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AQP4 (aquaporin 4)

Written2012-12Domenico Ribatti, Beatrice Nico
Department of Basic Medical Sciences, Neurosciences, Sensory Organs, University of Bari Medical School, Bari, Italy

(Note : for Links provided by Atlas : click)


HGNC (Hugo) AQP4
HGNC Alias symbMIWC
LocusID (NCBI) 361
Atlas_Id 684
Location 18q11.2  [Link to chromosome band 18q11]
Location_base_pair Starts at 26852038 and ends at 26862910 bp from pter ( according to GRCh38/hg38-Dec_2013)  [Mapping AQP4.png]
Fusion genes
(updated 2017)
Data from Atlas, Mitelman, Cosmic Fusion, Fusion Cancer, TCGA fusion databases with official HUGO symbols (see references in chromosomal bands)
AQP4 (18q11.2)::AQP4 (18q11.2)SYT1 (12q21.2)::AQP4 (18q11.2)


Description Sequence length: 323 AA.
Total number of exons: 5.


Description This gene encodes a member of the aquaporin family of intrinsic membrane proteins that function as water-selective channels in the plasma membranes of many cells. The encoded protein is the predominant aquaporin found in brain. Two alternatively spliced transcript variants encoding distinct isoforms have been found for this gene.
Subunit structure: homotetramer. Part of a complex containing MLC1, TRPV4, HEPACAM and ATP1B1.
Domain: contains two tandem repeats each containing three membrane-spanning domains and a pore-forming loop with the signature motiv Asn-Pro-Ala (NPA).
Post-translational modification: phosphorylation by PKC at Ser-180 reduces conductance by 50%. Phosphorylation by PKG at Ser-111 in response to glutamates increases conductance by 40%.
Structure: AQP4, a small 30-kDa monomer, is a hydrophobic transmembrane protein with cytosolic amino and carboxy terminal ends (Verkman, 2005). The molecule spans the cell membrane 6 times, forming 5 interhelical loops designated as A, C, and E on the extracellular surface and B and D on the intracellular surface. A consistent 3-amino acid hydrophobic motif, asparginine-proline-alanine (NPA), is present in both the B and E loops. Each monomer folds into a structure that forms an independent water channel, characterized by wide external openings and a narrow central constriction where the NPA motifs interact. AQP4 monomers assemble into tetramers, with each monomer being individually functional. Water movement through the channel is governed by an osmotic gradient across the membrane, with flow limited by size restriction and electrostatic repulsion.
Variants: AQP4 occurs in mainly two splices variants, the M1 and M23 isoform (Jung et al., 1994). M23 forms higher order assemblies within the plasma membrane, termed orthogonal arrays of particles (OAPs), whereas M1 exists as individuals tetramers. Phosphorylation of AQP4 can also regulate array formation.
Expression In the brain, AQP-4 is expressed at the glia limitans everywhere, ependymal lining, cerebellum, hippocampal dentate gyrus, and in the supraoptic and paraventricular nuclei of the hypothalamus. Low AQP-4 expression has also been found in the neocortex, hippocampal areas, nucleus of the stria terminalis, and the medial habenular nucleus (Venero et al., 1999). AQP-4 is expressed in a polarized way by astrocytic foot processes at the borders between major water compartments and the brain parenchyma (Nielsen et al., 1997; Rash et al., 1998). The perivascular expression of AQP4 coincides with the K+ channel protein Kir 4.1 at blood-brain barrier (BBB) level (Nagelhus et al., 1999).
Localisation Subcellular localization: membrane; multi-pass membrane protein.
Function AQP4 is implicated in the pathogenesis of normal pressure hydrocephalus, pseudotumor cerebri and cerebral edema (Badaut et al., 2002). AQP4-null mice have a much better outcome after water intoxication, meningitis and brain ischemia (Manley et al., 2004). AQP4-null mice have a significantly greater increase in brain water content and intracranial pressure than the wild-type mice, suggesting that brain water elimination is defective after AQP4 deletion (Papadopoulos et al., 2004a; Papadopoulos and Verkman, 2007). AQP4, by controlling the bidirectional water flux is responsible for the formation of cellular brain edema, but counteracts vasogenic edema (Saadoun et al., 2002). In vasogenic edema, AQP4 is thought to have a protective role, through brain water clearance, whereas in cytotoxic edema it is the main contributor to astrocytic cell swelling (Manley et al., 2004; Papadopoulos et al., 2004a; Papadopoulos et al., 2004 b). Water intoxicated AQP4-null mice show a significant reduction in astrocytic foot process swelling and a decrease in brain water content (Manley et al., 2000).
Nicchia et al. (2005) have shown that AQP-4 knockdown in rat and human cells was associated with a depolymerization of actin with a change of morphology characterized by a remarkable F-actin cytoskeleton rearrangement in AQP-4 knock-down mouse astrocytes. Moreover, AQP-4 can interact with α-syntrophin, a member rof the dystrophin-dystroglycan complex, indicating an involvement of AQP-4 protein in altering the cell cytoskeleton (Warth et al., 2004). Accordingly, Nico et al. have demonstrated that in the brain of mdx mouse, an animal model of the Duchenne muscular dystrophy, glial cells showed a significant reduction in both protein and mRNA content of the dystrophin-associated proteins (DAPs), including AQP-4, Kir 4.1, syntrophin and α-β-dystroglycan, coupled with a decrease in dystrophin isoform (Dp71) (Nico et al., 2010). Moreover, alterations of the vascular basement membrane and reduction of the expression of its components laminin and agrin and translocation of α-β-dystroglycan receptors in the glial cytoplasmic endfeet have been demonstrated (Nico et al., 2010).
Homology The AQP4 gene is conserved in chimpanzee, Rhesus monkey, dog, cow, mouse, rat, chicken, zebrafish, fruit fly, mosquito, M. oryzae, A. thaliana, and rice.

Implicated in

Entity Melanoma
Note Melanoma cells implanted into the striatum of wild type and AQP4-null mice produce peritumoral edema and comparable sized-tumors in both groups after a week. However, the AQP4-null mice have a higher intracerebral pressure and water content (Manley et al., 2004).
Entity Astrocytoma
Note AQP4 expression has also been demonstrated to be up-regulated in edematous astrocytomas and metastatic tumors (Saadoun et al., 2002). An increased AQP4 expression has been demonstrated in glioblastoma multiforme (GBM) together with loss of polarized expression around the vessels and an AQP4 redistribution in glioma cells (Warth et al., 2004; Warth et al., 2005; Warth et al., 2007). Warth et al. (2007) investigated grade I-IV glioma by immunohistochemistry and the prognostic significance for patients' survival. In gliomas, a remarkable de novo AQP4 redistribution was observed in comparison with normal central nervous system tissue. Moreover, the highest membranous staining levels were seen in pilocytic astrocytomas WHO grade I and grade IV glioblastomas, both significantly higher than in WHO grade II. AQP4 up-regulation was associated with brain edema formation and no association between survival and WHO grade-dependent AQP4 expression was seen. Moreover, in glioma cells co-localization of AQP4 with K+ channel protein Kir 4.1 is abolished and a mislocation of both Kir channels and AQP4 has been reported (Warth et al., 2007), suggesting that this molecular rearrangement occurs as a reaction to BBB damages, facilitating edema fluid flow. Mou et al. (2010) investigated changes of AQP4 protein expression in normal brain and in brain glioma tumor and peritumoral edematous tissues and analyzed the relationship of AQP-4 protein with edema index, VEGF and hypoxia inducible factor 1 alpha (HIF-1α) protein. They demonstrated that expression of AQP-4 was higher in the tumor and highest in the peritumor tissue. Moreover, AQP-4 protein in tumor tissue of gliomas of different grades was not statistically different. In normal brain tissues, AQP-4 was mainly expressed in the foot processes of astrocytes, but rare in the parenchyma. Finally, the degree of peritumoral edema positively correlated with the expression level of AQP-4 protein and this latter correlated with VEGF and HIF-1α expression. Nico et al. (2009) evaluated AQP4 expression and content in GBM and correlated with VEGF-VEGFR-2 expression. They demonstrated that in the relapse after chemotherapy and radiotherapy, AQP4 reduced in parallel with VEGF-VEGFR-2 expression as compared with primary tumors, and in the peripheral areas of relapsed tumors AQP4 mimicked normal findings of perivascular rearrangements. These data indicate that in GBM chemotherapy and radiotherapy induce a down-regulation in AQP4 expression restoring its perivascular rearrangement and suggest its potential role in the resolution of brain edema. Moreover, the normally polarized rearrangement of AQP4 in peripheral areas in tumor specimens obtained after combined chemotherapy and radiotherapy could be expression of a process of normalization of tumor blood vessels. Tumor implantation experiments into AQP4-null mice have demonstrated that these mice have an increased intracranial pressure than wild-type controls (Papadopoulos et al., 2004a; Papadopoulos et al., 2004b). McCoy et al. (2010) using D54MG glioma cells stably transfected with either AQP1 or AQP4 demonstrated that protein kinase C (PKC) activity regulates water permeability through phosphorylation of AQP4. Activation of PKC with either phorbol 12-myristate 13-acetate or thrombin enhanced AQP4 phosphorylation, reduced water permeability and significantly decreased tumor cell invasion. Conversely, inhibition of PKC activity with chlerythrine reduced AQP4 phosphorylation, enhanced water permeability and tumor cell invasion.
Entity Meningioma
Note Ng et al. (2009) demonstrated that overexpression of AQP4 in meningiomas was associated with significant peritumoral edema.
Entity Therapeutic perspectives
Note Inhibition of AQPs expression and/or AQP-mediated water influx by acetozolamide, cyclophosphamide, topiramate, thiopenthal, phenobarbital and propofol, affects cancer cell proliferation, migration, metastasis and angiogenic potential (Monzani et al., 2007).
Inhibition of AQP-4 expression (by small interference RNA technology) or their function (with a blocking antibody or a small inhibitory molecule) may result in increased intracellular acidosis and cytotoxicity and reduced invasive potential of glioma cells. Ding et al. (2011), using small interference RNA and a pharmaceutical inhibitor to knock down the expression of AQP-4, demonstrated a specific and massive impairment of glioblastoma cell migration and invasion in vitro and in vivo. Moreover, they showed that down-regulation of matrix metalloproteinase-2 (MMP-2) expression coincides with decreased cell invasive ability. Accordingly, Badaut et al. (2011) using RNA interference have demonstrated that brain water motility decreases after astrocyte AQP-4 inhibition.
Corticosteroids are largely used in combination with chemotherapy and contribute to significantly reduce peritumoral brain edema by decreasing the permeability of tumor vessels and/or enhance the clearance of extracellular water (Sinha et al., 2004). Animal experiments showed a decrease of cerebral AQP-4 protein expression upon dexamethasone treatment (Ron et al., 2005), suggesting that AQP-4 may be considered one of the major molecular targets of the well-functioning steroid treatment in brain edema formation. Moreover, corticosteroids reduced AQP-4 mRNA level in experimental brain tumor model and after intracerebral hemorrhage in rats (Heiss et al., 1996; Gu et al., 2007). The evidence that AQP-4 facilitates the migration of reactive astrocytes towards an injury site and the infiltration of malignant astrocytes in glioblastoma (Verkman et al., 2008) suggests that AQP-4 inhibitors may reduce reactive gliosis and infiltration of astrocytes.


Brain water mobility decreases after astrocytic aquaporin-4 inhibition using RNA interference.
Badaut J, Ashwal S, Adami A, Tone B, Recker R, Spagnoli D, Ternon B, Obenaus A.
J Cereb Blood Flow Metab. 2011 Mar;31(3):819-31. doi: 10.1038/jcbfm.2010.163. Epub 2010 Sep 29.
PMID 20877385
Aquaporins in brain: distribution, physiology, and pathophysiology.
Badaut J, Lasbennes F, Magistretti PJ, Regli L.
J Cereb Blood Flow Metab. 2002 Apr;22(4):367-78.
PMID 11919508
Role of aquaporin-4 in the regulation of migration and invasion of human glioma cells.
Ding T, Ma Y, Li W, Liu X, Ying G, Fu L, Gu F.
Int J Oncol. 2011 Jun;38(6):1521-31. doi: 10.3892/ijo.2011.983. Epub 2011 Mar 21.
PMID 21424125
Dexamethasone treatment modulates aquaporin-4 expression after intracerebral hemorrhage in rats.
Gu YT, Zhang H, Xue YX.
Neurosci Lett. 2007 Feb 14;413(2):126-31. Epub 2007 Jan 8.
PMID 17240062
Mechanism of dexamethasone suppression of brain tumor-associated vascular permeability in rats. Involvement of the glucocorticoid receptor and vascular permeability factor.
Heiss JD, Papavassiliou E, Merrill MJ, Nieman L, Knightly JJ, Walbridge S, Edwards NA, Oldfield EH.
J Clin Invest. 1996 Sep 15;98(6):1400-8.
PMID 8823305
Molecular characterization of an aquaporin cDNA from brain: candidate osmoreceptor and regulator of water balance.
Jung JS, Bhat RV, Preston GM, Guggino WB, Baraban JM, Agre P.
Proc Natl Acad Sci U S A. 1994 Dec 20;91(26):13052-6.
PMID 7528931
New insights into water transport and edema in the central nervous system from phenotype analysis of aquaporin-4 null mice.
Manley GT, Binder DK, Papadopoulos MC, Verkman AS.
Neuroscience. 2004;129(4):983-91.
PMID 15561413
Aquaporin-4 deletion in mice reduces brain edema after acute water intoxication and ischemic stroke.
Manley GT, Fujimura M, Ma T, Noshita N, Filiz F, Bollen AW, Chan P, Verkman AS.
Nat Med. 2000 Feb;6(2):159-63.
PMID 10655103
Water permeability through aquaporin-4 is regulated by protein kinase C and becomes rate-limiting for glioma invasion.
McCoy ES, Haas BR, Sontheimer H.
Neuroscience. 2010 Jul 28;168(4):971-81. doi: 10.1016/j.neuroscience.2009.09.020. Epub 2009 Sep 15.
PMID 19761816
The water channels, new druggable targets to combat cancer cell survival, invasiveness and metastasis.
Monzani E, Shtil AA, La Porta CA.
Curr Drug Targets. 2007 Oct;8(10):1132-7.
PMID 17979673
AQP-4 in peritumoral edematous tissue is correlated with the degree of glioma and with expression of VEGF and HIF-alpha.
Mou K, Chen M, Mao Q, Wang P, Ni R, Xia X, Liu Y.
J Neurooncol. 2010 Dec;100(3):375-83. doi: 10.1007/s11060-010-0205-x. Epub 2010 May 14.
PMID 20467785
Immunogold evidence suggests that coupling of K+ siphoning and water transport in rat retinal Muller cells is mediated by a coenrichment of Kir4.1 and AQP4 in specific membrane domains.
Nagelhus EA, Horio Y, Inanobe A, Fujita A, Haug FM, Nielsen S, Kurachi Y, Ottersen OP.
Glia. 1999 Mar;26(1):47-54.
PMID 10088671
Aquaporin-4 expression is increased in edematous meningiomas.
Ng WH, Hy JW, Tan WL, Liew D, Lim T, Ang BT, Ng I.
J Clin Neurosci. 2009 Mar;16(3):441-3. doi: 10.1016/j.jocn.2008.04.028. Epub 2009 Jan 18.
PMID 19153045
New possible roles for aquaporin-4 in astrocytes: cell cytoskeleton and functional relationship with connexin43.
Nicchia GP, Srinivas M, Li W, Brosnan CF, Frigeri A, Spray DC.
FASEB J. 2005 Oct;19(12):1674-6. Epub 2005 Aug 15.
PMID 16103109
Aquaporin-4 contributes to the resolution of peritumoural brain oedema in human glioblastoma multiforme after combined chemotherapy and radiotherapy.
Nico B, Mangieri D, Tamma R, Longo V, Annese T, Crivellato E, Pollo B, Maderna E, Ribatti D, Salmaggi A.
Eur J Cancer. 2009 Dec;45(18):3315-25. doi: 10.1016/j.ejca.2009.09.023. Epub 2009 Oct 14.
PMID 19836227
Glial dystrophin-associated proteins, laminin and agrin, are downregulated in the brain of mdx mouse.
Nico B, Tamma R, Annese T, Mangieri D, De Luca A, Corsi P, Benagiano V, Longo V, Crivellato E, Salmaggi A, Ribatti D.
Lab Invest. 2010 Nov;90(11):1645-60. doi: 10.1038/labinvest.2010.149. Epub 2010 Aug 16.
PMID 20714324
Specialized membrane domains for water transport in glial cells: high-resolution immunogold cytochemistry of aquaporin-4 in rat brain.
Nielsen S, Nagelhus EA, Amiry-Moghaddam M, Bourque C, Agre P, Ottersen OP.
J Neurosci. 1997 Jan 1;17(1):171-80.
PMID 8987746
Aquaporin-4 and brain edema.
Papadopoulos MC, Verkman AS.
Pediatr Nephrol. 2007 Jun;22(6):778-84. Epub 2007 Mar 9.
PMID 17347837
Direct immunogold labeling of aquaporin-4 in square arrays of astrocyte and ependymocyte plasma membranes in rat brain and spinal cord.
Rash JE, Yasumura T, Hudson CS, Agre P, Nielsen S.
Proc Natl Acad Sci U S A. 1998 Sep 29;95(20):11981-6.
PMID 9751776
Ontogeny and the effects of corticosteroid pretreatment on aquaporin water channels in the ovine cerebral cortex.
Ron NP, Kazianis JA, Padbury JF, Brown CM, McGonnigal BG, Sysyn GD, Sadowska GB, Stonestreet BS.
Reprod Fertil Dev. 2005;17(5):535-42.
PMID 15907279
Aquaporin-4 expression is increased in oedematous human brain tumours.
Saadoun S, Papadopoulos MC, Davies DC, Krishna S, Bell BA.
J Neurol Neurosurg Psychiatry. 2002 Feb;72(2):262-5.
PMID 11796780
Effects of dexamethasone on peritumoural oedematous brain: a DT-MRI study.
Sinha S, Bastin ME, Wardlaw JM, Armitage PA, Whittle IR.
J Neurol Neurosurg Psychiatry. 2004 Nov;75(11):1632-5.
PMID 15489404
Detailed localization of aquaporin-4 messenger RNA in the CNS: preferential expression in periventricular organs.
Venero JL, Vizuete ML, Ilundain AA, Machado A, Echevarria M, Cano J.
Neuroscience. 1999;94(1):239-50.
PMID 10613514
Aquaporins--new players in cancer biology.
Verkman AS, Hara-Chikuma M, Papadopoulos MC.
J Mol Med (Berl). 2008 May;86(5):523-9. doi: 10.1007/s00109-008-0303-9. Epub 2008 Mar 1.
PMID 18311471
More than just water channels: unexpected cellular roles of aquaporins.
Verkman AS.
J Cell Sci. 2005 Aug 1;118(Pt 15):3225-32.
PMID 16079275
Redistribution of aquaporin-4 in human glioblastoma correlates with loss of agrin immunoreactivity from brain capillary basal laminae.
Warth A, Kroger S, Wolburg H.
Acta Neuropathol. 2004 Apr;107(4):311-8. Epub 2004 Jan 20.
PMID 14735305
Redistribution of the water channel protein aquaporin-4 and the K+ channel protein Kir4.1 differs in low- and high-grade human brain tumors.
Warth A, Mittelbronn M, Wolburg H.
Acta Neuropathol. 2005 Apr;109(4):418-26. Epub 2005 Feb 19.
PMID 15723236
Expression pattern of the water channel aquaporin-4 in human gliomas is associated with blood-brain barrier disturbance but not with patient survival.
Warth A, Simon P, Capper D, Goeppert B, Tabatabai G, Herzog H, Dietz K, Stubenvoll F, Ajaaj R, Becker R, Weller M, Meyermann R, Wolburg H, Mittelbronn M.
J Neurosci Res. 2007 May 1;85(6):1336-46.
PMID 17335082


This paper should be referenced as such :
Ribatti, D ; Nico, B
AQP4 (aquaporin 4)
Atlas Genet Cytogenet Oncol Haematol. 2013;17(6):367-370.
Free journal version : [ pdf ]   [ DOI ]

External links


HGNC (Hugo)AQP4   637
Entrez_Gene (NCBI)AQP4    aquaporin 4
AliasesMIWC; WCH4
GeneCards (Weizmann)AQP4
Ensembl hg19 (Hinxton)ENSG00000171885 [Gene_View]
Ensembl hg38 (Hinxton)ENSG00000171885 [Gene_View]  ENSG00000171885 [Sequence]  chr18:26852038-26862910 [Contig_View]  AQP4 [Vega]
ICGC DataPortalENSG00000171885
TCGA cBioPortalAQP4
AceView (NCBI)AQP4
Genatlas (Paris)AQP4
SOURCE (Princeton)AQP4
Genetics Home Reference (NIH)AQP4
Genomic and cartography
GoldenPath hg38 (UCSC)AQP4  -     chr18:26852038-26862910 -  18q11.2   [Description]    (hg38-Dec_2013)
GoldenPath hg19 (UCSC)AQP4  -     18q11.2   [Description]    (hg19-Feb_2009)
GoldenPathAQP4 - 18q11.2 [CytoView hg19]  AQP4 - 18q11.2 [CytoView hg38]
Genome Data Viewer NCBIAQP4 [Mapview hg19]  
Gene and transcription
Genbank (Entrez)AB128929 AB209156 AK026728 AK222684 AK295069
RefSeq transcript (Entrez)NM_001317384 NM_001317387 NM_001364286 NM_001364287 NM_001364289 NM_001650 NM_004028
Consensus coding sequences : CCDS (NCBI)AQP4
Gene ExpressionAQP4 [ NCBI-GEO ]   AQP4 [ EBI - ARRAY_EXPRESS ]   AQP4 [ SEEK ]   AQP4 [ MEM ]
Gene Expression Viewer (FireBrowse)AQP4 [ Firebrowse - Broad ]
GenevisibleExpression of AQP4 in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
BioGPS (Tissue expression)361
GTEX Portal (Tissue expression)AQP4
Human Protein AtlasENSG00000171885-AQP4 [pathology]   [cell]   [tissue]
Protein : pattern, domain, 3D structure
UniProt/SwissProtP55087   [function]  [subcellular_location]  [family_and_domains]  [pathology_and_biotech]  [ptm_processing]  [expression]  [interaction]
NextProtP55087  [Sequence]  [Exons]  [Medical]  [Publications]
With graphics : InterProP55087
Domaine pattern : Prosite (Expaxy)MIP (PS00221)   
Domains : Interpro (EBI)Aquaporin-like    Aquaporin_transptr    MIP    MIP_CS   
Domain families : Pfam (Sanger)MIP (PF00230)   
Domain families : Pfam (NCBI)pfam00230   
Conserved Domain (NCBI)AQP4
PDB Europe3GD8   
PDB (PDBSum)3GD8   
PDB (IMB)3GD8   
Structural Biology KnowledgeBase3GD8   
SCOP (Structural Classification of Proteins)3GD8   
CATH (Classification of proteins structures)3GD8   
AlphaFold pdb e-kbP55087   
Human Protein Atlas [tissue]ENSG00000171885-AQP4 [tissue]
Protein Interaction databases
IntAct (EBI)P55087
Ontologies - Pathways
Ontology : AmiGOrenal water homeostasis  protein binding  extracellular region  cytoplasm  plasma membrane  plasma membrane  plasma membrane  integral component of plasma membrane  water transport  water transport  water transport  external side of plasma membrane  cellular water homeostasis  endosome membrane  water channel activity  water channel activity  water channel activity  integral component of membrane  basolateral plasma membrane  basolateral plasma membrane  water homeostasis  sarcolemma  multicellular organismal water homeostasis  protein homotetramerization  transmembrane transport  cellular response to interferon-gamma  cerebrospinal fluid circulation  astrocyte end-foot  
Ontology : EGO-EBIrenal water homeostasis  protein binding  extracellular region  cytoplasm  plasma membrane  plasma membrane  plasma membrane  integral component of plasma membrane  water transport  water transport  water transport  external side of plasma membrane  cellular water homeostasis  endosome membrane  water channel activity  water channel activity  water channel activity  integral component of membrane  basolateral plasma membrane  basolateral plasma membrane  water homeostasis  sarcolemma  multicellular organismal water homeostasis  protein homotetramerization  transmembrane transport  cellular response to interferon-gamma  cerebrospinal fluid circulation  astrocyte end-foot  
Pathways : KEGGVasopressin-regulated water reabsorption    Bile secretion   
REACTOMEP55087 [protein]
REACTOME PathwaysR-HSA-432047 [pathway]   
NDEx NetworkAQP4
Atlas of Cancer Signalling NetworkAQP4
Wikipedia pathwaysAQP4
Orthology - Evolution
GeneTree (enSembl)ENSG00000171885
Phylogenetic Trees/Animal Genes : TreeFamAQP4
Homologs : HomoloGeneAQP4
Homology/Alignments : Family Browser (UCSC)AQP4
Gene fusions - Rearrangements
Fusion : QuiverAQP4
Polymorphisms : SNP and Copy number variants
NCBI Variation ViewerAQP4 [hg38]
dbSNP Single Nucleotide Polymorphism (NCBI)AQP4
Exome Variant ServerAQP4
GNOMAD BrowserENSG00000171885
Varsome BrowserAQP4
ACMGAQP4 variants
Genomic Variants (DGV)AQP4 [DGVbeta]
DECIPHERAQP4 [patients]   [syndromes]   [variants]   [genes]  
CONAN: Copy Number AnalysisAQP4 
ICGC Data PortalAQP4 
TCGA Data PortalAQP4 
Broad Tumor PortalAQP4
OASIS PortalAQP4 [ Somatic mutations - Copy number]
Somatic Mutations in Cancer : COSMICAQP4  [overview]  [genome browser]  [tissue]  [distribution]  
Somatic Mutations in Cancer : COSMIC3DAQP4
Mutations and Diseases : HGMDAQP4
LOVD (Leiden Open Variation Database)[gene] [transcripts] [variants]
DgiDB (Drug Gene Interaction Database)AQP4
DoCM (Curated mutations)AQP4
CIViC (Clinical Interpretations of Variants in Cancer)AQP4
NCG (London)AQP4
Impact of mutations[PolyPhen2] [Provean] [Buck Institute : MutDB] [Mutation Assessor] [Mutanalyser]
Genetic Testing Registry AQP4
NextProtP55087 [Medical]
Target ValidationAQP4
Huge Navigator AQP4 [HugePedia]
Clinical trials, drugs, therapy
Protein Interactions : CTDAQP4
Pharm GKB GenePA24922
Clinical trialAQP4
DataMed IndexAQP4
PubMed307 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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