HNRPU

Heterogeneous nuclear ribonucleoprotein U is a protein that in humans is encoded by the HNRNPU gene.[4][5]

HNRNPU
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1ZRJ
Identifiers
Aliases	HNRNPU, HNRPU, SAF-A, U21.1, hnRNP U, SAFA, HNRNPU-AS1, heterogeneous nuclear ribonucleoprotein U (scaffold attachment factor A), heterogeneous nuclear ribonucleoprotein U, HNRNPU antisense RNA 1, C1orf199, NCRNA00201, EIEE54, pp120, GRIP120
External IDs	OMIM: 602869 MGI: 1858195 HomoloGene: 22991 GeneCards: HNRNPU
Gene location (Human) Chr. Chromosome 1 (human)[1] Band 1q44 Start 244,840,638 bp[1] End 244,864,560 bp[1]
RNA expression pattern More reference expression data
Gene ontology Molecular function • nucleotide binding • GO:0001948 protein binding • telomerase RNA binding • RNA binding • RNA polymerase II core binding • TFIIH-class transcription factor binding • DNA binding • chromatin binding • double-stranded DNA binding • single-stranded DNA binding • GO:0001106 transcription corepressor activity • double-stranded RNA binding • single-stranded RNA binding • mRNA 3'-UTR binding • actin binding • poly(A) binding • snRNA binding • poly(C) RNA binding • chromatin DNA binding • poly(G) binding • pre-mRNA binding • ribonucleoprotein complex binding • GO:0032403 macromolecular complex binding • sequence-specific double-stranded DNA binding • ATP binding • identical protein binding • sequence-specific DNA binding • RNA polymerase II C-terminal domain binding • promoter-specific chromatin binding • GO:0000980 RNA polymerase II cis-regulatory region sequence-specific DNA binding Cellular component • CRD-mediated mRNA stability complex • cytoplasm • catalytic step 2 spliceosome • membrane • nucleoplasm • telomerase holoenzyme complex • cytoplasmic ribonucleoprotein granule • spliceosomal complex • cell nucleus • extracellular matrix • nuclear chromosome • cell surface • nuclear matrix • nuclear speck • macromolecular complex • RNA polymerase II transcription factor complex • inactive sex chromosome • ribonucleoprotein • kinetochore • centrosome • midbody • mitotic spindle • mitotic spindle midzone • mitotic spindle microtubule • chromosome, centromeric region • condensed chromosome kinetochore • spindle pole • chromosome • microtubule organizing center • spindle • cytoskeleton • dendrite cytoplasm Biological process • CRD-mediated mRNA stabilization • mRNA splicing, via spliceosome • RNA processing • negative regulation of telomere maintenance via telomerase • rhythmic process • mRNA processing • osteoblast differentiation • RNA splicing • RNA metabolic process • positive regulation of gene expression • circadian regulation of gene expression • cardiac muscle cell development • cellular response to dexamethasone stimulus • negative regulation of transcription from RNA polymerase II promoter • regulation of alternative mRNA splicing, via spliceosome • dosage compensation by inactivation of X chromosome • negative regulation of kinase activity • negative regulation of transcription elongation from RNA polymerase II promoter • mRNA stabilization • maintenance of protein location in nucleus • cellular response to glucocorticoid stimulus • RNA localization to chromatin • positive regulation of DNA topoisomerase (ATP-hydrolyzing) activity • positive regulation of stem cell proliferation • regulation of mitotic cell cycle • positive regulation of transcription from RNA polymerase II promoter • regulation of mitotic spindle assembly • GO:1903308 regulation of chromatin organization • positive regulation of attachment of mitotic spindle microtubules to kinetochore • protein localization to spindle microtubule • cellular response to leukemia inhibitory factor • negative regulation of stem cell differentiation • chromatin organization • cell cycle • multicellular organism development • cell differentiation • cell division • positive regulation of brown fat cell differentiation • dendritic transport of messenger ribonucleoprotein complex • adaptive thermogenesis Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	3192	51810
Ensembl	ENSG00000153187	ENSMUSG00000039630
UniProt	Q00839 Q5RI18	Q8VEK3
RefSeq (mRNA)	NM_004501 NM_031844	NM_016805
RefSeq (protein)	NP_004492 NP_114032	NP_058085
Location (UCSC)	Chr 1: 244.84 – 244.86 Mb	n/a
PubMed search	[2]	[3]
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 that 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.[6]

Interactions

HNRPU has been shown to interact with:

• EP300,[7]
• GTF2F1,[8]
• Glucocorticoid receptor,[9] and
• NDN.[10]

References

1. GRCh38: Ensembl release 89: ENSG00000153187 - Ensembl, May 2017
2. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
3. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. Fackelmayer FO, Richter A (Mar 1994). "hnRNP-U/SAF-A is encoded by two differentially polyadenylated mRNAs in human cells". Biochim Biophys Acta. 1217 (2): 232–4. doi:10.1016/0167-4781(94)90044-2. PMID 7509195.
5. Fackelmayer FO, Richter A (Sep 1994). "Purification of two isoforms of hnRNP-U and characterization of their nucleic acid binding activity". Biochemistry. 33 (34): 10416–22. doi:10.1021/bi00200a024. PMID 8068679.
6. "Entrez Gene: HNRNPU heterogeneous nuclear ribonucleoprotein U (scaffold attachment factor A)".
7. Martens JH, Verlaan M, Kalkhoven E, Dorsman JC, Zantema A (Apr 2002). "Scaffold/matrix attachment region elements interact with a p300-scaffold attachment factor A complex and are bound by acetylated nucleosomes". Mol. Cell. Biol. 22 (8): 2598–606. doi:10.1128/mcb.22.8.2598-2606.2002. PMC 133732. PMID 11909954.
8. Kim MK, Nikodem VM (Oct 1999). "hnRNP U inhibits carboxy-terminal domain phosphorylation by TFIIH and represses RNA polymerase II elongation". Mol. Cell. Biol. 19 (10): 6833–44. doi:10.1128/MCB.19.10.6833. PMC 84680. PMID 10490622.
9. 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. PMID 9353307.
10. 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. PMID 11813259.

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. doi:10.1002/j.1460-2075.1992.tb05331.x. PMC 556741. PMID 1628625.
• 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. 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. doi:10.1073/pnas.92.2.359. PMC 42739. 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. doi:10.1021/bi00253a007. PMID 7993898.
• Liu Q, Dreyfuss G (1996). "A novel nuclear structure containing the survival of motor neurons protein". EMBO J. 15 (14): 3555–65. doi:10.1002/j.1460-2075.1996.tb00725.x. PMC 451956. PMID 8670859.
• Fujioka Y, Matozaki T, Noguchi T, Iwamatsu A, Yamao T, Takahashi N, Tsuda M, Takada T, Kasuga M (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. doi:10.1128/MCB.16.12.6887. PMC 231692. PMID 8943344.
• 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. 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. doi:10.1016/S0169-328X(96)00238-0. PMID 9105675.
• 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. PMID 9353307.
• Göhring F, Schwab BL, Nicotera P, Leist M, Fackelmayer FO (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. PMC 1170336. PMID 9405365.
• Hahm B, Cho OH, Kim JE, Kim YK, Kim JH, Oh YL, Jang SK (1998). "Polypyrimidine tract-binding protein interacts with HnRNP L.". FEBS Lett. 425 (3): 401–6. doi:10.1016/S0014-5793(98)00269-5. PMID 9563502.
• 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. 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. doi:10.1128/MCB.19.10.6833. PMC 84680. PMID 10490622.
• 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. PMID 10671544.
• 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. hdl:1842/742. 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. doi:10.1002/jcb.10047. 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. PMC 1084016. PMID 11850402.
• Davis M, Hatzubai A, Andersen JS, Ben-Shushan E, Fisher GZ, Yaron A, Bauskin A, Mercurio F, Mann M, Ben-Neriah Y (2002). "Pseudosubstrate regulation of the SCF(beta-TrCP) ubiquitin ligase by hnRNP-U". Genes Dev. 16 (4): 439–51. doi:10.1101/gad.218702. PMC 155337. PMID 11850407.