Heterogeneous nuclear ribonucleoprotein D0

Function

Binds with high affinity to RNA molecules that contain AU-rich elements (AREs) found within the 3'-UTR of many proto-oncogenes and cytokine mRNAs. Also binds to double- and single-stranded DNA sequences in a specific manner and functions a transcription factor. Each of the RNA-binding domains specifically can bind solely to a single-stranded non-monotonous 5'-UUAG-3' sequence and also weaker to the single-stranded 5'-TTAGGG-3' telomeric DNA repeat. Binds RNA oligonucleotides with 5'-UUAGGG-3' repeats more tightly than the telomeric single-stranded DNA 5'-TTAGGG-3' repeats. Binding of RRM1 to DNA inhibits the formation of DNA quadruplex structure which may play a role in telomere elongation. May be involved in translationally coupled mRNA turnover. Implicated with other RNA-binding proteins in the cytoplasmic deadenylation/translational and decay interplay of the FOS mRNA mediated by the major coding-region determinant of instability (mCRD) domain. May play a role in the regulation of the rhythmic expression of circadian clock core genes. Directly binds to the 3'UTR of CRY1 mRNA and induces CRY1 rhythmic translation. May also be involved in the regulation of PER2 translation.

Classification

Family (Pfam)

PF08143 CBFNT, PF00076 RRM_1

InterPro

CARG-binding_factor_N, Nucleotide-bd_a/b_plait_sf, RBD_domain_sf, RRM_dom

Functional cluster

Adenylate Kinases & Peroxiredoxins

Experimental structures · PDB · 7

• 1HD0 NMR
• 1HD1 NMR
• 1IQT NMR
• 1WTB NMR
• 1X0F NMR
• 2Z5N X-ray 3.20A
• 5IM0 X-ray 1.70A

A predicted model is available from AlphaFold.

Gene Ontology · 40

• GO:0000785 chromatin
• GO:0005829 cytosol
• GO:0098978 glutamatergic synapse
• GO:0005654 nucleoplasm
• GO:0005634 nucleus
• GO:0014069 postsynaptic density
• GO:1990904 ribonucleoprotein complex
• GO:0003682 chromatin binding
• GO:0042826 histone deacetylase binding
• GO:0003680 minor groove of adenine-thymine-rich DNA binding
• GO:0035925 mRNA 3'-UTR AU-rich region binding
• GO:0003723 RNA binding
• GO:0042162 telomeric DNA binding
• GO:0061158 3'-UTR-mediated mRNA destabilization
• GO:0071230 cellular response to amino acid stimulus
• GO:0071392 cellular response to estradiol stimulus
• GO:0071732 cellular response to nitric oxide
• GO:1904586 cellular response to putrescine
• GO:0021549 cerebellum development
• GO:0097167 circadian regulation of translation
• GO:0070934 CRD-mediated mRNA stabilization
• GO:0006351 DNA-templated transcription
• GO:1990828 hepatocyte dedifferentiation
• GO:0001889 liver development
• GO:1900152 negative regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay
• GO:2000767 positive regulation of cytoplasmic translation
• GO:0045893 positive regulation of DNA-templated transcription
• GO:1904355 positive regulation of telomere capping
• GO:0032212 positive regulation of telomere maintenance via telomerase
• GO:0045944 positive regulation of transcription by RNA polymerase II
• GO:0045727 positive regulation of translation
• GO:0042752 regulation of circadian rhythm
• GO:0006355 regulation of DNA-templated transcription
• GO:0010468 regulation of gene expression
• GO:0051592 response to calcium ion
• GO:0051602 response to electrical stimulus
• GO:1901355 response to rapamycin
• GO:1904383 response to sodium phosphate
• GO:0006401 RNA catabolic process
• GO:0006396 RNA processing

Neighborhood · nearest proteins

Related proteins · sequence + function similarity

• Heterogeneous nuclear ribonucleoprotein D0 1.00
• Heterogeneous nuclear ribonucleoprotein D0 0.99
• Heterogeneous nuclear ribonucleoprotein A/B 0.96
• Heterogeneous nuclear ribonucleoprotein D-like 0.92
• Heterogeneous nuclear ribonucleoprotein A/B 0.90
• Heterogeneous nuclear ribonucleoprotein D-like 0.90
• Heterogeneous nuclear ribonucleoprotein D-like 0.90
• Heterogeneous nuclear ribonucleoprotein D-like-A 0.89
• Heterogeneous nuclear ribonucleoprotein D-like 0.86
• Heterogeneous nuclear ribonucleoprotein D-like-B 0.83
• RNA-binding protein squid 0.82
• Heterogeneous nuclear ribonucleoprotein A0 0.79

Co-cited proteins · studied together in the literature

• Insulin-like growth factor 2 mRNA-binding protein 2 2 shared papers
• Nucleolin 2 shared papers
• GTP-binding protein 1 1 shared papers
• Heterogeneous nuclear ribonucleoprotein R 2 shared papers
• Heterogeneous nuclear ribonucleoprotein A/B 2 shared papers
• Heterogeneous nuclear ribonucleoprotein Q 3 shared papers
• GTP-binding protein 1 1 shared papers
• Polyadenylate-binding protein-interacting protein 1 1 shared papers
• Cold shock domain-containing protein E1 1 shared papers
• Small ribosomal subunit protein uS3 2 shared papers
• Eukaryotic translation initiation factor 3 subunit B 1 shared papers
• Eukaryotic translation initiation factor 4 gamma 1 1 shared papers

Literature · 36 cited papers

• Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation. Nat. Struct. Mol. Biol. · 2017
• N-terminome analysis of the human mitochondrial proteome. Proteomics · 2015
• Mapping of SUMO sites and analysis of SUMOylation changes induced by external stimuli. Proc. Natl. Acad. Sci. U.S.A. · 2014
• AUF1 contributes to Cryptochrome1 mRNA degradation and rhythmic translation. Nucleic Acids Res. · 2014
• An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. J. Proteomics · 2014
• Immunoaffinity enrichment and mass spectrometry analysis of protein methylation. Mol. Cell. Proteomics · 2014
• Toward a comprehensive characterization of a human cancer cell phosphoproteome. J. Proteome Res. · 2013
• Modulation of exosome-mediated mRNA turnover by interaction of GTP-binding protein 1 (GTPBP1) with its target mRNAs. FASEB J. · 2011
• System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation. Sci. Signal. · 2011
• Initial characterization of the human central proteome. BMC Syst. Biol. · 2011
• Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis. Sci. Signal. · 2010
• Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci. Signal. · 2009
• … and 24 more in the literature graph