This gene belongs to the subfamily of ubiquitously expressed heterogeneous nuclear ribonucleoproteins (hnRNPs). The hnRNPs are RNA binding proteins and they 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.
^Fackelmayer FO, Richter A (Sep 1994). "Purification of two isoforms of hnRNP-U and characterization of their nucleic acid binding activity". Biochemistry33 (34): 10416–22. doi:10.1021/bi00200a024. PMID8068679.
^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. PMID9353307.
^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. PMID11813259.
Barel M, Balbo M, Gauffre A, Frade R (1995). "Binding sites of the Epstein-Barr virus and C3d receptor (CR2, CD21) for its three intracellular ligands, the p53 anti-oncoprotein, the p68 calcium binding protein and the nuclear p120 ribonucleoprotein.". Mol. Immunol.32 (6): 389–97. doi:10.1016/0161-5890(95)00005-Y. PMID7753047.
Jordan P, Heid H, Kinzel V, Kübler D (1995). "Major cell surface-located protein substrates of an ecto-protein kinase are homologs of known nuclear proteins.". Biochemistry33 (49): 14696–706. doi:10.1021/bi00253a007. PMID7993898.
Dennehy KM, Broszeit R, Garnett D, Durrheim GA, Spruyt LL, Beyers AD (1997). "Thymocyte activation induces the association of phosphatidylinositol 3-kinase and pp120 with CD5.". Eur. J. Immunol.27 (3): 679–86. doi:10.1002/eji.1830270316. PMID9079809.
Malik KF, Jaffe H, Brady J, Young WS (1997). "The class III POU factor Brn-4 interacts with other class III POU factors and the heterogeneous nuclear ribonucleoprotein U.". Brain Res. Mol. Brain Res.45 (1): 99–107. doi:10.1016/S0169-328X(96)00238-0. PMID9105675.
Eggert M, Michel J, Schneider S, Bornfleth H, Baniahmad A, Fackelmayer FO, Schmidt S, Renkawitz R (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. PMID9353307.
Matsui M, Breau WC, Iwasaki S, Hagiwara S, Tamai Y, Mori C, Bloom ML, Jerry MB, Eddy EM, Taketo MM (1999). "Retrovirus integration site Mintb encoding the mouse homolog of hnRNP U.". J. Biochem.125 (6): 1104–14. doi:10.1093/oxfordjournals.jbchem.a022392. PMID10348913.
Kipp M, Schwab BL, Przybylski M, Nicotera P, Fackelmayer FO (2000). "Apoptotic cleavage of scaffold attachment factor A (SAF-A) by caspase-3 occurs at a noncanonical cleavage site.". J. Biol. Chem.275 (7): 5031–6. doi:10.1074/jbc.275.7.5031. PMID10671544.
Husi H, Ward MA, Choudhary JS, Blackstock WP, Grant SG (2000). "Proteomic analysis of NMDA receptor-adhesion protein signaling complexes.". Nat. Neurosci.3 (7): 661–9. doi:10.1038/76615. PMID10862698.
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. PMID11813259.