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→‎Interactions: Added more interacting partners.
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== Interactions ==
== Interactions ==


HNRNPR has been shown to [[Protein-protein interaction|interact]] with [[SMN1]]<ref name=pmid11574476>{{cite journal | vauthors = Mourelatos Z, Abel L, Yong J, Kataoka N, Dreyfuss G | title = SMN interacts with a novel family of hnRNP and spliceosomal proteins | journal = The EMBO Journal | volume = 20 | issue = 19 | pages = 5443–52 | date = October 2001 | pmid = 11574476 | pmc = 125643 | doi = 10.1093/emboj/20.19.5443 }}</ref><ref name=pmid11773003>{{cite journal | vauthors = Rossoll W, Kröning AK, Ohndorf UM, Steegborn C, Jablonka S, Sendtner M | title = 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? | journal = Human Molecular Genetics | volume = 11 | issue = 1 | pages = 93–105 | date = January 2002 | pmid = 11773003 | doi = 10.1093/hmg/11.1.93 | doi-access = free }}</ref> and [[PRMT1]].<ref name=pmid12183049>{{cite journal | vauthors = Wada K, Inoue K, Hagiwara M | title = Identification of methylated proteins by protein arginine N-methyltransferase 1, PRMT1, with a new expression cloning strategy | journal = Biochimica et Biophysica Acta (BBA) - Molecular Cell Research | volume = 1591 | issue = 1–3 | pages = 1–10 | date = August 2002 | pmid = 12183049 | doi = 10.1016/S0167-4889(02)00202-1 }}</ref><ref name=pmid16169070>{{cite journal | vauthors = 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 | title = A human protein-protein interaction network: a resource for annotating the proteome | journal = Cell | volume = 122 | issue = 6 | pages = 957–68 | date = September 2005 | pmid = 16169070 | doi = 10.1016/j.cell.2005.08.029 | hdl = 11858/00-001M-0000-0010-8592-0 | hdl-access = free }}</ref>
HNRNPR has been shown to [[Protein-protein interaction|interact]] with [[SMN1]]<ref name=pmid11574476>{{cite journal | vauthors = Mourelatos Z, Abel L, Yong J, Kataoka N, Dreyfuss G | title = SMN interacts with a novel family of hnRNP and spliceosomal proteins | journal = The EMBO Journal | volume = 20 | issue = 19 | pages = 5443–52 | date = October 2001 | pmid = 11574476 | pmc = 125643 | doi = 10.1093/emboj/20.19.5443 }}</ref><ref name=pmid11773003>{{cite journal | vauthors = Rossoll W, Kröning AK, Ohndorf UM, Steegborn C, Jablonka S, Sendtner M | title = 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? | journal = Human Molecular Genetics | volume = 11 | issue = 1 | pages = 93–105 | date = January 2002 | pmid = 11773003 | doi = 10.1093/hmg/11.1.93 | doi-access = free }}</ref>, [[PRMT1]],<ref name=pmid12183049>{{cite journal | vauthors = Wada K, Inoue K, Hagiwara M | title = Identification of methylated proteins by protein arginine N-methyltransferase 1, PRMT1, with a new expression cloning strategy | journal = Biochimica et Biophysica Acta (BBA) - Molecular Cell Research | volume = 1591 | issue = 1–3 | pages = 1–10 | date = August 2002 | pmid = 12183049 | doi = 10.1016/S0167-4889(02)00202-1 }}</ref><ref name=pmid16169070>{{cite journal | vauthors = 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 | title = A human protein-protein interaction network: a resource for annotating the proteome | journal = Cell | volume = 122 | issue = 6 | pages = 957–68 | date = September 2005 | pmid = 16169070 | doi = 10.1016/j.cell.2005.08.029 | hdl = 11858/00-001M-0000-0010-8592-0 | hdl-access = free }}</ref> [[TARDBP|TDP-43]],<ref name=pmid20624952>{{cite journal | vauthors = Ling SC, Albuquerque CP, Han JS, Lagier-Tourenne C, Tokunaga S, Zhou H, Cleveland DW | title = ALS-associated mutations in TDP-43 increase its stability and promote TDP-43 complexes with FUS/TLS | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 107 | issue = 30 | pages = 13318-23 | date = July 2010 | pmid = 20624952 | doi = 10.1073/pnas.1008227107 | doi-access = free }}</ref> and [[RNA-binding protein FUS|FUS/TLS]]<ref name="pmid20624952"/>




Revision as of 17:26, 11 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]

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], PRMT1,[9][10] TDP-43,[11] and FUS/TLS[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 (January 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. ^ a b "Entrez Gene: HNRPR heterogeneous nuclear ribonucleoprotein R".
  7. ^ Mourelatos Z, Abel L, Yong J, Kataoka N, Dreyfuss G (October 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 (January 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 (August 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 (September 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.
  11. ^ a b Ling SC, Albuquerque CP, Han JS, Lagier-Tourenne C, Tokunaga S, Zhou H, Cleveland DW (July 2010). "ALS-associated mutations in TDP-43 increase its stability and promote TDP-43 complexes with FUS/TLS". Proceedings of the National Academy of Sciences of the United States of America. 107 (30): 13318–23. doi:10.1073/pnas.1008227107. PMID 20624952.

Further reading

External links


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