphorylation and interaction with FMR1, promoting formation of cytoplasmic ribonucleoprotein granules that concentrate mRNAs with factors that inhibit translation and mediate deadenylation of target mRNAs (PubMed:31439799). In these cytoplasmic ribonucleoprotein granules, CAPRIN1 mediates recruitment of CNOT7 deadenylase, leading to mRNA deadenylation and degradation (PubMed:31439799). Binds directly and selectively to MYC and CCND2 mRNAs (PubMed:17210633). In neuronal cells, directly binds to several mRNAs associated with RNA granules, including BDNF, CAMK2A, CREB1, MAP2, NTRK2 mRNAs, as well as to GRIN1 and KPNB1 mRNAs, but not to rRNAs (PubMed:17210633).ACTIVITY REGULATION Ability to mediate liquid-liquid phase separation is regulated by ATP: moderate concentrations of ATP enhance phase separation, whereas high concentrations of ATP lead to inhibition of phase separation.SUBUNIT May form homomultimers (PubMed:14764709). Interacts with G3BP1; interaction is direct and promotes stress granule formation (PubMed:17210633, PubMed:27022092, PubMed:32302570, PubMed:32302571, PubMed:32302572, PubMed:35977029, PubMed:36183834, PubMed:36279435). Interacts with G3BP2; interaction is direct and promotes stress granule formation (PubMed:27022092, PubMed:35977029). Interacts with PQBP1 (PubMed:21933836). Interacts with DDX3X (PubMed:28733330). Interacts (when phosphorylated by EPHA4) with FMR1; interaction with FMR1 promotes formation of a membraneless compartment (PubMed:31439799).SUBUNIT (Microbial infection) Interacts with Zika virus capsid protein C; this interaction is probably linked to the inhibition of stress granules formation by the virus.SUBUNIT (Microbial infection) Interacts with rotavirus A non-structural protein 5; this interaction probably plays a role in the sequestration of CAPRIN1 in viral factories.SUBUNIT (Microbial infection) Interacts with Japanese encephalitis virus capsid protein C; this interaction is involved in the suppression of the integrated stress response by the virus.INTERACTION Mediates formation and localizes to cytoplasmic ribonucleoprotein membraneless compartments (PubMed:31439799). Associated with RNA granules. At the leading edge of migrating fibroblasts, colocalizes with DDX3X (PubMed:28733330).SUBCELLULAR LOCATION (Microbial infection) In case of reovirus infection, associates with the outer peripheries of viral factories in a G3BP1 dependent manner.ALTERNATIVE PRODUCTS Ubiquitous.DOMAIN The C-terminal disordered region undergoes liquid-liquid phase separation (LLPS) for the formation of a membraneless compartment that concentrates mRNAs with associated regulatory factors (PubMed:31439799, PubMed:34074792, PubMed:36040869). CAPRIN1 molecules in the condensed phase are neutral (PubMed:36040869). mRNA-binding promotes phase separation (PubMed:31439799). Moderate concentrations of ATP enhance phase separation by reducing the electrostatic potential of CAPRIN1, thereby promoting intermolecular interactions (PubMed:34074792, PubMed:36040869). In contrast, high concentrations of ATP invert the electrostatic potential of CAPRIN1, so that CAPRIN1 molecules become negatively charged, lead to inhibition of phase separation (PubMed:36040869).PTM Tyrosine phosphorylation by EPHA4 promotes interaction with FMR1 and liquid-liquid phase separation (LLPS) for the formation of a membraneless compartment that concentrates mRNAs with associated regulatory factors.PTM O-glycosylated (O-GlcNAcylated), in a cell cycle-dependent manner (PubMed:22967762). O-glycosylation by OGT inhibit ability to undergo liquid-liquid phase separation (LLPS) (PubMed:34074792).DISEASE The disease is caused by variants affecting the gene represented in this entry.DISEASE The disease is caused by variants affecting the gene represented in this entry.SIMILARITY Belongs to the caprin family.CAUTION Was originally thought to be a GPI-anchored membrane protein. |
| created | [InstanceEdit:9948485] Weiser, Joel, 2025-05-21 |
| description | recommendedName: fullName evidence="27"Caprin-1 alternativeName: Cell cycle-associated protein 1 alternativeName: Cytoplasmic activation- and proliferation-associated protein 1 alternativeName: GPI-anchored membrane protein 1 alternativeName: fullName evidence="29"GPI-anchored protein p137 shortName evidence="29"GPI-p137 shortName evidence="29"p137GPI alternativeName: Membrane component chromosome 11 surface marker 1 alternativeName: RNA granule protein 105 |
| geneName | CAPRIN1 GPIAP1 GPIP137 M11S1 RNG105 |
| identifier | Q14444 |
| isoformParent | |
| isSequenceChanged | FALSE |
| keyword | 3D-structure Acetylation Alternative splicing ATP-binding Autism Autism spectrum disorder Cell projection Coiled coil Cytoplasm Differentiation Direct protein sequencing Disease variant Glycoprotein Intellectual disability Methylation Neurodegeneration Nucleotide-binding Phosphoprotein Protein synthesis inhibitor Proteomics identification Reference proteome RNA-binding |
| modified | [InstanceEdit:9963647] Weiser, Joel, 2025-08-15 |
| name | CAPRIN1 |
| referenceGene | [ReferenceDNASequence:8988299] ENSEMBL:ENSG00000135387 CAPRIN1 [Homo sapiens] |
| secondaryIdentifier | CAPR1_HUMAN A6NMY7 D3DR06 Q15074 Q6IMN4 Q6IMN7 Q9BV09 |
| sequenceLength | 709 |
| species | [Species:48887] Homo sapiens |
| variantIdentifier | Q14444-3 |
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No pathways have been reviewed or authored by Unknown:Q14444-3 CAPRIN1 (9948491)
