HNRPAB: Difference between revisions

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*{{cite journal  |vauthors=Percipalle P, Jonsson A, Nashchekin D, etal |title=Nuclear actin is associated with a specific subset of hnRNP A/B-type proteins. |journal=Nucleic Acids Res. |volume=30 |issue= 8 |pages= 1725–34 |year= 2002 |pmid= 11937625 |doi=10.1093/nar/30.8.1725  | pmc=113215  }}
*{{cite journal  |vauthors=Percipalle P, Jonsson A, Nashchekin D, etal |title=Nuclear actin is associated with a specific subset of hnRNP A/B-type proteins. |journal=Nucleic Acids Res. |volume=30 |issue= 8 |pages= 1725–34 |year= 2002 |pmid= 11937625 |doi=10.1093/nar/30.8.1725  | pmc=113215  }}
*{{cite journal  |vauthors=Angenstein F, Evans AM, Settlage RE, etal |title=A receptor for activated C kinase is part of messenger ribonucleoprotein complexes associated with polyA-mRNAs in neurons. |journal=J. Neurosci. |volume=22 |issue= 20 |pages= 8827–37 |year= 2002 |pmid= 12388589 |doi=  }}
*{{cite journal  |vauthors=Angenstein F, Evans AM, Settlage RE, etal |title=A receptor for activated C kinase is part of messenger ribonucleoprotein complexes associated with polyA-mRNAs in neurons. |journal=J. Neurosci. |volume=22 |issue= 20 |pages= 8827–37 |year= 2002 |pmid= 12388589 |doi=  }}
*{{cite journal  |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899  | pmc=139241 }}
*{{cite journal  |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899  | pmc=139241 |bibcode=2002PNAS...9916899M }}
*{{cite journal  |vauthors=Fomenkov A, Huang YP, Topaloglu O, etal |title=P63 alpha mutations lead to aberrant splicing of keratinocyte growth factor receptor in the Hay-Wells syndrome. |journal=J. Biol. Chem. |volume=278 |issue= 26 |pages= 23906–14 |year= 2003 |pmid= 12692135 |doi= 10.1074/jbc.M300746200 }}
*{{cite journal  |vauthors=Fomenkov A, Huang YP, Topaloglu O, etal |title=P63 alpha mutations lead to aberrant splicing of keratinocyte growth factor receptor in the Hay-Wells syndrome. |journal=J. Biol. Chem. |volume=278 |issue= 26 |pages= 23906–14 |year= 2003 |pmid= 12692135 |doi= 10.1074/jbc.M300746200 }}
*{{cite journal  |vauthors=Ota T, Suzuki Y, Nishikawa T, etal |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
*{{cite journal  |vauthors=Ota T, Suzuki Y, Nishikawa T, etal |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
*{{cite journal  |vauthors=Zhang S, Schlott B, Görlach M, Grosse F |title=DNA-dependent protein kinase (DNA-PK) phosphorylates nuclear DNA helicase II/RNA helicase A and hnRNP proteins in an RNA-dependent manner. |journal=Nucleic Acids Res. |volume=32 |issue= 1 |pages= 1–10 |year= 2004 |pmid= 14704337 |doi= 10.1093/nar/gkg933  | pmc=373260 }}
*{{cite journal  |vauthors=Zhang S, Schlott B, Görlach M, Grosse F |title=DNA-dependent protein kinase (DNA-PK) phosphorylates nuclear DNA helicase II/RNA helicase A and hnRNP proteins in an RNA-dependent manner. |journal=Nucleic Acids Res. |volume=32 |issue= 1 |pages= 1–10 |year= 2004 |pmid= 14704337 |doi= 10.1093/nar/gkg933  | pmc=373260 }}
*{{cite journal  |vauthors=Gao C, Guo H, Wei J, etal |title=S-nitrosylation of heterogeneous nuclear ribonucleoprotein A/B regulates osteopontin transcription in endotoxin-stimulated murine macrophages. |journal=J. Biol. Chem. |volume=279 |issue= 12 |pages= 11236–43 |year= 2004 |pmid= 14722087 |doi= 10.1074/jbc.M313385200 }}
*{{cite journal  |vauthors=Gao C, Guo H, Wei J, etal |title=S-nitrosylation of heterogeneous nuclear ribonucleoprotein A/B regulates osteopontin transcription in endotoxin-stimulated murine macrophages. |journal=J. Biol. Chem. |volume=279 |issue= 12 |pages= 11236–43 |year= 2004 |pmid= 14722087 |doi= 10.1074/jbc.M313385200 |pmc=5336185 }}
*{{cite journal  |vauthors=Gerhard DS, Wagner L, Feingold EA, etal |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504  | pmc=528928 }}
*{{cite journal  |vauthors=Gerhard DS, Wagner L, Feingold EA, etal |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504  | pmc=528928 }}
*{{cite journal  |vauthors=Ong SE, Mittler G, Mann M |title=Identifying and quantifying in vivo methylation sites by heavy methyl SILAC. |journal=Nat. Methods |volume=1 |issue= 2 |pages= 119–26 |year= 2005 |pmid= 15782174 |doi= 10.1038/nmeth715 }}
*{{cite journal  |vauthors=Ong SE, Mittler G, Mann M |title=Identifying and quantifying in vivo methylation sites by heavy methyl SILAC. |journal=Nat. Methods |volume=1 |issue= 2 |pages= 119–26 |year= 2005 |pmid= 15782174 |doi= 10.1038/nmeth715 }}

Latest revision as of 21:00, 23 June 2018

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

n/a

n/a

Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Heterogeneous nuclear ribonucleoprotein A/B, also known as HNRPAB, is a protein which in humans is encoded by the HNRPAB gene.[1] Although this gene is named HNRNPAB in reference to its first cloning as an RNA binding protein with similarity to HNRNP A and HNRNP B,[2] it is not a member of the HNRNP A/B subfamily of HNRNPs, but groups together closely with HNRNPD/AUF1 and HNRNPDL.[3][4]

Function

This gene belongs to the subfamily of ubiquitously expressed heterogeneous nuclear ribonucleoproteins (hnRNPs). The hnRNPs are produced by RNA polymerase II and are components of the heterogeneous nuclear RNA (hnRNA) complexes. They 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, which binds to one of the components of the multiprotein editosome complex, has two repeats of quasi-RRM (RNA recognition motif) domains that bind to RNAs. Two alternatively spliced transcript variants encoding different isoforms have been described for this gene.[1]

Interactions

HNRPAB has been shown to interact with TP63.[5]

References

  1. 1.0 1.1 "Entrez Gene: HNRPAB heterogeneous nuclear ribonucleoprotein A/B".
  2. Khan FA, Jaiswal AK, Szer W (September 1991). "Cloning and sequence analysis of a human type A/B hnRNP protein". FEBS Lett. 290 (1–2): 159–61. doi:10.1016/0014-5793(91)81249-8. PMID 1717314.
  3. Akindahunsi AA, Bandiera A, Manzini G (February 2005). "Vertebrate 2xRBD hnRNP proteins: a comparative analysis of genome, mRNA and protein sequences". Comput Biol Chem. 29 (1): 13–23. doi:10.1016/j.compbiolchem.2004.11.002. PMID 15680582.
  4. Czaplinski K, Köcher T, Schelder M, Segref A, Wilm M, Mattaj IW (April 2005). "Identification of 40LoVe, a Xenopus hnRNP D family protein involved in localizing a TGF-beta-related mRNA during oogenesis". Dev. Cell. 8 (4): 505–15. doi:10.1016/j.devcel.2005.01.012. PMID 15809033.
  5. Fomenkov, Alexey; Huang Yi-Ping; Topaloglu Ozlem; Brechman Anna; Osada Motonobo; Fomenkova Tanya; Yuriditsky Eugene; Trink Barry; Sidransky David; Ratovitski Edward (Jun 2003). "P63 alpha mutations lead to aberrant splicing of keratinocyte growth factor receptor in the Hay-Wells syndrome". J. Biol. Chem. United States. 278 (26): 23906–14. doi:10.1074/jbc.M300746200. ISSN 0021-9258. PMID 12692135.

Further reading