HNRNPAB

HNRNPAB
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	3S7R
Identifiers
Aliases	HNRNPAB , ABBP1, HNRPAB, heterogeneous nuclear ribonucleoprotein A/B
External IDs	OMIM: 602688 MGI: 1330294 HomoloGene: 74950 GeneCards: HNRNPAB
Gene location (Human)
Chr.	Chromosome 5 (human)
End	178,211,163 bp
Gene location (Mouse)
Chr.	Chromosome 11 (mouse)
End	51,497,674 bp
RNA expression pattern
	Top expressed in
	embryo; ; ganglionic eminence; ; human penis; ; rectum; ; vulva; ; gums; ; thymus; ; nipple; ; epithelium of esophagus; ; cecum;
	Top expressed in
	primitive streak; ; abdominal wall; ; medial ganglionic eminence; ; condyle; ; hair follicle; ; vas deferens; ; renal corpuscle; ; fossa; ; conjunctival fornix; ; medullary collecting duct;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	DNA-binding transcription factor activity ; nucleic acid binding ; sequence-specific DNA binding ; protein binding ; mRNA binding ; RNA binding ; sequence-specific double-stranded DNA binding ;
Cellular component	cytoplasm ; RNA polymerase II transcription regulator complex ; nucleus ; nucleoplasm ; ribonucleoprotein complex ;
Biological process	positive regulation of transcription, DNA-templated ; epithelial to mesenchymal transition ;
	Sources:Amigo / QuickGO
Orthologs
	3182
	15384
	ENSG00000197451
	ENSMUSG00000020358
	Q99729
	Q99020
	NM_031266 ; NM_004499
	NM_001048061 ; NM_010448
	NP_004490 ; NP_112556
	NP_001041526 ; NP_034578
	Wikidata
View/Edit Human	View/Edit Mouse

Last updated April 02, 2024

Heterogeneous nuclear ribonucleoprotein A/B, also known as HNRNPAB, is a protein which in humans is encoded by the HNRNPAB gene.^[5] Although this gene is named HNRNPAB in reference to its first cloning as an RNA binding protein with similarity to HNRNP A and HNRNP B,^[6] it is not a member of the HNRNP A/B subfamily of HNRNPs, but groups together closely with HNRNPD/AUF1 and HNRNPDL.^[7]^[8]

Function

This gene belongs to the subfamily of ubiquitously expressed heterogeneous nuclear ribonucleoproteins (hnRNPs). The hnRNPs are produced by RNA polymerase II and are components of the heterogeneous nuclear RNA (hnRNA) complexes. They 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, which binds to one of the components of the multiprotein editosome complex, has two repeats of quasi-RRM (RNA recognition motif) domains that bind to RNAs. Two alternatively spliced transcript variants encoding different isoforms have been described for this gene.^[5]

Interactions

HNRNPAB has been shown to interact with TP63.^[9]

Related Research Articles

<span class="mw-page-title-main">Heterogeneous ribonucleoprotein particle</span>

Heterogeneous nuclear ribonucleoproteins (hnRNPs) are complexes of RNA and protein present in the cell nucleus during gene transcription and subsequent post-transcriptional modification of the newly synthesized RNA (pre-mRNA). The presence of the proteins bound to a pre-mRNA molecule serves as a signal that the pre-mRNA is not yet fully processed and therefore not ready for export to the cytoplasm. Since most mature RNA is exported from the nucleus relatively quickly, most RNA-binding protein in the nucleus exist as heterogeneous ribonucleoprotein particles. After splicing has occurred, the proteins remain bound to spliced introns and target them for degradation.

Heterogeneous nuclear ribonucleoprotein K is a protein that in humans is encoded by the HNRNPK gene. It is found in the cell nucleus that binds to pre-messenger RNA (mRNA) as a component of heterogeneous ribonucleoprotein particles. The simian homolog is known as protein H16. Both proteins bind to single-stranded DNA as well as to RNA and can stimulate the activity of RNA polymerase II, the protein responsible for most gene transcription. The relative affinities of the proteins for DNA and RNA vary with solution conditions and are inversely correlated, so that conditions promoting strong DNA binding result in weak RNA binding.

Heterogeneous nuclear ribonucleoproteins A2/B1 is a protein that in humans is encoded by the HNRNPA2B1 gene.

snRNP70 also known as U1 small nuclear ribonucleoprotein 70 kDa is a protein that in humans is encoded by the SNRNP70 gene. snRNP70 is a small nuclear ribonucleoprotein that associates with U1 spliceosomal RNA, forming the U1snRNP a core component of the spliceosome. The U1-70K protein and other components of the spliceosome complex form detergent-insoluble aggregates in both sporadic and familial human cases of Alzheimer's disease. U1-70K co-localizes with Tau in neurofibrillary tangles in Alzheimer's disease.

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

Poly(rC)-binding protein 1 is a protein that in humans is encoded by the PCBP1 gene.

Heterogeneous nuclear ribonucleoprotein D0 (HNRNPD) also known as AU-rich element RNA-binding protein 1 (AUF1) is a protein that in humans is encoded by the HNRNPD gene. Alternative splicing of this gene results in four transcript variants.

Heterogeneous nuclear ribonucleoproteins C1/C2 is a protein that in humans is encoded by the HNRNPC gene.

Scaffold attachment factor B, also known as SAFB, is a gene with homologs that have been studied in humans and mice.

Synaptotagmin-binding, cytoplasmic RNA-interacting protein (SYNCRIP), also known as heterogeneous nuclear ribonucleoprotein (hnRNP) Q or NS1-associated protein-1 (NSAP-1), is a protein that in humans is encoded by the SYNCRIP gene. As the name implies, SYNCRIP is localized predominantly in the cytoplasm. It is evolutionarily conserved across eukaryotes and participates in several cellular and disease pathways, especially in neuronal and muscular development. In humans, there are three isoforms, all of which are associated in vitro with pre-mRNAs, mRNA splicing intermediates, and mature mRNA-protein complexes, including mRNA turnover.

Heterogeneous nuclear ribonucleoprotein F is a protein that in humans is encoded by the HNRNPF gene.

Heterogeneous nuclear ribonucleoprotein H is a protein that in humans is encoded by the HNRNPH1 gene.

Heterogeneous nuclear ribonucleoprotein L is a protein that in humans is encoded by the HNRNPL gene.

Heterogeneous nuclear ribonucleoprotein H3 is a protein that in humans is encoded by the HNRNPH3 gene.

Heterogeneous nuclear ribonucleoprotein R is a protein that in humans is encoded by the HNRNPR gene.

Heterogeneous nuclear ribonucleoprotein H2 is a protein that in humans is encoded by the HNRNPH2 gene.

Heterogeneous nuclear ribonucleoprotein A0 is a protein that in humans is encoded by the HNRNPA0 gene.

Heterogeneous nuclear ribonucleoprotein D-like, also known as HNRPDL, is a protein which in humans is encoded by the HNRPDL gene.

Transportin-2 is a protein that in humans is encoded by the TNPO2 gene.

Polypyrimidine tract-binding protein 1 is a protein that in humans is encoded by the PTBP1 gene.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000197451 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000020358 - Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
1 2 "HNRNPAB heterogeneous nuclear ribonucleoprotein A/B [ Homo sapiens (human) ]".
↑ Khan FA, Jaiswal AK, Szer W (September 1991). "Cloning and sequence analysis of a human type A/B hnRNP protein". FEBS Letters. 290 (1–2): 159–61. doi: 10.1016/0014-5793(91)81249-8 . PMID 1717314. S2CID 11348906.
↑ Akindahunsi AA, Bandiera A, Manzini G (February 2005). "Vertebrate 2xRBD hnRNP proteins: a comparative analysis of genome, mRNA and protein sequences". Computational Biology and Chemistry. 29 (1): 13–23. doi:10.1016/j.compbiolchem.2004.11.002. PMID 15680582.
↑ Czaplinski K, Köcher T, Schelder M, Segref A, Wilm M, Mattaj IW (April 2005). "Identification of 40LoVe, a Xenopus hnRNP D family protein involved in localizing a TGF-beta-related mRNA during oogenesis". Developmental Cell. 8 (4): 505–15. doi: 10.1016/j.devcel.2005.01.012 . PMID 15809033.
↑ Fomenkov A, Huang YP, Topaloglu O, Brechman A, Osada M, Fomenkova T, et al. (June 2003). "P63 alpha mutations lead to aberrant splicing of keratinocyte growth factor receptor in the Hay-Wells syndrome". The Journal of Biological Chemistry. 278 (26): 23906–14. doi: 10.1074/jbc.M300746200 . PMID 12692135.

Khan FA, Jaiswal AK, Szer W (September 1991). "Cloning and sequence analysis of a human type A/B hnRNP protein". FEBS Letters. 290 (1–2): 159–61. doi: 10.1016/0014-5793(91)81249-8 . PMID 1717314. S2CID 11348906.
Maruyama K, Sugano S (January 1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
Gress TM, Müller-Pillasch F, Geng M, Zimmerhackl F, Zehetner G, Friess H, et al. (October 1996). "A pancreatic cancer-specific expression profile". Oncogene. 13 (8): 1819–30. PMID 8895530.
Lau PP, Zhu HJ, Nakamuta M, Chan L (January 1997). "Cloning of an Apobec-1-binding protein that also interacts with apolipoprotein B mRNA and evidence for its involvement in RNA editing". The Journal of Biological Chemistry. 272 (3): 1452–5. doi: 10.1074/jbc.272.3.1452 . PMID 8999813.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (October 1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
Hay DC, Kemp GD, Dargemont C, Hay RT (May 2001). "Interaction between hnRNPA1 and IkappaBalpha is required for maximal activation of NF-kappaB-dependent transcription". Molecular and Cellular Biology. 21 (10): 3482–90. doi:10.1128/MCB.21.10.3482-3490.2001. PMC 100270 . PMID 11313474.
Lau PP, Chang BH, Chan L (April 2001). "Two-hybrid cloning identifies an RNA-binding protein, GRY-RBP, as a component of apobec-1 editosome". Biochemical and Biophysical Research Communications. 282 (4): 977–83. doi:10.1006/bbrc.2001.4679. PMID 11352648.
Andersen JS, Lyon CE, Fox AH, Leung AK, Lam YW, Steen H, et al. (January 2002). "Directed proteomic analysis of the human nucleolus". Current Biology. 12 (1): 1–11. Bibcode:2002CBio...12....1A. doi: 10.1016/S0960-9822(01)00650-9 . PMID 11790298. S2CID 14132033.
Percipalle P, Jonsson A, Nashchekin D, Karlsson C, Bergman T, Guialis A, et al. (April 2002). "Nuclear actin is associated with a specific subset of hnRNP A/B-type proteins". Nucleic Acids Research. 30 (8): 1725–34. doi:10.1093/nar/30.8.1725. PMC 113215 . PMID 11937625.
Angenstein F, Evans AM, Settlage RE, Moran ST, Ling SC, Klintsova AY, et al. (October 2002). "A receptor for activated C kinase is part of messenger ribonucleoprotein complexes associated with polyA-mRNAs in neurons". The Journal of Neuroscience. 22 (20): 8827–37. doi: 10.1523/jneurosci.22-20-08827.2002 . PMC 6757688 . PMID 12388589.
Fomenkov A, Huang YP, Topaloglu O, Brechman A, Osada M, Fomenkova T, et al. (June 2003). "P63 alpha mutations lead to aberrant splicing of keratinocyte growth factor receptor in the Hay-Wells syndrome". The Journal of Biological Chemistry. 278 (26): 23906–14. doi: 10.1074/jbc.M300746200 . PMID 12692135.
Zhang S, Schlott B, Görlach M, Grosse F (2004). "DNA-dependent protein kinase (DNA-PK) phosphorylates nuclear DNA helicase II/RNA helicase A and hnRNP proteins in an RNA-dependent manner". Nucleic Acids Research. 32 (1): 1–10. doi:10.1093/nar/gkg933. PMC 373260 . PMID 14704337.
Gao C, Guo H, Wei J, Mi Z, Wai P, Kuo PC (March 2004). "S-nitrosylation of heterogeneous nuclear ribonucleoprotein A/B regulates osteopontin transcription in endotoxin-stimulated murine macrophages". The Journal of Biological Chemistry. 279 (12): 11236–43. doi: 10.1074/jbc.M313385200 . PMID 14722087.
Ong SE, Mittler G, Mann M (November 2004). "Identifying and quantifying in vivo methylation sites by heavy methyl SILAC". Nature Methods. 1 (2): 119–26. doi:10.1038/nmeth715. PMID 15782174. S2CID 6654604.
Beausoleil SA, Villén J, Gerber SA, Rush J, Gygi SP (October 2006). "A probability-based approach for high-throughput protein phosphorylation analysis and site localization". Nature Biotechnology. 24 (10): 1285–92. doi:10.1038/nbt1240. PMID 16964243. S2CID 14294292.
Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S, et al. (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Molecular Systems Biology. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948 . PMID 17353931.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000197451 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000020358 - Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[entrez-5] 1 2 "HNRNPAB heterogeneous nuclear ribonucleoprotein A/B [ Homo sapiens (human) ]".

[pmid1717314-6] Khan FA, Jaiswal AK, Szer W (September 1991). "Cloning and sequence analysis of a human type A/B hnRNP protein". FEBS Letters. 290 (1–2): 159–61. doi: 10.1016/0014-5793(91)81249-8 . PMID 1717314. S2CID 11348906.

[pmid15680582-7] Akindahunsi AA, Bandiera A, Manzini G (February 2005). "Vertebrate 2xRBD hnRNP proteins: a comparative analysis of genome, mRNA and protein sequences". Computational Biology and Chemistry. 29 (1): 13–23. doi:10.1016/j.compbiolchem.2004.11.002. PMID 15680582.

[pmid15809033-8] Czaplinski K, Köcher T, Schelder M, Segref A, Wilm M, Mattaj IW (April 2005). "Identification of 40LoVe, a Xenopus hnRNP D family protein involved in localizing a TGF-beta-related mRNA during oogenesis". Developmental Cell. 8 (4): 505–15. doi: 10.1016/j.devcel.2005.01.012 . PMID 15809033.

[pmid12692135-9] Fomenkov A, Huang YP, Topaloglu O, Brechman A, Osada M, Fomenkova T, et al. (June 2003). "P63 alpha mutations lead to aberrant splicing of keratinocyte growth factor receptor in the Hay-Wells syndrome". The Journal of Biological Chemistry. 278 (26): 23906–14. doi: 10.1074/jbc.M300746200 . PMID 12692135.

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HNRNPAB

Contents

Function

Interactions

Related Research Articles

References

Further reading