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HNRNPA1 (Heterogeneous Nuclear Ribonucleoprotein A1)

Written2018-10Murat Erdem, Ibrahim Özgül, Ayse Elif Erson-Bensan
Department of Biological Sciences, Middle East Technical University, Ankara, TURKEY, E-mail:;;

Abstract Heterogeneous nuclear ribonucleoprotein (HNRNPA1) gene maps to chromosome 12, plus strand and has 13 exons and 12 introns. There are three reported transcripts due to the alternative splicing.
HNRNPA1 is one of the most abundant and ubiquitously expressed nuclear proteins. HNRNPA1 is a member of RNA-binding protein family comprising of 20 members in humans (Dreyfuss, 1993; Pinol-Roma, Choi, Matunis, & Dreyfuss, 1988). HNRNPA1 has diverse roles in RNA splicing, telomere length maintenance, miRNA maturation and mRNA transport from nucleus to cytoplasm.

Keywords HNRNPA1; RNA-binding protein; RNA splicing; telomere length maintenance; miRNA maturation; mRNA transport

(Note : for Links provided by Atlas : click)


Alias_symbol (synonym)hnRNPA1
Other aliasALS20 (Amyotrophic lateral sclerosis 20)
hnRNP A1
IBMPFD3 (inclusion body myopathy with Paget disease)
UP 1
LocusID (NCBI) 3178
Atlas_Id 43803
Location 12q13.13  [Link to chromosome band 12q13]
Location_base_pair Starts at 54280690 and ends at 54285246 bp from pter ( according to hg19-Feb_2009)  [Mapping HNRNPA1.png]
Local_order From telomere to centromere: LOC105369777, CBX5, ENSG00000257596, HNRNPA1, NFE2, ENSG00000258344, COPZ1, GPR84
  Local order of HNRNPA1 together with neighboring upstream and downstream genes on chromosome 12. The direction of arrows indicates direction of transcription and arrow sizes approximate gene sizes.
Fusion genes
(updated 2017)
Data from Atlas, Mitelman, Cosmic Fusion, Fusion Cancer, TCGA fusion databases with official HUGO symbols (see references in chromosomal bands)


Note HNRNPA1 gene consists of 13 exons and 12 introns. The gene maps to 12q13.13 and is 6399 bps long (NCBI Reference Sequence: NC_000012.12: 54280690-54287088). Highlighted in red is the protein coding sequence from exons 1-10. (Figure 2)
  HNRNPA1 gene has 13 exons and 12 introns. Numbers indicate the exons. Red exons show protein-coding regions while blue color represents untranslated regions.
Description The HNRNPA1 gene is 6399 bases long and is on the plus strand. HNRNPA1 gene has 13 exons (Jean-Philippe et al., 2013).
Transcription HNRNPA1 produces two coding transcripts (Exon 1-11). The difference between these coding transcripts is the presence or absence of exon 8 (only longer mRNA contains exon 8). A third one was reported as a potential non-coding transcript (Mendell et al, 2004). This non-coding RNA transcript has exons 12 and 13, and it does not contain exon 8.


Note HNRNPA1 gene encodes a 372 amino acid protein. The protein is a member of heterogeneous nuclear ribonucleoproteins (hnRNPs) and has an estimated molecular weight of 38-39 kDa (Jean-Philippe, Paz, & Caputi, 2013).
  HNRNPA1 has three functional regions; two RNA-recognition motifs and one Glycine-rich Prion like domain. Numbers above the bars indicate amino acids harboring the domains.
Description HNRNPA1 has two RNA recognition motifs; RRM1 and RRM2. These domains are known for binding to single-stranded RNAs (Dreyfuss, Swanson, & Piñol-Roma, 1988). HNRNPA1 also possesses a prion-like domain (PLD). This domain is reported in RNA binding proteins that have been associated with neurodegenerative disorders such as Amyotrophic Lateral Sclerosis (Kim et al., 2013). In addition, glycine-rich region mediates subcellular localization and protein-protein interactions (Han, Tang, & Smith, 2010).
Expression HNRNPA1 mRNA is expressed in all human tissues including brain, skin, lung, breast and kidney (The Human Protein Atlas, 2018).
  Expression of HNRNPA1 in different types of tissues is shown (The Human Protein Atlas, 2018).
Localisation HNRNPA1 protein is mainly nuclear; however, under certain conditions the protein is also present in the cytosol (Roy et al., 2014). In fact, HNRNPA1 may shuttle between nucleus and cytoplasm along with mRNAs (Jønson et al., 2007).
Function HNRNPA1 has a very broad range of reported functions including transcriptional regulation, alternative splicing, mRNA transport, translation and miRNA processing. Most surprisingly, HNRNPA1 can interact with certain promoters and induce transcriptional repression or activation of target genes. VDR (Vitamin D receptor) (H. Chen, Hewison, Hu, & Adams, 2003), FGG (γ-fibrinogen) (Xia, 2005) and TK1 (thymidine kinase) (Lau et al., 2000) promoters are transcriptionally repressed while APOE promoter is activated by HNRNPA1 (Campillos et al., 2003).
HNRNPA1 has an important role in mRNA splicing. The protein modulates alternative splicing of various genes including INSR (Insulin Receptor) (Talukdar et al., 2011), BRCA1 (Breast Cancer 1) (Goina, Skoko, & Pagani, 2008), PKM (Pyruvate Kinase M1/2) (David, Chen, Assanah, Canoll, & Manley, 2010) and its own HNRNPA1 mRNA (Hutchison, LeBel, Blanchette, & Chabot, 2002). mRNA splicing is modulated by HNRNPA1 by exon skipping and splice site repression (Jean-Philippe et al., 2013).
HNRNPA1 contributes to telomere regulation by promoting telomerase activity via binding to telomeric sequences, potentially as an auxiliary factor for the telomerase enzyme (Zhang, Manche, Xu, & Krainer, 2006).
HNRNPA1 has roles in mRNA transport between nucleus and cytoplasm. Although the exact mechanism is unknown, HNRNPA1 binds to poly(A) tailed mRNAs both in the nucleus and cytoplasm (Mili, Shu, Zhao, & Pinol-Roma, 2001), and possibly aid their transfer through nuclear pores (Piñol-Roma & Dreyfuss, 1992).
Another function attributed to HNRNPA1 is during translation. HNRNPA1 binds to internal ribosomal entry sites (IRES) that initiates 5' cap-independent translation of certain cellular and viral mRNAs (such as, MYC), CSDE1 (Upstream of NRAS), CCND1 (Cyclin D1), VEGFA (Vascular Endothelial Growth Factor), FGF2 (Fibroblast Growth Factor), APAF1, and XIAP mRNAs (Cammas et al. 2007). In addition, the HIV-1 IRES is stimulated by hnRNPA1 (Martènez-Salas, Piñeiro, & Fernández, 2012).
In addition to mRNA processing and transport , HNRNPA1 interacts directly and specifically with C-terminal region of NF-kB alpha inhibitory subunit via its RNA-binding domain (between residues 95 and 207) resulting in the activation of nuclear factor k B (Hay, Kemp, Dargemont, & Hay, 2001). The exact mechanism of HNRNPA1 and NF-kB interaction is not completely understood. However, in cells lacking HNRNPA1, activation of NF-kB is defected. When HNRNPA1 loss is rescued, an effective NF-kB response to signal induction is observed only upon ligand induction.
As for the microRNA processing, HNRNPA1 binds to the terminal loop of pri-miR-18a, and facilitates MIR18A production by creating favorable cleavage site for DROSHA (Guil & Cáceres, 2007). In contrast, HNRNPA1 negatively affects MIRNLET7A1 (let-7a) biogenesis. HNRNPA1 binds to terminal loop of pri-let-7a-1 and interferes with the binding of KHSRP (component of both Drosha and Dicer complexes, known to promote let-7a biogenesis); hence, inhibiting processing of pri-let-7a by Drosha (Michlewski & Cáceres, 2010).
Homology HNRNPA1 gene has homologs across Amniota including P. troglodytes, M. mulatta, B. taurus, R. norvegicus, G. gallus, M. musculus and H. sapiens (NCBI HomoloGene, 2018). There is also a well-studied HNRNPA1 homolog in D. melanogaster called Hrp36 (Singh & Lakhotia, 2012). In total, there are 97 species including invertebrates that have genes orthologous to A1 (NCBI Ensembl, 2018).


Note Up to 106 substitution mutations were reported in the HNRNPA1 gene in 42,067 cancer patients. Reported mutations are generally missense mutations (70 of 106). There are also 4 nonsense mutations, 30 synonymous substitutions and 2 frameshift deletions (COSMIC database, 2018). One of the frameshift deletions found in cancer patients is discovered in the Sanger Institute Cancer Genome Project (study ID :COSU652) while the other is discovered in 619 incident colorectal cancer patients in the study conducted by Giannakis et al(2016).
Yu et al. (2018) also reported a recessive frameshift mutation in HNRNPA1 leading to deregulation of cardiac transcription network and multiple signaling pathways, including Bone Morphogenetic Protein, Notch and Fibroblast growth factor signaling.

Implicated in

Note HNRNPA1 has been implicated in diverse diseases.
Entity Amyotrophic Lateral Sclerosis (ALS)
Note Immunohistochemistry and immunofluorescence results showed that HNRNPA1 protein was decreased in the nuclei of neurons and the significant loss of HNRNPA1 in motor neurons with concomitant cytoplasmic aggregation in ALS cases while HNRNPA1 was mainly located in nucleus of motor neurons in normal cases (Honda et al., 2015). Mutations in prion-like domain (PrLD), enriched in uncharged polar amino acids and glycine, promote excess incorporation of HNRNPA1 into stress granules and cause the formation of cytoplasmic inclusions in animal models (H. J. Kim et al., 2013b). Whole-exome sequencing conducted by Liu et al.(2016) showed a missense mutation in HNRNPA1 in Flail-Arm ALS patients leading to cytoplasmic inclusions that co-localized with stress granules in Flail-Arm ALS.
Entity Breast Cancer
Note Invasive breast cancer cells (MDA-MB-231) express the CD44v6 variants, which are regulated by HNRNPA1. Downregulation of HNRNPA1 induces a significant change in the expression levels of CD44 isoforms through alternative splicing. Silencing of HNRNPA1 significantly induced cell death and caused a decrease in cell invasion in the MDA-MB-231 cells (Loh et al., 2015). HNRNPA1 silencing through siRNAs significantly lowers the cell proliferation in MDA-MB-231 cells (Otsuka, Yamamoto, Ochiya, 2018).
Prognosis In basal-like breast cancer, Kaplan-Meier survival analysis showed that patients (309 samples) showing high HNRNPA1 expression, had an distinctively shorter relapse-free survival than patients (309 samples) expressing low level of HNRNPA1 and that patients (121 samples) showing high HNRNPA1 expression had a shorter overall survival than patients (120 samples) with low level of HNRNPA1 expression. (Otsuka, Yamamoto, Ochiya, 2018).
Entity Cervical Carcinoma
Note HNRNPA1 has higher expression in cervical carcinoma compared with normal tissue samples in 32 patients with cervical cancer (Y. J. Kim et al., 2017).
HNRNPA1 expression is upregulated during differentiation of virus-infected epithelial cells in monolayer and 3D cell cultures. HNRNPA1 interacts directly with the Human papillomavirus type 16 (HPV16) late regulatory element (LRE) (which has an important role in temporally controlling virus late gene expression during epithelial differentiation) in the nucleus of differentiated W12 cells in vitro and may facilitate the alternative splicing of late transcripts of virus  in differentiated epithelial cells (Cheunim, Zhang, Milligan, McPhillips, & Graham, 2008).
Entity Colon Cancer
Note HNRNPA1 mRNA is overexpressed in 40-78% of colon cancer stages, compared with normal colon (Ubagai, Fukuda, & Tsuchiya, 2005).
A cell line based study showed HNRNPA1 to be suppressed by MIR18a in SW620 cells through autophagolysosomal degradation and thus, HNRNPA1 silencing resulted in the suppression of colon cancer cell progression (Fujiya et al., 2014).
Entity Gastric Cancer (GC)
Note GC tissues have elevated levels of HNRNPA1 protein compared with normal tissues. HNRNPA1 silencing significantly prevented anchorage-dependent growth in GC cells and HNRNPA1 was important to cell growth and progression of GC. HNRNPA1 knockdown caused reduction in cell growth, invasion, migration and reversal of EMT (Epithelial to Mesenchymal Transition) in GC cells. Collectively, these results pointed out that HNRNPA1 may have a pivotal role in GC cell invasion and metastasis (Chen et al., 2018).
Entity Hepatocellular Carcinoma (HCC)
Note High expression of HNRNPA1 was reported in the highly metastatic HCC cell lines and in tumor tissues of patients with recurrent HCC. HNRNPA1 silencing reduced cell invasion in highly metastatic HCC cells while overexpression of HNRNPA1 caused a significant increase in invasive behavior of poorly metastatic HCC cells HNRNPA1 was reported to regulate the invasive capacity of HCC cells through regulating the CD44v6 expression(Zhou et al., 2013).
Entity Lung Cancer
Note The HNRNPA1 protein expression was reported to be upregulated in most tissue samples from lung cancer patients by immunohistochemistry (Boukakis, Patrinou-Georgoula, Lekarakou, Valavanis, & Guialis, 2010). HNRNPA1 knockdown inhibited cell viability and colony formation of lung cancer cells and arrested cells in the G0/G1 phase (Liu, Zhou, Lou, & Zhong, 2016).


Deregulated expression of hnRNP A/B proteins in human non-small cell lung cancer: parallel assessment of protein and mRNA levels in paired tumour/non-tumour tissues
Boukakis G, Patrinou-Georgoula M, Lekarakou M, Valavanis C, Guialis A
BMC Cancer 2010 Aug 17;10:434
PMID 20716340
Cytoplasmic relocalization of heterogeneous nuclear ribonucleoprotein A1 controls translation initiation of specific mRNAs
Cammas A, Pileur F, Bonnal S, Lewis SM, Lévêque N, Holcik M, Vagner S
Mol Biol Cell 2007 Dec;18(12):5048-59
PMID 17898077
Specific interaction of heterogeneous nuclear ribonucleoprotein A1 with the -219T allelic form modulates APOE promoter activity
Campillos M, Lamas JR, García MA, Bullido MJ, Valdivieso F, Vázquez J
Nucleic Acids Res 2003 Jun 15;31(12):3063-70
PMID 12799433
Heterogeneous nuclear ribonucleoprotein (hnRNP) binding to hormone response elements: a cause of vitamin D resistance
Chen H, Hewison M, Hu B, Adams JS
Proc Natl Acad Sci U S A 2003 May 13;100(10):6109-14
PMID 12716975
High expression of hnRNPA1 promotes cell invasion by inducing EMT in gastric cancer
Chen Y, Liu J, Wang W, Xiang L, Wang J, Liu S, Zhou H, Guo Z
Oncol Rep 2018 Apr;39(4):1693-1701
PMID 29484423
The alternative splicing factor hnRNP A1 is up-regulated during virus-infected epithelial cell differentiation and binds the human papillomavirus type 16 late regulatory element
Cheunim T, Zhang J, Milligan SG, McPhillips MG, Graham SV
Virus Res 2008 Feb;131(2):189-98
PMID 17950949
HnRNP proteins controlled by c-Myc deregulate pyruvate kinase mRNA splicing in cancer
David CJ, Chen M, Assanah M, Canoll P, Manley JL
Nature 2010 Jan 21;463(7279):364-8
PMID 20010808
Heterogeneous nuclear ribonucleoprotein particles and the pathway of mRNA formation
Dreyfuss G, Swanson MS, Piñol-Roma S
Trends Biochem Sci 1988 Mar;13(3):86-91
PMID 3072706
microRNA-18a induces apoptosis in colon cancer cells via the autophagolysosomal degradation of oncogenic heterogeneous nuclear ribonucleoprotein A1
Fujiya M, Konishi H, Mohamed Kamel MK, Ueno N, Inaba Y, Moriichi K, Tanabe H, Ikuta K, Ohtake T, Kohgo Y
Oncogene 2014 Oct 2;33(40):4847-56
PMID 24166503
Genomic Correlates of Immune-Cell Infiltrates in Colorectal Carcinoma
Giannakis M, Mu XJ, Shukla SA, Qian ZR, Cohen O, Nishihara R, Bahl S, Cao Y, Amin-Mansour A, Yamauchi M, Sukawa Y, Stewart C, Rosenberg M, Mima K, Inamura K, Nosho K, Nowak JA, Lawrence MS, Giovannucci EL, Chan AT, Ng K, Meyerhardt JA, Van Allen EM, Getz G, Gabriel SB, Lander ES, Wu CJ, Fuchs CS, Ogino S, Garraway LA
Cell Rep 2016 Apr 26;15(4):857-865
PMID 27149842
Binding of DAZAP1 and hnRNPA1/A2 to an exonic splicing silencer in a natural BRCA1 exon 18 mutant
Goina E, Skoko N, Pagani F
Mol Cell Biol 2008 Jun;28(11):3850-60
PMID 18391021
The multifunctional RNA-binding protein hnRNP A1 is required for processing of miR-18a
Guil S, Cáceres JF
Nat Struct Mol Biol 2007 Jul;14(7):591-6
PMID 17558416
Functional diversity of the hnRNPs: past, present and perspectives
Han SP, Tang YH, Smith R
Biochem J 2010 Sep 15;430(3):379-92
PMID 20795951
Interaction between hnRNPA1 and IkappaBalpha is required for maximal activation of NF-kappaB-dependent transcription
Hay DC, Kemp GD, Dargemont C, Hay RT
Mol Cell Biol 2001 May;21(10):3482-90
PMID 11313474
Loss of hnRNPA1 in ALS spinal cord motor neurons with TDP-43-positive inclusions
Honda H, Hamasaki H, Wakamiya T, Koyama S, Suzuki SO, Fujii N, Iwaki T
Neuropathology 2015 Feb;35(1):37-43
PMID 25338872
Distinct sets of adjacent heterogeneous nuclear ribonucleoprotein (hnRNP) A1/A2 binding sites control 5' splice site selection in the hnRNP A1 mRNA precursor
Hutchison S, LeBel C, Blanchette M, Chabot B
J Biol Chem 2002 Aug 16;277(33):29745-52
PMID 12060656
Isolated inclusion body myopathy caused by a multisystem proteinopathy-linked hnRNPA1 mutation
Izumi R, Warita H, Niihori T, Takahashi T, Tateyama M, Suzuki N, Nishiyama A, Shirota M, Funayama R, Nakayama K, Mitsuhashi S, Nishino I, Aoki Y, Aoki M
Neurol Genet 2015 Sep 24;1(3):e23
PMID 27066560
Molecular composition of IMP1 ribonucleoprotein granules
Jønson L, Vikesaa J, Krogh A, Nielsen LK, Hansen Tv, Borup R, Johnsen AH, Christiansen J, Nielsen FC
Mol Cell Proteomics 2007 May;6(5):798-811
PMID 17289661
hnRNP A1: the Swiss army knife of gene expression
Jean-Philippe J, Paz S, Caputi M
Int J Mol Sci 2013 Sep 16;14(9):18999-9024
PMID 24065100
Mutations in prion-like domains in hnRNPA2B1 and hnRNPA1 cause multisystem proteinopathy and ALS
Kim HJ, Kim NC, Wang YD, Scarborough EA, Moore J, Diaz Z, MacLea KS, Freibaum B, Li S, Molliex A, Kanagaraj AP, Carter R, Boylan KB, Wojtas AM, Rademakers R, Pinkus JL, Greenberg SA, Trojanowski JQ, Traynor BJ, Smith BN, Topp S, Gkazi AS, Miller J, Shaw CE, Kottlors M, Kirschner J, Pestronk A, Li YR, Ford AF, Gitler AD, Benatar M, King OD, Kimonis VE, Ross ED, Weihl CC, Shorter J, Taylor JP
Nature 2013 Mar 28;495(7442):467-73
PMID 23455423
HNRNPA1, a Splicing Regulator, Is an Effective Target Protein for Cervical Cancer Detection: Comparison With Conventional Tumor Markers
Kim YJ, Kim BR, Ryu JS, Lee GO, Kim HR, Choi KH, Ryu JW, Na KS, Park MC, So HS, Cho JH, Park DS
Int J Gynecol Cancer 2017 Feb;27(2):326-331
PMID 27984373
Heterogeneous nuclear ribonucleoproteins as regulators of gene expression through interactions with the human thymidine kinase promoter
Lau JS, Baumeister P, Kim E, Roy B, Hsieh TY, Lai M, Lee AS
J Cell Biochem 2000 Sep 7;79(3):395-406
PMID 10972977
Whole-exome sequencing identifies a missense mutation in hnRNPA1 in a family with flail arm ALS
Liu Q, Shu S, Wang RR, Liu F, Cui B, Guo XN, Lu CX, Li XG, Liu MS, Peng B, Cui LY, Zhang X
Neurology 2016 Oct 25;87(17):1763-1769
PMID 27694260
Knockdown of HNRNPA1 inhibits lung adenocarcinoma cell proliferation through cell cycle arrest at G0/G1 phase
Liu X, Zhou Y, Lou Y, Zhong H
Gene 2016 Feb 1;576(2 Pt 2):791-7
PMID 26581508
CD44 alternative splicing and hnRNP A1 expression are associated with the metastasis of breast cancer
Loh TJ, Moon H, Cho S, Jang H, Liu YC, Tai H, Jung DW, Williams DR, Kim HR, Shin MG, Liao DJ, Zhou J, Shi W, Zheng X, Shen H
Oncol Rep 2015 Sep;34(3):1231-8
PMID 26151392
Alternative Mechanisms to Initiate Translation in Eukaryotic mRNAs
Martínez-Salas E, Piñeiro D, Fernández N
Comp Funct Genomics 2012;2012:391546
PMID 22536116
Nonsense surveillance regulates expression of diverse classes of mammalian transcripts and mutes genomic noise
Mendell JT, Sharifi NA, Meyers JL, Martinez-Murillo F, Dietz HC
Nat Genet 2004 Oct;36(10):1073-8
PMID 15448691
Antagonistic role of hnRNP A1 and KSRP in the regulation of let-7a biogenesis
Michlewski G, Cáceres JF
Nat Struct Mol Biol 2010 Aug;17(8):1011-8
PMID 20639884
Distinct RNP complexes of shuttling hnRNP proteins with pre-mRNA and mRNA: candidate intermediates in formation and export of mRNA
Mili S, Shu HJ, Zhao Y, Piñol-Roma S
Mol Cell Biol 2001 Nov;21(21):7307-19
PMID 11585913
Regulatory role of resveratrol, a microRNA-controlling compound, in HNRNPA1 expression, which is associated with poor prognosis in breast cancer
Otsuka K, Yamamoto Y, Ochiya T
Oncotarget 2018 May 15;9(37):24718-24730
PMID 29872500
Shuttling of pre-mRNA binding proteins between nucleus and cytoplasm
Piñol-Roma S, Dreyfuss G
Nature 1992 Feb 20;355(6362):730-2
PMID 1371331
hnRNPA1 couples nuclear export and translation of specific mRNAs downstream of FGF-2/S6K2 signalling
Roy R, Durie D, Li H, Liu BQ, Skehel JM, Mauri F, Cuorvo LV, Barbareschi M, Guo L, Holcik M, Seckl MJ, Pardo OE
Nucleic Acids Res 2014 Nov 10;42(20):12483-97
PMID 25324306
The hnRNP A1 homolog Hrp36 is essential for normal development, female fecundity, omega speckle formation and stress tolerance in Drosophila melanogaster
Singh AK, Lakhotia SC
J Biosci 2012 Sep;37(4):659-78
PMID 22922191
hnRNP A1 and hnRNP F modulate the alternative splicing of exon 11 of the insulin receptor gene
Talukdar I, Sen S, Urbano R, Thompson J, Yates JR 3rd, Webster NJ
PLoS One 2011;6(11):e27869
PMID 22132154
Endocrine disruptors fludioxonil and fenhexamid stimulate miR-21 expression in breast cancer cells
Teng Y, Manavalan TT, Hu C, Medjakovic S, Jungbauer A, Klinge CM
Toxicol Sci 2013 Jan;131(1):71-83
PMID 23052036
Up-regulation of hnRNP A1 gene in sporadic human colorectal cancers
Ushigome M, Ubagai T, Fukuda H, Tsuchiya N, Sugimura T, Takatsuka J, Nakagama H
Int J Oncol 2005 Mar;26(3):635-40
PMID 15703818
Regulation of gamma-fibrinogen chain expression by heterogeneous nuclear ribonucleoprotein A1
Xia H
J Biol Chem 2005 Apr 1;280(13):13171-8
PMID 15671034
Mutations in Hnrnpa1 cause congenital heart defects
Yu Z, Tang PL, Wang J, Bao S, Shieh JT, Leung AW, Zhang Z, Gao F, Wong SY, Hui AL, Gao Y, Dung N, Zhang ZG, Fan Y, Zhou X, Zhang Y, Wong DS, Sham PC, Azhar A, Kwok PY, Tam PP, Lian Q, Cheah KS, Wang B, Song YQ
JCI Insight 2018 Jan 25;3(2)
PMID 29367466
hnRNP A1 associates with telomere ends and stimulates telomerase activity
Zhang QS, Manche L, Xu RM, Krainer AR
RNA 2006 Jun;12(6):1116-28
PMID 16603717
Overexpression of HnRNP A1 promotes tumor invasion through regulating CD44v6 and indicates poor prognosis for hepatocellular carcinoma
Zhou ZJ, Dai Z, Zhou SL, Fu XT, Zhao YM, Shi YH, Zhou J, Fan J
Int J Cancer 2013 Mar 1;132(5):1080-9
PMID 22821376


This paper should be referenced as such :
Murat Erdem, Ibrahim zgül, Ayse Elif Erson-Bensan
HNRNPA1 (heterogeneous nuclear ribonucleoprotein A1)
Atlas Genet Cytogenet Oncol Haematol. 2019;23(6):137-142.
Free journal version : [ pdf ]   [ DOI ]
On line version :

Other Solid tumors implicated (Data extracted from papers in the Atlas) [ 1 ]
  t(2;12)(p23;q13) HNRNPA1/ALK

External links

HGNC (Hugo)HNRNPA1   5031
Entrez_Gene (NCBI)HNRNPA1  3178  heterogeneous nuclear ribonucleoprotein A1
AliasesALS19; ALS20; HNRPA1; HNRPA1L3; 
GeneCards (Weizmann)HNRNPA1
Ensembl hg19 (Hinxton)ENSG00000135486 [Gene_View]
Ensembl hg38 (Hinxton)ENSG00000135486 [Gene_View]  ENSG00000135486 [Sequence]  chr12:54280690-54285246 [Contig_View]  HNRNPA1 [Vega]
ICGC DataPortalENSG00000135486
Genatlas (Paris)HNRNPA1
Genetics Home Reference (NIH)HNRNPA1
Genomic and cartography
GoldenPath hg38 (UCSC)HNRNPA1  -     chr12:54280690-54285246 +  12q13.13   [Description]    (hg38-Dec_2013)
GoldenPath hg19 (UCSC)HNRNPA1  -     12q13.13   [Description]    (hg19-Feb_2009)
GoldenPathHNRNPA1 - 12q13.13 [CytoView hg19]  HNRNPA1 - 12q13.13 [CytoView hg38]
Mapping of homologs : NCBIHNRNPA1 [Mapview hg19]  HNRNPA1 [Mapview hg38]
OMIM164017   615424   615426   
Gene and transcription
Genbank (Entrez)AK129814 AK291113 AK298176 AK303303 AK308679
RefSeq transcript (Entrez)NM_002136 NM_031157
RefSeq genomic (Entrez)
Consensus coding sequences : CCDS (NCBI)HNRNPA1
Cluster EST : UnigeneHs.655424 [ NCBI ]
CGAP (NCI)Hs.655424
Alternative Splicing GalleryENSG00000135486
Gene Expression Viewer (FireBrowse)HNRNPA1 [ Firebrowse - Broad ]
SOURCE (Princeton)Expression in : [Datasets]   [Normal Tissue Atlas]  [carcinoma Classsification]  [NCI60]
GenevestigatorExpression in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
BioGPS (Tissue expression)3178
GTEX Portal (Tissue expression)HNRNPA1
Human Protein AtlasENSG00000135486-HNRNPA1 [pathology]   [cell]   [tissue]
Protein : pattern, domain, 3D structure
UniProt/SwissProtP09651   [function]  [subcellular_location]  [family_and_domains]  [pathology_and_biotech]  [ptm_processing]  [expression]  [interaction]
NextProtP09651  [Sequence]  [Exons]  [Medical]  [Publications]
With graphics : InterProP09651
Splice isoforms : SwissVarP09651
Domaine pattern : Prosite (Expaxy)RRM (PS50102)   
Domains : Interpro (EBI)HnRNPA1    hnRNPA1_RRM1    hnRNPA1_RRM2    Nucleotide-bd_a/b_plait_sf    RBD_domain_sf    RRM_dom   
Domain families : Pfam (Sanger)HnRNPA1 (PF11627)    RRM_1 (PF00076)   
Domain families : Pfam (NCBI)pfam11627    pfam00076   
Domain families : Smart (EMBL)RRM (SM00360)  
Conserved Domain (NCBI)HNRNPA1
DMDM Disease mutations3178
Blocks (Seattle)HNRNPA1
PDB (RSDB)1HA1    1L3K    1PGZ    1PO6    1U1K    1U1L    1U1M    1U1N    1U1O    1U1P    1U1Q    1U1R    1UP1    2H4M    2LYV    2UP1    4YOE    5MPG    5MPL   
PDB Europe1HA1    1L3K    1PGZ    1PO6    1U1K    1U1L    1U1M    1U1N    1U1O    1U1P    1U1Q    1U1R    1UP1    2H4M    2LYV    2UP1    4YOE    5MPG    5MPL   
PDB (PDBSum)1HA1    1L3K    1PGZ    1PO6    1U1K    1U1L    1U1M    1U1N    1U1O    1U1P    1U1Q    1U1R    1UP1    2H4M    2LYV    2UP1    4YOE    5MPG    5MPL   
PDB (IMB)1HA1    1L3K    1PGZ    1PO6    1U1K    1U1L    1U1M    1U1N    1U1O    1U1P    1U1Q    1U1R    1UP1    2H4M    2LYV    2UP1    4YOE    5MPG    5MPL   
Structural Biology KnowledgeBase1HA1    1L3K    1PGZ    1PO6    1U1K    1U1L    1U1M    1U1N    1U1O    1U1P    1U1Q    1U1R    1UP1    2H4M    2LYV    2UP1    4YOE    5MPG    5MPL   
SCOP (Structural Classification of Proteins)1HA1    1L3K    1PGZ    1PO6    1U1K    1U1L    1U1M    1U1N    1U1O    1U1P    1U1Q    1U1R    1UP1    2H4M    2LYV    2UP1    4YOE    5MPG    5MPL   
CATH (Classification of proteins structures)1HA1    1L3K    1PGZ    1PO6    1U1K    1U1L    1U1M    1U1N    1U1O    1U1P    1U1Q    1U1R    1UP1    2H4M    2LYV    2UP1    4YOE    5MPG    5MPL   
Human Protein Atlas [tissue]ENSG00000135486-HNRNPA1 [tissue]
Peptide AtlasP09651
IPIIPI00215965   IPI00465365   IPI00797148   IPI01021324   IPI00908994   IPI01022060   IPI01021812   IPI01022460   IPI01022641   IPI01022218   IPI01022306   IPI01021093   IPI01022801   IPI00644968   
Protein Interaction databases
IntAct (EBI)P09651
Ontologies - Pathways
Ontology : AmiGOregulation of alternative mRNA splicing, via spliceosome  mRNA splicing, via spliceosome  mRNA splicing, via spliceosome  single-stranded DNA binding  RNA binding  RNA binding  single-stranded RNA binding  mRNA binding  protein binding  nucleus  nucleus  nucleoplasm  nucleoplasm  spliceosomal complex  cytoplasm  RNA export from nucleus  fibroblast growth factor receptor signaling pathway  membrane  viral process  RNA metabolic process  protein domain specific binding  negative regulation of telomere maintenance via telomerase  positive regulation of telomere maintenance via telomerase  miRNA binding  pre-mRNA binding  cellular response to glucose starvation  mRNA transport  nuclear export  import into nucleus  telomeric repeat-containing RNA binding  extracellular exosome  catalytic step 2 spliceosome  G-rich strand telomeric DNA binding  cellular response to sodium arsenite  ribonucleoprotein complex  ribonucleoprotein complex  
Ontology : EGO-EBIregulation of alternative mRNA splicing, via spliceosome  mRNA splicing, via spliceosome  mRNA splicing, via spliceosome  single-stranded DNA binding  RNA binding  RNA binding  single-stranded RNA binding  mRNA binding  protein binding  nucleus  nucleus  nucleoplasm  nucleoplasm  spliceosomal complex  cytoplasm  RNA export from nucleus  fibroblast growth factor receptor signaling pathway  membrane  viral process  RNA metabolic process  protein domain specific binding  negative regulation of telomere maintenance via telomerase  positive regulation of telomere maintenance via telomerase  miRNA binding  pre-mRNA binding  cellular response to glucose starvation  mRNA transport  nuclear export  import into nucleus  telomeric repeat-containing RNA binding  extracellular exosome  catalytic step 2 spliceosome  G-rich strand telomeric DNA binding  cellular response to sodium arsenite  ribonucleoprotein complex  ribonucleoprotein complex  
Pathways : KEGGSpliceosome   
REACTOMEP09651 [protein]
REACTOME PathwaysR-HSA-72203 [pathway]   
Atlas of Cancer Signalling NetworkHNRNPA1
Wikipedia pathwaysHNRNPA1
Orthology - Evolution
GeneTree (enSembl)ENSG00000135486
Phylogenetic Trees/Animal Genes : TreeFamHNRNPA1
Homologs : HomoloGeneHNRNPA1
Homology/Alignments : Family Browser (UCSC)HNRNPA1
Gene fusions - Rearrangements
Fusion : FusionGDB16520    16521    3747    40688    41366    5718    8109   
HNRNPA1--RBBP8    JA040723--HNRNPA1    JA040725--HNRNPA1    KRT13--HNRNPA1    SMN1--HNRNPA1    TTC13--HNRNPA1    VAT1--HNRNPA1   
Fusion : QuiverHNRNPA1
Polymorphisms : SNP and Copy number variants
NCBI Variation ViewerHNRNPA1 [hg38]
dbSNP Single Nucleotide Polymorphism (NCBI)HNRNPA1
Exome Variant ServerHNRNPA1
ExAC (Exome Aggregation Consortium)ENSG00000135486
GNOMAD BrowserENSG00000135486
Varsome BrowserHNRNPA1
Genetic variants : HAPMAP3178
Genomic Variants (DGV)HNRNPA1 [DGVbeta]
DECIPHERHNRNPA1 [patients]   [syndromes]   [variants]   [genes]  
CONAN: Copy Number AnalysisHNRNPA1 
ICGC Data PortalHNRNPA1 
TCGA Data PortalHNRNPA1 
Broad Tumor PortalHNRNPA1
OASIS PortalHNRNPA1 [ Somatic mutations - Copy number]
Somatic Mutations in Cancer : COSMICHNRNPA1  [overview]  [genome browser]  [tissue]  [distribution]  
Somatic Mutations in Cancer : COSMIC3DHNRNPA1
Mutations and Diseases : HGMDHNRNPA1
LOVD (Leiden Open Variation Database)Whole genome datasets
LOVD (Leiden Open Variation Database)LOVD 3.0 shared installation
BioMutasearch HNRNPA1
DgiDB (Drug Gene Interaction Database)HNRNPA1
DoCM (Curated mutations)HNRNPA1 (select the gene name)
CIViC (Clinical Interpretations of Variants in Cancer)HNRNPA1 (select a term)
NCG5 (London)HNRNPA1
Cancer3DHNRNPA1(select the gene name)
Impact of mutations[PolyPhen2] [Provean] [Buck Institute : MutDB] [Mutation Assessor] [Mutanalyser]
OMIM164017    615424    615426   
Orphanet106    10698   
Genetic Testing Registry HNRNPA1
NextProtP09651 [Medical]
Target ValidationHNRNPA1
Huge Navigator HNRNPA1 [HugePedia]
snp3D : Map Gene to Disease3178
Clinical trials, drugs, therapy
Chemical/Protein Interactions : CTD3178
Chemical/Pharm GKB GenePA162391113
Clinical trialHNRNPA1
canSAR (ICR)HNRNPA1 (select the gene name)
DataMed IndexHNRNPA1
PubMed330 Pubmed reference(s) in Entrez
GeneRIFsGene References Into Functions (Entrez)
REVIEW articlesautomatic search in PubMed
Last year publicationsautomatic search in PubMed

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indexed on : Wed Nov 13 21:27:29 CET 2019

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