HNRPU

From Wikipedia, the free encyclopedia

Heterogeneous nuclear ribonucleoprotein U (scaffold attachment factor A)

Identifiers

HNRPU; HNRNPU; SAF-A; U21.1

External IDs

OMIM: 602869 MGI: 1858195 HomoloGene: 22991

Gene ontology
Molecular Function:	• nucleotide binding • DNA binding • RNA binding • ATP binding
Cellular Component:	• nucleus • spliceosome • ribonucleoprotein complex • heterogeneous nuclear ribonucleoprotein complex
Biological Process:	• mRNA processing • RNA splicing

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

n/a

Refseq

NM_004501 (mRNA)
NP_004492 (protein)

XM_975248 (mRNA)
XP_980342 (protein)

Location

Chr 1: 243.08 - 243.09 Mb

Chr 1: 180.17 - 180.17 Mb

Pubmed search

[1]

[2]

Heterogeneous nuclear ribonucleoprotein U (scaffold attachment factor A), also known as HNRPU, is a human gene.

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.^[1]

[edit] References

^ Entrez Gene: HNRPU heterogeneous nuclear ribonucleoprotein U (scaffold attachment factor A).

[edit] Further reading

Kiledjian M, Dreyfuss G (1992). "Primary structure and binding activity of the hnRNP U protein: binding RNA through RGG box.". EMBO J. 11 (7): 2655–64. PMID 1628625.
Fackelmayer FO, Richter A (1994). "hnRNP-U/SAF-A is encoded by two differentially polyadenylated mRNAs in human cells.". Biochim. Biophys. Acta 1217 (2): 232–4. PMID 7509195.
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. PMID 7753047.
Sidorenko SP, Law CL, Chandran KA, Clark EA (1995). "Human spleen tyrosine kinase p72Syk associates with the Src-family kinase p53/56Lyn and a 120-kDa phosphoprotein.". Proc. Natl. Acad. Sci. U.S.A. 92 (2): 359–63. PMID 7831290.
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.". Biochemistry 33 (49): 14696–706. PMID 7993898.
Fackelmayer FO, Richter A (1994). "Purification of two isoforms of hnRNP-U and characterization of their nucleic acid binding activity.". Biochemistry 33 (34): 10416–22. PMID 8068679.
Liu Q, Dreyfuss G (1996). "A novel nuclear structure containing the survival of motor neurons protein.". EMBO J. 15 (14): 3555–65. PMID 8670859.
Fujioka Y, Matozaki T, Noguchi T, et al. (1997). "A novel membrane glycoprotein, SHPS-1, that binds the SH2-domain-containing protein tyrosine phosphatase SHP-2 in response to mitogens and cell adhesion.". Mol. Cell. Biol. 16 (12): 6887–99. PMID 8943344.
Dennehy KM, Broszeit R, Garnett D, et al. (1997). "Thymocyte activation induces the association of phosphatidylinositol 3-kinase and pp120 with CD5.". Eur. J. Immunol. 27 (3): 679–86. PMID 9079809.
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. PMID 9105675.
Eggert M, Michel J, Schneider S, et al. (1997). "The glucocorticoid receptor is associated with the RNA-binding nuclear matrix protein hnRNP U.". J. Biol. Chem. 272 (45): 28471–8. PMID 9353307.
Göhring F, Schwab BL, Nicotera P, et al. (1998). "The novel SAR-binding domain of scaffold attachment factor A (SAF-A) is a target in apoptotic nuclear breakdown.". EMBO J. 16 (24): 7361–71. doi:10.1093/emboj/16.24.7361. PMID 9405365.
Hahm B, Cho OH, Kim JE, et al. (1998). "Polypyrimidine tract-binding protein interacts with HnRNP L.". FEBS Lett. 425 (3): 401–6. PMID 9563502.
Matsui M, Breau WC, Iwasaki S, et al. (1999). "Retrovirus integration site Mintb encoding the mouse homolog of hnRNP U.". J. Biochem. 125 (6): 1104–14. PMID 10348913.
Kim MK, Nikodem VM (2000). "hnRNP U inhibits carboxy-terminal domain phosphorylation by TFIIH and represses RNA polymerase II elongation.". Mol. Cell. Biol. 19 (10): 6833–44. PMID 10490622.
Kipp M, Schwab BL, Przybylski M, et al. (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. PMID 10671544.
Husi H, Ward MA, Choudhary JS, et al. (2000). "Proteomic analysis of NMDA receptor-adhesion protein signaling complexes.". Nat. Neurosci. 3 (7): 661–9. doi:10.1038/76615. PMID 10862698.
Taniura H, Yoshikawa K (2002). "Necdin interacts with the ribonucleoprotein hnRNP U in the nuclear matrix.". J. Cell. Biochem. 84 (3): 545–55. PMID 11813259.
Lee J, Bedford MT (2002). "PABP1 identified as an arginine methyltransferase substrate using high-density protein arrays.". EMBO Rep. 3 (3): 268–73. doi:10.1093/embo-reports/kvf052. PMID 11850402.
Davis M, Hatzubai A, Andersen JS, et al. (2002). "Pseudosubstrate regulation of the SCF(beta-TrCP) ubiquitin ligase by hnRNP-U.". Genes Dev. 16 (4): 439–51. doi:10.1101/gad.218702. PMID 11850407.