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ANP32A (acidic (leucine-rich) nuclear phosphoprotein 32 family, member A)

Identity

Other namesC15orf1
HPPCn
I1PP2A
LANP
MAPM
PHAP1
PHAPI
PP32
HGNC (Hugo) ANP32A
LocusID (NCBI) 8125
Location 15q23
Location_base_pair Starts at 69070875 and ends at 69113261 bp from pter ( according to hg19-Feb_2009)  [Mapping]
Local_order The gene is 73682 bases long and oriented on the minus strand.

DNA/RNA

 
Description One of 1265 total genes on chromosome 15 according to NCBI Mapviewer. According to Ensembl, a predicted 76 base pair non-coding RNA (ncRNA) for MIR4312-201 is present within the gene sequence on the reverse strand at chromosome 15: 69094189-69094264.
Pseudogene There are multiple genomic regions that have a high degree of similarity with the ANP32A sequence (including anti-sense regions that are most likely abundantly expressed, our data not shown).

Protein

Note N-terminal contains nuclear localizing signals in amphipathic alpha helix with exceptionally acidic c-terminus with aspartic and glutamic acid residues making up about 70% of the domain (Chen et al., 1996). Important features contributing to protein function include the secondary structure of N-terminal leucine-rich repeat domains (Huyton and Wolberger, 2007). Protein is approximately 90% identical to family members pp32r1 and pp32r2, though function is dramatically different and ANP32A tumor suppressor function is dependent upon the region between amino acids 150-174 (Brody et al., 1999). Function is, in part, dependent on phosphorylation status. Casein kinase II has been identified as a mediator of ANP32A phosphorylation in vivo, specifically at serines 158 and 204 (Hong et al., 2004).
Description ANP32A is a 249 amino acid protein (32 kDa) (Li et al., 1996) and represents the first member identified in a family of evolutionarily-conserved phosphoproteins that are involved in an array of gene regulatory and diverse network regulatory functions primarily through protein-protein interactions such as binding to phosphorylated retinoblastoma (Rb) gene product (Adegbola and Pasternack, 2005).
Expression Ubiquitously expressed in human tissues.
Localisation ANP32A is primarily nuclear (Matsuoka et al., 1994; Matilla et al., 1997; Kovacech et al., 2007; Khan et al., 2011) with variable cytoplasmic localization. It participates in nuclear-to-cytoplasmic shuttling as a multi-protein complex with its binding partners (Williams et al., 2010; Santa-Coloma, 2003; Higashino et al., 2005; Mazroui et al., 2008; Pan et al., 2009; Fukumoto et al., 2011). This cytoplasmic translocation is dependent upon the nuclear export factor chromosomal region maintenance protein 1, or CRM1 (Brennan et al., 2000). Of particular importance is the capacity of ANP32A to translocate from the nucleus to the cytoplasm upon cellular stress to disrupt the pro-tumorigenic function of associated protein HuR (Hostetter et al., 2008; Williams et al., 2010). In some cases, ANP32A mediated disruption of HuR function can precipitate caspase-mediated cleavage of HuR (Mazroui et al., 2008). A trimeric form has been found to be located primarily in the cytosol in hamster models (Ulitzur et al., 1997; Itin et al., 1999).
Function ANP32A has a diverse array of functions. The role of ANP32A in oncogenesis, tumor suppression, and cellular differentiation is well established. It has marked tumor suppressor activity and acts in part through the inhibition of ras/Kras-mediated transformation in both in vitro and in vivo studies (Bai et al., 2001). ANP32A participates in transcriptional gene regulation through histone modification as a member of the inhibitor of histone acetyl transferase (INHAT) protein complex (Brody et al., 2004; Santa-Coloma, 2003; Kular et al., 2009; Khan et al., 2011) and through interferon-dependent binding to gene promoters in conjunction with STAT1/STAT2 (Kadota and Nagata, 2011). Participation as a component of the INHAT protein complex is dependent upon its highly-acidic c-terminus interacting with template activating factor-lbeta, or TAF-lbeta (Seo et al., 2002; Lee et al., 2006). It participates in mRNA nuclear-to-cytoplasmic translocation and post-transcriptional gene regulation (Williams et al., 2010; Santa-Coloma, 2003; Fries et al., 2007; Mazroui et al., 2008; Pan et al., 2009) as a key binding partner of HuR and in an importin-alpha dependent manner (Fukumoto et al., 2011). It is a central component of the SET complex at the core of the granzyme A-mediated apoptosis pathway and affects the activation of caspase-9, cytochrome c-induced caspase activation, Apaf-1, and caspase-3 (Hill et al., 2004; Hoffarth et al., 2008; Kim et al., 2008; Li et al., 2012). ANP32A has also been identified as an inhibitor of protein phosphatase 2A, leading to changes in the ERK, MEK, and WNT signaling pathways (Li et al., 1995; Li et al., 1996; Yu et al., 2004; Stelzl et al., 2005; Habrukowich et al., 2010). It is associated with neuronal cell development, neurotoxicity, and microtubule-based cellular vesicular transport through interactions with microtubule associated proteins tau, MAP2, and MAP4 (Ulitzur et al., 1997; Itin et al., 1999; Kovacech et al., 2007; Kular et al., 2009). Also protective of neuronal excitotoxicity and apoptosis through interaction with the retinoblastoma (Rb) gene product (Adegbola and Pasternack, 2005; Khan et al., 2011) and may play a role in the pathogenesis of spinocerebellar ataxia type 1 through an interaction with ataxin-1 in a manner that is enhanced with expanding CAG repeats of the gene (Matilla et al., 1997). As a necessary component of the template activating factor-1/SET oncoprotein complex it is associated with andeno-associated virus replication (Pegoraro et al., 2006). Finally, its association with the alpha chain of HLA class II molecule DR2 is of unclear significance (Vaesen et al., 1994).

Mutations

Note There are currently 607 known single nucleotide polymorphisms (SNP) registered with the NCBI SNP database. Of these, only one is suggested to have clinical relevance thus far.
A single nucleotide polymorphism of the minor allele (rs7164503) appears to be associated with the pathogenesis of osteoarthritis of the hip (Valdes et al., 2009).

Implicated in

Entity Prostate adenocarcinoma
Note In 1998, Kadkol et al. used in situ hybridization techniques to compare ANP32A expression in prostatic adenocarcinoma with expression in benign prostatic hyperplasia. While finding only moderate expression in the basal cells, 98% of prostatic adenocarcinomas with high Gleason scores demonstrated elevated levels of ANP32A (Kadkol et al., 1998).
In an effort to clarify the paradoxical finding of elevated levels of a tumor suppressor in transformed pancreatic adenocarcinoma tissue, in 1999 Kadkol and colleagues compared the sequence and function of members of this phosphoprotein family in a series of three patient tumors (compared to adjacent normal prostate tissue). They found ANP32A to be expressed in normal tissue, while closely related gene products pp32r1 and pp32r2 were dominant in the tumor samples (Kadkol et al., 1999).
In 2001, Bai et al. continued the focus from this laboratory on ANP32A with experiments aimed to clarify its tumor suppressor function. They utilized the fibroblast cell line NIH3T3 and showed that anti-sense inhibition of ANP32A lead to reduced serum dependence and loss of contact inhibition. They further demonstrated that ANP32A expression abrogated ras-mediated transformation in both in-vitro and in-vivo models (Bai et al., 2001).
Continuing work from the same laboratory, Brody and colleagues reported in 2004 that reduction of ANP32A expression in a prostate carcinoma cell line induced transformation into a neuronal phenotype associated with growth arrest. This change was associated with reduced SET expression and changes to the acetylation status of histone H4. Further downstream changes in gene expression were noted with effects pathways including: cell cycle, MAP kinases, apoptosis, cytokines, metabolism, PP2A, p53 stabilization, and growth factor receptors (Brody et al., 2004).
Finally, in 2011 Schramedei et al. reported results from a proteomic analysis of changes following miR-21 expression in LNCaP prostate cancer cells. They found ANP32A to be the most strongly down-regulated protein upon miR-21 expression suggesting a regulatory role of miR-21 on ANP32A expression. They also found that enhanced cell viability conferred by miR-21 expression in this prostate cancer cell line was mimicked by direct ANP32A knock-down and mitigated by ANP32A overexpression (Schramedei et al., 2011).
Prognosis Increased ANP32A is associated with higher Gleason score in prostate adenocarcinoma despite equivalent rates of capsular invasion, seminal vesical invasion, and positive surgical margins at the time of resection (Kadkol et al., 1998).
  
Entity Pancreatic cancer
Note In 2007, Brody et al. found dramatically decreased levels of ANP32A in poorly differentiated pancreatic tumors and intraductal papillary mucinous neoplasms with moderate dysplasia when compared to healthy pancreatic tissue or well-to-moderately differentiated tumors. Exogenous overexpression of ANP32A in a low-expression pancreatic cancer cell line lead to increased G1 arrest (Brody et al., 2007).
In 2010, Williams and colleagues extended earlier work from the same group by associating low nuclear ANP32A levels with both high grade pancreatic tumors and the presence of lymph node metastasis. Overexpression of ANP32A conferred resistance to therapy with nucleoside analogs gemcitabine and cytarabine while increasing sensitivity to 5-fluorouracil therapy. In accordance with this result, silencing of ANP32A enhanced sensitivity to gemcitabine. A novel interaction with the RNA-binding protein ELAVL1 was described, whereby ANP32A disrupted binding between ELAVL1 and mRNA transcripts such as doxycytidine kinase (dCK) and VEGF. Notably, dCK is the enzyme responsible for metabolism of gemcitabine from its prodrug to active metabolites (Williams et al., 2010).
Prognosis In contrast to findings in the prostate, in pancreatic adenocarcinoma ANP32A is absent or greatly reduced in poorly differentiated tumor when compared to normal pancreatic tissue, early dysplasia, and even well differentiated adenocarcinomas (Brody et al., 2007; Williams et al., 2010).
  
Entity Breast cancer
Note In 2001, Kadkol and colleagues investigated the interplay between members of this phosphoprotein family (ANP32A, pp32r1, and pp32r2) in human breast cancer specimens as compared to benign tissue. After showing abundant protein belonging to this family in 100 of 102 specimens examined, they compared relative expression of each family member in five infiltrating breast carcinomas (compared to matching benign breast tissue). Four of five carcinomas continued to express ANP32A (at levels similar to that of the benign samples), however the expression of pp32r1 and pp32r2 was unique to the carcinomas (Kadkol et al., 2001).
In 2006, Schafer et al. utilized a breast cancer model of chemotherapeutic-induced cytochrome-c mediated apoptosis. They found that breast cancer cells were hyper-sensitive to cytochrome-c mediated apoptosis as compared to normal cells. This hypersensitivity resulted in increased caspase 9 activation in a manner that was mediated by increased ANP32A protein (Schafer et al., 2006).
  
Entity Non-small cell lung cancer
Note In 2008, Hoffarth and colleagues evaluated the effects of exogenous ANP32A expression on drug resistant non-small cell lung cancer cell (NSCLC) lines. They were able to correlate drug resistance with impaired caspase 9 and caspase 3 activation despite formation of the cytochrome-c induced apoptosome. Expression of ANP32A restored apoptosome activation both in vitro and murine in vivo models. Finally, they correlated improved outcomes following chemotherapy in human NSCLC patients with expression of ANP32A on immunohistochemical staining of tumor samples (Hoffarth et al., 2008).
  
Entity Hepatocellular carcinoma
Note In 2012, Li and colleagues surveyed abnormal protein expression in hepatocellular carcinoma utilizing two-dimensional liquid chromatography-tandem mass spectrometry. Elevated expression of ANP32A was validated by western blot analysis and immunohistochemical staining of a tissue microarray comprised of 59 cases (Li et al., 2012).
  
Entity Colorectal cancer
Note In 2011, Shi et al. profiled the proteome changes found in laser capture microdissection samples of colorectal cancer. Amongst several novel protein changes found, ANP32A was overexpressed in tumor when compared to normal tissue (Shi et al., 2011).
  
Entity Neurotoxicity/neurodegenerative disease
Note An association with Rb-mediated gene repression plays a key role in neuronal protection against excitotoxicity (Khan et al., 2011). May contribute to altered tau protein phosphorylation contributing to the pathophysiology of Alzheimer's disease (Tsujio et al., 2005; Kovacech et al., 2007). In the cerebellum it is primarily located in the nucleus of Purkinje cells where it interacts with ataxin-1, the gene product in spinocerebellar ataxia type 1 (Matilla et al., 1997).
Disease Proposed: Alzheimer's disease, spinocerebellar ataxia type 1.
  
Entity Cellular response to immunomodulatory and inflammatory factors
Note Interacts with STAT1/STAT2 and modulates transcriptional complex binding to interferon-stimulated gene promoters (Kadota and Nagata, 2011). Regulates cell signaling in response to inflammatory gene expression through target inhibition of protein phosphatase 2A (Khan et al., 2011). Association with HLA class II molecule DR2 alpha chain has yet to be fully elucidated (Vaesen et al., 1994).
  
Entity Embryogenesis
Note In a survey of this family of leucine-rich repeat genes, ANP32A was necessary for murine embryogenesis in a background of ANP32B absence (Reilly et al., 2011).
  
Entity Virology
Note ANP32A is required for adeno-associated virus replication in human cell line studies as a member of the template activating factor-I/SET oncoprotein complex (Pegoraro et al., 2006). As part of this process, nuclear-to-cytoplasmic shuttling with HuR takes place in a manner dependent on E4orf6 protein function (Higashino et al., 2005).
  

External links

Nomenclature
HGNC (Hugo)ANP32A   13233
Cards
AtlasANP32AID647ch15q23
Entrez_Gene (NCBI)ANP32A  8125  acidic (leucine-rich) nuclear phosphoprotein 32 family, member A
GeneCards (Weizmann)ANP32A
Ensembl (Hinxton)ENSG00000140350 [Gene_View]  chr15:69070875-69113261 [Contig_View]  ANP32A [Vega]
AceView (NCBI)ANP32A
Genatlas (Paris)ANP32A
WikiGenes8125
SOURCE (Princeton)NM_006305
Genomic and cartography
GoldenPath (UCSC)ANP32A  -  15q23   chr15:69070875-69113261 -  15q23   [Description]    (hg19-Feb_2009)
EnsemblANP32A - 15q23 [CytoView]
Mapping of homologs : NCBIANP32A [Mapview]
OMIM600832   
Gene and transcription
Genbank (Entrez)AF025684 AK127498 AK223280 AK312703 AW383928
RefSeq transcript (Entrez)NM_006305
RefSeq genomic (Entrez)AC_000147 NC_000015 NC_018926 NT_010194 NW_001838218 NW_004929398
Consensus coding sequences : CCDS (NCBI)ANP32A
Cluster EST : UnigeneHs.458747 [ NCBI ]
CGAP (NCI)Hs.458747
Alternative Splicing : Fast-db (Paris)GSHG0010545
Alternative Splicing GalleryENSG00000140350
Gene ExpressionANP32A [ NCBI-GEO ]     ANP32A [ SEEK ]   ANP32A [ MEM ]
Protein : pattern, domain, 3D structure
UniProt/SwissProtP39687 (Uniprot)
NextProtP39687  [Medical]
With graphics : InterProP39687
Splice isoforms : SwissVarP39687 (Swissvar)
Domaine pattern : Prosite (Expaxy)LRR (PS51450)   
Domains : Interpro (EBI)Leu-rich_rpt    U2A'_phosphoprotein32A_C   
Related proteins : CluSTrP39687
Domain families : Pfam (Sanger)
Domain families : Pfam (NCBI)
Domain families : Smart (EMBL)LRRcap (SM00446)  
DMDM Disease mutations8125
Blocks (Seattle)P39687
PDB (SRS)2JE0    2JE1   
PDB (PDBSum)2JE0    2JE1   
PDB (IMB)2JE0    2JE1   
PDB (RSDB)2JE0    2JE1   
Human Protein AtlasENSG00000140350
Peptide AtlasP39687
HPRD09014
Protein Interaction databases
DIP (DOE-UCLA)P39687
IntAct (EBI)P39687
FunCoupENSG00000140350
BioGRIDANP32A
InParanoidP39687
Interologous Interaction database P39687
IntegromeDBANP32A
STRING (EMBL)ANP32A
Ontologies - Pathways
Ontology : AmiGOprotein binding  nucleus  nucleoplasm  cytoplasm  endoplasmic reticulum  transcription, DNA-templated  regulation of transcription, DNA-dependent  nucleocytoplasmic transport  nucleocytoplasmic transport  gene expression  RNA metabolic process  mRNA metabolic process  intracellular signal transduction  perinuclear region of cytoplasm  
Ontology : EGO-EBIprotein binding  nucleus  nucleoplasm  cytoplasm  endoplasmic reticulum  transcription, DNA-templated  regulation of transcription, DNA-dependent  nucleocytoplasmic transport  nucleocytoplasmic transport  gene expression  RNA metabolic process  mRNA metabolic process  intracellular signal transduction  perinuclear region of cytoplasm  
Pathways : BIOCARTAGranzyme A mediated Apoptosis Pathway [Genes]   
REACTOMEANP32A
Protein Interaction DatabaseANP32A
Wikipedia pathwaysANP32A
Gene fusion - rearrangments
Polymorphisms : SNP, mutations, diseases
SNP Single Nucleotide Polymorphism (NCBI)ANP32A
SNP (GeneSNP Utah)ANP32A
SNP : HGBaseANP32A
Genetic variants : HAPMAPANP32A
1000_GenomesANP32A 
ICGC programENSG00000140350 
Somatic Mutations in Cancer : COSMICANP32A 
CONAN: Copy Number AnalysisANP32A 
Mutations and Diseases : HGMDANP32A
OMIM600832   
GENETestsANP32A
Disease Genetic AssociationANP32A
Huge Navigator ANP32A [HugePedia]  ANP32A [HugeCancerGEM]
Genomic VariantsANP32A  ANP32A [DGVbeta]
Exome VariantANP32A
dbVarANP32A
ClinVarANP32A
snp3D : Map Gene to Disease8125
General knowledge
Homologs : HomoloGeneANP32A
Homology/Alignments : Family Browser (UCSC)ANP32A
Phylogenetic Trees/Animal Genes : TreeFamANP32A
Chemical/Protein Interactions : CTD8125
Chemical/Pharm GKB GenePA24811
Clinical trialANP32A
Cancer Resource (Charite)ENSG00000140350
Other databases
Probes
Litterature
PubMed66 Pubmed reference(s) in Entrez
CoreMineANP32A
iHOPANP32A

Bibliography

A nuclear factor containing the leucine-rich repeats expressed in murine cerebellar neurons.
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Purification and characterization of two putative HLA class II associated proteins: PHAPI and PHAPII.
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Purification and characterization of two potent heat-stable protein inhibitors of protein phosphatase 2A from bovine kidney.
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Structure of pp32, an acidic nuclear protein which inhibits oncogene-induced formation of transformed foci.
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Molecular identification of I1PP2A, a novel potent heat-stable inhibitor protein of protein phosphatase 2A.
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The cerebellar leucine-rich acidic nuclear protein interacts with ataxin-1.
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Biochemical characterization of mapmodulin, a protein that binds microtubule-associated proteins.
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Novel nuclear phosphoprotein pp32 is highly expressed in intermediate- and high-grade prostate cancer.
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Identification of sequences required for inhibition of oncogene-mediated transformation by pp32.
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Mapmodulin, cytoplasmic dynein, and microtubules enhance the transport of mannose 6-phosphate receptors from endosomes to the trans-golgi network.
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Modulation of oncogenic potential by alternative gene use in human prostate cancer.
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Protein ligands to HuR modulate its interaction with target mRNAs in vivo.
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J Cell Biol. 2000 Oct 2;151(1):1-14.
PMID 11018049
 
Tumor suppression and potentiation by manipulation of pp32 expression.
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Oncogene. 2001 Apr 19;20(17):2153-60.
PMID 11360199
 
Expression of pp32 gene family members in breast cancer.
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Breast Cancer Res Treat. 2001 Jul;68(1):65-73.
PMID 11678310
 
Regulation of histone acetylation and transcription by nuclear protein pp32, a subunit of the INHAT complex.
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J Biol Chem. 2002 Apr 19;277(16):14005-10. Epub 2002 Feb 5.
PMID 11830591
 
Anp32e (Cpd1) and related protein phosphatase 2 inhibitors.
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pp32 reduction induces differentiation of TSU-Pr1 cells.
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Am J Pathol. 2004 Jan;164(1):273-83.
PMID 14695340
 
Analysis of the composition, assembly kinetics and activity of native Apaf-1 apoptosomes.
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PMID 15103327
 
The identification of phosphorylation sites of pp32 and biochemical purification of a cellular pp32-kinase.
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Biochemistry. 2004 Aug 10;43(31):10157-65.
PMID 15287743
 
Protein phosphatase 2A, a negative regulator of the ERK signaling pathway, is activated by tyrosine phosphorylation of putative HLA class II-associated protein I (PHAPI)/pp32 in response to the antiproliferative lectin, jacalin.
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J Biol Chem. 2004 Oct 1;279(40):41377-83. Epub 2004 Jul 7.
PMID 15247276
 
Phosphorylated retinoblastoma protein complexes with pp32 and inhibits pp32-mediated apoptosis.
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J Biol Chem. 2005 Apr 22;280(16):15497-502. Epub 2005 Feb 16.
PMID 15716273
 
Adenovirus E4orf6 targets pp32/LANP to control the fate of ARE-containing mRNAs by perturbing the CRM1-dependent mechanism.
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PMID 15983058
 
A human protein-protein interaction network: a resource for annotating the proteome.
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PMID 16169070
 
Inhibitors of protein phosphatase-2A from human brain structures, immunocytological localization and activities towards dephosphorylation of the Alzheimer type hyperphosphorylated tau.
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FEBS Lett. 2005 Jan 17;579(2):363-72.
PMID 15642345
 
Highly acidic C-terminal domain of pp32 is required for the interaction with histone chaperone, TAF-Ibeta.
Lee IS, Oh SM, Kim SM, Lee DS, Seo SB.
Biol Pharm Bull. 2006 Dec;29(12):2395-8.
PMID 17142970
 
Regulation of adeno-associated virus DNA replication by the cellular TAF-I/set complex.
Pegoraro G, Marcello A, Myers MP, Giacca M.
J Virol. 2006 Jul;80(14):6855-64.
PMID 16809291
 
Enhanced sensitivity to cytochrome c-induced apoptosis mediated by PHAPI in breast cancer cells.
Schafer ZT, Parrish AB, Wright KM, Margolis SS, Marks JR, Deshmukh M, Kornbluth S.
Cancer Res. 2006 Feb 15;66(4):2210-8.
PMID 16489023
 
Reduction of pp32 expression in poorly differentiated pancreatic ductal adenocarcinomas and intraductal papillary mucinous neoplasms with moderate dysplasia.
Brody JR, Witkiewicz A, Williams TK, Kadkol SS, Cozzitorto J, Durkan B, Pasternack GR, Yeo CJ.
Mod Pathol. 2007 Dec;20(12):1238-44. Epub 2007 Sep 28.
PMID 17906614
 
Analysis of nucleocytoplasmic trafficking of the HuR ligand APRIL and its influence on CD83 expression.
Fries B, Heukeshoven J, Hauber I, Gruttner C, Stocking C, Kehlenbach RH, Hauber J, Chemnitz J.
J Biol Chem. 2007 Feb 16;282(7):4504-15. Epub 2006 Dec 18.
PMID 17178712
 
The crystal structure of the tumor suppressor protein pp32 (Anp32a): structural insights into Anp32 family of proteins.
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Protein Sci. 2007 Jul;16(7):1308-15. Epub 2007 Jun 13.
PMID 17567741
 
A novel monoclonal antibody DC63 reveals that inhibitor 1 of protein phosphatase 2A is preferentially nuclearly localised in human brain.
Kovacech B, Kontsekova E, Zilka N, Novak P, Skrabana R, Filipcik P, Iqbal K, Novak M.
FEBS Lett. 2007 Feb 20;581(4):617-22. Epub 2007 Jan 18.
PMID 17266954
 
pp32/PHAPI determines the apoptosis response of non-small-cell lung cancer.
Hoffarth S, Zitzer A, Wiewrodt R, Hahnel PS, Beyer V, Kreft A, Biesterfeld S, Schuler M.
Cell Death Differ. 2008 Jan;15(1):161-70. Epub 2007 Oct 26.
PMID 17962813
 
Cytoplasmic accumulation of the RNA binding protein HuR is central to tamoxifen resistance in estrogen receptor positive breast cancer cells.
Hostetter C, Licata LA, Witkiewicz A, Costantino CL, Yeo CJ, Brody JR, Keen JC.
Cancer Biol Ther. 2008 Sep;7(9):1496-506. Epub 2008 Sep 23.
PMID 18769129
 
PHAPI, CAS, and Hsp70 promote apoptosome formation by preventing Apaf-1 aggregation and enhancing nucleotide exchange on Apaf-1.
Kim HE, Jiang X, Du F, Wang X.
Mol Cell. 2008 Apr 25;30(2):239-47. doi: 10.1016/j.molcel.2008.03.014.
PMID 18439902
 
Caspase-mediated cleavage of HuR in the cytoplasm contributes to pp32/PHAP-I regulation of apoptosis.
Mazroui R, Di Marco S, Clair E, von Roretz C, Tenenbaum SA, Keene JD, Saleh M, Gallouzi IE.
J Cell Biol. 2008 Jan 14;180(1):113-27. doi: 10.1083/jcb.200709030. Epub 2008 Jan 7.
PMID 18180367
 
Neuronal differentiation is regulated by leucine-rich acidic nuclear protein (LANP), a member of the inhibitor of histone acetyltransferase complex.
Kular RK, Cvetanovic M, Siferd S, Kini AR, Opal P.
J Biol Chem. 2009 Mar 20;284(12):7783-92. doi: 10.1074/jbc.M806150200. Epub 2009 Jan 9.
PMID 19136565
 
PHAPI/pp32 suppresses tumorigenesis by stimulating apoptosis.
Pan W, da Graca LS, Shao Y, Yin Q, Wu H, Jiang X.
J Biol Chem. 2009 Mar 13;284(11):6946-54. doi: 10.1074/jbc.M805801200. Epub 2009 Jan 2.
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Variation at the ANP32A gene is associated with risk of hip osteoarthritis in women.
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Written03-2013Richard A Burkhart, Jonathan R Brody
Thomas Jefferson University, Department of Surgery, Philadelphia, PA, USA

Citation

This paper should be referenced as such :
Burkhart RA, Brody JR . ANP32A (acidic (leucine-rich) nuclear phosphoprotein 32 family, member A). Atlas Genet Cytogenet Oncol Haematol. March 2013 .
URL : http://AtlasGeneticsOncology.org/Genes/ANP32AID647ch15q23.html

The various updated versions of this paper are referenced and archived by INIST as such :
http://documents.irevues.inist.fr/bitstream/handle/2042/51143/03-2013-ANP32AID647ch15q23.pdf   [ Bibliographic record ]

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