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P41181 (AQP2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 141. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:AQP2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length271 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subcellular location

Apical cell membrane; Multi-pass membrane protein. Basolateral cell membrane; Multi-pass membrane protein By similarity. Cytoplasmic vesicle membrane; Multi-pass membrane protein. Golgi apparatustrans-Golgi network membrane; Multi-pass membrane protein. 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. Ref.7

Tissue specificity

Expressed in renal collecting tubules.

Domain

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

Post-translational modification

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

Involvement in disease

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.3 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22

Sequence similarities

Belongs to the MIP/aquaporin (TC 1.A.8) family. [View classification]

Ontologies

Keywords
   Biological processTransport
   Cellular componentCell membrane
Cytoplasmic vesicle
Golgi apparatus
Membrane
   Coding sequence diversityPolymorphism
   DiseaseDiabetes insipidus
Disease mutation
   DomainRepeat
Transmembrane
Transmembrane helix
   PTMGlycoprotein
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactin filament depolymerization

Inferred from electronic annotation. Source: Ensembl

aging

Inferred from electronic annotation. Source: Ensembl

apoptotic process

Inferred from electronic annotation. Source: Ensembl

cell volume homeostasis

Inferred from electronic annotation. Source: Ensembl

cellular response to copper ion

Inferred from direct assay PubMed 8584435. Source: UniProtKB

cellular response to mercury ion

Inferred from direct assay PubMed 8584435. Source: UniProtKB

cellular response to water deprivation

Inferred from electronic annotation. Source: Ensembl

excretion

Traceable author statement PubMed 7532304. Source: ProtInc

female pregnancy

Inferred from electronic annotation. Source: Ensembl

glycerol transport

Inferred from direct assay PubMed 8584435. Source: UniProtKB

hyperosmotic response

Inferred from electronic annotation. Source: Ensembl

metanephric collecting duct development

Inferred from electronic annotation. Source: Ensembl

positive regulation of calcium ion transport

Inferred from electronic annotation. Source: Ensembl

renal water transport

Inferred from electronic annotation. Source: Ensembl

response to calcium ion

Inferred from electronic annotation. Source: Ensembl

response to glucagon

Inferred from electronic annotation. Source: Ensembl

response to lipopolysaccharide

Inferred from electronic annotation. Source: Ensembl

response to lithium ion

Inferred from electronic annotation. Source: Ensembl

response to salt stress

Inferred from electronic annotation. Source: Ensembl

response to starvation

Inferred from electronic annotation. Source: Ensembl

transmembrane transport

Traceable author statement. Source: Reactome

water transport

Inferred from direct assay PubMed 8584435PubMed 9321919. Source: UniProtKB

   Cellular_componentGolgi apparatus

Inferred from electronic annotation. Source: UniProtKB-SubCell

apical plasma membrane

Inferred from direct assay PubMed 16928804. Source: UniProtKB

basolateral plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

clathrin-coated vesicle

Inferred from electronic annotation. Source: Ensembl

early endosome

Inferred from electronic annotation. Source: Ensembl

exocytic vesicle

Inferred from electronic annotation. Source: Ensembl

extracellular vesicular exosome

Inferred from direct assay PubMed 15326289PubMed 19056867. Source: UniProt

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

lysosome

Inferred from electronic annotation. Source: Ensembl

membrane

Inferred from direct assay PubMed 22375059. Source: MGI

plasma membrane

Inferred from direct assay PubMed 9321919. Source: UniProtKB

protein complex

Inferred from electronic annotation. Source: Ensembl

recycling endosome

Inferred from electronic annotation. Source: Ensembl

rough endoplasmic reticulum

Inferred from electronic annotation. Source: Ensembl

trans-Golgi network

Inferred from electronic annotation. Source: Ensembl

transport vesicle membrane

Traceable author statement. Source: Reactome

   Molecular_functionglycerol transmembrane transporter activity

Inferred from direct assay PubMed 8584435. Source: UniProtKB

water channel activity

Inferred from experiment. Source: Reactome

water transmembrane transporter activity

Inferred from direct assay PubMed 8584435PubMed 9321919. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 271271Aquaporin-2
PRO_0000063934

Regions

Topological domain1 – 1616Cytoplasmic Potential
Transmembrane17 – 3418Helical; Potential
Topological domain35 – 406Extracellular Potential
Transmembrane41 – 5919Helical; Potential
Topological domain60 – 8526Cytoplasmic Potential
Transmembrane86 – 10722Helical; Potential
Topological domain108 – 12720Extracellular Potential
Transmembrane128 – 14821Helical; Potential
Topological domain149 – 1568Cytoplasmic Potential
Transmembrane157 – 17620Helical; Potential
Topological domain177 – 20226Extracellular Potential
Transmembrane203 – 22422Helical; Potential
Topological domain225 – 27147Cytoplasmic Potential
Motif68 – 703NPA 1
Motif184 – 1863NPA 2

Amino acid modifications

Modified residue2561Phosphoserine; by PKA Ref.7
Glycosylation1231N-linked (GlcNAc...) Potential

Natural variations

Natural variant221L → V in ANDI. Ref.9
VAR_015239
Natural variant281L → P in ANDI. Ref.15
VAR_015240
Natural variant471A → V in ANDI. Ref.15
VAR_015241
Natural variant571Q → P in ANDI. Ref.16
Corresponds to variant rs28931580 [ dbSNP | Ensembl ].
VAR_015256
Natural variant641G → R in ANDI. Ref.3
VAR_004401
Natural variant681N → S in ANDI. Ref.10
VAR_015242
Natural variant701A → D in ANDI. Ref.19
VAR_062585
Natural variant711V → M in ANDI. Ref.15
VAR_015243
Natural variant1001G → R in ANDI. Ref.20
VAR_062586
Natural variant1001G → V in ANDI. Ref.16
Corresponds to variant rs28929477 [ dbSNP | Ensembl ].
VAR_015257
Natural variant1211L → F.
Corresponds to variant rs11169226 [ dbSNP | Ensembl ].
VAR_037577
Natural variant1251T → M in ANDI. Ref.12 Ref.14 Ref.15
VAR_015244
Natural variant1261T → M in ANDI. Ref.10
VAR_015245
Natural variant1471A → T in ANDI. Ref.10
VAR_015246
Natural variant1681V → M in ANDI. Ref.11
VAR_015247
Natural variant1751G → R in ANDI. Ref.12 Ref.14 Ref.15
VAR_015248
Natural variant1801G → S in ANDI. Ref.20
VAR_062587
Natural variant1811C → W in ANDI. Ref.9
VAR_015249
Natural variant1851P → A in ANDI. Ref.15
VAR_015250
Natural variant1871R → C in ANDI; mutant protein does not fold properly and is not functional. Ref.3 Ref.17
VAR_004402
Natural variant1871R → H in ANDI. Ref.19
VAR_062588
Natural variant1901A → T in ANDI; mutant protein does not fold properly and is not functional. Ref.12 Ref.17
VAR_015251
Natural variant1941V → I. Ref.15
VAR_015252
Natural variant2021W → C in ANDI. Ref.8
VAR_015253
Natural variant2161S → P in ANDI. Ref.3 Ref.11
VAR_004403
Natural variant2541R → L in ANDI; results in the loss of arginine vasopressin-mediated phosphorylation at S-256. Ref.18
VAR_062589
Natural variant2541R → 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. Ref.21
VAR_062590
Natural variant2581E → K in ANDI; retained in the Golgi compartment. Ref.13 Ref.22
VAR_015254
Natural variant2621P → 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. Ref.12 Ref.17
VAR_015255

Experimental info

Mutagenesis1481S → A: No effect on sorting from the ER to the vesicles, redistribution to apical membrane, or endocytosis. Ref.7
Mutagenesis1481S → D: Retained in the endoplasmic reticulum. Ref.7
Mutagenesis2291S → A: No effect on sorting from the ER to the vesicles, redistribution to apical membrane, or endocytosis. Ref.7
Mutagenesis2291S → D: No effect on sorting from the ER to the vesicles, redistribution to apical membrane, or endocytosis. Ref.7
Mutagenesis2311S → A: No effect on sorting from the ER to the vesicles, redistribution to apical membrane, or endocytosis. Ref.7
Mutagenesis2311S → D: No effect on sorting from the ER to the vesicles, redistribution to apical membrane, or endocytosis. Ref.7
Mutagenesis2441T → A: No effect on sorting from the ER to the vesicles, redistribution to apical membrane, or endocytosis. Ref.7
Mutagenesis2441T → E: No effect on sorting from the ER to the vesicles, redistribution to apical membrane, or endocytosis. Ref.7
Mutagenesis2561S → A: Retained in vesicles. Ref.7
Mutagenesis2561S → D: Expressed in the apical membrane. Ref.7
Sequence conflict35 – 384PQAL → ATAP Ref.4
Sequence conflict831V → F Ref.4

Sequences

Sequence LengthMass (Da)Tools
P41181 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: C2DDE2AF4DDD192A

FASTA27128,837
        10         20         30         40         50         60 
MWELRSIAFS RAVFAEFLAT LLFVFFGLGS ALNWPQALPS VLQIAMAFGL GIGTLVQALG 

        70         80         90        100        110        120 
HISGAHINPA VTVACLVGCH VSVLRAAFYV AAQLLGAVAG AALLHEITPA DIRGDLAVNA 

       130        140        150        160        170        180 
LSNSTTAGQA VTVELFLTLQ LVLCIFASTD ERRGENPGTP ALSIGFSVAL GHLLGIHYTG 

       190        200        210        220        230        240 
CSMNPARSLA PAVVTGKFDD HWVFWIGPLV GAILGSLLYN YVLFPPAKSL SERLAVLKGL 

       250        260        270 
EPDTDWEERE VRRRQSVELH SPQSLPRGTK A 

« Hide

References

« Hide 'large scale' references
[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRA53442.
I64818.
RefSeqNP_000477.1. NM_000486.5.
UniGeneHs.130730.

3D structure databases

ProteinModelPortalP41181.
SMRP41181. Positions 3-239.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106855. 2 interactions.
STRING9606.ENSP00000199280.

Chemistry

GuidetoPHARMACOLOGY689.

Protein family/group databases

TCDB1.A.8.8.8. the major intrinsic protein (mip) family.

PTM databases

PhosphoSiteP41181.

Polymorphism databases

DMDM728874.

Proteomic databases

PaxDbP41181.
PRIDEP41181.

Protocols and materials databases

DNASU359.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000199280; ENSP00000199280; ENSG00000167580.
GeneID359.
KEGGhsa:359.
UCSCuc001rvn.3. human.

Organism-specific databases

CTD359.
GeneCardsGC12P050400.
HGNCHGNC:634. AQP2.
HPAHPA046834.
MIM107777. gene.
125800. phenotype.
neXtProtNX_P41181.
Orphanet223. Nephrogenic diabetes insipidus.
PharmGKBPA24920.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0580.
HOGENOMHOG000288286.
HOVERGENHBG000312.
InParanoidP41181.
KOK09865.
OMAHEITPAN.
PhylomeDBP41181.
TreeFamTF312940.

Enzyme and pathway databases

ReactomeREACT_15518. Transmembrane transport of small molecules.

Gene expression databases

ArrayExpressP41181.
BgeeP41181.
CleanExHS_AQP2.
GenevestigatorP41181.

Family and domain databases

Gene3D1.20.1080.10. 1 hit.
InterProIPR023271. Aquaporin-like.
IPR000425. MIP.
IPR022357. MIP_CS.
[Graphical view]
PANTHERPTHR19139. PTHR19139. 1 hit.
PfamPF00230. MIP. 1 hit.
[Graphical view]
PRINTSPR00783. MINTRINSICP.
SUPFAMSSF81338. SSF81338. 1 hit.
TIGRFAMsTIGR00861. MIP. 1 hit.
PROSITEPS00221. MIP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiAquaporin_2.
GenomeRNAi359.
NextBio1501.
PROP41181.
SOURCESearch...

Entry information

Entry nameAQP2_HUMAN
AccessionPrimary (citable) accession number: P41181
Secondary accession number(s): Q9UD68
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: April 16, 2014
This is version 141 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM