FXR1
entrez
8087
canonical
uniprot
P51114
canonical
ensembl
ENSG00000114416
resolver
ensp
ENSP00000307633
resolver
ensp
ENSP00000350170
resolver
ensp
ENSP00000388828
resolver
ensp
ENSP00000418027
resolver
ensp
ENSP00000420515
resolver
ensp
ENSP00000420643
resolver
ensp
ENSP00000513936
resolver
ensp
ENSP00000513937
resolver
ensp
ENSP00000643112
resolver
ensp
ENSP00000643113
resolver
enst
ENST00000468861
resolver
enst
ENST00000491062
resolver
enst
ENST00000698793
resolver
enst
ENST00000698794
resolver
genesymbol
FXR1
resolver
hgnc
HGNC:4023
resolver
uniprot
A0A0F7KYT8
resolver
uniprot
A0A0F7L0Q8
resolver
uniprot
A0A0F7L1S3
resolver
uniprot
A0A8V8TMQ1
resolver
uniprot
A0A8V8TNP6
resolver
uniprot
A8K9B8
resolver
uniprot
E7EU85
resolver
uniprot
E9PFF5
resolver
uniprot
Q7Z450
resolver
uniprot
Q8N6R8
resolver
uniprot_entry
A0A0F7KYT8_HUMAN
resolver
uniprot_entry
A0A0F7L0Q8_HUMAN
resolver
uniprot_entry
A0A0F7L1S3_HUMAN
resolver
uniprot_entry
A0A8V8TMQ1_HUMAN
resolver
uniprot_entry
A0A8V8TNP6_HUMAN
resolver
uniprot_entry
E7EU85_HUMAN
resolver
uniprot_entry
E9PFF5_HUMAN
resolver
uniprot_entry
FXR1_HUMAN
resolver
uniprot_sec
A8K9B8
resolver
uniprot_sec
Q7Z450
resolver
uniprot_sec
Q8N6R8
resolver
amino_acid_sequence
MAELTVEVRGSNGAFYKGFIKDVHEDSLTVVFENNWQPERQVPFNEVRLPPPPDIKKEISEGDEVEVYSRANDQEPCGWWLAKVRMMKGEFYVIEYAACDATYNEIVTFERLRPVNQNKTVKKNTFFKCTVDVPEDLREACANENAHKDFKKAVGACRIFYHPETTQLMILSASEATVKRVNILSDMHLRSIRTKLMLMSRNEEATKHLECTKQLAAAFHEEFVVREDLMGLAIGTHGSNIQQARKVPGVTAIELDEDTGTFRIYGESADAVKKARGFLEFVEDFIQVPRNLVGKVIGKNGKVIQEIVDKSGVVRVRIEGDNENKLPREDGMVPFVFVGTKESIGNVQVLLEYHIAYLKEVEQLRMERLQIDEQLRQIGSRSYSGRGRGRRGPNYTSGYGTNSELSNPSETESERKDELSDWSLAGEDDRDSRHQRDSRRRPGGRGRSVSGGRGRGGPRGGKSSISSVLKDPDSNPYSLLDNTESDQTADTDASESHHSTNRRRRSRRRRTDEDAVLMDGMTESDTASVNENGLVTVADYISRAESQSRQRNLPRETLAKNKKEMAKDVIEEHGPSEKAINGPTSASGDDISKLQRTPGEEKINTLKEENTQEAAVLNGVS
uniprot
proteins
disease_involvement
DISEASE: Congenital myopathy 9A (CMYO9A) [MIM:618822]: An autosomal recessive muscular disorder characterized by severe hypotonia apparent at birth, poor feeding, ulnar deviation of the hands, laterally deviated feet, fractures of the long bones, respiratory insufficiency due to muscle weakness, and death in infancy. {ECO:0000269|PubMed:30770808}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Congenital myopathy 9B, proximal, with minicore lesions (CMYO9B) [MIM:618823]: An autosomal recessive, slowly progressive muscular disorder characterized by primarily proximal muscle weakness, neonatal hypotonia leading to delayed motor development, mildly delayed walking in childhood, and difficulty running or climbing. Cardiac function is unaffected, but most patients have obstructive sleep apnea. Muscle biopsy shows type 1 fiber predominance with disorganized Z-lines and minicores that disrupt the myofibrillar striation pattern. {ECO:0000269|PubMed:30770808}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: mRNA-binding protein that acts as a regulator of mRNAs translation and/or stability, and which is required for various processes, such as neurogenesis, muscle development and spermatogenesis (PubMed:17382880, PubMed:20417602, PubMed:30067974, PubMed:34731628, PubMed:35989368, PubMed:36306353). Specifically binds to AU-rich elements (AREs) in the 3'-UTR of target mRNAs (PubMed:17382880, PubMed:34731628). Promotes formation of some phase-separated membraneless compartment by undergoing liquid-liquid phase separation upon binding to AREs-containing mRNAs, leading to assemble mRNAs into cytoplasmic ribonucleoprotein granules that concentrate mRNAs with associated regulatory factors (By similarity). Required to activate translation of stored mRNAs during late spermatogenesis: acts by undergoing liquid-liquid phase separation to assemble target mRNAs into cytoplasmic ribonucleoprotein granules that recruit translation initiation factor EIF4G3 to activate translation of stored mRNAs in late spermatids (By similarity). Promotes translation of MYC transcripts by recruiting the eIF4F complex to the translation start site (PubMed:34731628). Acts as a negative regulator of inflammation in response to IL19 by promoting destabilization of pro-inflammatory transcripts (PubMed:30067974). Also acts as an inhibitor of inflammation by binding to TNF mRNA, decreasing TNF protein production (By similarity). Acts as a negative regulator of AMPA receptor GRIA2/GluA2 synthesis during long-lasting synaptic potentiation of hippocampal neurons by binding to GRIA2/GluA2 mRNA, thereby inhibiting its translation (By similarity). Regulates proliferation of adult neural stem cells by binding to CDKN1A mRNA and promoting its expression (By similarity). Acts as a regulator of sleep and synaptic homeostasis by regulating translation of transcripts in neurons (By similarity). Required for embryonic and postnatal development of muscle tissue by undergoing liquid-liquid phase separation to assemble target mRNAs into cytoplasmic ribonucleoprotein granules (PubMed:30770808). Involved in the nuclear pore complex localization to the nuclear envelope by preventing cytoplasmic aggregation of nucleoporins: acts by preventing ectopic phase separation of nucleoporins in the cytoplasm via a microtubule-dependent mechanism (PubMed:32706158). Plays a role in the stabilization of PKP2 mRNA and therefore protein abundance, via its interaction with PKP3 (PubMed:25225333). May also do the same for PKP2, PKP3 and DSP via its interaction with PKP1 (PubMed:25225333). Forms a cytoplasmic messenger ribonucleoprotein (mRNP) network by packaging long mRNAs, serving as a scaffold that recruits proteins and signaling molecules. This network facilitates signaling reactions by maintaining proximity between kinases and substrates, crucial for processes like actomyosin reorganization (PubMed:39106863). {ECO:0000250|UniProtKB:Q61584, ECO:0000269|PubMed:17382880, ECO:0000269|PubMed:20417602, ECO:0000269|PubMed:25225333, ECO:0000269|PubMed:30067974, ECO:0000269|PubMed:30770808, ECO:0000269|PubMed:32706158, ECO:0000269|PubMed:34731628, ECO:0000269|PubMed:35989368, ECO:0000269|PubMed:36306353, ECO:0000269|PubMed:39106863}.
uniprot
proteins
mass_dalton
69721
uniprot
proteins
mutagenesis
MUTAGEN 202; /note="N->S: Loss of RNA-binding. Disrupts FXR1-network."; /evidence="ECO:0000269|PubMed:39106863"; MUTAGEN 266; /note="G->E: Loss of RNA-binding. Disrupts FXR1-network."; /evidence="ECO:0000269|PubMed:39106863"; MUTAGEN 304; /note="I->N: Abolished binding to PAK1. Loss of RNA-binding. Disrupts FXR1-network."; /evidence="ECO:0000269|PubMed:20417602, ECO:0000269|PubMed:39106863"; MUTAGEN 345..346; /note="GN->DA: Does not affect binding to PAK1."; /evidence="ECO:0000269|PubMed:20417602"; MUTAGEN 348..352; /note="QVLLE->KVLLA: Abolished binding to PAK1."; /evidence="ECO:0000269|PubMed:20417602"; MUTAGEN 352..353; /note="EY->AA: Reduced binding to PAK1."; /evidence="ECO:0000269|PubMed:20417602"; MUTAGEN 420; /note="S->A: Abolished phosphorylation by PAK1, leading to impaired activity."; /evidence="ECO:0000269|PubMed:20417602"; MUTAGEN 420; /note="S->D: Mimics phosphorylation state; leading to increased activity."; /evidence="ECO:0000269|PubMed:20417602
uniprot
proteins
post_translational_modification
PTM: Phosphorylation at Ser-420 by PAK1 promotes its relocalization to stress granules and activity (PubMed:20417602). Phosphorylated by MAPK1/ERK2, promoting subsequent phosphorylation by GSK3B (By similarity). Phosphorylated by GSK3B, promoting ubiquitination and degradation by the proteasome (By similarity). {ECO:0000250|UniProtKB:Q61584, ECO:0000269|PubMed:20417602}.; PTM: Ubiquitinated by the SCF(FBXO4) complex, leading to its degradation by the proteasome: ubiquitination by the SCF(FBXO4) complex takes place following phosphorylation by GSK3B (PubMed:29142209). Ubiquitinated and degraded in a GSK3B-dependent manner in during both scaling and sleep deprivation (By similarity). Ubiquitinated via 'Lys-63'-linked ubiquitin, leading to its degradation: interaction with CEP63 inhibits 'Lys-63'-linked ubiquitination (PubMed:35989368). {ECO:0000250|UniProtKB:Q61584, ECO:0000269|PubMed:29142209, ECO:0000269|PubMed:35989368}.
uniprot
proteins
protein_family
FMR1 family
uniprot
proteins
pubmed
11157796
uniprot
proteins
pubmed
14532325
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16959974
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
17382880
uniprot
proteins
pubmed
18664458
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20417602
uniprot
proteins
pubmed
21072162
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
21771594
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25225333
uniprot
proteins
pubmed
27509095
uniprot
proteins
pubmed
28112733
uniprot
proteins
pubmed
29142209
uniprot
proteins
pubmed
30067974
uniprot
proteins
pubmed
30770808
uniprot
proteins
pubmed
32706158
uniprot
proteins
pubmed
34731628
uniprot
proteins
pubmed
35989368
uniprot
proteins
pubmed
36306353
uniprot
proteins
pubmed
39106863
uniprot
proteins
pubmed
7489725
uniprot
proteins
pubmed
7781595
uniprot
proteins
pubmed
8668200
uniprot
proteins
pubmed
9259278
uniprot
proteins
sequence_length
621
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, Cytoplasmic ribonucleoprotein granule {ECO:0000269|PubMed:32706158, ECO:0000269|PubMed:39106863}. Cytoplasm, Stress granule {ECO:0000269|PubMed:20417602}. Cytoplasm {ECO:0000269|PubMed:30770808, ECO:0000269|PubMed:7781595, ECO:0000269|PubMed:9259278}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q61584}. Cell projection, dendritic spine {ECO:0000250|UniProtKB:Q61584}. Cell projection, axon {ECO:0000250|UniProtKB:Q61584}. Nucleus envelope {ECO:0000269|PubMed:32706158}. Postsynapse {ECO:0000250|UniProtKB:Q61584}. Note=Specifically localizes to cytoplasmic ribonucleoprotein membraneless compartments (By similarity). Localizes to stress granules following phosphorylation at Ser-420 by PAK1 (PubMed:20417602). Adjacent to Z-lines in muscles (By similarity). {ECO:0000250|UniProtKB:Q61584, ECO:0000269|PubMed:20417602}.
uniprot
proteins