P51116 · FXR2_HUMAN
- ProteinRNA-binding protein FXR2
- GeneFXR2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids673 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
mRNA-binding protein that acts as a regulator of mRNAs translation and/or stability, and which is required for adult hippocampal neurogenesis (By similarity).
Specifically binds to AU-rich elements (AREs) in the 3'-UTR of target mRNAs (By similarity).
Promotes formation of some phase-separated membraneless compartment by undergoing liquid-liquid phase separation upon binding to AREs-containing mRNAs: mRNAs storage into membraneless compartments regulates their translation and/or stability (By similarity).
Acts as a regulator of adult hippocampal neurogenesis by regulating translation and/or stability of NOG mRNA, thereby preventing NOG protein expression in the dentate gyrus (By similarity).
Specifically binds to AU-rich elements (AREs) in the 3'-UTR of target mRNAs (By similarity).
Promotes formation of some phase-separated membraneless compartment by undergoing liquid-liquid phase separation upon binding to AREs-containing mRNAs: mRNAs storage into membraneless compartments regulates their translation and/or stability (By similarity).
Acts as a regulator of adult hippocampal neurogenesis by regulating translation and/or stability of NOG mRNA, thereby preventing NOG protein expression in the dentate gyrus (By similarity).
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | cytoplasmic stress granule | |
Cellular Component | cytosol | |
Cellular Component | membrane | |
Cellular Component | neuron projection | |
Cellular Component | nucleus | |
Cellular Component | postsynapse | |
Cellular Component | presynapse | |
Molecular Function | identical protein binding | |
Molecular Function | mRNA 3'-UTR binding | |
Molecular Function | protein heterodimerization activity | |
Molecular Function | protein homodimerization activity | |
Molecular Function | RNA binding | |
Molecular Function | translation regulator activity | |
Biological Process | animal organ development | |
Biological Process | dentate gyrus development | |
Biological Process | mRNA destabilization | |
Biological Process | mRNA transport | |
Biological Process | positive regulation of long-term neuronal synaptic plasticity | |
Biological Process | positive regulation of translation | |
Biological Process | regulation of mRNA stability | |
Biological Process | regulation of translation at presynapse, modulating synaptic transmission |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameRNA-binding protein FXR2
- Short namesFXR2P
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP51116
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Specifically localizes to cytoplasmic ribonucleoprotein membraneless compartments (By similarity).
Localization to the post-synaptic region is dependent on FMR1 (By similarity).
Localization to the post-synaptic region is dependent on FMR1 (By similarity).
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_067039 | 252 | in dbSNP:rs17854734 | |||
Sequence: Q → H | ||||||
Natural variant | VAR_055979 | 591 | in dbSNP:rs36013555 | |||
Sequence: R → P |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 600 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000050110 | 1-673 | UniProt | RNA-binding protein FXR2 | |||
Sequence: MGGLASGGDVEPGLPVEVRGSNGAFYKGFVKDVHEDSVTIFFENNWQSERQIPFGDVRLPPPADYNKEITEGDEVEVYSRANEQEPCGWWLARVRMMKGDFYVIEYAACDATYNEIVTLERLRPVNPNPLATKGSFFKVTMAVPEDLREACSNENVHKEFKKALGANCIFLNITNSELFILSTTEAPVKRASLLGDMHFRSLRTKLLLMSRNEEATKHLETSKQLAAAFQEEFTVREDLMGLAIGTHGANIQQARKVPGVTAIELGEETCTFRIYGETPEACRQARSYLEFSEDSVQVPRNLVGKVIGKNGKVIQEIVDKSGVVRVRVEGDNDKKNPREEGMVPFIFVGTRENISNAQALLEYHLSYLQEVEQLRLERLQIDEQLRQIGLGFRPPGSGRGSGGSDKAGYSTDESSSSSLHATRTYGGSYGGRGRGRRTGGPAYGPSSDVSTASETESEKREEPNRAGPGDRDPPTRGEESRRRPTGGRGRGPPPAPRPTSRYNSSSISSVLKDPDSNPYSLLDTSEPEPPVDSEPGEPPPASARRRRSRRRRTDEDRTVMDGGLESDGPNMTENGLEDESRPQRRNRSRRRRNRGNRTDGSISGDRQPVTVADYISRAESQSRQRPPLERTKPSEDSLSGQKGDSVSKLPKGPSENGELSAPLELGSMVNGVS | |||||||
Modified residue | 78 | UniProt | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 192 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 192 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 401 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 404 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 409 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 410 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 410 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 411 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 411 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 414 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 418 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 450 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 453 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 453 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 504 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 506 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 525 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 533 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 533 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 542 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 566 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 566 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 580 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 598 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 598 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 601 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 601 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 603 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 603 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 610 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 616 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 620 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 622 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 634 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 637 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 639 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 654 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in all tissues examined including heart, brain, kidney and testis (PubMed:9259278).
In brain, present at high level in neurons and especially in the Purkinje cells at the interface between the granular layer and the molecular layer (at protein level) (PubMed:9259278).
In brain, present at high level in neurons and especially in the Purkinje cells at the interface between the granular layer and the molecular layer (at protein level) (PubMed:9259278).
Gene expression databases
Organism-specific databases
Interaction
Subunit
Interacts with FMR1 (PubMed:11157796, PubMed:7489725, PubMed:8668200).
Interacts with FXR1 (PubMed:7489725).
Interacts with TDRD3 (PubMed:18664458).
Interacts with HABP4 (PubMed:21771594).
Interacts with CYFIP2 but not with CYFIP1 (By similarity).
Interacts with FXR1 (PubMed:7489725).
Interacts with TDRD3 (PubMed:18664458).
Interacts with HABP4 (PubMed:21771594).
Interacts with CYFIP2 but not with CYFIP1 (By similarity).
(Microbial infection) Interacts with Sindbis virus non-structural protein 3 (via C-terminus); this interaction inhibits the formation of host stress granules on viral mRNAs and the nsp3-FXR2 complexes bind viral RNAs and probably orchestrate the assembly of viral replication complexes.
Binary interactions
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 14-60 | Agenet-like 1 | ||||
Sequence: LPVEVRGSNGAFYKGFVKDVHEDSVTIFFENNWQSERQIPFGDVRLP | ||||||
Domain | 73-125 | Agenet-like 2 | ||||
Sequence: DEVEVYSRANEQEPCGWWLARVRMMKGDFYVIEYAACDATYNEIVTLERLRPV | ||||||
Domain | 232-261 | KH 1 | ||||
Sequence: EFTVREDLMGLAIGTHGANIQQARKVPGVT | ||||||
Domain | 295-324 | KH 2 | ||||
Sequence: SVQVPRNLVGKVIGKNGKVIQEIVDKSGVV | ||||||
Region | 389-673 | Disordered | ||||
Sequence: GLGFRPPGSGRGSGGSDKAGYSTDESSSSSLHATRTYGGSYGGRGRGRRTGGPAYGPSSDVSTASETESEKREEPNRAGPGDRDPPTRGEESRRRPTGGRGRGPPPAPRPTSRYNSSSISSVLKDPDSNPYSLLDTSEPEPPVDSEPGEPPPASARRRRSRRRRTDEDRTVMDGGLESDGPNMTENGLEDESRPQRRNRSRRRRNRGNRTDGSISGDRQPVTVADYISRAESQSRQRPPLERTKPSEDSLSGQKGDSVSKLPKGPSENGELSAPLELGSMVNGVS | ||||||
Compositional bias | 407-424 | Polar residues | ||||
Sequence: AGYSTDESSSSSLHATRT | ||||||
Compositional bias | 453-486 | Basic and acidic residues | ||||
Sequence: SETESEKREEPNRAGPGDRDPPTRGEESRRRPTG | ||||||
Compositional bias | 500-523 | Polar residues | ||||
Sequence: SRYNSSSISSVLKDPDSNPYSLLD | ||||||
Compositional bias | 623-637 | Basic and acidic residues | ||||
Sequence: RQRPPLERTKPSEDS |
Domain
The tandem Agenet-like domains preferentially recognize trimethylated histone peptides.
Disordered region at the C-terminus undergoes liquid-liquid phase separation (LLPS) for the formation of a membraneless compartment that stores mRNAs.
Sequence similarities
Belongs to the FMR1 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length673
- Mass (Da)74,223
- Last updated2006-03-07 v2
- ChecksumB8A498C3F634D41F
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
I3L1Z2 | I3L1Z2_HUMAN | FXR2 | 118 | ||
A0A994J7P9 | A0A994J7P9_HUMAN | FXR2 | 746 |
Features
Showing features for compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 407-424 | Polar residues | ||||
Sequence: AGYSTDESSSSSLHATRT | ||||||
Compositional bias | 453-486 | Basic and acidic residues | ||||
Sequence: SETESEKREEPNRAGPGDRDPPTRGEESRRRPTG | ||||||
Compositional bias | 500-523 | Polar residues | ||||
Sequence: SRYNSSSISSVLKDPDSNPYSLLD | ||||||
Compositional bias | 623-637 | Basic and acidic residues | ||||
Sequence: RQRPPLERTKPSEDS | ||||||
Sequence conflict | 625-626 | in Ref. 1; AAC50292 | ||||
Sequence: RP → SA |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U31501 EMBL· GenBank· DDBJ | AAC50292.1 EMBL· GenBank· DDBJ | mRNA | ||
BT009817 EMBL· GenBank· DDBJ | AAP88819.1 EMBL· GenBank· DDBJ | mRNA | ||
AK313836 EMBL· GenBank· DDBJ | BAG36569.1 EMBL· GenBank· DDBJ | mRNA | ||
CH471108 EMBL· GenBank· DDBJ | EAW90154.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471108 EMBL· GenBank· DDBJ | EAW90155.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC020090 EMBL· GenBank· DDBJ | AAH20090.1 EMBL· GenBank· DDBJ | mRNA | ||
BC051907 EMBL· GenBank· DDBJ | AAH51907.1 EMBL· GenBank· DDBJ | mRNA | ||
BC067272 EMBL· GenBank· DDBJ | AAH67272.1 EMBL· GenBank· DDBJ | mRNA | ||
AF044263 EMBL· GenBank· DDBJ | AAC03357.1 EMBL· GenBank· DDBJ | Genomic DNA |