HNRNPA1 | ENSG00000135486 | NCBI 3178

Cell ID: Standard Cell Ontology term used for mapping and comparing cells across experiments. Ensures consistency in analyzing cellular functions across tissues.
Fold Change: Represents the ratio of the current Cell Significance Index to the Cell Significance Index Threshold, indicating how much the gene expression has changed compared to a baseline.
Cell Significance Index: Reflects how strongly a gene is expressed in this specific cell.

Network Configuration

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Other Information

This section provides additional information about the gene, including a description generated by an AI language model and details about associated proteins.

Description
Proteins

## Summary [HNRNPA1](/details-gene/3178) encodes the heterogeneous nuclear ribonucleoprotein A1, a highly abundant, multifunctional RNA-binding protein. It is fundamentally involved in the processing and metabolism of RNA, playing critical roles in pre-mRNA splicing, mRNA transport from the nucleus to the cytoplasm, and telomere maintenance. Expression data indicates that **Overall**, [HNRNPA1](/details-gene/3178) is a key functional component in highly proliferative and transcriptionally active cells, particularly within the hematopoietic system. It shows the highest significance in [hematopoietic stem cells](/details-cell/CL0000037), various progenitor cells, and both innate and adaptive lymphocytes, such as [central memory CD8-positive, alpha-beta T cells](/details-cell/CL0000907). Mutations in this gene are associated with neurological disorders, including amyotrophic lateral sclerosis and multisystem proteinopathy ([164017](https://omim.org/entry/164017)). ## Cellular Roles and Expression Landscape The expression profile of [HNRNPA1](/details-gene/3178) highlights its indispensable role in the development and function of the hematopoietic and immune systems. **Overall**, it exhibits its highest significance scores in progenitor populations, including [hematopoietic stem cells](/details-cell/CL0000037) (CSI: 139.86), [common myeloid progenitors](/details-cell/CL0000049) (CSI: 112.76), and [pro-B cells](/details-cell/CL0000826) (CSI: 106.09). This suggests a foundational role in regulating the complex transcriptional and post-transcriptional programs that govern cell fate decisions and differentiation within these lineages. Beyond progenitors, [HNRNPA1](/details-gene/3178) is also highly significant in mature, active immune cells. It is a prominent marker in both naive and memory T cell populations, such as [central memory CD8-positive, alpha-beta T cell](/details-cell/CL0000907) (CSI: 121.46) and [naive thymus-derived CD8-positive, alpha-beta T cell](/details-cell/CL0000900) (CSI: 106.36), as well as in innate lymphocytes like [group 3 innate lymphoid cells](/details-cell/CL0001071) (CSI: 104.19) and natural killer cells. This broad expression across diverse and dynamic immune cell types underscores its continuous requirement for maintaining cellular function through RNA processing. Conversely, the gene's significance is markedly low in terminally differentiated and structurally specialized cell types. For instance, it is a strong anti-marker in [pulmonary capillary endothelial cells](/details-cell/CL4028001) (CSI: -48.97), various neurons like [inhibitory interneurons](/details-cell/CL0000498) (CSI: -21.88), and hepatocytes. This pattern suggests a specialized function for [HNRNPA1](/details-gene/3178) in contexts requiring high levels of cellular proliferation, differentiation, and transcriptional plasticity, rather than in maintaining the function of static, mature tissues. ## Pathways and Molecular Function The functions of [HNRNPA1](/details-gene/3178) are centered on RNA biology, consistent with its role as a core component of the ribonucleoprotein complex ([GO:1990904](https://www.ebi.ac.uk/QuickGO/term/GO:1990904)). It is a key player in the [Metabolism of RNA](/details-gene/R-HSA-8953854), particularly in pathways related to mRNA processing. Its involvement in [mRNA splicing, via spliceosome](/details-gene/GO:0000398) and its regulation ([GO:0000381](https://www.ebi.ac.uk/QuickGO/term/GO:0000381)) is well-defined, being a component of the spliceosomal complex ([GO:0005681](https://www.ebi.ac.uk/QuickGO/term/GO:0005681)). This function is critical in the hematopoietic cells where it is highly expressed, as alternative splicing is essential for generating the protein diversity required for immune cell differentiation and function. [HNRNPA1](/details-gene/3178) also facilitates the movement of molecules between the nucleus and cytoplasm, participating in both [import into nucleus](/details-gene/GO:0051170) and [RNA export from nucleus](/details-gene/GO:0006405). This shuttling capability, mediated by distinct nuclear localization and export signals ([Link](https://doi.org/10.1083/jcb.129.3.551); [Link](https://doi.org/10.1016/0092-8674(95)90119-1)), is vital for controlling gene expression by regulating the accessibility of mature mRNAs to the translation machinery in the cytoplasm. Furthermore, it is involved in telomere maintenance through its ability to bind G-rich strand telomeric DNA ([GO:0098505](https://www.ebi.ac.uk/QuickGO/term/GO:0098505)) and telomeric repeat-containing RNA ([GO:0061752](https://www.ebi.ac.uk/QuickGO/term/GO:0061752)). Interestingly, functional annotation also implicates [HNRNPA1](/details-gene/3178) in host-pathogen interactions, particularly in the context of [SARS-CoV infections](/details-gene/R-HSA-9679506). Research has shown that the SARS coronavirus nucleocapsid protein binds with high affinity to human [HNRNPA1](/details-gene/3178), suggesting the virus may co-opt this host protein to facilitate its replication cycle ([Link](https://doi.org/10.1016/j.febslet.2005.03.080)). ## Research Directions The widespread and critical functions of [HNRNPA1](/details-gene/3178) in RNA biology, coupled with its specific expression pattern, suggest several avenues for future research. **Proposed Hypotheses:** 1. Given its high significance in hematopoietic precursors and its core role in alternative splicing, it is hypothesized that [HNRNPA1](/details-gene/3178) acts as a master regulator of lineage-specific splicing events that are critical for the commitment of [hematopoietic stem cells](/details-cell/CL0000037) into either lymphoid or myeloid fates. 2. Based on its interaction with the SARS-CoV nucleocapsid protein, we hypothesize that [HNRNPA1](/details-gene/3178) is a pivotal host factor for viral replication, where its RNA export function is hijacked by the virus to facilitate the efficient transport of viral genomic RNA from the nucleus to the cytoplasm for packaging into new virions. 3. The dual involvement of [HNRNPA1](/details-gene/3178) in both positive ([GO:0032212](https://www.ebi.ac.uk/QuickGO/term/GO:0032212)) and negative ([GO:0032211](https://www.ebi.ac.uk/QuickGO/term/GO:0032211)) regulation of telomere maintenance suggests it acts as a molecular switch. We hypothesize that post-translational modifications of [HNRNPA1](/details-gene/3178) dictate its regulatory role at the telomere, thereby controlling cellular senescence and proliferation in long-lived cells like [hematopoietic stem cells](/details-cell/CL0000037). **Experimental Approach:** To test the first hypothesis regarding its role in hematopoietic lineage commitment, a conditional knockout of [HNRNPA1](/details-gene/3178) could be generated in murine hematopoietic stem and progenitor cells (HSPCs). These modified HSPCs would then be cultured *in vitro* under conditions that promote differentiation towards myeloid and lymphoid lineages. Cell fate decisions could be tracked using flow cytometry for lineage-specific markers, while parallel single-cell RNA sequencing (scRNA-seq) would be performed to comprehensively map changes in the transcriptome and, crucially, to identify global alterations in alternative splicing patterns associated with differentiation defects. **Therapeutic Potential:** As a ubiquitously expressed and essential gene, direct systemic inhibition of [HNRNPA1](/details-gene/3178) would likely cause significant toxicity. However, its role in aberrant splicing is frequently implicated in various cancers. Therefore, it represents a potential therapeutic target for strategies aimed at modulating specific splicing events rather than broad inhibition. For example, developing small molecules or antisense oligonucleotides that disrupt the interaction of [HNRNPA1](/details-gene/3178) with specific oncogenic pre-mRNAs could offer a more targeted therapeutic window. This inhibition-based approach would aim to correct pathological splicing patterns that drive malignancy.

Disclaimer: This in-silico analysis is generated by an AI language model and may contain inaccuracies or hallucinations. However, it is cross-referenced with curated gene expression data from major biological sources. Please verify the information before use.

Heterogeneous nuclear ribonucleoprotein A1
A0A024RB53_HUMAN

Genular Protein ID: 1882053567

Symbol: ROA1_HUMAN

Name: Heterogeneous nuclear ribonucleoprotein A1

UniProtKB Accession Codes:

P09651 A8K4Z8 Q3MIB7 Q6PJZ7

Database IDs:

Citations:

PubMed ID: 2760922

Title: Isolation of an active gene encoding human hnRNP protein A1. Evidence for alternative splicing.

PubMed ID: 2760922

DOI: 10.1016/0022-2836(89)90459-2

PubMed ID: 2836799

Title: cDNA cloning of human hnRNP protein A1 reveals the existence of multiple mRNA isoforms.

PubMed ID: 2836799

DOI: 10.1093/nar/16.9.3751

PubMed ID: 14702039

Title: Complete sequencing and characterization of 21,243 full-length human cDNAs.

PubMed ID: 14702039

DOI: 10.1038/ng1285

PubMed ID: 16541075

Title: The finished DNA sequence of human chromosome 12.

PubMed ID: 16541075

DOI: 10.1038/nature04569

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

PubMed ID: 3023065

Title: Mammalian single-stranded DNA binding protein UP I is derived from the hnRNP core protein A1.

PubMed ID: 3023065

DOI: 10.1002/j.1460-2075.1986.tb04494.x

PubMed ID: 1691095

Title: Alternative splicing in the human gene for the core protein A1 generates another hnRNP protein.

PubMed ID: 1691095

DOI: 10.1002/j.1460-2075.1990.tb08230.x

PubMed ID: 7730395

Title: A nuclear localization domain in the hnRNP A1 protein.

PubMed ID: 7730395

DOI: 10.1083/jcb.129.3.551

PubMed ID: 8521471

Title: A nuclear export signal in hnRNP A1: a signal-mediated, temperature-dependent nuclear protein export pathway.

PubMed ID: 8521471

DOI: 10.1016/0092-8674(95)90119-1

PubMed ID: 7769000

Title: Nucleo-cytoplasmic distribution of human hnRNP proteins: a search for the targeting domains in hnRNP A1.

PubMed ID: 7769000

DOI: 10.1242/jcs.108.2.545

PubMed ID: 11991638

Title: Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis.

PubMed ID: 11991638

DOI: 10.1017/s1355838202021088

PubMed ID: 15782174

Title: Identifying and quantifying in vivo methylation sites by heavy methyl SILAC.

PubMed ID: 15782174

DOI: 10.1038/nmeth715

PubMed ID: 15161980

Title: Sumoylation of heterogeneous nuclear ribonucleoproteins, zinc finger proteins, and nuclear pore complex proteins: a proteomic analysis.

PubMed ID: 15161980

DOI: 10.1073/pnas.0402889101

PubMed ID: 16111636

Title: The Mnks are novel components in the control of TNF alpha biosynthesis and phosphorylate and regulate hnRNP A1.

PubMed ID: 16111636

DOI: 10.1016/j.immuni.2005.06.009

PubMed ID: 15862300

Title: The nucleocapsid protein of SARS coronavirus has a high binding affinity to the human cellular heterogeneous nuclear ribonucleoprotein A1.

PubMed ID: 15862300

DOI: 10.1016/j.febslet.2005.03.080

PubMed ID: 17081983

Title: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.

PubMed ID: 17081983

DOI: 10.1016/j.cell.2006.09.026

PubMed ID: 17371836

Title: The RNA-binding protein Sam68 modulates the alternative splicing of Bcl-x.

PubMed ID: 17371836

DOI: 10.1083/jcb.200701005

PubMed ID: 17924679

Title: Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.

PubMed ID: 17924679

DOI: 10.1021/pr070152u

PubMed ID: 17229681

Title: An RNA-binding protein, hnRNP A1, and a scaffold protein, septin 6, facilitate hepatitis C virus replication.

PubMed ID: 17229681

DOI: 10.1128/jvi.01311-06

PubMed ID: 17289661

Title: Molecular composition of IMP1 ribonucleoprotein granules.

PubMed ID: 17289661

DOI: 10.1074/mcp.m600346-mcp200

PubMed ID: 19367720

Title: Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment.

PubMed ID: 19367720

DOI: 10.1021/pr800500r

PubMed ID: 18669648

Title: A quantitative atlas of mitotic phosphorylation.

PubMed ID: 18669648

DOI: 10.1073/pnas.0805139105

PubMed ID: 19413330

Title: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.

PubMed ID: 19413330

DOI: 10.1021/ac9004309

PubMed ID: 19690332

Title: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.

PubMed ID: 19690332

DOI: 10.1126/scisignal.2000007

PubMed ID: 19608861

Title: Lysine acetylation targets protein complexes and co-regulates major cellular functions.

PubMed ID: 19608861

DOI: 10.1126/science.1175371

PubMed ID: 20010808

Title: HnRNP proteins controlled by c-Myc deregulate pyruvate kinase mRNA splicing in cancer.

PubMed ID: 20010808

DOI: 10.1038/nature08697

PubMed ID: 20068231

Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.

PubMed ID: 20068231

DOI: 10.1126/scisignal.2000475

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

PubMed ID: 21406692

Title: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.

PubMed ID: 21406692

DOI: 10.1126/scisignal.2001570

PubMed ID: 22814378

Title: N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.

PubMed ID: 22814378

DOI: 10.1073/pnas.1210303109

PubMed ID: 23186163

Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.

PubMed ID: 23186163

DOI: 10.1021/pr300630k

PubMed ID: 24549040

Title: C9ORF72, implicated in amytrophic lateral sclerosis and frontotemporal dementia, regulates endosomal trafficking.

PubMed ID: 24549040

DOI: 10.1093/hmg/ddu068

PubMed ID: 24275569

Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.

PubMed ID: 24275569

DOI: 10.1016/j.jprot.2013.11.014

PubMed ID: 24129315

Title: Immunoaffinity enrichment and mass spectrometry analysis of protein methylation.

PubMed ID: 24129315

DOI: 10.1074/mcp.o113.027870

PubMed ID: 25678563

Title: Peptidylprolyl isomerase A governs TARDBP function and assembly in heterogeneous nuclear ribonucleoprotein complexes.

PubMed ID: 25678563

DOI: 10.1093/brain/awv005

PubMed ID: 25755297

Title: System-wide analysis of SUMOylation dynamics in response to replication stress reveals novel small ubiquitin-like modified target proteins and acceptor lysines relevant for genome stability.

PubMed ID: 25755297

DOI: 10.1074/mcp.o114.044792

PubMed ID: 25944712

Title: N-terminome analysis of the human mitochondrial proteome.

PubMed ID: 25944712

DOI: 10.1002/pmic.201400617

PubMed ID: 28431233

Title: A Compendium of RNA-Binding Proteins that Regulate MicroRNA Biogenesis.

PubMed ID: 28431233

DOI: 10.1016/j.molcel.2017.03.014

PubMed ID: 28985503

Title: A Peptide Encoded by a Putative lncRNA HOXB-AS3 Suppresses Colon Cancer Growth.

PubMed ID: 28985503

DOI: 10.1016/j.molcel.2017.09.015

PubMed ID: 28112733

Title: Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation.

PubMed ID: 28112733

DOI: 10.1038/nsmb.3366

PubMed ID: 31498791

Title: EV71 3C protease induces apoptosis by cleavage of hnRNP A1 to promote apaf-1 translation.

PubMed ID: 31498791

DOI: 10.1371/journal.pone.0221048

PubMed ID: 33360543

Title: Overexpression of SARS-CoV-2 protein ORF6 dislocates RAE1 and NUP98 from the nuclear pore complex.

PubMed ID: 33360543

DOI: 10.1016/j.bbrc.2020.11.115

PubMed ID: 2176620

Title: Modeling by homology of RNA binding domain in A1 hnRNP protein.

PubMed ID: 2176620

DOI: 10.1016/0014-5793(90)80863-e

PubMed ID: 9164463

Title: Crystal structure of the two RNA binding domains of human hnRNP A1 at 1.75-A resolution.

PubMed ID: 9164463

DOI: 10.1038/nsb0397-215

PubMed ID: 9115444

Title: Crystal structure of human UP1, the domain of hnRNP A1 that contains two RNA-recognition motifs.

PubMed ID: 9115444

DOI: 10.1016/s0969-2126(97)00211-6

PubMed ID: 23455423

Title: Mutations in prion-like domains in hnRNPA2B1 and hnRNPA1 cause multisystem proteinopathy and ALS.

PubMed ID: 23455423

DOI: 10.1038/nature11922

PubMed ID: 25616961

Title: ALS-linked mutations in ubiquilin-2 or hnRNPA1 reduce interaction between ubiquilin-2 and hnRNPA1.

PubMed ID: 25616961

DOI: 10.1093/hmg/ddv020

PubMed ID: 27694260

Title: Whole-exome sequencing identifies a missense mutation in hnRNPA1 in a family with flail arm ALS.

PubMed ID: 27694260

DOI: 10.1212/wnl.0000000000003256

PubMed ID: 34722876

Title: Dominant Distal Myopathy 3 (MPD3) Caused by a Deletion in the HNRNPA1 Gene.

PubMed ID: 34722876

DOI: 10.1212/nxg.0000000000000632

Sequence Information:

Length: 372
Mass: 38747
Checksum: A06683571C6C109F
Sequence:

MSKSESPKEP EQLRKLFIGG LSFETTDESL RSHFEQWGTL TDCVVMRDPN TKRSRGFGFV 
TYATVEEVDA AMNARPHKVD GRVVEPKRAV SREDSQRPGA HLTVKKIFVG GIKEDTEEHH 
LRDYFEQYGK IEVIEIMTDR GSGKKRGFAF VTFDDHDSVD KIVIQKYHTV NGHNCEVRKA 
LSKQEMASAS SSQRGRSGSG NFGGGRGGGF GGNDNFGRGG NFSGRGGFGG SRGGGGYGGS 
GDGYNGFGND GGYGGGGPGY SGGSRGYGSG GQGYGNQGSG YGGSGSYDSY NNGGGGGFGG 
GSGSNFGGGG SYNDFGNYNN QSSNFGPMKG GNFGGRSSGP YGGGGQYFAK PRNQGGYGGS 
SSSSSYGSGR RF

Genular Protein ID: 96568368

Symbol: A0A024RB53_HUMAN

Name: N/A

UniProtKB Accession Codes:

A0A024RB53

Database IDs:

Sequence Information:

Length: 320
Mass: 34196
Checksum: 59485C9FA1FF8AE1
Sequence:

MSKSESPKEP EQLRKLFIGG LSFETTDESL RSHFEQWGTL TDCVVMRDPN TKRSRGFGFV 
TYATVEEVDA AMNARPHKVD GRVVEPKRAV SREDSQRPGA HLTVKKIFVG GIKEDTEEHH 
LRDYFEQYGK IEVIEIMTDR GSGKKRGFAF VTFDDHDSVD KIVIQKYHTV NGHNCEVRKA 
LSKQEMASAS SSQRGRSGSG NFGGGRGGGF GGNDNFGRGG NFSGRGGFGG SRGGGGYGGS 
GDGYNGFGND GSNFGGGGSY NDFGNYNNQS SNFGPMKGGN FGGRSSGPYG GGGQYFAKPR 
NQGGYGGSSS SSSYGSGRRF

	Overall overall
	Acute kidney failure MONDO0002492
	Adrenal gland UBERON0002369
	Ascending colon UBERON0001156
	\|— Ascending colon Healthy UBERON0001156_PATO0000461
	Axilla UBERON0009472
	Basal cell carcinoma MONDO0020804
	Blood UBERON0000178
	\|— Blood COVID-19 UBERON0000178_MONDO0100096
	\|— Blood Cytomegalovirus infection UBERON0000178_MONDO0005132
	\|— Blood Healthy UBERON0000178_PATO0000461
	Body of stomach UBERON0001161
	Bone marrow UBERON0002371
	\|— Bone marrow Healthy UBERON0002371_PATO0000461
	Brain UBERON0000955
	\|— Brain Healthy UBERON0000955_PATO0000461
	Breast UBERON0000310
	\|— Breast Healthy UBERON0000310_PATO0000461
	\|— Breast cancer MONDO0007254
	Bronchus UBERON0002185
	Caecum UBERON0001153
	\|— Caecum Healthy UBERON0001153_PATO0000461
	Caudate lobe of liver UBERON0001117
	Cerebellum UBERON0002037
	\|— Cerebellum Healthy UBERON0002037_PATO0000461
	Cerebral cortex UBERON0000956
	\|— Cerebral cortex Healthy UBERON0000956_PATO0000461
	Cerebrospinal fluid UBERON0001359
	Chronic kidney disease MONDO0005300
	Colon UBERON0001155
	\|— Colon Healthy UBERON0001155_PATO0000461
	\|— Colonic epithelium UBERON0000397
	\|— Colonic epithelium Healthy UBERON0000397_PATO0000461
	Colorectal cancer MONDO0005575
	Colorectum UBERON0012652
	Cortex of kidney UBERON0001225
	\|— Cortex of kidney Healthy UBERON0001225_PATO0000461
	COVID-19 MONDO0100096
	Crohn disease MONDO0005011
	Cytomegalovirus infection MONDO0005132
	Dental pulp UBERON0001754
	Dorsolateral prefrontal cortex UBERON0009834
	\|— Dorsolateral prefrontal cortex Healthy UBERON0009834_PATO0000461
	Duodenum UBERON0002114
	\|— Duodenum Healthy UBERON0002114_PATO0000461
	Fallopian tube UBERON0003889
	Fovea centralis UBERON0001786
	\|— Fovea centralis Healthy UBERON0001786_PATO0000461
	Frontal cortex UBERON0001870
	Glioblastoma MONDO0018177
	Healthy PATO0000461
	Heart left ventricle UBERON0002084
	\|— Heart left ventricle Healthy UBERON0002084_PATO0000461
	Heart right ventricle UBERON0002080
	\|— Heart right ventricle Healthy UBERON0002080_PATO0000461
	Hippocampal formation UBERON0002421
	\|— Hippocampal formation Healthy UBERON0002421_PATO0000461
	Hypothalamus UBERON0001898
	\|— Hypothalamus Healthy UBERON0001898_PATO0000461
	Ileal epithelium UBERON0008345
	Ileum UBERON0002116
	\|— Ileum Healthy UBERON0002116_PATO0000461
	\|— Ileum lamina propria UBERON8600035
	Islet of Langerhans UBERON0000006
	Isolated focal cortical dysplasia type II MONDO0011818
	Kidney UBERON0002113
	\|— Kidney Healthy UBERON0002113_PATO0000461
	Lamina propria of small intestine UBERON0001238
	Liver UBERON0002107
	\|— Liver Breast cancer UBERON0002107_MONDO0007254
	\|— Liver Healthy UBERON0002107_PATO0000461
	Lung UBERON0002048
	\|— Lung Healthy UBERON0002048_PATO0000461
	\|— Lung Renal cell carcinoma UBERON0002048_MONDO0005086
	\|— Lung adenocarcinoma MONDO0005061
	\|— Lung parenchyma UBERON0008946
	Lymph node UBERON0000029
	\|— Lymph node Healthy UBERON0000029_PATO0000461
	\|— Lymph node Metastatic melanoma UBERON0000029_MONDO0005191
	Malignant ovarian serous tumor MONDO0024885
	Medial orbital frontal cortex UBERON0022352
	Mesenteric lymph node UBERON0002509
	\|— Mesenteric lymph node Healthy UBERON0002509_PATO0000461
	Metastatic melanoma MONDO0005191
	Midbrain UBERON0001891
	\|— Midbrain Healthy UBERON0001891_PATO0000461
	Middle lobe of right lung UBERON0002174
	Nasopharynx UBERON0001728
	Neuroblastoma MONDO0005072
	Nonpapillary renal cell carcinoma MONDO0007763
	Ovary UBERON0000992
	\|— Ovary Healthy UBERON0000992_PATO0000461
	Pancreas UBERON0001264
	\|— Pancreas Healthy UBERON0001264_PATO0000461
	Peripheral region of retina UBERON0013682
	\|— Peripheral region of retina Healthy UBERON0013682_PATO0000461
	Pleural effusion UBERON0000175
	Pons UBERON0000988
	\|— Pons Healthy UBERON0000988_PATO0000461
	Primary motor cortex UBERON0001384
	Prostate gland UBERON0002367
	Renal cell carcinoma MONDO0005086
	Renal medulla UBERON0000362
	\|— Renal medulla Healthy UBERON0000362_PATO0000461
	Respiratory airway UBERON0001005
	\|— Respiratory airway COVID-19 UBERON0001005_MONDO0100096
	Retina UBERON0000966
	\|— Retina Healthy UBERON0000966_PATO0000461
	Sigmoid colon UBERON0001159
	\|— Sigmoid colon Healthy UBERON0001159_PATO0000461
	Skin of body UBERON0002097
	\|— Skin of body Healthy UBERON0002097_PATO0000461
	Small cell lung carcinoma MONDO0008433
	Small intestine UBERON0002108
	\|— Small intestine Healthy UBERON0002108_PATO0000461
	Spleen UBERON0002106
	\|— Spleen Healthy UBERON0002106_PATO0000461
	Stomach UBERON0000945
	\|— Stomach Healthy UBERON0000945_PATO0000461
	Telencephalon UBERON0001893
	\|— Telencephalon Healthy UBERON0001893_PATO0000461
	Thymus UBERON0002370
	\|— Thymus Healthy UBERON0002370_PATO0000461
	Trachea UBERON0003126
	Transverse colon UBERON0001157
	\|— Transverse colon Healthy UBERON0001157_PATO0000461
	Upper lobe of left lung UBERON0008952

Details for: HNRNPA1

Cell Significance Landscape

Associated with

Significant Cells

Network Configuration

Legend:

Other Information

Isolation of an active gene encoding human hnRNP protein A1. Evidence for alternative splicing. PubMed ID: 2760922

cDNA cloning of human hnRNP protein A1 reveals the existence of multiple mRNA isoforms. PubMed ID: 2836799

Complete sequencing and characterization of 21,243 full-length human cDNAs. PubMed ID: 14702039

The finished DNA sequence of human chromosome 12. PubMed ID: 16541075

The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). PubMed ID: 15489334

Mammalian single-stranded DNA binding protein UP I is derived from the hnRNP core protein A1. PubMed ID: 3023065

Alternative splicing in the human gene for the core protein A1 generates another hnRNP protein. PubMed ID: 1691095

A nuclear localization domain in the hnRNP A1 protein. PubMed ID: 7730395

A nuclear export signal in hnRNP A1: a signal-mediated, temperature-dependent nuclear protein export pathway. PubMed ID: 8521471

Nucleo-cytoplasmic distribution of human hnRNP proteins: a search for the targeting domains in hnRNP A1. PubMed ID: 7769000

Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis. PubMed ID: 11991638

Identifying and quantifying in vivo methylation sites by heavy methyl SILAC. PubMed ID: 15782174

Sumoylation of heterogeneous nuclear ribonucleoproteins, zinc finger proteins, and nuclear pore complex proteins: a proteomic analysis. PubMed ID: 15161980

The Mnks are novel components in the control of TNF alpha biosynthesis and phosphorylate and regulate hnRNP A1. PubMed ID: 16111636

The nucleocapsid protein of SARS coronavirus has a high binding affinity to the human cellular heterogeneous nuclear ribonucleoprotein A1. PubMed ID: 15862300

Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. PubMed ID: 17081983

The RNA-binding protein Sam68 modulates the alternative splicing of Bcl-x. PubMed ID: 17371836

Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra. PubMed ID: 17924679

An RNA-binding protein, hnRNP A1, and a scaffold protein, septin 6, facilitate hepatitis C virus replication. PubMed ID: 17229681

Molecular composition of IMP1 ribonucleoprotein granules. PubMed ID: 17289661

Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment. PubMed ID: 19367720

A quantitative atlas of mitotic phosphorylation. PubMed ID: 18669648

Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. PubMed ID: 19413330

Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. PubMed ID: 19690332

Lysine acetylation targets protein complexes and co-regulates major cellular functions. PubMed ID: 19608861

HnRNP proteins controlled by c-Myc deregulate pyruvate kinase mRNA splicing in cancer. PubMed ID: 20010808

Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis. PubMed ID: 20068231

Initial characterization of the human central proteome. PubMed ID: 21269460

System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation. PubMed ID: 21406692

N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB. PubMed ID: 22814378

Toward a comprehensive characterization of a human cancer cell phosphoproteome. PubMed ID: 23186163

C9ORF72, implicated in amytrophic lateral sclerosis and frontotemporal dementia, regulates endosomal trafficking. PubMed ID: 24549040

An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. PubMed ID: 24275569

Immunoaffinity enrichment and mass spectrometry analysis of protein methylation. PubMed ID: 24129315

Peptidylprolyl isomerase A governs TARDBP function and assembly in heterogeneous nuclear ribonucleoprotein complexes. PubMed ID: 25678563

System-wide analysis of SUMOylation dynamics in response to replication stress reveals novel small ubiquitin-like modified target proteins and acceptor lysines relevant for genome stability. PubMed ID: 25755297

N-terminome analysis of the human mitochondrial proteome. PubMed ID: 25944712

A Compendium of RNA-Binding Proteins that Regulate MicroRNA Biogenesis. PubMed ID: 28431233

A Peptide Encoded by a Putative lncRNA HOXB-AS3 Suppresses Colon Cancer Growth. PubMed ID: 28985503

Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation. PubMed ID: 28112733

EV71 3C protease induces apoptosis by cleavage of hnRNP A1 to promote apaf-1 translation. PubMed ID: 31498791

Overexpression of SARS-CoV-2 protein ORF6 dislocates RAE1 and NUP98 from the nuclear pore complex. PubMed ID: 33360543

Modeling by homology of RNA binding domain in A1 hnRNP protein. PubMed ID: 2176620

Crystal structure of the two RNA binding domains of human hnRNP A1 at 1.75-A resolution. PubMed ID: 9164463

Crystal structure of human UP1, the domain of hnRNP A1 that contains two RNA-recognition motifs. PubMed ID: 9115444

Mutations in prion-like domains in hnRNPA2B1 and hnRNPA1 cause multisystem proteinopathy and ALS. PubMed ID: 23455423

ALS-linked mutations in ubiquilin-2 or hnRNPA1 reduce interaction between ubiquilin-2 and hnRNPA1. PubMed ID: 25616961

Whole-exome sequencing identifies a missense mutation in hnRNPA1 in a family with flail arm ALS. PubMed ID: 27694260

Dominant Distal Myopathy 3 (MPD3) Caused by a Deletion in the HNRNPA1 Gene. PubMed ID: 34722876