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P41181

- AQP2_HUMAN

UniProt

P41181 - AQP2_HUMAN

Protein

Aquaporin-2

Gene

AQP2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 145 (01 Oct 2014)
      Sequence version 1 (01 Feb 1995)
      Previous versions | rss
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    Functioni

    Forms a water-specific channel that provides the plasma membranes of renal collecting duct with high permeability to water, thereby permitting water to move in the direction of an osmotic gradient.

    GO - Molecular functioni

    1. glycerol transmembrane transporter activity Source: UniProtKB
    2. water channel activity Source: Reactome
    3. water transmembrane transporter activity Source: UniProtKB

    GO - Biological processi

    1. actin filament depolymerization Source: Ensembl
    2. aging Source: Ensembl
    3. apoptotic process Source: Ensembl
    4. cellular response to copper ion Source: UniProtKB
    5. cellular response to mercury ion Source: UniProtKB
    6. cellular response to water deprivation Source: Ensembl
    7. cell volume homeostasis Source: Ensembl
    8. excretion Source: ProtInc
    9. female pregnancy Source: Ensembl
    10. glycerol transport Source: UniProtKB
    11. hyperosmotic response Source: Ensembl
    12. metanephric collecting duct development Source: Ensembl
    13. positive regulation of calcium ion transport Source: Ensembl
    14. renal water transport Source: Ensembl
    15. response to calcium ion Source: Ensembl
    16. response to glucagon Source: Ensembl
    17. response to lipopolysaccharide Source: Ensembl
    18. response to lithium ion Source: Ensembl
    19. response to salt stress Source: Ensembl
    20. response to starvation Source: Ensembl
    21. transmembrane transport Source: Reactome
    22. water transport Source: UniProtKB

    Keywords - Biological processi

    Transport

    Enzyme and pathway databases

    ReactomeiREACT_23826. Passive transport by Aquaporins.
    REACT_24023. Regulation of water balance by renal Aquaporins.

    Protein family/group databases

    TCDBi1.A.8.8.8. the major intrinsic protein (mip) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Aquaporin-2
    Short name:
    AQP-2
    Alternative name(s):
    ADH water channel
    Aquaporin-CD
    Short name:
    AQP-CD
    Collecting duct water channel protein
    WCH-CD
    Water channel protein for renal collecting duct
    Gene namesi
    Name:AQP2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:634. AQP2.

    Subcellular locationi

    Apical cell membrane 1 Publication; Multi-pass membrane protein 1 Publication. Basolateral cell membrane By similarity; Multi-pass membrane protein By similarity. Cytoplasmic vesicle membrane 1 Publication; Multi-pass membrane protein 1 Publication. Golgi apparatustrans-Golgi network membrane 1 Publication; Multi-pass membrane protein 1 Publication
    Note: Shuttles from vesicles to the apical membrane. Vasopressin-regulated phosphorylation is required for translocation to the apical cell membrane. PLEKHA8/FAPP2 is required to transport AQP2 from the TGN to sites where AQP2 is phosphorylated.

    GO - Cellular componenti

    1. apical plasma membrane Source: UniProtKB
    2. basolateral plasma membrane Source: UniProtKB-SubCell
    3. clathrin-coated vesicle Source: Ensembl
    4. early endosome Source: Ensembl
    5. exocytic vesicle Source: Ensembl
    6. extracellular vesicular exosome Source: UniProtKB
    7. integral component of membrane Source: UniProtKB-KW
    8. lysosome Source: Ensembl
    9. membrane Source: MGI
    10. plasma membrane Source: UniProtKB
    11. protein complex Source: Ensembl
    12. recycling endosome Source: Ensembl
    13. rough endoplasmic reticulum Source: Ensembl
    14. trans-Golgi network Source: Ensembl
    15. transport vesicle membrane Source: Reactome

    Keywords - Cellular componenti

    Cell membrane, Cytoplasmic vesicle, Golgi apparatus, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Diabetes insipidus, nephrogenic, autosomal (ANDI) [MIM:125800]: A disorder caused by the inability of the renal collecting ducts to absorb water in response to arginine vasopressin. Characterized by excessive water drinking (polydipsia), excessive urine excretion (polyuria), persistent hypotonic urine, and hypokalemia. Inheritance can be autosomal dominant or recessive.15 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti22 – 221L → V in ANDI. 1 Publication
    VAR_015239
    Natural varianti28 – 281L → P in ANDI. 1 Publication
    VAR_015240
    Natural varianti47 – 471A → V in ANDI. 1 Publication
    VAR_015241
    Natural varianti57 – 571Q → P in ANDI. 1 Publication
    Corresponds to variant rs28931580 [ dbSNP | Ensembl ].
    VAR_015256
    Natural varianti64 – 641G → R in ANDI. 1 Publication
    VAR_004401
    Natural varianti68 – 681N → S in ANDI. 1 Publication
    VAR_015242
    Natural varianti70 – 701A → D in ANDI. 1 Publication
    VAR_062585
    Natural varianti71 – 711V → M in ANDI. 1 Publication
    VAR_015243
    Natural varianti100 – 1001G → R in ANDI. 1 Publication
    VAR_062586
    Natural varianti100 – 1001G → V in ANDI. 1 Publication
    Corresponds to variant rs28929477 [ dbSNP | Ensembl ].
    VAR_015257
    Natural varianti125 – 1251T → M in ANDI. 3 Publications
    VAR_015244
    Natural varianti126 – 1261T → M in ANDI. 1 Publication
    VAR_015245
    Natural varianti147 – 1471A → T in ANDI. 1 Publication
    VAR_015246
    Natural varianti168 – 1681V → M in ANDI. 1 Publication
    VAR_015247
    Natural varianti175 – 1751G → R in ANDI. 3 Publications
    VAR_015248
    Natural varianti180 – 1801G → S in ANDI. 1 Publication
    VAR_062587
    Natural varianti181 – 1811C → W in ANDI. 1 Publication
    VAR_015249
    Natural varianti185 – 1851P → A in ANDI. 1 Publication
    VAR_015250
    Natural varianti187 – 1871R → C in ANDI; mutant protein does not fold properly and is not functional. 2 Publications
    VAR_004402
    Natural varianti187 – 1871R → H in ANDI. 1 Publication
    VAR_062588
    Natural varianti190 – 1901A → T in ANDI; mutant protein does not fold properly and is not functional. 2 Publications
    VAR_015251
    Natural varianti202 – 2021W → C in ANDI. 1 Publication
    VAR_015253
    Natural varianti216 – 2161S → P in ANDI. 2 Publications
    VAR_004403
    Natural varianti254 – 2541R → L in ANDI; results in the loss of arginine vasopressin-mediated phosphorylation at S-256. 1 Publication
    VAR_062589
    Natural varianti254 – 2541R → Q in ANDI; exerts a dominant-negative effect on wild-type-AQP2 in that it interferes with its trafficking to the apical membrane; is a loss of function instead of a gain of function mutation on dominant nephrogenic diabetes insipidus. 1 Publication
    VAR_062590
    Natural varianti258 – 2581E → K in ANDI; retained in the Golgi compartment. 1 Publication
    VAR_015254
    Natural varianti262 – 2621P → L in ANDI; mutant protein folds properly and is functional but is retained in intracellular vesicles and does not localize to the ER; upon coexpression with wild-type AQP2 mutant protein interacts with wild-type AQP2 and the resulting heterotetramer properly localizes to the apical membrane. 2 Publications
    VAR_015255

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi148 – 1481S → A: No effect on sorting from the ER to the vesicles, redistribution to apical membrane, or endocytosis. 1 Publication
    Mutagenesisi148 – 1481S → D: Retained in the endoplasmic reticulum. 1 Publication
    Mutagenesisi229 – 2291S → A: No effect on sorting from the ER to the vesicles, redistribution to apical membrane, or endocytosis. 1 Publication
    Mutagenesisi229 – 2291S → D: No effect on sorting from the ER to the vesicles, redistribution to apical membrane, or endocytosis. 1 Publication
    Mutagenesisi231 – 2311S → A: No effect on sorting from the ER to the vesicles, redistribution to apical membrane, or endocytosis. 1 Publication
    Mutagenesisi231 – 2311S → D: No effect on sorting from the ER to the vesicles, redistribution to apical membrane, or endocytosis. 1 Publication
    Mutagenesisi244 – 2441T → A: No effect on sorting from the ER to the vesicles, redistribution to apical membrane, or endocytosis. 1 Publication
    Mutagenesisi244 – 2441T → E: No effect on sorting from the ER to the vesicles, redistribution to apical membrane, or endocytosis. 1 Publication
    Mutagenesisi256 – 2561S → A: Retained in vesicles. 1 Publication
    Mutagenesisi256 – 2561S → D: Expressed in the apical membrane. 1 Publication

    Keywords - Diseasei

    Diabetes insipidus, Disease mutation

    Organism-specific databases

    MIMi125800. phenotype.
    Orphaneti223. Nephrogenic diabetes insipidus.
    PharmGKBiPA24920.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 271271Aquaporin-2PRO_0000063934Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi123 – 1231N-linked (GlcNAc...)Sequence Analysis
    Modified residuei256 – 2561Phosphoserine; by PKA1 Publication

    Post-translational modificationi

    Ser-256 phosphorylation is necessary and sufficient for expression at the apical membrane. Endocytosis is not phosphorylation-dependent.1 Publication

    Keywords - PTMi

    Glycoprotein, Phosphoprotein

    Proteomic databases

    PaxDbiP41181.
    PRIDEiP41181.

    PTM databases

    PhosphoSiteiP41181.

    Expressioni

    Tissue specificityi

    Expressed in renal collecting tubules.

    Gene expression databases

    ArrayExpressiP41181.
    BgeeiP41181.
    CleanExiHS_AQP2.
    GenevestigatoriP41181.

    Organism-specific databases

    HPAiHPA046834.

    Interactioni

    Protein-protein interaction databases

    BioGridi106855. 2 interactions.
    STRINGi9606.ENSP00000199280.

    Structurei

    Secondary structure

    1
    271
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi7 – 3226
    Beta strandi35 – 373
    Helixi41 – 6323
    Helixi69 – 779
    Helixi83 – 10725
    Helixi110 – 1134
    Helixi127 – 14822
    Helixi159 – 17921
    Helixi185 – 19511
    Turni199 – 2024
    Helixi203 – 22119
    Helixi232 – 2376

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4NEFX-ray2.75A/B/C/D3-241[»]
    4OJ2X-ray3.05X1-271[»]
    ProteinModelPortaliP41181.
    SMRiP41181. Positions 3-239.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 1616CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini35 – 406ExtracellularSequence Analysis
    Topological domaini60 – 8526CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini108 – 12720ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini149 – 1568CytoplasmicSequence Analysis
    Topological domaini177 – 20226ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini225 – 27147CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei17 – 3418HelicalSequence AnalysisAdd
    BLAST
    Transmembranei41 – 5919HelicalSequence AnalysisAdd
    BLAST
    Transmembranei86 – 10722HelicalSequence AnalysisAdd
    BLAST
    Transmembranei128 – 14821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei157 – 17620HelicalSequence AnalysisAdd
    BLAST
    Transmembranei203 – 22422HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi68 – 703NPA 1
    Motifi184 – 1863NPA 2

    Domaini

    Aquaporins contain two tandem repeats each containing three membrane-spanning domains and a pore-forming loop with the signature motif Asn-Pro-Ala (NPA).

    Sequence similaritiesi

    Keywords - Domaini

    Repeat, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0580.
    HOGENOMiHOG000288286.
    HOVERGENiHBG000312.
    InParanoidiP41181.
    KOiK09865.
    OMAiHEITPAN.
    PhylomeDBiP41181.
    TreeFamiTF312940.

    Family and domain databases

    Gene3Di1.20.1080.10. 1 hit.
    InterProiIPR023271. Aquaporin-like.
    IPR000425. MIP.
    IPR022357. MIP_CS.
    [Graphical view]
    PANTHERiPTHR19139. PTHR19139. 1 hit.
    PfamiPF00230. MIP. 1 hit.
    [Graphical view]
    PRINTSiPR00783. MINTRINSICP.
    SUPFAMiSSF81338. SSF81338. 1 hit.
    TIGRFAMsiTIGR00861. MIP. 1 hit.
    PROSITEiPS00221. MIP. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P41181-1 [UniParc]FASTAAdd to Basket

    « Hide

    MWELRSIAFS RAVFAEFLAT LLFVFFGLGS ALNWPQALPS VLQIAMAFGL    50
    GIGTLVQALG HISGAHINPA VTVACLVGCH VSVLRAAFYV AAQLLGAVAG 100
    AALLHEITPA DIRGDLAVNA LSNSTTAGQA VTVELFLTLQ LVLCIFASTD 150
    ERRGENPGTP ALSIGFSVAL GHLLGIHYTG CSMNPARSLA PAVVTGKFDD 200
    HWVFWIGPLV GAILGSLLYN YVLFPPAKSL SERLAVLKGL EPDTDWEERE 250
    VRRRQSVELH SPQSLPRGTK A 271
    Length:271
    Mass (Da):28,837
    Last modified:February 1, 1995 - v1
    Checksum:iC2DDE2AF4DDD192A
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti35 – 384PQAL → ATAP(PubMed:7510718)Curated
    Sequence conflicti83 – 831V → F(PubMed:7510718)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti22 – 221L → V in ANDI. 1 Publication
    VAR_015239
    Natural varianti28 – 281L → P in ANDI. 1 Publication
    VAR_015240
    Natural varianti47 – 471A → V in ANDI. 1 Publication
    VAR_015241
    Natural varianti57 – 571Q → P in ANDI. 1 Publication
    Corresponds to variant rs28931580 [ dbSNP | Ensembl ].
    VAR_015256
    Natural varianti64 – 641G → R in ANDI. 1 Publication
    VAR_004401
    Natural varianti68 – 681N → S in ANDI. 1 Publication
    VAR_015242
    Natural varianti70 – 701A → D in ANDI. 1 Publication
    VAR_062585
    Natural varianti71 – 711V → M in ANDI. 1 Publication
    VAR_015243
    Natural varianti100 – 1001G → R in ANDI. 1 Publication
    VAR_062586
    Natural varianti100 – 1001G → V in ANDI. 1 Publication
    Corresponds to variant rs28929477 [ dbSNP | Ensembl ].
    VAR_015257
    Natural varianti121 – 1211L → F.
    Corresponds to variant rs11169226 [ dbSNP | Ensembl ].
    VAR_037577
    Natural varianti125 – 1251T → M in ANDI. 3 Publications
    VAR_015244
    Natural varianti126 – 1261T → M in ANDI. 1 Publication
    VAR_015245
    Natural varianti147 – 1471A → T in ANDI. 1 Publication
    VAR_015246
    Natural varianti168 – 1681V → M in ANDI. 1 Publication
    VAR_015247
    Natural varianti175 – 1751G → R in ANDI. 3 Publications
    VAR_015248
    Natural varianti180 – 1801G → S in ANDI. 1 Publication
    VAR_062587
    Natural varianti181 – 1811C → W in ANDI. 1 Publication
    VAR_015249
    Natural varianti185 – 1851P → A in ANDI. 1 Publication
    VAR_015250
    Natural varianti187 – 1871R → C in ANDI; mutant protein does not fold properly and is not functional. 2 Publications
    VAR_004402
    Natural varianti187 – 1871R → H in ANDI. 1 Publication
    VAR_062588
    Natural varianti190 – 1901A → T in ANDI; mutant protein does not fold properly and is not functional. 2 Publications
    VAR_015251
    Natural varianti194 – 1941V → I.1 Publication
    VAR_015252
    Natural varianti202 – 2021W → C in ANDI. 1 Publication
    VAR_015253
    Natural varianti216 – 2161S → P in ANDI. 2 Publications
    VAR_004403
    Natural varianti254 – 2541R → L in ANDI; results in the loss of arginine vasopressin-mediated phosphorylation at S-256. 1 Publication
    VAR_062589
    Natural varianti254 – 2541R → Q in ANDI; exerts a dominant-negative effect on wild-type-AQP2 in that it interferes with its trafficking to the apical membrane; is a loss of function instead of a gain of function mutation on dominant nephrogenic diabetes insipidus. 1 Publication
    VAR_062590
    Natural varianti258 – 2581E → K in ANDI; retained in the Golgi compartment. 1 Publication
    VAR_015254
    Natural varianti262 – 2621P → L in ANDI; mutant protein folds properly and is functional but is retained in intracellular vesicles and does not localize to the ER; upon coexpression with wild-type AQP2 mutant protein interacts with wild-type AQP2 and the resulting heterotetramer properly localizes to the apical membrane. 2 Publications
    VAR_015255

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z29491 Genomic DNA. Translation: CAA82627.1.
    D31846 Genomic DNA. Translation: BAA06632.1.
    S73196 mRNA. Translation: AAB31999.1.
    S73197 mRNA. Translation: AAB31998.1.
    AF147093, AF147092 Genomic DNA. Translation: AAD38692.1.
    BC042496 mRNA. Translation: AAH42496.1.
    CCDSiCCDS8792.1.
    PIRiA53442.
    I64818.
    RefSeqiNP_000477.1. NM_000486.5.
    UniGeneiHs.130730.

    Genome annotation databases

    EnsembliENST00000199280; ENSP00000199280; ENSG00000167580.
    GeneIDi359.
    KEGGihsa:359.
    UCSCiuc001rvn.3. human.

    Polymorphism databases

    DMDMi728874.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    Nephrogenic and neurogenic Diabetes Insipidus

    AQP2 pages

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z29491 Genomic DNA. Translation: CAA82627.1 .
    D31846 Genomic DNA. Translation: BAA06632.1 .
    S73196 mRNA. Translation: AAB31999.1 .
    S73197 mRNA. Translation: AAB31998.1 .
    AF147093 , AF147092 Genomic DNA. Translation: AAD38692.1 .
    BC042496 mRNA. Translation: AAH42496.1 .
    CCDSi CCDS8792.1.
    PIRi A53442.
    I64818.
    RefSeqi NP_000477.1. NM_000486.5.
    UniGenei Hs.130730.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4NEF X-ray 2.75 A/B/C/D 3-241 [» ]
    4OJ2 X-ray 3.05 X 1-271 [» ]
    ProteinModelPortali P41181.
    SMRi P41181. Positions 3-239.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106855. 2 interactions.
    STRINGi 9606.ENSP00000199280.

    Chemistry

    GuidetoPHARMACOLOGYi 689.

    Protein family/group databases

    TCDBi 1.A.8.8.8. the major intrinsic protein (mip) family.

    PTM databases

    PhosphoSitei P41181.

    Polymorphism databases

    DMDMi 728874.

    Proteomic databases

    PaxDbi P41181.
    PRIDEi P41181.

    Protocols and materials databases

    DNASUi 359.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000199280 ; ENSP00000199280 ; ENSG00000167580 .
    GeneIDi 359.
    KEGGi hsa:359.
    UCSCi uc001rvn.3. human.

    Organism-specific databases

    CTDi 359.
    GeneCardsi GC12P050400.
    GeneReviewsi AQP2.
    HGNCi HGNC:634. AQP2.
    HPAi HPA046834.
    MIMi 107777. gene.
    125800. phenotype.
    neXtProti NX_P41181.
    Orphaneti 223. Nephrogenic diabetes insipidus.
    PharmGKBi PA24920.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0580.
    HOGENOMi HOG000288286.
    HOVERGENi HBG000312.
    InParanoidi P41181.
    KOi K09865.
    OMAi HEITPAN.
    PhylomeDBi P41181.
    TreeFami TF312940.

    Enzyme and pathway databases

    Reactomei REACT_23826. Passive transport by Aquaporins.
    REACT_24023. Regulation of water balance by renal Aquaporins.

    Miscellaneous databases

    GeneWikii Aquaporin_2.
    GenomeRNAii 359.
    NextBioi 1501.
    PROi P41181.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P41181.
    Bgeei P41181.
    CleanExi HS_AQP2.
    Genevestigatori P41181.

    Family and domain databases

    Gene3Di 1.20.1080.10. 1 hit.
    InterProi IPR023271. Aquaporin-like.
    IPR000425. MIP.
    IPR022357. MIP_CS.
    [Graphical view ]
    PANTHERi PTHR19139. PTHR19139. 1 hit.
    Pfami PF00230. MIP. 1 hit.
    [Graphical view ]
    PRINTSi PR00783. MINTRINSICP.
    SUPFAMi SSF81338. SSF81338. 1 hit.
    TIGRFAMsi TIGR00861. MIP. 1 hit.
    PROSITEi PS00221. MIP. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Requirement of human renal water channel aquaporin-2 for vasopressin-dependent concentration of urine."
      Deen P.M.T., Verdijk M.A.J., Knoers V.V.A.M., Wieringa B., Monnens L.A.H., van Os C.H., van Oost B.A.
      Science 264:92-94(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Isolation of human aquaporin-CD gene."
      Uchida S., Sasaki S., Fushimi K., Marumo F.
      J. Biol. Chem. 269:23451-23455(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Patients with autosomal nephrogenic diabetes insipidus homozygous for mutations in the aquaporin 2 water-channel gene."
      van Lieburg A.F., Verdijk M.A.J., Knoers V.V.A.M., van Essen A.J., Proesmans W., Mallmann R., Monnens L.A.H., van Oost B.A., van Os C.H., Deen P.M.T.
      Am. J. Hum. Genet. 55:648-652(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS ANDI ARG-64; CYS-187 AND PRO-216.
    4. "Cloning, characterization, and chromosomal mapping of human aquaporin of collecting duct."
      Sasaki S., Fushimi K., Saito H., Saito F., Uchida S., Ishibashi K., Kuwahara M., Ikeuchi T., Inui K., Nakajima K.
      J. Clin. Invest. 93:1250-1256(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Tissue: Kidney.
    5. "Heteroligomerization of an aquaporin-2 mutant with wild-type aquaporin-2 and their misrouting to late endosomes/lysosomes explains dominant nephrogenic diabetes insipidus."
      Marr N., Bichet D.G., Lonergan M., Arthus M.-F., Jeck N., Seyberth H.W., Rosenthal W., van Os C.H., Oksche A., Deen P.M.T.
      Hum. Mol. Genet. 11:779-789(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Tissue: Kidney.
    6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Colon.
    7. "The role of putative phosphorylation sites in the targeting and shuttling of the aquaporin-2 water channel."
      van Balkom B.W.M., Savelkoul P.J.M., Markovich D., Hofman E., Nielsen S., van der Sluijs P., Deen P.M.T.
      J. Biol. Chem. 277:41473-41479(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-256, MUTAGENESIS OF SER-148; SER-229; SER-231; THR-244 AND SER-256.
    8. "Two novel mutations in the aquaporin-2 and the vasopressin V2 receptor genes in patients with congenital nephrogenic diabetes insipidus."
      Oksche A., Moeller A., Dickson J., Rosendahl W., Rascher W., Bichet D.G., Rosenthal W.
      Hum. Genet. 98:587-589(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT ANDI CYS-202.
    9. "Identification and characterization of aquaporin-2 water channel mutations causing nephrogenic diabetes insipidus with partial vasopressin response."
      Canfield M.C., Tamarappoo B.K., Moses A.M., Verkman A.S., Holtzman E.J.
      Hum. Mol. Genet. 6:1865-1871(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS ANDI VAL-22 AND TRP-181.
    10. "New mutations in the AQP2 gene in nephrogenic diabetes insipidus resulting in functional but misrouted water channels."
      Mulders S.M., Knoers N.V., Van Lieburg A.F., Monnens L.A., Leumann E., Wuhl E., Schober E., Rijss J.P.L., Van Os C.H., Deen P.M.T.
      J. Am. Soc. Nephrol. 8:242-248(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS ANDI SER-68; MET-126 AND THR-147.
    11. "Mutations in the vasopressin V2 receptor and aquaporin-2 genes in 12 families with congenital nephrogenic diabetes insipidus."
      Vargas-Poussou R., Forestier L., Dautzenberg M.D., Niaudet P., Dechaux M., Antignac C.
      J. Am. Soc. Nephrol. 8:1855-1862(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS ANDI MET-168 AND PRO-216.
    12. "Aquaporin-2, a vasopressin-sensitive water channel, and nephrogenic diabetes insipidus."
      Kuwahara M.
      Intern. Med. 37:215-217(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS ANDI MET-125; ARG-175; THR-190 AND LEU-262.
    13. "An aquaporin-2 water channel mutant which causes autosomal dominant nephrogenic diabetes insipidus is retained in the Golgi complex."
      Mulders S.M., Bichet D.G., Rijss J.P.L., Kamsteeg E.-J., Arthus M.-F., Lonergan M., Fujiwara M., Morgan K., Leijendekker R., van der Sluijs P., van Os C.H., Deen P.M.T.
      J. Clin. Invest. 102:57-66(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT ANDI LYS-258.
    14. "Novel mutations in aquaporin-2 gene in female siblings with nephrogenic diabetes insipidus: evidence of disrupted water channel function."
      Goji K., Kuwahara M., Gu Y., Matsuo M., Marumo F., Sasaki S.
      J. Clin. Endocrinol. Metab. 83:3205-3209(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS ANDI MET-125 AND ARG-175.
    15. "Cell-biologic and functional analyses of five new Aquaporin-2 missense mutations that cause recessive nephrogenic diabetes insipidus."
      Marr N., Bichet D.G., Hoefs S., Savelkoul P.J.M., Konings I.B., De Mattia F., Graat M.P., Arthus M.-F., Lonergan M., Fujiwara T.M., Knoers N.V., Landau D., Balfe W.J., Oksche A., Rosenthal W., Muller D., Van Os C.H., Deen P.M.
      J. Am. Soc. Nephrol. 13:2267-2277(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS ANDI PRO-28; VAL-47; MET-71; MET-125; ARG-175 AND ALA-185, VARIANT ILE-194.
    16. "Two novel aquaporin-2 mutations responsible for congenital nephrogenic diabetes insipidus in Chinese families."
      Lin S.H., Bichet D.G., Sasaki S., Kuwahara M., Arthus M.-F., Lonergan M., Lin Y.-F.
      J. Clin. Endocrinol. Metab. 87:2694-2700(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS ANDI PRO-57 AND VAL-100.
    17. "A novel mechanism in recessive nephrogenic diabetes insipidus: wild-type aquaporin-2 rescues the apical membrane expression of intracellularly retained AQP2-P262L."
      de Mattia F., Savelkoul P.J.M., Bichet D.G., Kamsteeg E.-J., Konings I.B.M., Marr N., Arthus M.-F., Lonergan M., van Os C.H., van der Sluijs P., Robertson G., Deen P.M.T.
      Hum. Mol. Genet. 13:3045-3056(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS ANDI CYS-187; THR-190 AND LEU-262, CHARACTERIZATION OF VARIANTS ANDI CYS-187; THR-190 AND LEU-262.
    18. "Lack of arginine vasopressin-induced phosphorylation of aquaporin-2 mutant AQP2-R254L explains dominant nephrogenic diabetes insipidus."
      de Mattia F., Savelkoul P.J.M., Kamsteeg E.-J., Konings I.B.M., van der Sluijs P., Mallmann R., Oksche A., Deen P.M.T.
      J. Am. Soc. Nephrol. 16:2872-2880(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT ANDI LEU-254, CHARACTERIZATION OF VARIANT ANDI LEU-254.
    19. "Two novel mutations in the aquaporin 2 gene in a girl with congenital nephrogenic diabetes insipidus."
      Cheong H.I., Cho S.J., Zheng S.H., Cho H.Y., Ha I.S., Choi Y.
      J. Korean Med. Sci. 20:1076-1078(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS ANDI ASP-70 AND HIS-187.
    20. "Novel mutations underlying nephrogenic diabetes insipidus in Arab families."
      Carroll P., Al-Mojalli H., Al-Abbad A., Al-Hassoun I., Al-Hamed M., Al-Amr R., Butt A.I., Meyer B.F.
      Genet. Med. 8:443-447(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS ANDI ARG-100 AND SER-180.
    21. "p.R254Q mutation in the aquaporin-2 water channel causing dominant nephrogenic diabetes insipidus is due to a lack of arginine vasopressin-induced phosphorylation."
      Savelkoul P.J.M., De Mattia F., Li Y., Kamsteeg E.-J., Konings I.B.M., van der Sluijs P., Deen P.M.T.
      Hum. Mutat. 30:E891-E903(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT ANDI GLN-254, CHARACTERIZATION OF VARIANT ANDI GLN-254.
    22. "Repulsion between Lys258 and upstream arginines explains the missorting of the AQP2 mutant p.Glu258Lys in nephrogenic diabetes insipidus."
      Kamsteeg E.-J., Stoffels M., Tamma G., Konings I.B.M., Deen P.M.T.
      Hum. Mutat. 30:1387-1396(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: MISSORTING MOTIF OF VARIANT ANDI LYS-258.

    Entry informationi

    Entry nameiAQP2_HUMAN
    AccessioniPrimary (citable) accession number: P41181
    Secondary accession number(s): Q9UD68
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: February 1, 1995
    Last modified: October 1, 2014
    This is version 145 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 12
      Human chromosome 12: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

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