HNRNPR

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

HNRNPR
Available structures PDB Human UniProt search: PDBe RCSB List of PDB id codes 2DK2
Identifiers
Aliases	HNRNPR, HNRPR, hnRNP-R, heterogeneous nuclear ribonucleoprotein R
External IDs	OMIM: 607201 MGI: 1891692 HomoloGene: 4251 GeneCards: HNRNPR
Gene location (Human) Chr. Chromosome 1 (human)[1] Band 1p36.12 Start 23,303,771 bp[1] End 23,344,336 bp[1]
Gene location (Mouse) Chr. Chromosome 4 (mouse)[2] Band 4|4 D3 Start 136,310,942 bp[2] End 136,359,447 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • mRNA 3'-UTR binding • nucleic acid binding • GO:0001948 protein binding • RNA binding • mRNA binding Cellular component • nucleolus • cytoplasm • axon terminus • growth cone • cell nucleus • intracellular membrane-bounded organelle • dendrite • endoplasmic reticulum • catalytic step 2 spliceosome • spliceosomal complex • nucleoplasm • ribonucleoprotein Biological process • circadian rhythm • positive regulation of mRNA catabolic process • mRNA destabilization • GO:0048553 negative regulation of catalytic activity • mRNA processing • mRNA splicing, via spliceosome • RNA splicing • RNA metabolic process Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	10236	74326
Ensembl	ENSG00000282958 ENSG00000125944	ENSMUSG00000066037
UniProt	O43390	n/a
RefSeq (mRNA)	NM_001102397 NM_001102398 NM_001102399 NM_001297620 NM_001297621 NM_001297622 NM_005826	NM_001277121 NM_001277122 NM_001277123 NM_028871 NM_001355182
RefSeq (protein)	NP_001095867 NP_001095868 NP_001095869 NP_001284549 NP_001284550 NP_001284551 NP_005817	n/a
Location (UCSC)	Chr 1: 23.3 – 23.34 Mb	Chr 4: 136.31 – 136.36 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

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. 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 three repeats of quasi-RRM domains that bind to RNAs and also contains a nuclear localization motif.[6]

Interactions

HNRNPR has been shown to interact with SMN1[7][8] and PRMT1.[9][10]

References

1. ENSG00000125944 GRCh38: Ensembl release 89: ENSG00000282958, ENSG00000125944 - Ensembl, May 2017
2. 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. 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.
8. 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.
9. 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.
10. 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

• 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.
• 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.
• Jurica MS, Licklider LJ, Gygi SR, Grigorieff N, Moore MJ (Apr 2002). "Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis". RNA. 8 (4): 426–39. doi:10.1017/S1355838202021088. PMC 1370266. PMID 11991638.
• 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.
• Angenstein F, Evans AM, Settlage RE, Moran ST, Ling SC, Klintsova AY, Shabanowitz J, Hunt DF, Greenough WT (Oct 2002). "A receptor for activated C kinase is part of messenger ribonucleoprotein complexes associated with polyA-mRNAs in neurons". The Journal of Neuroscience. 22 (20): 8827–37. doi:10.1523/jneurosci.22-20-08827.2002. PMC 6757688. PMID 12388589.
• Hassel S, Eichner A, Yakymovych M, Hellman U, Knaus P, Souchelnytskyi S (May 2004). "Proteins associated with type II bone morphogenetic protein receptor (BMPR-II) and identified by two-dimensional gel electrophoresis and mass spectrometry". Proteomics. 4 (5): 1346–58. doi:10.1002/pmic.200300770. PMID 15188402.
• Andersen JS, Lam YW, Leung AK, Ong SE, Lyon CE, Lamond AI, Mann M (Jan 2005). "Nucleolar proteome dynamics". Nature. 433 (7021): 77–83. doi:10.1038/nature03207. PMID 15635413.
• Huang J, Chen XH, Wu K, Xu P (May 2005). "Cloning and expression of a novel isoform of heterogeneous nuclear ribonucleoprotein-R". NeuroReport. 16 (7): 727–30. doi:10.1097/00001756-200505120-00014. PMID 15858414.
• Kimura K, Wakamatsu A, Suzuki Y, Ota T, Nishikawa T, Yamashita R, Yamamoto J, Sekine M, Tsuritani K, Wakaguri H, Ishii S, Sugiyama T, Saito K, Isono Y, Irie R, Kushida N, Yoneyama T, Otsuka R, Kanda K, Yokoi T, Kondo H, Wagatsuma M, Murakawa K, Ishida S, Ishibashi T, Takahashi-Fujii A, Tanase T, Nagai K, Kikuchi H, Nakai K, Isogai T, Sugano S (Jan 2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes". Genome Research. 16 (1): 55–65. doi:10.1101/gr.4039406. PMC 1356129. PMID 16344560.
• Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S, McBroom-Cerajewski L, Robinson MD, O'Connor L, Li M, Taylor R, Dharsee M, Ho Y, Heilbut A, Moore L, Zhang S, Ornatsky O, Bukhman YV, Ethier M, Sheng Y, Vasilescu J, Abu-Farha M, Lambert JP, Duewel HS, Stewart II, Kuehl B, Hogue K, Colwill K, Gladwish K, Muskat B, Kinach R, Adams SL, Moran MF, Morin GB, Topaloglou T, Figeys D (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Molecular Systems Biology. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.
• Szafranski K, Schindler S, Taudien S, Hiller M, Huse K, Jahn N, Schreiber S, Backofen R, Platzer M (2007). "Violating the splicing rules: TG dinucleotides function as alternative 3' splice sites in U2-dependent introns". Genome Biology. 8 (8): R154. doi:10.1186/gb-2007-8-8-r154. PMC 2374985. PMID 17672918.

External links

• HNRNPR human gene location in the UCSC Genome Browser.
• HNRNPR human gene details in the UCSC Genome Browser.
• Overview of all the structural information available in the PDB for UniProt: O43390 (Heterogeneous nuclear ribonucleoprotein R) at the PDBe-KB.