Heterogeneous nuclear ribonucleoprotein A1

PDB rendering based on 1ha1.

Available structures
PDB	1HA1, 1L3K, 1PGZ, 1PO6, 1U1K, 1U1L, 1U1M, 1U1N, 1U1O, 1U1P, 1U1Q, 1U1R, 1UP1, 2H4M, 2UP1

Identifiers

Symbols

HNRNPA1; HNRPA1; HNRPA1L3; MGC102835; hnRNP A1; hnRNP-A1

External IDs

OMIM: 164017 MGI: 104820 HomoloGene: 88614 GeneCards: HNRNPA1 Gene

Gene Ontology
Molecular function	• nucleotide binding • single-stranded DNA binding • RNA binding • single-stranded RNA binding • protein binding
Cellular component	• nucleus • nucleoplasm • nucleoplasm • spliceosomal complex • nucleolus • cytoplasm • ribonucleoprotein complex • heterogeneous nuclear ribonucleoprotein complex • catalytic step 2 spliceosome
Biological process	• nuclear mRNA splicing, via spliceosome • nuclear mRNA splicing, via spliceosome • mRNA processing • RNA export from nucleus • transport • RNA splicing • gene expression • interspecies interaction between organisms • mRNA transport • nuclear export • nuclear import

Orthologs

Species

Human

Mouse

n/a

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 12:
54.67 – 54.68 Mb

Chr 15:
103.07 – 103.07 Mb

PubMed search

[1]

[2]

Heterogeneous nuclear ribonucleoprotein A1 is a protein that in humans is encoded by the HNRNPA1 gene.^[1]

This gene belongs to the A/B subfamily of ubiquitously expressed heterogeneous nuclear ribonucleoproteins (hnRNPs). The hnRNPs are RNA binding proteins and they complex 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 has two repeats of quasi-RRM domains that bind to RNAs. It is one of the most abundant core proteins of hnRNP complexes and it is localized to the nucleoplasm. This protein, along with other hnRNP proteins, is exported from the nucleus, probably bound to mRNA, and is immediately re-imported. Its M9 domain acts as both a nuclear localization and nuclear export signal. The encoded protein is involved in the packaging of pre-mRNA into hnRNP particles, transport of poly A+ mRNA from the nucleus to the cytoplasm, and may modulate splice site selection. Multiple alternatively spliced transcript variants have been found for this gene but only two transcripts are fully described. These variants have multiple alternative transcription initiation sites and multiple polyA sites.^[2]

1 Interactions
2 Role during childbirth
3 References
4 Further reading

Interactions

Heterogeneous nuclear ribonucleoprotein A1 has been shown to interact with BAT2,^[3] Flap structure-specific endonuclease 1^[4] and IκBα.^[5]

Role during childbirth

hnRNP A1 is thought to have a primary role in the formation of specific myometrial protein species during childbirth (parurition).

References

^ Saccone S, Biamonti G, Maugeri S, Bassi MT, Bunone G, Riva S, Della Valle G (Mar 1992). "Assignment of the human heterogeneous nuclear ribonucleoprotein A1 gene (HNRPA1) to chromosome 12q13.1 by cDNA competitive in situ hybridization". Genomics 12 (1): 171–4. doi:10.1016/0888-7543(92)90424-Q. PMID 1733858.
^ "Entrez Gene: HNRPA1 heterogeneous nuclear ribonucleoprotein A1". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3178.
^ Lehner, Ben; Semple Jennifer I, Brown Stephanie E, Counsell Damian, Campbell R Duncan, Sanderson Christopher M (Jan. 2004). "Analysis of a high-throughput yeast two-hybrid system and its use to predict the function of intracellular proteins encoded within the human MHC class III region". Genomics (United States) 83 (1): 153–67. doi:10.1016/S0888-7543(03)00235-0. ISSN 0888-7543. PMID 14667819.
^ Chai, Qing; Zheng Li, Zhou Mian, Turchi John J, Shen Binghui (Dec. 2003). "Interaction and stimulation of human FEN-1 nuclease activities by heterogeneous nuclear ribonucleoprotein A1 in alpha-segment processing during Okazaki fragment maturation". Biochemistry (United States) 42 (51): 15045–52. doi:10.1021/bi035364t. ISSN 0006-2960. PMID 14690413.
^ Hay, D C; Kemp G D, Dargemont C, Hay R T (May. 2001). "Interaction between hnRNPA1 and IkappaBalpha is required for maximal activation of NF-kappaB-dependent transcription". Mol. Cell. Biol. (United States) 21 (10): 3482–90. doi:10.1128/MCB.21.10.3482-3490.2001. ISSN 0270-7306. PMC 100270. PMID 11313474. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=100270.

Kim S, Park GH, Paik WK (1999). "Recent advances in protein methylation: enzymatic methylation of nucleic acid binding proteins.". Amino Acids 15 (4): 291–306. doi:10.1007/BF01320895. PMID 9891755.
Buvoli M, Cobianchi F, Bestagno MG, et al. (1990). "Alternative splicing in the human gene for the core protein A1 generates another hnRNP protein.". EMBO J. 9 (4): 1229–35. PMC 551799. PMID 1691095. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=551799.
Ghetti A, Bolognesi M, Cobianchi F, Morandi C (1991). "Modeling by homology of RNA binding domain in A1 hnRNP protein.". FEBS Lett. 277 (1-2): 272–6. doi:10.1016/0014-5793(90)80863-E. PMID 2176620.
Biamonti G, Buvoli M, Bassi MT, et al. (1989). "Isolation of an active gene encoding human hnRNP protein A1. Evidence for alternative splicing.". J. Mol. Biol. 207 (3): 491–503. doi:10.1016/0022-2836(89)90459-2. PMID 2760922.
Buvoli M, Biamonti G, Tsoulfas P, et al. (1988). "cDNA cloning of human hnRNP protein A1 reveals the existence of multiple mRNA isoforms.". Nucleic Acids Res. 16 (9): 3751–70. doi:10.1093/nar/16.9.3751. PMC 336554. PMID 2836799. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=336554.
Riva S, Morandi C, Tsoulfas P, et al. (1986). "Mammalian single-stranded DNA binding protein UP I is derived from the hnRNP core protein A1.". EMBO J. 5 (9): 2267–73. PMC 1167110. PMID 3023065. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1167110.
Epplen C, Epplen JT (1994). "Expression of (cac)n/(gtg)n simple repetitive sequences in mRNA of human lymphocytes.". Hum. Genet. 93 (1): 35–41. doi:10.1007/BF00218910. PMID 7505766.
Siomi H, Dreyfuss G (1995). "A nuclear localization domain in the hnRNP A1 protein.". J. Cell Biol. 129 (3): 551–60. doi:10.1083/jcb.129.3.551. PMC 2120450. PMID 7730395. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2120450.
Weighardt F, Biamonti G, Riva S (1995). "Nucleo-cytoplasmic distribution of human hnRNP proteins: a search for the targeting domains in hnRNP A1.". J. Cell. Sci. 108 ( Pt 2): 545–55. PMID 7769000.
Rajpurohit R, Lee SO, Park JO, et al. (1994). "Enzymatic methylation of recombinant heterogeneous nuclear RNP protein A1. Dual substrate specificity for S-adenosylmethionine:histone-arginine N-methyltransferase.". J. Biol. Chem. 269 (2): 1075–82. PMID 8288564.
Hamilton BJ, Nagy E, Malter JS, et al. (1993). "Association of heterogeneous nuclear ribonucleoprotein A1 and C proteins with reiterated AUUUA sequences.". J. Biol. Chem. 268 (12): 8881–7. PMID 8473331.
Michael WM, Choi M, Dreyfuss G (1996). "A nuclear export signal in hnRNP A1: a signal-mediated, temperature-dependent nuclear protein export pathway.". Cell 83 (3): 415–22. doi:10.1016/0092-8674(95)90119-1. PMID 8521471.
Black AC, Luo J, Chun S, et al. (1997). "Specific binding of polypyrimidine tract binding protein and hnRNP A1 to HIV-1 CRS elements.". Virus Genes 12 (3): 275–85. PMID 8883365.
Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery.". Genome Res. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
Xu RM, Jokhan L, Cheng X, et al. (1997). "Crystal structure of human UP1, the domain of hnRNP A1 that contains two RNA-recognition motifs.". Structure 5 (4): 559–70. doi:10.1016/S0969-2126(97)00211-6. PMID 9115444.
Bonifaci N, Moroianu J, Radu A, Blobel G (1997). "Karyopherin beta2 mediates nuclear import of an mRNA binding protein.". Proc. Natl. Acad. Sci. U.S.A. 94 (10): 5055–60. doi:10.1073/pnas.94.10.5055. PMC 24630. PMID 9144189. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=24630.
Shamoo Y, Krueger U, Rice LM, et al. (1997). "Crystal structure of the two RNA binding domains of human hnRNP A1 at 1.75 A resolution.". Nat. Struct. Biol. 4 (3): 215–22. doi:10.1038/nsb0397-215. PMID 9164463.
Neubauer G, King A, Rappsilber J, et al. (1998). "Mass spectrometry and EST-database searching allows characterization of the multi-protein spliceosome complex.". Nat. Genet. 20 (1): 46–50. doi:10.1038/1700. PMID 9731529.

PDB gallery

1ha1: HNRNP A1 (RBD1,2) FROM HOMO SAPIENS

1l3k: UP1, THE TWO RNA-RECOGNITION MOTIF DOMAIN OF HNRNP A1

1pgz: Crystal Structure of UP1 Complexed With d(TTAGGGTTAG(6-MI)G); A Human Telomeric Repeat Containing 6-methyl-8-(2-deoxy-beta-ribofuranosyl)isoxanthopteridine (6-MI)

1po6: Crystal Structure of UP1 Complexed With d(TAGG(6MI)TTAGGG): A Human Telomeric Repeat Containing 6-methyl-8-(2-deoxy-beta-ribofuranosyl)isoxanthopteridine (6MI)

1u1k: Crystal Structure of UP1 Complexed With d(TTAGGGTT 7DA GGG); A Human Telomeric Repeat Containing 7-deaza-adenine

1u1l: Crystal Structure of UP1 Complexed With d(TTAGGGTT PRN GGG); A Human Telomeric Repeat Containing nebularine

1u1m: Crystal Structure of UP1 Complexed With d(TTAGGGTTA 7GU GG); A Human Telomeric Repeat Containing 7-deaza-guanine

1u1n: Crystal Structure of UP1 Complexed With d(TTAGGGTTA (PRN)GG); A Human Telomeric Repeat Containing Nebularine

1u1o: Crystal Structure of UP1 Complexed With d(TTAGGGTTAG(DI)G); A Human Telomeric Repeat Containing Inosine

1u1p: Crystal Structure of UP1 Complexed With d(TTAGGGTTA 2PR GG); A Human Telomeric Repeat Containing 2-aminopurine

1u1q: Crystal Structure of UP1 Complexed With d(TTAGGGTTA(DI)GG); A Human Telomeric Repeat Containing Inosine

1u1r: Crystal Structure of UP1 Complexed With d(TTAGGGTTAG(2PR)G); A Human Telomeric Repeat Containing 2-aminopurine

1up1: UP1, THE TWO RNA-RECOGNITION MOTIF DOMAIN OF HNRNP A1

2h4m: Karyopherin Beta2/Transportin-M9NLS

2up1: STRUCTURE OF UP1-TELOMERIC DNA COMPLEX

Heterogeneous nuclear ribonucleoprotein A1

Contents

Interactions

Role during childbirth

References

Further reading