HNRPUL1

Heterogeneous nuclear ribonucleoprotein U-like 1

Identifiers

HNRNPUL1; E1B-AP5; E1BAP5; FLJ12944; HNRPUL1

External IDs

OMIM: 605800 MGI: 2443517 HomoloGene: 31419 GeneCards: HNRNPUL1 Gene

Gene Ontology
Molecular function	• RNA binding • protein binding • enzyme binding
Cellular component	• nucleus • nucleoplasm • heterogeneous nuclear ribonucleoprotein complex
Biological process	• nuclear mRNA splicing, via spliceosome • regulation of transcription, DNA-dependent • RNA processing • RNA splicing • response to virus • gene expression
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 19:
41.77 – 41.81 Mb

Chr 7:
26.51 – 26.54 Mb

PubMed search

[1]

[2]

Heterogeneous nuclear ribonucleoprotein U-like protein 1 is a protein that in humans is encoded by the HNRNPUL1 gene.^[1]^[2]^[3]

This gene encodes a nuclear RNA-binding protein of the heterogeneous nuclear ribonucleoprotein (hnRNP) family. This protein binds specifically to adenovirus E1B-55kDa oncoprotein. It may play an important role in nucleocytoplasmic RNA transport, and its function is modulated by E1B-55kDa in adenovirus-infected cells. HNRPUL1 also participates in ATR protein kinase signalling pathways during adenovirus infection. Two transcript variants encoding different isoforms have been found for this gene. Additional variants have also been found, but their full-length natures have not been determined.^[3]

Interactions

HNRPUL1 has been shown to interact with BRD7^[2] and PRMT2.^[4]

References

^ Gabler S, Schutt H, Groitl P, Wolf H, Shenk T, Dobner T (Oct 1998). "E1B 55-kilodalton-associated protein: a cellular protein with RNA-binding activity implicated in nucleocytoplasmic transport of adenovirus and cellular mRNAs". J Virol 72 (10): 7960–71. PMC 110131. PMID 9733834. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=110131.
^ ^a ^b Kzhyshkowska J, Rusch A, Wolf H, Dobner T (Apr 2003). "Regulation of transcription by the heterogeneous nuclear ribonucleoprotein E1B-AP5 is mediated by complex formation with the novel bromodomain-containing protein BRD7". Biochem J 371 (Pt 2): 385–93. doi:10.1042/BJ20021281. PMC 1223277. PMID 12489984. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1223277.
^ ^a ^b "Entrez Gene: HNRPUL1 heterogeneous nuclear ribonucleoprotein U-like 1". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=11100.
^ Kzhyshkowska, J; Schütt H, Liss M, Kremmer E, Stauber R, Wolf H, Dobner T (Sep. 2001). "Heterogeneous nuclear ribonucleoprotein E1B-AP5 is methylated in its Arg-Gly-Gly (RGG) box and interacts with human arginine methyltransferase HRMT1L1". Biochem. J. (England) 358 (Pt 2): 305–14. doi:10.1042/0264-6021:3580305. ISSN 0264-6021. PMC 1222062. PMID 11513728. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1222062.

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Bachi A, Braun IC, Rodrigues JP, et al. (2000). "The C-terminal domain of TAP interacts with the nuclear pore complex and promotes export of specific CTE-bearing RNA substrates.". RNA 6 (1): 136–58. doi:10.1017/S1355838200991994. PMC 1369901. PMID 10668806. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1369901.
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Kzhyshkowska J, Schütt H, Liss M, et al. (2001). "Heterogeneous nuclear ribonucleoprotein E1B-AP5 is methylated in its Arg-Gly-Gly (RGG) box and interacts with human arginine methyltransferase HRMT1L1.". Biochem. J. 358 (Pt 2): 305–14. doi:10.1042/0264-6021:3580305. PMC 1222062. PMID 11513728. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1222062.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241.
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Brill LM, Salomon AR, Ficarro SB, et al. (2004). "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry.". Anal. Chem. 76 (10): 2763–72. doi:10.1021/ac035352d. PMID 15144186.
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Kzhyshkowska J, Kremmer E, Hofmann M, et al. (2005). "Protein arginine methylation during lytic adenovirus infection.". Biochem. J. 383 (Pt 2): 259–65. doi:10.1042/BJ20040210. PMC 1134066. PMID 15242333. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1134066.
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Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=528928.
Barral PM, Rusch A, Turnell AS, et al. (2005). "The interaction of the hnRNP family member E1B-AP5 with p53.". FEBS Lett. 579 (13): 2752–8. doi:10.1016/j.febslet.2005.03.095. PMID 15907477.
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Shiffman D, Rowland CM, Louie JZ, et al. (2006). "Gene variants of VAMP8 and HNRPUL1 are associated with early-onset myocardial infarction.". Arterioscler. Thromb. Vasc. Biol. 26 (7): 1613–8. doi:10.1161/01.ATV.0000226543.77214.e4. PMID 16690874.
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Kollers S, Musilova P, Rubes J, Rocha D (2007). "Comparative mapping reveals multiple rearrangements between pig chromosome 6 and human 19q13.". Anim. Genet. 37 (6): 595–6. doi:10.1111/j.1365-2052.2006.01516.x. PMID 17121608.

HNRPUL1

Interactions

References

Further reading