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Sep. 10, 2014:
A total of 174 experimentally verified S-nitrosylation sites on 94 S-nitrosylated proteins from individualized human colorectal cancer tissues using a label-free quantitation strategy.

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Protein Name: RNA-binding protein FXR1

UniprotKB/SwissProt ID: P51114 (P51114)

Gene Name: FXR1

Organism: Homo sapiens (Human)

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)

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Cytoplasm, Cytoplasmic ribonucleoprotein granule. Cytoplasm, Stress granule. Cytoplasm. Cell projection, dendrite. Cell projection, dendritic spine. Cell projection, axon. Nucleus envelope. Postsynapse

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR008395 Agenet-like_dom
IPR040148 FMR1
IPR022034 FMR1-like_C_core
IPR040472 FMRP_KH0
IPR032172 FXR1_C1
IPR032177 FXR_C3
IPR004087 KH_dom
IPR004088 KH_dom_type_1
IPR036612 KH_dom_type_1_sf
IPR047494 KH_I_FXR1_rpt1
IPR047495 KH_I_FXR1_rpt2
IPR047496 KH_I_FXR1_rpt3
IPR047425 Tudor_Agenet_FXR1_rpt1
IPR047427 Tudor_Agenet_FXR1_rpt2
IPR041560 Tudor_FRM1

The S-nitrosylation sites of P51114

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 129 KTVKKNTFFK C TVDVPEDLRE   
2 141 VDVPEDLREA C ANENAHKDFK   
3 211 RNEEATKHLE C TKQLAAAFHE   
4 77 VYSRANDQEP C GWWLAKVRMM   
5 99 GEFYVIEYAA C DATYNEIVTF