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P29972

- AQP1_HUMAN

UniProt

P29972 - AQP1_HUMAN

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Protein

Aquaporin-1

Gene
AQP1, CHIP28
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 red cells and kidney proximal tubules with high permeability to water, thereby permitting water to move in the direction of an osmotic gradient.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei56 – 561Substrate discrimination
Sitei180 – 1801Substrate discrimination
Sitei189 – 1891Hg(2+)-sensitive residue
Sitei195 – 1951Substrate discrimination

GO - Molecular functioni

  1. ammonium transmembrane transporter activity Source: UniProtKB
  2. carbon dioxide transmembrane transporter activity Source: UniProtKB
  3. glycerol transmembrane transporter activity Source: UniProtKB
  4. intracellular cGMP activated cation channel activity Source: UniProtKB
  5. nitric oxide transmembrane transporter activity Source: UniProtKB
  6. potassium channel activity Source: UniProtKB
  7. potassium ion transmembrane transporter activity Source: UniProtKB
  8. protein binding Source: UniProtKB
  9. transmembrane transporter activity Source: UniProtKB
  10. water channel activity Source: UniProtKB
  11. water transmembrane transporter activity Source: UniProtKB

GO - Biological processi

  1. ammonium transmembrane transport Source: GOC
  2. ammonium transport Source: UniProtKB
  3. bicarbonate transport Source: Reactome
  4. carbon dioxide transmembrane transport Source: UniProtKB
  5. carbon dioxide transport Source: UniProtKB
  6. cellular homeostasis Source: UniProtKB
  7. cellular hyperosmotic response Source: UniProtKB
  8. cellular response to cAMP Source: UniProtKB
  9. cellular response to copper ion Source: UniProtKB
  10. cellular response to dexamethasone stimulus Source: UniProtKB
  11. cellular response to hydrogen peroxide Source: UniProtKB
  12. cellular response to hypoxia Source: UniProtKB
  13. cellular response to inorganic substance Source: UniProtKB
  14. cellular response to mechanical stimulus Source: UniProtKB
  15. cellular response to mercury ion Source: UniProtKB
  16. cellular response to nitric oxide Source: UniProtKB
  17. cellular response to retinoic acid Source: UniProtKB
  18. cellular response to salt stress Source: UniProtKB
  19. cellular response to stress Source: UniProtKB
  20. cellular response to UV Source: UniProtKB
  21. cell volume homeostasis Source: UniProtKB
  22. cerebrospinal fluid secretion Source: UniProtKB
  23. cGMP biosynthetic process Source: UniProtKB
  24. establishment or maintenance of actin cytoskeleton polarity Source: UniProtKB
  25. glycerol transport Source: UniProtKB
  26. lateral ventricle development Source: UniProtKB
  27. maintenance of symbiont-containing vacuole by host Source: UniProtKB
  28. multicellular organismal water homeostasis Source: UniProtKB
  29. negative regulation of apoptotic process Source: UniProtKB
  30. negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
  31. nitric oxide transport Source: UniProtKB
  32. odontogenesis Source: UniProtKB
  33. pancreatic juice secretion Source: UniProtKB
  34. positive regulation of angiogenesis Source: UniProtKB
  35. positive regulation of fibroblast proliferation Source: UniProtKB
  36. positive regulation of saliva secretion Source: UniProtKB
  37. potassium ion transmembrane transport Source: GOC
  38. potassium ion transport Source: UniProtKB
  39. renal water transport Source: UniProtKB
  40. response to drug Source: UniProtKB
  41. small molecule metabolic process Source: Reactome
  42. transepithelial water transport Source: UniProtKB
  43. transmembrane transport Source: Reactome
  44. water transport Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Blood group antigen

Keywords - Biological processi

Transport

Enzyme and pathway databases

ReactomeiREACT_121329. Erythrocytes take up carbon dioxide and release oxygen.
REACT_121380. Erythrocytes take up oxygen and release carbon dioxide.
REACT_23826. Passive transport by Aquaporins.
REACT_24023. Regulation of water balance by renal Aquaporins.

Protein family/group databases

TCDBi1.A.8.8.1. the major intrinsic protein (mip) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Aquaporin-1
Short name:
AQP-1
Alternative name(s):
Aquaporin-CHIP
Urine water channel
Water channel protein for red blood cells and kidney proximal tubule
Gene namesi
Name:AQP1
Synonyms:CHIP28
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 7

Organism-specific databases

HGNCiHGNC:633. AQP1.

Subcellular locationi

Cell membrane; Multi-pass membrane protein 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 76Cytoplasmic1 Publication
Transmembranei8 – 3629Helical; Name=Helix 1Add
BLAST
Topological domaini37 – 4812Extracellular1 PublicationAdd
BLAST
Transmembranei49 – 6618Helical; Name=Helix 2Add
BLAST
Topological domaini67 – 704Cytoplasmic1 Publication
Intramembranei71 – 766
Intramembranei77 – 848Helical; Name=Helix B
Topological domaini85 – 9410Cytoplasmic1 Publication
Transmembranei95 – 11521Helical; Name=Helix 3Add
BLAST
Topological domaini116 – 13621Extracellular1 PublicationAdd
BLAST
Transmembranei137 – 15519Helical; Name=Helix 4Add
BLAST
Topological domaini156 – 16611Cytoplasmic1 PublicationAdd
BLAST
Transmembranei167 – 18317Helical; Name=Helix 5Add
BLAST
Topological domaini184 – 1863Extracellular1 Publication
Intramembranei187 – 1926
Intramembranei193 – 2008Helical; Name=Helix E
Topological domaini201 – 2077Extracellular1 Publication
Transmembranei208 – 22821Helical; Name=Helix 6Add
BLAST
Topological domaini229 – 26941Cytoplasmic1 PublicationAdd
BLAST

GO - Cellular componenti

  1. apical part of cell Source: UniProtKB
  2. apical plasma membrane Source: UniProtKB
  3. basal plasma membrane Source: UniProtKB
  4. basolateral plasma membrane Source: UniProtKB
  5. brush border Source: UniProtKB
  6. brush border membrane Source: UniProtKB
  7. cytoplasm Source: UniProtKB
  8. extracellular vesicular exosome Source: UniProt
  9. integral component of plasma membrane Source: ProtInc
  10. nuclear membrane Source: UniProtKB
  11. nucleus Source: UniProtKB
  12. plasma membrane Source: UniProtKB
  13. sarcolemma Source: UniProtKB
  14. symbiont-containing vacuole Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Organism-specific databases

MIMi110450. phenotype.
PharmGKBiPA24918.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 269268Aquaporin-1PRO_0000063920Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi42 – 421N-linked (GlcNAc...)
Glycosylationi205 – 2051N-linked (GlcNAc...) Reviewed prediction
Modified residuei262 – 2621Phosphoserine By similarity

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP29972.
PRIDEiP29972.

PTM databases

PhosphoSiteiP29972.

Expressioni

Tissue specificityi

Detected in erythrocytes (at protein level). Expressed in a number of tissues including erythrocytes, renal tubules, retinal pigment epithelium, heart, lung, skeletal muscle, kidney and pancreas. Weakly expressed in brain, placenta and liver.1 Publication

Gene expression databases

ArrayExpressiP29972.
BgeeiP29972.
CleanExiHS_AQP1.
GenevestigatoriP29972.

Organism-specific databases

HPAiCAB001707.
HPA019206.

Interactioni

Subunit structurei

Homotetramer. Interacts with EPHB2; involved in endolymph production in the inner ear By similarity. Identified in a complex with STOM.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
MDFIQ997504EBI-745213,EBI-724076

Protein-protein interaction databases

BioGridi106854. 7 interactions.
DIPiDIP-29607N.
IntActiP29972. 8 interactions.
MINTiMINT-1439356.
STRINGi9606.ENSP00000311165.

Structurei

Secondary structure

1
269
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi8 – 3528
Beta strandi37 – 426
Helixi48 – 6518
Beta strandi68 – 714
Helixi76 – 838
Helixi94 – 11421
Turni119 – 1224
Beta strandi132 – 1354
Helixi136 – 15419
Helixi166 – 18217
Turni183 – 1853
Helixi192 – 1998
Helixi207 – 22721

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FQYX-ray3.80A1-269[»]
1H6IX-ray3.54A1-269[»]
1IH5X-ray3.70A1-269[»]
ProteinModelPortaliP29972.
SMRiP29972. Positions 9-233.

Miscellaneous databases

EvolutionaryTraceiP29972.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi76 – 783NPA 1
Motifi192 – 1943NPA 2

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi159 – 1624Poly-Arg

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.
InParanoidiP29972.
KOiK09864.
OMAiITHNFKD.
OrthoDBiEOG7N8ZWD.
PhylomeDBiP29972.
TreeFamiTF312940.

Family and domain databases

Gene3Di1.20.1080.10. 1 hit.
InterProiIPR023271. Aquaporin-like.
IPR023274. Aquaporin_1.
IPR000425. MIP.
IPR022357. MIP_CS.
[Graphical view]
PANTHERiPTHR19139. PTHR19139. 1 hit.
PfamiPF00230. MIP. 1 hit.
[Graphical view]
PRINTSiPR02013. AQUAPORIN1.
PR00783. MINTRINSICP.
SUPFAMiSSF81338. SSF81338. 1 hit.
TIGRFAMsiTIGR00861. MIP. 1 hit.
PROSITEiPS00221. MIP. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P29972-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

MASEFKKKLF WRAVVAEFLA TTLFVFISIG SALGFKYPVG NNQTAVQDNV    50
KVSLAFGLSI ATLAQSVGHI SGAHLNPAVT LGLLLSCQIS IFRALMYIIA 100
QCVGAIVATA ILSGITSSLT GNSLGRNDLA DGVNSGQGLG IEIIGTLQLV 150
LCVLATTDRR RRDLGGSAPL AIGLSVALGH LLAIDYTGCG INPARSFGSA 200
VITHNFSNHW IFWVGPFIGG ALAVLIYDFI LAPRSSDLTD RVKVWTSGQV 250
EEYDLDADDI NSRVEMKPK 269
Length:269
Mass (Da):28,526
Last modified:January 23, 2007 - v3
Checksum:iBA204D82FB26352E
GO
Isoform 2 (identifier: P29972-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-45: MASEFKKKLF...KYPVGNNQTA → MPGARPLPLV...LGRVGPGSRQ
     46-128: Missing.

Note: No experimental confirmation available.

Show »
Length:186
Mass (Da):19,956
Checksum:i5C132B4A21FCC8BC
GO
Isoform 3 (identifier: P29972-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-128: MASEFKKKLF...LTGNSLGRND → MFWTFGYEAV...LGRVGPGSRQ

Note: Gene prediction based on EST data.

Show »
Length:218
Mass (Da):23,425
Checksum:i409D14C5A0F352CE
GO
Isoform 4 (identifier: P29972-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-13: MASEFKKKLFWRA → MQSGMGWNVLDFW
     14-128: Missing.

Note: Gene prediction based on EST data.

Show »
Length:154
Mass (Da):16,677
Checksum:i764FA0B49CB3B1FE
GO

Polymorphismi

AQP1 is responsible for the Colton blood group system. Approximately 92% of Caucasians are Co(A+B-) (Ala-46), approximately 8% are Co(A+B+), and only 0.2% are Co(A-B+) (Val-46). Co(A-B-) which is very rare, is due to a complete absence of AQP1.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti38 – 381P → L in Co(A-B-) antigen; non functional AQP1; red cells show low osmotic water permeability. 1 Publication
VAR_013279
Natural varianti45 – 451A → V in Co(A-B+) antigen. 2 Publications
Corresponds to variant rs28362692 [ dbSNP | Ensembl ].
VAR_004400
Natural varianti165 – 1651G → D.1 Publication
Corresponds to variant rs28362731 [ dbSNP | Ensembl ].
VAR_022318

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 128128MASEF…LGRND → MFWTFGYEAVSPAGPSHLFA SLLLGVLLTITFMPGARPLP LVLVPQNTLAWMQLDAKAPA HPRPLQLLGRVGPGSRQ in isoform 3. VSP_046679Add
BLAST
Alternative sequencei1 – 4545MASEF…NNQTA → MPGARPLPLVLVPQNTLAWM QLDAKAPAHPRPLQLLGRVG PGSRQ in isoform 2. VSP_046109Add
BLAST
Alternative sequencei1 – 1313MASEF…LFWRA → MQSGMGWNVLDFW in isoform 4. VSP_046680Add
BLAST
Alternative sequencei14 – 128115Missing in isoform 4. VSP_046681Add
BLAST
Alternative sequencei46 – 12883Missing in isoform 2. VSP_046110Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti45 – 451A → T in AAH22486. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M77829 mRNA. Translation: AAA58425.1.
U41517 mRNA. Translation: AAC50648.1.
U41518 mRNA. Translation: AAC50649.1.
S73482 mRNA. Translation: AAB31193.1.
AK309608 mRNA. No translation available.
AY953319 Genomic DNA. Translation: AAX24129.1.
AC004691 Genomic DNA. Translation: AAC16481.1.
AC005155 Genomic DNA. Translation: AAC23788.1.
AB451275 mRNA. Translation: BAG70089.1.
AB451402 mRNA. Translation: BAG70216.1.
CH471073 Genomic DNA. Translation: EAW93971.1.
BC022486 mRNA. Translation: AAH22486.1.
AF480415 Genomic DNA. Translation: AAL87136.1.
CCDSiCCDS5431.1. [P29972-1]
CCDS55096.1. [P29972-4]
CCDS55097.1. [P29972-3]
CCDS55098.1. [P29972-2]
PIRiA41616.
I52366.
RefSeqiNP_001171989.1. NM_001185060.1. [P29972-2]
NP_001171990.1. NM_001185061.1. [P29972-3]
NP_001171991.1. NM_001185062.1. [P29972-4]
NP_932766.1. NM_198098.2. [P29972-1]
UniGeneiHs.76152.

Genome annotation databases

EnsembliENST00000311813; ENSP00000311165; ENSG00000240583. [P29972-1]
ENST00000409611; ENSP00000387178; ENSG00000240583. [P29972-3]
ENST00000409899; ENSP00000386712; ENSG00000240583. [P29972-4]
ENST00000441328; ENSP00000405698; ENSG00000240583. [P29972-2]
GeneIDi358.
KEGGihsa:358.
UCSCiuc003tbv.2. human. [P29972-1]

Polymorphism databases

DMDMi267412.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

dbRBC/BGMUT

Blood group antigen gene mutation database

SeattleSNPs
Protein Spotlight

Liquid states - Issue 36 of July 2003

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M77829 mRNA. Translation: AAA58425.1 .
U41517 mRNA. Translation: AAC50648.1 .
U41518 mRNA. Translation: AAC50649.1 .
S73482 mRNA. Translation: AAB31193.1 .
AK309608 mRNA. No translation available.
AY953319 Genomic DNA. Translation: AAX24129.1 .
AC004691 Genomic DNA. Translation: AAC16481.1 .
AC005155 Genomic DNA. Translation: AAC23788.1 .
AB451275 mRNA. Translation: BAG70089.1 .
AB451402 mRNA. Translation: BAG70216.1 .
CH471073 Genomic DNA. Translation: EAW93971.1 .
BC022486 mRNA. Translation: AAH22486.1 .
AF480415 Genomic DNA. Translation: AAL87136.1 .
CCDSi CCDS5431.1. [P29972-1 ]
CCDS55096.1. [P29972-4 ]
CCDS55097.1. [P29972-3 ]
CCDS55098.1. [P29972-2 ]
PIRi A41616.
I52366.
RefSeqi NP_001171989.1. NM_001185060.1. [P29972-2 ]
NP_001171990.1. NM_001185061.1. [P29972-3 ]
NP_001171991.1. NM_001185062.1. [P29972-4 ]
NP_932766.1. NM_198098.2. [P29972-1 ]
UniGenei Hs.76152.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1FQY X-ray 3.80 A 1-269 [» ]
1H6I X-ray 3.54 A 1-269 [» ]
1IH5 X-ray 3.70 A 1-269 [» ]
ProteinModelPortali P29972.
SMRi P29972. Positions 9-233.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 106854. 7 interactions.
DIPi DIP-29607N.
IntActi P29972. 8 interactions.
MINTi MINT-1439356.
STRINGi 9606.ENSP00000311165.

Chemistry

DrugBanki DB00819. Acetazolamide.
GuidetoPHARMACOLOGYi 688.

Protein family/group databases

TCDBi 1.A.8.8.1. the major intrinsic protein (mip) family.

PTM databases

PhosphoSitei P29972.

Polymorphism databases

DMDMi 267412.

Proteomic databases

PaxDbi P29972.
PRIDEi P29972.

Protocols and materials databases

DNASUi 358.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000311813 ; ENSP00000311165 ; ENSG00000240583 . [P29972-1 ]
ENST00000409611 ; ENSP00000387178 ; ENSG00000240583 . [P29972-3 ]
ENST00000409899 ; ENSP00000386712 ; ENSG00000240583 . [P29972-4 ]
ENST00000441328 ; ENSP00000405698 ; ENSG00000240583 . [P29972-2 ]
GeneIDi 358.
KEGGi hsa:358.
UCSCi uc003tbv.2. human. [P29972-1 ]

Organism-specific databases

CTDi 358.
GeneCardsi GC07P030894.
HGNCi HGNC:633. AQP1.
HPAi CAB001707.
HPA019206.
MIMi 107776. gene.
110450. phenotype.
neXtProti NX_P29972.
PharmGKBi PA24918.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0580.
HOGENOMi HOG000288286.
HOVERGENi HBG000312.
InParanoidi P29972.
KOi K09864.
OMAi ITHNFKD.
OrthoDBi EOG7N8ZWD.
PhylomeDBi P29972.
TreeFami TF312940.

Enzyme and pathway databases

Reactomei REACT_121329. Erythrocytes take up carbon dioxide and release oxygen.
REACT_121380. Erythrocytes take up oxygen and release carbon dioxide.
REACT_23826. Passive transport by Aquaporins.
REACT_24023. Regulation of water balance by renal Aquaporins.

Miscellaneous databases

EvolutionaryTracei P29972.
GeneWikii Aquaporin_1.
GenomeRNAii 358.
NextBioi 1497.
PROi P29972.
SOURCEi Search...

Gene expression databases

ArrayExpressi P29972.
Bgeei P29972.
CleanExi HS_AQP1.
Genevestigatori P29972.

Family and domain databases

Gene3Di 1.20.1080.10. 1 hit.
InterProi IPR023271. Aquaporin-like.
IPR023274. Aquaporin_1.
IPR000425. MIP.
IPR022357. MIP_CS.
[Graphical view ]
PANTHERi PTHR19139. PTHR19139. 1 hit.
Pfami PF00230. MIP. 1 hit.
[Graphical view ]
PRINTSi PR02013. AQUAPORIN1.
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. "Isolation of the cDNA for erythrocyte integral membrane protein of 28 kilodaltons: member of an ancient channel family."
    Preston G.M., Agre P.
    Proc. Natl. Acad. Sci. U.S.A. 88:11110-11114(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE.
  2. "The human aquaporin-CHIP gene. Structure, organization, and chromosomal localization."
    Moon C., Preston G.M., Griffin C.A., Jabs E.W., Agre P.
    J. Biol. Chem. 268:15772-15778(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Characterization of the 3' UTR sequence encoded by the AQP-1 gene in human retinal pigment epithelium."
    Ruiz A.C., Bok D.
    Biochim. Biophys. Acta 1282:174-178(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Retinal pigment epithelium.
  4. "The water channel gene in human uterus."
    Li X., Yu H., Koide S.S.
    Biochem. Mol. Biol. Int. 32:371-377(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Uterus.
  5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Mesangial cell.
  6. SeattleSNPs variation discovery resource
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS VAL-45 AND ASP-165.
  7. "Human protein factory for converting the transcriptome into an in vitro-expressed proteome."
    Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.
    , Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., Nomura N.
    Nat. Methods 5:1011-1017(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  8. "The DNA sequence of human chromosome 7."
    Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
    , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
    Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  10. "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] (ISOFORM 1).
    Tissue: Brain.
  11. "Human chondrocytes in situ express aquaporin water channels: changes in AQP1 abundance in pathologies of articular cartilage."
    Trujillo E., Gonzalez T., Martin-Vasallo P., Marples D., Mobasheri A.
    Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 5-269.
    Tissue: Articular cartilage.
  12. "Erythrocyte Mr 28,000 transmembrane protein exists as a multisubunit oligomer similar to channel proteins."
    Smith B.L., Agre P.
    J. Biol. Chem. 266:6407-6415(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-36.
  13. "Appearance of water channels in Xenopus oocytes expressing red cell CHIP28 protein."
    Preston G.M., Carroll T.P., Guggino W.B., Agre P.
    Science 256:385-387(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  14. "The mercury-sensitive residue at cysteine 189 in the CHIP28 water channel."
    Preston G.M., Jung J.S., Guggino W.B., Agre P.
    J. Biol. Chem. 268:17-20(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: TARGET OF MERCURY INHIBITION.
  15. "Membrane topology of aquaporin CHIP. Analysis of functional epitope-scanning mutants by vectorial proteolysis."
    Preston G.M., Jung J.S., Guggino W.B., Agre P.
    J. Biol. Chem. 269:1668-1673(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY.
  16. "Stomatin interacts with GLUT1/SLC2A1, band 3/SLC4A1, and aquaporin-1 in human erythrocyte membrane domains."
    Rungaldier S., Oberwagner W., Salzer U., Csaszar E., Prohaska R.
    Biochim. Biophys. Acta 1828:956-966(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, IDENTIFICATION IN A COMPLEX WITH STOM, SUBUNIT.
  17. "The three-dimensional structure of human erythrocyte aquaporin CHIP."
    Walz T., Smith B.L., Agre P., Engel A.
    EMBO J. 13:2985-2993(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY ELECTRON MICROSCOPY (1.6 ANGSTROMS).
  18. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (6 ANGSTROMS).
  19. "Structural determinants of water permeation through aquaporin-1."
    Murata K., Mitsuoka K., Hirai T., Walz T., Agre P., Heymann J.B., Engel A., Fujiyoshi Y.
    Nature 407:599-605(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.8 ANGSTROMS).
  20. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.54 ANGSTROMS).
  21. "Visualization of a water-selective pore by electron crystallography in vitreous ice."
    Ren G., Reddy V.S., Cheng A., Melnyk P., Mitra A.K.
    Proc. Natl. Acad. Sci. U.S.A. 98:1398-1403(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.7 ANGSTROMS).
  22. "Human red cell aquaporin CHIP. I. Molecular characterization of ABH and Colton blood group antigens."
    Smith B.L., Preston G.M., Spring F., Anstee D.J., Agre P.
    J. Clin. Invest. 94:1043-1049(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT BLOOD GROUP COLTON VAL-45.
  23. "Mutations in aquaporin-1 in phenotypically normal humans without functional CHIP water channels."
    Preston G.M., Smith B.L., Zeidel M.L., Moulds J.J., Agre P.
    Science 265:1585-1587(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT LEU-38.

Entry informationi

Entry nameiAQP1_HUMAN
AccessioniPrimary (citable) accession number: P29972
Secondary accession number(s): B5BU39
, E7EM69, E9PC21, F5GY19, Q8TBI5, Q8TDC1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 166 of the entry and version 3 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

Miscellaneous

Pharmacologically inhibited by submillimolar concentrations of mercury.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Blood group antigen proteins
    Nomenclature of blood group antigens and list of entries
  2. Human chromosome 7
    Human chromosome 7: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
  8. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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