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→‎Structure and function: Added information on hnRNP R and removed a technically incorrect piece of information, which stated that all hnRNPs are solely localized in the nucleus. This is not true. Some, like SYNCRIP, are predominantly localized in the cytoplasm.
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== Structure and function ==
== Structure and function ==


This gene belongs to the subfamily of ubiquitously expressed [[Heterogeneous ribonucleoprotein particle|heterogeneous nuclear ribonucleoproteins]] (hnRNPs). The hnRNPs are RNA 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.
This gene belongs to the subfamily of ubiquitously expressed [[Heterogeneous ribonucleoprotein particle|heterogeneous nuclear ribonucleoproteins]] (hnRNPs). The hnRNPs are [[RNA-binding protein]]s 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.


HnRNP R is made up of an N-terminal [[alpha helix|helix]] bundle known as the “acidic domain” (AcD), followed by three sequential [[RNA recognition motif]]s (RRMs) separated by short linkers, and an [[arginine]]-[[glycine]]-rich domain called the “RGG box” at the C-terminus. The RRMs play a role in RNA binding, while the AcD engages in [[protein-protein interactions]] (PPIs). The RGG box is involved in both RNA binding and in PPIs. The AcD is unique to hnRNP R and its cytoplasmic [[homology (biology)|homolog]] [[SYNCRIP]] (hnRNP Q), and is involved in interactions with [[APOBEC1|APOCBEC-1]].<ref name="pmid27081926"> {{cite journal | vauthors = Beuck C, Williamson JR, Wüthrich K, Serrano P | title = The acidic domain is a unique structural feature of the splicing factor SYNCRIP | journal = Protein Science | volume = 25 | issue = 8 | pages = 1545-50 | date = August 2016 | pmid = 27081926 | doi = 10.1002/pro.2935 }}</ref>
HnRNP R is made up of an N-terminal [[alpha helix|helix]] bundle known as the “acidic domain” (AcD), followed by three sequential [[RNA recognition motif]]s (RRMs) separated by short linkers, and an [[arginine]]-[[glycine]]-rich domain called the “RGG box” at the C-terminus. The RRMs play a role in RNA binding, while the AcD engages in [[protein-protein interactions]] (PPIs). The RGG box is involved in both RNA binding and in PPIs. The AcD is unique to hnRNP R and its cytoplasmic [[homology (biology)|homolog]] [[SYNCRIP]] (hnRNP Q), and is involved in interactions with [[APOBEC1|APOCBEC-1]].<ref name="pmid27081926"> {{cite journal | vauthors = Beuck C, Williamson JR, Wüthrich K, Serrano P | title = The acidic domain is a unique structural feature of the splicing factor SYNCRIP | journal = Protein Science | volume = 25 | issue = 8 | pages = 1545-50 | date = August 2016 | pmid = 27081926 | doi = 10.1002/pro.2935 }}</ref>

Revision as of 18:03, 10 December 2020

HNRNPR
Available structures
PDBHuman UniProt search: PDBe RCSB
Identifiers
AliasesHNRNPR, HNRPR, hnRNP-R, heterogeneous nuclear ribonucleoprotein R
External IDsOMIM: 607201; MGI: 1891692; HomoloGene: 4251; GeneCards: HNRNPR; OMA:HNRNPR - orthologs
Orthologs
SpeciesHumanMouse
Entrez

10236

74326

Ensembl

ENSG00000282958
ENSG00000125944

ENSMUSG00000066037

UniProt

O43390

n/a

RefSeq (mRNA)

NM_001277121
NM_001277122
NM_001277123
NM_028871
NM_001355182

RefSeq (protein)

n/a

Location (UCSC)Chr 1: 23.3 – 23.34 MbChr 4: 136.04 – 136.09 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Heterogeneous nuclear ribonucleoprotein R is a protein that in humans is encoded by the HNRNPR gene.[5][6]

Structure and function

This gene belongs to the subfamily of ubiquitously expressed heterogeneous nuclear ribonucleoproteins (hnRNPs). The hnRNPs are RNA-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.

HnRNP R is made up of an N-terminal helix bundle known as the “acidic domain” (AcD), followed by three sequential RNA recognition motifs (RRMs) separated by short linkers, and an arginine-glycine-rich domain called the “RGG box” at the C-terminus. The RRMs play a role in RNA binding, while the AcD engages in protein-protein interactions (PPIs). The RGG box is involved in both RNA binding and in PPIs. The AcD is unique to hnRNP R and its cytoplasmic homolog SYNCRIP (hnRNP Q), and is involved in interactions with APOCBEC-1.[7]

Interactions

HnRNP R has been shown to interact with SMN1[8][9] and PRMT1.[10][11]

References

  1. ^ a b c ENSG00000125944 GRCh38: Ensembl release 89: ENSG00000282958, ENSG00000125944 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000066037 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Hassfeld W, Chan EK, Mathison DA, Portman D, Dreyfuss G, Steiner G, Tan EM (Jan 1998). "Molecular definition of heterogeneous nuclear ribonucleoprotein R (hnRNP R) using autoimmune antibody: immunological relationship with hnRNP P". Nucleic Acids Research. 26 (2): 439–45. doi:10.1093/nar/26.2.439. PMC 147279. PMID 9421497.
  6. ^ "Entrez Gene: HNRPR heterogeneous nuclear ribonucleoprotein R".
  7. ^ Beuck C, Williamson JR, Wüthrich K, Serrano P (August 2016). "The acidic domain is a unique structural feature of the splicing factor SYNCRIP". Protein Science. 25 (8): 1545–50. doi:10.1002/pro.2935. PMID 27081926.
  8. ^ Mourelatos Z, Abel L, Yong J, Kataoka N, Dreyfuss G (Oct 2001). "SMN interacts with a novel family of hnRNP and spliceosomal proteins". The EMBO Journal. 20 (19): 5443–52. doi:10.1093/emboj/20.19.5443. PMC 125643. PMID 11574476.
  9. ^ Rossoll W, Kröning AK, Ohndorf UM, Steegborn C, Jablonka S, Sendtner M (Jan 2002). "Specific interaction of Smn, the spinal muscular atrophy determining gene product, with hnRNP-R and gry-rbp/hnRNP-Q: a role for Smn in RNA processing in motor axons?". Human Molecular Genetics. 11 (1): 93–105. doi:10.1093/hmg/11.1.93. PMID 11773003.
  10. ^ Wada K, Inoue K, Hagiwara M (Aug 2002). "Identification of methylated proteins by protein arginine N-methyltransferase 1, PRMT1, with a new expression cloning strategy". Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 1591 (1–3): 1–10. doi:10.1016/S0167-4889(02)00202-1. PMID 12183049.
  11. ^ Stelzl U, Worm U, Lalowski M, Haenig C, Brembeck FH, Goehler H, Stroedicke M, Zenkner M, Schoenherr A, Koeppen S, Timm J, Mintzlaff S, Abraham C, Bock N, Kietzmann S, Goedde A, Toksöz E, Droege A, Krobitsch S, Korn B, Birchmeier W, Lehrach H, Wanker EE (Sep 2005). "A human protein-protein interaction network: a resource for annotating the proteome". Cell. 122 (6): 957–68. doi:10.1016/j.cell.2005.08.029. hdl:11858/00-001M-0000-0010-8592-0. PMID 16169070.

Further reading

External links


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