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UniProtKB/Swiss-Prot entry P05023


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name AT1A1_HUMAN
Primary accession number P05023
Secondary accession numbers Q16689 Q6LDM4 Q9UJ20 Q9UJ21
Integrated into Swiss-Prot on August 13, 1987
Sequence was last modified on August 13, 1987 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 112)
Name and origin of the protein
Protein name Sodium/potassium-transporting ATPase subunit alpha-1 [Precursor]
Synonyms Sodium pump subunit alpha-1
EC 3.6.3.9
Na(+)/K(+) ATPase alpha-1 subunit
Gene name
Name: ATP1A1
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
PubMed=2430951 [NCBI, ExPASy, EBI, Israel, Japan]
Kawakami K., Ohta T., Nojima H., Nagano K.;
"Primary structure of the alpha-subunit of human Na,K-ATPase deduced from cDNA sequence.";
J. Biochem. 100:389-397(1986).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
TISSUE=Retinal pigment epithelium;
DOI=10.1016/0378-1119(94)00812-7; PubMed=7536695 [NCBI, ExPASy, EBI, Israel, Japan]
Ruiz A., Bhat S.P., Bok D.;
"Characterization and quantification of full-length and truncated Na,K-ATPase alpha 1 and beta 1 RNA transcripts expressed in human retinal pigment epithelium.";
Gene 155:179-184(1995).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature04727; PubMed=16710414 [NCBI, ExPASy, EBI, Israel, Japan]
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
TISSUE=Brain, Cervix, and Skin;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 471-619.
Ovchinnikov Y.A., Monastyrskaya G.S., Arsenyan S.G., Broude N.E., Petrukhin K.E., Grishin A.V., Arzamazova N.M., Severtsova I.V., Modyanov N.N.;
"Amino acid sequence of the 17-kilodalton fragment of the cytoplasmic region of the alpha-subunit of NA+,K+-ATPase.";
Dokl. Biochem. 288:270-272(1986).
[6]
NUCLEOTIDE SEQUENCE OF 253-341 AND 420-444.
DOI=10.1016/0014-5793(87)80677-4; PubMed=3036582 [NCBI, ExPASy, EBI, Israel, Japan]
Sverdlov E.D., Monastyrskaya G.S., Broude N.E., Ushkaryov Y.A., Allikmets R.L., Melkov A.M., Smirnov Y.V., Malyshev I.V., Dulubova I.E., Petrukhin K.E., Gryshin A.V., Kiyatkin N.I., Kostina M.B., Sverdlov V.E., Modyanov N.N., Ovchinnikov Y.A.;
"The family of human Na+,K+-ATPase genes. No less than five genes and/or pseudogenes related to the alpha-subunit.";
FEBS Lett. 217:275-278(1987).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 198-943.
TISSUE=Placenta;
PubMed=2891135 [NCBI, ExPASy, EBI, Israel, Japan]
Chehab F.F., Kan Y.W., Law M.L., Hartz J., Kao F.T., Blostein R.;
"Human placental Na+,K+-ATPase alpha subunit: cDNA cloning, tissue expression, DNA polymorphism, and chromosomal localization.";
Proc. Natl. Acad. Sci. U.S.A. 84:7901-7905(1987).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-61.
DOI=10.1016/0888-7543(90)90475-A; PubMed=1970326 [NCBI, ExPASy, EBI, Israel, Japan]
Shull M.M., Pugh D.G., Lingrel J.B.;
"The human Na, K-ATPase alpha 1 gene: characterization of the 5'-flanking region and identification of a restriction fragment length polymorphism.";
Genomics 6:451-460(1990).
[9]
NUCLEOTIDE SEQUENCE OF 85-148.
TISSUE=Placenta;
Zhang J.-S., Yang J.X., Fang M.W., Lu S.D.;
Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [MRNA] OF 168-189 AND 213-244.
PubMed=3035563 [NCBI, ExPASy, EBI, Israel, Japan]
Shull M.M., Lingrel J.B.;
"Multiple genes encode the human Na+,K+-ATPase catalytic subunit.";
Proc. Natl. Acad. Sci. U.S.A. 84:4039-4043(1987).
[11]
SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
DOI=10.1186/gb-2004-5-2-r8; PubMed=14759258 [NCBI, ExPASy, EBI, Israel, Japan]
Hillman R.T., Green R.E., Brenner S.E.;
"An unappreciated role for RNA surveillance.";
Genome Biol. 5:RESEARCH008.1-RESEARCH008.16(2004).
[12]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
DOI=10.1021/pr060363j; PubMed=17081065 [NCBI, ExPASy, EBI, Israel, Japan]
Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F.;
"Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes.";
J. Proteome Res. 5:3135-3144(2006).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-260, AND MASS SPECTROMETRY.
DOI=10.1016/j.cell.2007.11.025; PubMed=18083107 [NCBI, ExPASy, EBI, Israel, Japan]
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer.";
Cell 131:1190-1203(2007).
Comments
  • FUNCTION: This is the catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of sodium and potassium ions across the plasma membrane. This action creates the electrochemical gradient of sodium and potassium ions, providing the energy for active transport of various nutrients.
  • CATALYTIC ACTIVITY: ATP + H2O + Na+(In) + K+(Out) = ADP + phosphate + Na+(Out) + K+(In).
  • SUBUNIT: Composed of three subunits: alpha (catalytic), beta and gamma.
  • INTERACTION:
    Q92597:NDRG1; NbExp=1; IntAct=EBI-358778, EBI-716486;
  • SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. Melanosome. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV.
  • ALTERNATIVE PRODUCTS: 2 named isoforms [FASTA] produced by alternative splicing.
    NameLong
    Isoform IDP05023-1
    This is the isoform sequence displayed in this entry.
    NameShort
    Isoform IDP05023-2
    Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
    Features which should be applied to build the isoform sequence: VSP_000415, VSP_000416.
  • PTM: Phosphorylation on Tyr-10 modulates pumping activity (By similarity).
  • SIMILARITY: Belongs to the cation transport ATPase (P-type) family. Type IIC subfamily.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
D00099; BAA00061.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U16798; AAC50131.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL136376; CAI22199.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC003077; AAH03077.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC001330; AAH01330.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC050359; AAH50359.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X04297; CAA27840.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X03757; CAA27390.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M27572; AAA35573.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M27579; AAA35574.2; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
J03007; AAA51803.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L76938; AAA92713.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M30310; AAA51801.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M30309; AAA51801.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M16793; AAD56251.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M16794; AAD56252.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A24414; A24414.
RefSeq NP_000692.2; -.
NP_001001586.1; -.
UniGene Hs.371889
3D structure databases
HSSP P06685; 1MO7. [HSSP ENTRY / PDB]
SMR P05023; 383-595.
ModBase P05023.
Protein-protein interaction databases
IntAct P05023; -.
PTM databases
PhosphoSite P05023; -.
Organism-specific databases
H-InvDB HIX0000926; -.
HIX0057009; -.
HGNC HGNC:799; ATP1A1.
GenAtlas ATP1A1.
HPA CAB001988; -.
MIM 182310; gene. [NCBI / EBI]
PharmGKB PA62; -.
GeneCards P05023.
Gene expression databases
ArrayExpress P05023; -.
CleanEx HS_ATP1A1; -.
GermOnline ENSG00000163399; Homo sapiens.
Ontologies
GO
GO:0005624; Cellular component: membrane fraction (traceable author statement from ProtInc).
GO:0005890; Cellular component: sodium:potassium-exchanging ATPase complex (traceable author statement from ProtInc).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from UniProtKB).
GO:0005391; Molecular function: sodium:potassium-exchanging ATPase activity (traceable author statement from ProtInc).
GO:0030641; Biological process: regulation of cellular pH (inferred from sequence or structural similarity from UniProtKB).
GO:0030317; Biological process: sperm motility (inferred from sequence or structural similarity from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR006069; ATPase_cat_a.
IPR005775; ATPase_cat_a_euk.
IPR001757; ATPase_P.
IPR006068; ATPase_P_cat_C.
IPR004014; ATPase_P_cat_N.
IPR005834; Dehalogen-like_hydro.
IPR008250; E1-E2_ATPase_reg.
Graphical view of domain structure.
PANTHER PTHR11939; ATPase_P; 1.
Pfam PF00689; Cation_ATPase_C; 1.
PF00690; Cation_ATPase_N; 1.
PF00122; E1-E2_ATPase; 1.
PF00702; Hydrolase; 1.
Pfam graphical view of domain structure.
PRINTS PR00119; CATATPASE.
PR00121; NAKATPASE.
TIGRFAMs TIGR01106; ATPase-IIC_X-K; 1.
TIGR01494; ATPase_P-type; 4.
PROSITE PS00154; ATPASE_E1_E2; 1.
BLOCKS P05023.
ProtoNet P05023.
Proteomic databases
PeptideAtlas P05023; -.
Genome annotation databases
Ensembl ENSG00000163399; Homo sapiens. [Contig view]
GeneID 476; -.
KEGG hsa:476; -.
Phylogenomic databases
HOGENOM P05023; -.
HOVERGEN P05023; -.
Other
DrugBank DB00511; Acetyldigitoxin.
DB01430; Almitrine.
DB01370; Aluminium.
DB01244; Bepridil.
DB01158; Bretylium.
DB01197; Captopril.
DB01078; Deslanoside.
DB01119; Diazoxide.
DB01396; Digitoxin.
DB00390; Digoxin.
DB00736; Esomeprazole.
DB00903; Ethacrynic acid.
DB00695; Furosemide.
DB00774; Hydroflumethiazide.
DB00232; Methyclothiazide.
DB01092; Ouabain.
DB00213; Pantoprazole.
DB01021; Trichlormethiazide.
NextBio 1971; -.
SOURCE ATP1A1; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Alternative splicing; ATP-binding; Hydrolase; Ion transport; Magnesium; Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein; Potassium; Potassium transport; Sodium; Sodium transport; Sodium/potassium transport; Transmembrane; Transport.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom    To Length Description FTId
PROPEP   1      5  5      PRO_0000002483
CHAIN   6   1023  1018     Sodium/potassium-transporting ATPase subunit alpha-1. PRO_0000002484
TOPO_DOM   6     87  82     Cytoplasmic (Potential). 
TRANSMEM   88    108  21     Potential. 
TOPO_DOM   109    131  23     Lumenal (Potential). 
TRANSMEM   132    152  21     Potential. 
TOPO_DOM   153    288  136     Cytoplasmic (Potential). 
TRANSMEM   289    308  20     Potential. 
TOPO_DOM   309    320  12     Lumenal (Potential). 
TRANSMEM   321    338  18     Potential. 
TOPO_DOM   339    772  434     Cytoplasmic (Potential). 
TRANSMEM   773    792  20     Potential. 
TOPO_DOM   793    802  10     Lumenal (Potential). 
TRANSMEM   803    823  21     Potential. 
TOPO_DOM   824    843  20     Cytoplasmic (Potential). 
TRANSMEM   844    866  23     Potential. 
TOPO_DOM   867    918  52     Lumenal (Potential). 
TRANSMEM   919    938  20     Potential. 
TOPO_DOM   939    951  13     Cytoplasmic (Potential). 
TRANSMEM   952    970  19     Potential. 
TOPO_DOM   971    985  15     Lumenal (Potential). 
TRANSMEM   986   1006  21     Potential. 
TOPO_DOM   1007   1023  17     Cytoplasmic (Potential). 
REGION   82     84  3     Phosphoinositide-3 kinase binding (By similarity). 
ACT_SITE   376    376        4-aspartylphosphate intermediate (By similarity). 
METAL   717    717        Magnesium (By similarity). 
METAL   721    721        Magnesium (By similarity). 
MOD_RES   10     10        Phosphotyrosine (By similarity). 
MOD_RES   16     16        Phosphoserine; by PKC (By similarity). 
MOD_RES   47     47        Phosphoserine (By similarity). 
MOD_RES   217    217        Phosphoserine (By similarity). 
MOD_RES   219    219        Phosphothreonine (By similarity). 
MOD_RES   228    228        Phosphoserine (By similarity). 
MOD_RES   260    260        Phosphotyrosine. 
MOD_RES   452    452        Phosphoserine (By similarity). 
MOD_RES   943    943        Phosphoserine; by PKA (By similarity). 
VAR_SEQ   638    681        NETVEDIAARLNIPVSQVNPRDAKACVVHGSDLKDMTSE QLDDI -> SGPMSRGKSWSSPATQPSSSVSWWCSGPTWSSVRPGGIR SSSRG (in isoform Short). VSP_000415
VAR_SEQ   682   1023        Missing (in isoform Short). VSP_000416
CONFLICT   475    475        A -> T (in Ref. 5). 
CONFLICT   499    499        S -> A (in Ref. 5). 
CONFLICT   502    502        Q -> R (in Ref. 5). 
CONFLICT   523    523        L -> I (in Ref. 5; CAA27390). 
Sequence information
Length: 1023 AA [This is the length of the unprocessed precursor] Molecular weight: 112896 Da [This is the MW of the unprocessed precursor] CRC64: F3C6FDE04FB3F667 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MGKGVGRDKY EPAAVSEQGD KKGKKGKKDR DMDELKKEVS MDDHKLSLDE LHRKYGTDLS 

        70         80         90        100        110        120 
RGLTSARAAE ILARDGPNAL TPPPTTPEWI KFCRQLFGGF SMLLWIGAIL CFLAYSIQAA 

       130        140        150        160        170        180 
TEEEPQNDNL YLGVVLSAVV IITGCFSYYQ EAKSSKIMES FKNMVPQQAL VIRNGEKMSI 

       190        200        210        220        230        240 
NAEEVVVGDL VEVKGGDRIP ADLRIISANG CKVDNSSLTG ESEPQTRSPD FTNENPLETR 

       250        260        270        280        290        300 
NIAFFSTNCV EGTARGIVVY TGDRTVMGRI ATLASGLEGG QTPIAAEIEH FIHIITGVAV 

       310        320        330        340        350        360 
FLGVSFFILS LILEYTWLEA VIFLIGIIVA NVPEGLLATV TVCLTLTAKR MARKNCLVKN 

       370        380        390        400        410        420 
LEAVETLGST STICSDKTGT LTQNRMTVAH MWFDNQIHEA DTTENQSGVS FDKTSATWLA 

       430        440        450        460        470        480 
LSRIAGLCNR AVFQANQENL PILKRAVAGD ASESALLKCI ELCCGSVKEM RERYAKIVEI 

       490        500        510        520        530        540 
PFNSTNKYQL SIHKNPNTSE PQHLLVMKGA PERILDRCSS ILLHGKEQPL DEELKDAFQN 

       550        560        570        580        590        600 
AYLELGGLGE RVLGFCHLFL PDEQFPEGFQ FDTDDVNFPI DNLCFVGLIS MIDPPRAAVP 

       610        620        630        640        650        660 
DAVGKCRSAG IKVIMVTGDH PITAKAIAKG VGIISEGNET VEDIAARLNI PVSQVNPRDA 

       670        680        690        700        710        720 
KACVVHGSDL KDMTSEQLDD ILKYHTEIVF ARTSPQQKLI IVEGCQRQGA IVAVTGDGVN 

       730        740        750        760        770        780 
DSPALKKADI GVAMGIAGSD VSKQAADMIL LDDNFASIVT GVEEGRLIFD NLKKSIAYTL 

       790        800        810        820        830        840 
TSNIPEITPF LIFIIANIPL PLGTVTILCI DLGTDMVPAI SLAYEQAESD IMKRQPRNPK 

       850        860        870        880        890        900 
TDKLVNERLI SMAYGQIGMI QALGGFFTYF VILAENGFLP IHLLGLRVDW DDRWINDVED 

       910        920        930        940        950        960 
SYGQQWTYEQ RKIVEFTCHT AFFVSIVVVQ WADLVICKTR RNSVFQQGMK NKILIFGLFE 

       970        980        990       1000       1010       1020 
ETALAAFLSY CPGMGVALRM YPLKPTWWFC AFPYSLLIFV YDEVRKLIIR RRPGGWVEKE 


TYY 

P05023 in FASTA format

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