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P41181

- AQP2_HUMAN

UniProt

P41181 - AQP2_HUMAN

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Protein

Aquaporin-2

Gene

AQP2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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
Complete GO annotation...

Keywords - Biological processi

Transport

Enzyme and pathway databases

ReactomeiREACT_23826. Passive transport by Aquaporins.
REACT_24023. Vasopressin regulates renal water homeostasis via 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.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1616CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei17 – 3418HelicalSequence AnalysisAdd
BLAST
Topological domaini35 – 406ExtracellularSequence Analysis
Transmembranei41 – 5919HelicalSequence AnalysisAdd
BLAST
Topological domaini60 – 8526CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei86 – 10722HelicalSequence AnalysisAdd
BLAST
Topological domaini108 – 12720ExtracellularSequence AnalysisAdd
BLAST
Transmembranei128 – 14821HelicalSequence AnalysisAdd
BLAST
Topological domaini149 – 1568CytoplasmicSequence Analysis
Transmembranei157 – 17620HelicalSequence AnalysisAdd
BLAST
Topological domaini177 – 20226ExtracellularSequence AnalysisAdd
BLAST
Transmembranei203 – 22422HelicalSequence AnalysisAdd
BLAST
Topological domaini225 – 27147CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. apical plasma membrane Source: UniProtKB
  2. basolateral plasma membrane Source: Ensembl
  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
Complete GO annotation...

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.16 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 varianti108 – 1081T → M in ANDI. 1 Publication
VAR_071370
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

BgeeiP41181.
CleanExiHS_AQP2.
ExpressionAtlasiP41181. baseline and differential.
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 – 3226Combined sources
Beta strandi35 – 373Combined sources
Helixi41 – 6323Combined sources
Helixi69 – 779Combined sources
Helixi83 – 10725Combined sources
Helixi110 – 1134Combined sources
Helixi127 – 14822Combined sources
Helixi159 – 17921Combined sources
Helixi185 – 19511Combined sources
Turni199 – 2024Combined sources
Helixi203 – 22119Combined sources
Helixi232 – 2376Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4NEFX-ray2.75A/B/C/D3-241[»]
4OJ2X-ray3.05X1-271[»]
ProteinModelPortaliP41181.
SMRiP41181. Positions 3-240.
ModBaseiSearch...
MobiDBiSearch...

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.
GeneTreeiENSGT00760000119223.
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

        10         20         30         40         50
MWELRSIAFS RAVFAEFLAT LLFVFFGLGS ALNWPQALPS VLQIAMAFGL
60 70 80 90 100
GIGTLVQALG HISGAHINPA VTVACLVGCH VSVLRAAFYV AAQLLGAVAG
110 120 130 140 150
AALLHEITPA DIRGDLAVNA LSNSTTAGQA VTVELFLTLQ LVLCIFASTD
160 170 180 190 200
ERRGENPGTP ALSIGFSVAL GHLLGIHYTG CSMNPARSLA PAVVTGKFDD
210 220 230 240 250
HWVFWIGPLV GAILGSLLYN YVLFPPAKSL SERLAVLKGL EPDTDWEERE
260 270
VRRRQSVELH SPQSLPRGTK A
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 varianti108 – 1081T → M in ANDI. 1 Publication
VAR_071370
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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 3-240.
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.
GeneTreei ENSGT00760000119223.
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. Vasopressin regulates renal water homeostasis via Aquaporins.

Miscellaneous databases

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

Gene expression databases

Bgeei P41181.
CleanExi HS_AQP2.
ExpressionAtlasi P41181. baseline and differential.
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

« Hide 'large scale' publications
  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: INVOLVEMENT IN ANDI, 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.
  23. "Congenital nephrogenic diabetes insipidus with a novel mutation in the aquaporin 2 gene."
    Park Y.J., Baik H.W., Cheong H.I., Kang J.H.
    Biomed. Rep. 2:596-598(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT ANDI MET-108.

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: November 26, 2014
This is version 147 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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