HNRPU

Last updated
HNRNPU
Available structures
PDB Ortholog search: PDBe RCSB
Identifiers
Aliases HNRNPU , HNRPU, SAF-A, U21.1, hnRNP U, SAFA, HNRNPU-AS1, heterogeneous nuclear ribonucleoprotein U (scaffold attachment factor A), heterogeneous nuclear ribonucleoprotein U, HNRNPU antisense RNA 1, C1orf199, NCRNA00201, EIEE54, pp120, GRIP120, DEE54
External IDs OMIM: 602869 MGI: 1858195 HomoloGene: 22991 GeneCards: HNRNPU
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_004501
NM_031844

NM_016805

RefSeq (protein)

NP_004492
NP_114032

NP_058085

Location (UCSC) Chr 1: 244.84 – 244.86 Mb n/a
PubMed search [2] [3]
Wikidata
View/Edit Human View/Edit Mouse

Heterogeneous nuclear ribonucleoprotein U is a protein that in humans is encoded by the HNRNPU gene. [4] [5]

Contents

Function

This gene belongs to the subfamily of ubiquitously expressed heterogeneous nuclear ribonucleoproteins (hnRNPs). The hnRNPs are RNA binding proteins that form complexes 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 contains a RNA binding domain and scaffold-associated region (SAR)-specific bipartite DNA-binding domain. This protein is also thought to be involved in the packaging of hnRNA into large ribonucleoprotein complexes. During apoptosis, this protein is cleaved in a caspase-dependent way. Cleavage occurs at the SALD site, resulting in a loss of DNA-binding activity and a concomitant detachment of this protein from nuclear structural sites. But this cleavage does not affect the function of the encoded protein in RNA metabolism. At least two alternatively spliced transcript variants have been identified for this gene. [6]

Interactions

HNRPU has been shown to interact with:

Related Research Articles

Gideon Dreyfuss is an American biochemist, the Isaac Norris Professor of Biochemistry and Biophysics at the University of Pennsylvania School of Medicine, and an investigator of the Howard Hughes Medical Institute. He was elected to the National Academy of Sciences in 2012.

<span class="mw-page-title-main">Heterogeneous ribonucleoprotein particle</span>

Heterogeneous nuclear ribonucleoproteins (hnRNPs) are complexes of RNA and protein present in the cell nucleus during gene transcription and subsequent post-transcriptional modification of the newly synthesized RNA (pre-mRNA). The presence of the proteins bound to a pre-mRNA molecule serves as a signal that the pre-mRNA is not yet fully processed and therefore not ready for export to the cytoplasm. Since most mature RNA is exported from the nucleus relatively quickly, most RNA-binding protein in the nucleus exist as heterogeneous ribonucleoprotein particles. After splicing has occurred, the proteins remain bound to spliced introns and target them for degradation.

<span class="mw-page-title-main">U7 small nuclear RNA</span>

The U7 small nuclear RNA is an RNA molecule and a component of the small nuclear ribonucleoprotein complex. The U7 snRNA is required for histone pre-mRNA processing.

<span class="mw-page-title-main">HNRNPA1</span> Protein-coding gene in the species Homo sapiens

Heterogeneous nuclear ribonucleoprotein A1 is a protein that in humans is encoded by the HNRNPA1 gene. Mutations in hnRNP A1 are causative of amyotrophic lateral sclerosis and the syndrome multisystem proteinopathy.

<span class="mw-page-title-main">HNRNPK</span> Human protein and coding gene

Heterogeneous nuclear ribonucleoprotein K is a protein that in humans is encoded by the HNRNPK gene. It is found in the cell nucleus that binds to pre-messenger RNA (mRNA) as a component of heterogeneous ribonucleoprotein particles. The simian homolog is known as protein H16. Both proteins bind to single-stranded DNA as well as to RNA and can stimulate the activity of RNA polymerase II, the protein responsible for most gene transcription. The relative affinities of the proteins for DNA and RNA vary with solution conditions and are inversely correlated, so that conditions promoting strong DNA binding result in weak RNA binding.

<span class="mw-page-title-main">HNRNPA2B1</span> Protein-coding gene in the species Homo sapiens

Heterogeneous nuclear ribonucleoproteins A2/B1 is a protein that in humans is encoded by the HNRNPA2B1 gene.

<span class="mw-page-title-main">PCBP1</span> Protein-coding gene in the species Homo sapiens

Poly(rC)-binding protein 1 is a protein that in humans is encoded by the PCBP1 gene.

<span class="mw-page-title-main">PCBP2</span> Protein-coding gene in the species Homo sapiens

Poly(rC)-binding protein 2 is a protein that in humans is encoded by the PCBP2 gene.

<span class="mw-page-title-main">HNRPD</span> Protein-coding gene in the species Homo sapiens

Heterogeneous nuclear ribonucleoprotein D0 (HNRNPD) also known as AU-rich element RNA-binding protein 1 (AUF1) is a protein that in humans is encoded by the HNRNPD gene. Alternative splicing of this gene results in four transcript variants.

<span class="mw-page-title-main">HNRNPC</span> Protein-coding gene in the species Homo sapiens

Heterogeneous nuclear ribonucleoproteins C1/C2 is a protein that in humans is encoded by the HNRNPC gene.

<span class="mw-page-title-main">SAFB</span> Protein-coding gene in the species Homo sapiens

Scaffold attachment factor B, also known as SAFB, is a gene with homologs that have been studied in humans and mice.

<span class="mw-page-title-main">SYNCRIP</span> Protein-coding gene in the species Homo sapiens

Synaptotagmin-binding, cytoplasmic RNA-interacting protein (SYNCRIP), also known as heterogeneous nuclear ribonucleoprotein (hnRNP) Q or NS1-associated protein-1 (NSAP-1), is a protein that in humans is encoded by the SYNCRIP gene. As the name implies, SYNCRIP is localized predominantly in the cytoplasm. It is evolutionarily conserved across eukaryotes and participates in several cellular and disease pathways, especially in neuronal and muscular development. In humans, there are three isoforms, all of which are associated in vitro with pre-mRNAs, mRNA splicing intermediates, and mature mRNA-protein complexes, including mRNA turnover.

<span class="mw-page-title-main">HNRPF</span> Protein-coding gene in the species Homo sapiens

Heterogeneous nuclear ribonucleoprotein F is a protein that in humans is encoded by the HNRNPF gene.

<span class="mw-page-title-main">HNRPH1</span> Protein-coding gene in the species Homo sapiens

Heterogeneous nuclear ribonucleoprotein H is a protein that in humans is encoded by the HNRNPH1 gene.

<span class="mw-page-title-main">HNRNPL</span> Protein-coding gene in the species Homo sapiens

Heterogeneous nuclear ribonucleoprotein L is a protein that in humans is encoded by the HNRNPL gene.

<span class="mw-page-title-main">HNRNPR</span> Protein-coding gene in the species Homo sapiens

Heterogeneous nuclear ribonucleoprotein R is a protein that in humans is encoded by the HNRNPR gene.

<span class="mw-page-title-main">HNRPH2</span> Protein-coding gene in the species Homo sapiens

Heterogeneous nuclear ribonucleoprotein H2 is a protein that in humans is encoded by the HNRNPH2 gene.

<span class="mw-page-title-main">HNRPDL</span> Mammalian protein found in Homo sapiens

Heterogeneous nuclear ribonucleoprotein D-like, also known as HNRPDL, is a protein which in humans is encoded by the HNRPDL gene.

<span class="mw-page-title-main">PTBP1</span> Protein-coding gene in the species Homo sapiens

Polypyrimidine tract-binding protein 1 is a protein that in humans is encoded by the PTBP1 gene.

<span class="mw-page-title-main">HSUR</span>

HSURs are viral small regulatory RNAs. They are found in Herpesvirus saimiri which is responsible for aggressive T-cell leukemias in primates. They are nuclear RNAs which bind host proteins to form small nuclear ribonucleoproteins (snRNPs). The RNAs are 114–143 nucleotides in length and the HSUR family has been subdivided into HSURs numbered 1 to 7. The function of HSURs has not yet been identified; they do not affect transcription so are thought to act post-transcriptionally, potentially influencing the stability of host mRNAs.

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000153187 Ensembl, May 2017
  2. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  3. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. Fackelmayer FO, Richter A (Mar 1994). "hnRNP-U/SAF-A is encoded by two differentially polyadenylated mRNAs in human cells". Biochim Biophys Acta. 1217 (2): 232–4. doi:10.1016/0167-4781(94)90044-2. PMID   7509195.
  5. Fackelmayer FO, Richter A (Sep 1994). "Purification of two isoforms of hnRNP-U and characterization of their nucleic acid binding activity". Biochemistry. 33 (34): 10416–22. doi:10.1021/bi00200a024. PMID   8068679.
  6. "Entrez Gene: HNRNPU heterogeneous nuclear ribonucleoprotein U (scaffold attachment factor A)".
  7. Martens JH, Verlaan M, Kalkhoven E, Dorsman JC, Zantema A (Apr 2002). "Scaffold/matrix attachment region elements interact with a p300-scaffold attachment factor A complex and are bound by acetylated nucleosomes". Mol. Cell. Biol. 22 (8): 2598–606. doi:10.1128/mcb.22.8.2598-2606.2002. PMC   133732 . PMID   11909954.
  8. Kim MK, Nikodem VM (Oct 1999). "hnRNP U inhibits carboxy-terminal domain phosphorylation by TFIIH and represses RNA polymerase II elongation". Mol. Cell. Biol. 19 (10): 6833–44. doi:10.1128/MCB.19.10.6833. PMC   84680 . PMID   10490622.
  9. Eggert M, Michel J, Schneider S, Bornfleth H, Baniahmad A, Fackelmayer FO, Schmidt S, Renkawitz R (Nov 1997). "The glucocorticoid receptor is associated with the RNA-binding nuclear matrix protein hnRNP U". J. Biol. Chem. 272 (45): 28471–8. doi: 10.1074/jbc.272.45.28471 . PMID   9353307.
  10. Taniura H, Yoshikawa K (2002). "Necdin interacts with the ribonucleoprotein hnRNP U in the nuclear matrix". J. Cell. Biochem. 84 (3): 545–55. doi:10.1002/jcb.10047. PMID   11813259. S2CID   5988824.

Further reading