Rabbit Anti-HNRNPD (Phosphorylated S83) Polyclonal Antibody (PTM-CBPAB-0766YC) (PTM-CBPAB-0766YC)

heterogeneous nuclear ribonucleoprotein D

HNRNPD belongs to the subfamily of ubiquitously expressed heterogeneous nuclear ribonucleoproteins (hnRNPs). The hnRNPs are nucleic acid binding proteins and they complex with heterogeneous nuclear RNA (hnRNA). These proteins are associated with pre-mRNAs in the nucleus and appear to influence pre-mRNA processing and other aspects of mRNA metabolism and transport. While all of the hnRNPs are present in the nucleus, some seem to shuttle between the nucleus and the cytoplasm. The hnRNP proteins have distinct nucleic acid binding properties. The protein encoded by this gene has two repeats of quasi-RRM domains that bind to RNAs. It localizes to both the nucleus and the cytoplasm. This protein is implicated in the regulation of mRNA stability. Alternative splicing of this gene results in four transcript variants.

Heterogeneous Nuclear Ribonucleoprotein D; AU-Rich Element RNA Binding Protein 1, 37kDa; HnRNP D0; HNRPD; AUF1; Heterogeneous Nuclear Ribonucleoprotein D (AU-Rich Element RNA-Binding Protein 1, 37kD); Heterogeneous Nuclear Ribonucleoprotein D0;

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.

3'-UTR-mediated mRNA destabilization Source: Ensembl
Cellular response to amino acid stimulus Source: Ensembl
Cellular response to estradiol stimulus Source: Ensembl
Cellular response to nitric oxide Source: Ensembl
Cellular response to putrescine Source: Ensembl
Cerebellum development Source: Ensembl
Circadian regulation of translation Source: UniProtKB
CRD-mediated mRNA stabilization Source: ComplexPortal
Hepatocyte dedifferentiation Source: Ensembl
Liver development Source: Ensembl
mRNA transcription by RNA polymerase II Source: BHF-UCL
Negative regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay Source: ComplexPortal
Positive regulation of cytoplasmic translation Source: ComplexPortal
Positive regulation of telomerase RNA reverse transcriptase activity Source: BHF-UCL
Positive regulation of telomere capping Source: BHF-UCL
Positive regulation of transcription, DNA-templated Source: UniProtKB
Positive regulation of transcription by RNA polymerase II Source: BHF-UCL
Positive regulation of translation Source: UniProtKB
Regulation of circadian rhythm Source: UniProtKB
Regulation of gene expression Source: GO_Central
Regulation of telomere maintenance Source: BHF-UCL
Regulation of transcription, DNA-templated Source: UniProtKB
Response to calcium ion Source: Ensembl
Response to electrical stimulus Source: Ensembl
Response to rapamycin Source: Ensembl
Response to sodium phosphate Source: Ensembl
RNA catabolic process Source: ProtInc
RNA processing Source: ProtInc

Nucleus; Cytoplasm. Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Component of ribonucleosomes. Cytoplasmic localization oscillates diurnally.

Arg-345 is dimethylated, probably to asymmetric dimethylarginine.
Methylated by PRMT1, in an insulin-dependent manner. The PRMT1-mediated methylation regulates tyrosine phosphorylation (By similarity).