Sodium/potassium-transporting ATPase subunit alpha-1

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functionⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityⁱ

• ATP

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  + H₂O

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  + K⁺

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  (out) + Na⁺

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  (in) = ADP

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  + H⁺

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  + K⁺

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  (in) + Na⁺

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  (out) + phosphate

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  EC:7.2.2.13
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  Source: Rhea

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  ATP

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  +

  H₂O

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  +

  K⁺

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  (out)

  

  +

  Na⁺

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  (in)

  

  =

  ADP

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  +

  H⁺

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  +

  K⁺

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  (in)

  

  +

  Na⁺

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  (out)

  

  +

  phosphate

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  zoom

Sites

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functionⁱ

• ADP binding Source: RGD <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ
  • Ref.21

    "ATP-induced conformational changes of the nucleotide-binding domain of Na,K-ATPase."
    Hilge M., Siegal G., Vuister G.W., Guntert P., Gloor S.M., Abrahams J.P.
    Nat. Struct. Biol. 10:468-474(2003) [PubMed] [Europe PMC] [Abstract]

    Cited for: STRUCTURE BY NMR OF 383-595 ALONE AND IN COMPLEX WITH ATP, ATP-BINDING SITE.
• ankyrin binding Source: BHF-UCL <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#ipi">GO evidence code guide</a></p> Inferred from physical interactionⁱ
  • "Ankyrin binds to two distinct cytoplasmic domains of Na,K-ATPase alpha subunit."
    Devarajan P., Scaramuzzino D.A., Morrow J.S.
    Proc Natl Acad Sci U S A 91:2965-2969(1994) [PubMed] [Europe PMC] [Abstract]
• ATP binding Source: BHF-UCLInferred from direct assayⁱ
  • "Crystal structure of the sodium-potassium pump."
    Morth J.P., Pedersen B.P., Toustrup-Jensen M.S., Sorensen T.L., Petersen J., Andersen J.P., Vilsen B., Nissen P.
    Nature 450:1043-1049(2007) [PubMed] [Europe PMC] [Abstract]
• chaperone binding Source: BHF-UCLInferred from direct assayⁱ
  • "Ankyrin facilitates intracellular trafficking of alpha1-Na+-K+-ATPase in polarized cells."
    Stabach P.R., Devarajan P., Stankewich M.C., Bannykh S., Morrow J.S.
    Am J Physiol Cell Physiol 295:C1202-14(2008) [PubMed] [Europe PMC] [Abstract]
• phosphatase activity Source: RGD
• phosphatidylinositol 3-kinase binding Source: RGDInferred from physical interactionⁱ
  • "Association of PI3K-Akt signaling pathway with digitalis-induced hypertrophy of cardiac myocytes."
    Liu L., Zhao X., Pierre S.V., Askari A.
    Am J Physiol Cell Physiol 293:C1489-97(2007) [PubMed] [Europe PMC] [Abstract]
• potassium ion binding Source: BHF-UCLInferred from direct assayⁱ
  • "Crystal structure of the sodium-potassium pump."
    Morth J.P., Pedersen B.P., Toustrup-Jensen M.S., Sorensen T.L., Petersen J., Andersen J.P., Vilsen B., Nissen P.
    Nature 450:1043-1049(2007) [PubMed] [Europe PMC] [Abstract]
• protein domain specific binding Source: RGDInferred from physical interactionⁱ
  • "Role of the transmembrane domain of FXYD7 in structural and functional interactions with Na,K-ATPase."
    Li C., Crambert G., Thuillard D., Roy S., Schaer D., Geering K.
    J Biol Chem 280:42738-42743(2005) [PubMed] [Europe PMC] [Abstract]
• protein heterodimerization activity Source: ARUK-UCLInferred from physical interactionⁱ
  • "The alpha2beta2 isoform combination dominates the astrocytic Napisup>+pi/sup> /Kpisup>+pi/sup> -ATPase activity and is rendered nonfunctional by the alpha2.G301R familial hemiplegic migraine type 2-associated mutation."
    Stoica A., Larsen B.R., Assentoft M., Holm R., Holt L.M., Vilhardt F., Vilsen B., Lykke-Hartmann K., Olsen M.L., MacAulay N.
    Glia 65:1777-1793(2017) [PubMed] [Europe PMC] [Abstract]
• protein kinase binding Source: UniProtKBInferred from physical interactionⁱ
  • Ref.15

    "SIK1 is part of a cell sodium-sensing network that regulates active sodium transport through a calcium-dependent process."
    Sjostrom M., Stenstrom K., Eneling K., Zwiller J., Katz A.I., Takemori H., Bertorello A.M.
    Proc. Natl. Acad. Sci. U.S.A. 104:16922-16927(2007) [PubMed] [Europe PMC] [Abstract]

    Cited for: PHOSPHORYLATION, DEPHOSPHORYLATION, INTERACTION WITH SIK1.
• sodium:potassium-exchanging ATPase activity Source: UniProtKBInferred from direct assayⁱ
  • Ref.15

    "SIK1 is part of a cell sodium-sensing network that regulates active sodium transport through a calcium-dependent process."
    Sjostrom M., Stenstrom K., Eneling K., Zwiller J., Katz A.I., Takemori H., Bertorello A.M.
    Proc. Natl. Acad. Sci. U.S.A. 104:16922-16927(2007) [PubMed] [Europe PMC] [Abstract]

    Cited for: PHOSPHORYLATION, DEPHOSPHORYLATION, INTERACTION WITH SIK1.
• sodium ion binding Source: RGDInferred from direct assayⁱ
  • "Role of the transmembrane domain of FXYD7 in structural and functional interactions with Na,K-ATPase."
    Li C., Crambert G., Thuillard D., Roy S., Schaer D., Geering K.
    J Biol Chem 280:42738-42743(2005) [PubMed] [Europe PMC] [Abstract]
• steroid hormone binding Source: RGD

GO - Biological processⁱ

• cardiac muscle contraction Source: BHF-UCL <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#tas">GO evidence code guide</a></p> Traceable author statementⁱ
  • "The Na+/K+-ATPase alpha2-isoform regulates cardiac contractility in rat cardiomyocytes."
    Swift F., Tovsrud N., Enger U.H., Sjaastad I., Sejersted O.M.
    Cardiovasc Res 75:109-117(2007) [PubMed] [Europe PMC] [Abstract]
• cellular potassium ion homeostasis Source: RGD
• cellular response to mechanical stimulus Source: RGDInferred from direct assayⁱ
  • "Effects of different magnitudes of cyclic stretch on Na+-K+-ATPase in skeletal muscle cells in vitro."
    Yuan X., Lin Z., Luo S., Ji G., Yuan C., Wu Y.
    J Cell Physiol 212:509-518(2007) [PubMed] [Europe PMC] [Abstract]
• cellular response to steroid hormone stimulus Source: RGD
• cellular sodium ion homeostasis Source: RGD
• energy coupled proton transmembrane transport, against electrochemical gradient Source: RGDTraceable author statementⁱ
  • "Role of the transmembrane domain of FXYD7 in structural and functional interactions with Na,K-ATPase."
    Li C., Crambert G., Thuillard D., Roy S., Schaer D., Geering K.
    J Biol Chem 280:42738-42743(2005) [PubMed] [Europe PMC] [Abstract]
• establishment or maintenance of transmembrane electrochemical gradient Source: BHF-UCL <p>Inferred by Curator</p> <p>Used for cases where an annotation is not supported by any evidence but can be reasonably inferred by a curator from other GO annotations for which evidence<br />is available.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#ic">GO evidence code guide</a></p> Inferred by curatorⁱ
  • "Crystal structure of the sodium-potassium pump."
    Morth J.P., Pedersen B.P., Toustrup-Jensen M.S., Sorensen T.L., Petersen J., Andersen J.P., Vilsen B., Nissen P.
    Nature 450:1043-1049(2007) [PubMed] [Europe PMC] [Abstract]
• membrane hyperpolarization Source: RGD <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypeⁱ
  • "Na+-K+-ATPase is involved in the sustained ACh-induced hyperpolarization of endothelial cells from rat aorta."
    Bondarenko A., Sagach V.
    Br J Pharmacol 149:958-965(2006) [PubMed] [Europe PMC] [Abstract]
• membrane repolarization Source: RGD
• negative regulation of glucocorticoid biosynthetic process Source: RGD
• negative regulation of heart contraction Source: RGD
• positive regulation of heart contraction Source: RGD
• positive regulation of striated muscle contraction Source: RGD
• potassium ion import across plasma membrane Source: BHF-UCLInferred from direct assayⁱ
  • "Crystal structure of the sodium-potassium pump."
    Morth J.P., Pedersen B.P., Toustrup-Jensen M.S., Sorensen T.L., Petersen J., Andersen J.P., Vilsen B., Nissen P.
    Nature 450:1043-1049(2007) [PubMed] [Europe PMC] [Abstract]
• potassium ion transport Source: RGDInferred from direct assayⁱ
  • "FXYD7 is a brain-specific regulator of Na,K-ATPase alpha 1-beta isozymes."
    Beguin P., Crambert G., Monnet-Tschudi F., Uldry M., Horisberger J.D., Garty H., Geering K.
    EMBO J 21:3264-3273(2002) [PubMed] [Europe PMC] [Abstract]
  • "Beta-subunit of cardiac Na+-K+-ATPase dictates the concentration of the functional enzyme in caveolae."
    Liu L., Askari A.
    Am J Physiol Cell Physiol 291:C569-78(2006) [PubMed] [Europe PMC] [Abstract]
• proton transmembrane transport Source: GO_Central <p>Inferred from Biological aspect of Ancestor</p> <p>A type of phylogenetic evidence whereby an aspect of a descendent is inferred through the characterization of an aspect of a ancestral gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#iba">GO evidence code guide</a></p> Inferred from biological aspect of ancestorⁱ
  • "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
    Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
    Brief Bioinform 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
• regulation of blood pressure Source: RGD
• regulation of cardiac muscle cell contraction Source: RGDInferred from mutant phenotypeⁱ
  • "Evidence that the H1-H2 domain of alpha1 subunit of (Na++K+)-ATPase participates in the regulation of cardiac contraction."
    Xu K.Y., Takimoto E., Juang G.J., Zhang Q., Rohde H., Myers A.C.
    FASEB J 19:53-61(2005) [PubMed] [Europe PMC] [Abstract]
• regulation of sodium ion transport Source: UniProtKBInferred from direct assayⁱ
  • Ref.15

    "SIK1 is part of a cell sodium-sensing network that regulates active sodium transport through a calcium-dependent process."
    Sjostrom M., Stenstrom K., Eneling K., Zwiller J., Katz A.I., Takemori H., Bertorello A.M.
    Proc. Natl. Acad. Sci. U.S.A. 104:16922-16927(2007) [PubMed] [Europe PMC] [Abstract]

    Cited for: PHOSPHORYLATION, DEPHOSPHORYLATION, INTERACTION WITH SIK1.
• regulation of the force of heart contraction Source: RGD
• relaxation of cardiac muscle Source: BHF-UCLTraceable author statementⁱ
  • "The Na+/K+-ATPase alpha2-isoform regulates cardiac contractility in rat cardiomyocytes."
    Swift F., Tovsrud N., Enger U.H., Sjaastad I., Sejersted O.M.
    Cardiovasc Res 75:109-117(2007) [PubMed] [Europe PMC] [Abstract]
• response to drug Source: RGD
• response to glycoside Source: RGD
• sodium ion export across plasma membrane Source: BHF-UCLInferred from direct assayⁱ
  • "Crystal structure of the sodium-potassium pump."
    Morth J.P., Pedersen B.P., Toustrup-Jensen M.S., Sorensen T.L., Petersen J., Andersen J.P., Vilsen B., Nissen P.
    Nature 450:1043-1049(2007) [PubMed] [Europe PMC] [Abstract]
• sodium ion transport Source: RGDInferred from direct assayⁱ
  • "FXYD7 is a brain-specific regulator of Na,K-ATPase alpha 1-beta isozymes."
    Beguin P., Crambert G., Monnet-Tschudi F., Uldry M., Horisberger J.D., Garty H., Geering K.
    EMBO J 21:3264-3273(2002) [PubMed] [Europe PMC] [Abstract]
  • "Importance of conserved Thr214 in domain A of the Na+,K+ -ATPase for stabilization of the phosphoryl transition state complex in E2P dephosphorylation."
    Toustrup-Jensen M., Vilsen B.
    J Biol Chem 278:11402-11410(2003) [PubMed] [Europe PMC] [Abstract]
  • "Beta-subunit of cardiac Na+-K+-ATPase dictates the concentration of the functional enzyme in caveolae."
    Liu L., Askari A.
    Am J Physiol Cell Physiol 291:C569-78(2006) [PubMed] [Europe PMC] [Abstract]
• transmembrane transport Source: BHF-UCLInferred from direct assayⁱ
  • "Crystal structure of the sodium-potassium pump."
    Morth J.P., Pedersen B.P., Toustrup-Jensen M.S., Sorensen T.L., Petersen J., Andersen J.P., Vilsen B., Nissen P.
    Nature 450:1043-1049(2007) [PubMed] [Europe PMC] [Abstract]

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsⁱ

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyⁱ

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationⁱ

Topology

Keywords - Cellular componentⁱ

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechⁱ

Mutagenesis

Chemistry databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingⁱ

Molecule processing

Amino acid modifications

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationⁱ

Keywords - PTMⁱ

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressionⁱ

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityⁱ

Gene expression databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactionⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structureⁱ

GO - Molecular functionⁱ

• ankyrin binding Source: BHF-UCLInferred from physical interactionⁱ
  • "Ankyrin binds to two distinct cytoplasmic domains of Na,K-ATPase alpha subunit."
    Devarajan P., Scaramuzzino D.A., Morrow J.S.
    Proc Natl Acad Sci U S A 91:2965-2969(1994) [PubMed] [Europe PMC] [Abstract]
• chaperone binding Source: BHF-UCLInferred from direct assayⁱ
  • "Ankyrin facilitates intracellular trafficking of alpha1-Na+-K+-ATPase in polarized cells."
    Stabach P.R., Devarajan P., Stankewich M.C., Bannykh S., Morrow J.S.
    Am J Physiol Cell Physiol 295:C1202-14(2008) [PubMed] [Europe PMC] [Abstract]
• phosphatidylinositol 3-kinase binding Source: RGDInferred from physical interactionⁱ
  • "Association of PI3K-Akt signaling pathway with digitalis-induced hypertrophy of cardiac myocytes."
    Liu L., Zhao X., Pierre S.V., Askari A.
    Am J Physiol Cell Physiol 293:C1489-97(2007) [PubMed] [Europe PMC] [Abstract]
• protein domain specific binding Source: RGDInferred from physical interactionⁱ
  • "Role of the transmembrane domain of FXYD7 in structural and functional interactions with Na,K-ATPase."
    Li C., Crambert G., Thuillard D., Roy S., Schaer D., Geering K.
    J Biol Chem 280:42738-42743(2005) [PubMed] [Europe PMC] [Abstract]
• protein heterodimerization activity Source: ARUK-UCLInferred from physical interactionⁱ
  • "The alpha2beta2 isoform combination dominates the astrocytic Napisup>+pi/sup> /Kpisup>+pi/sup> -ATPase activity and is rendered nonfunctional by the alpha2.G301R familial hemiplegic migraine type 2-associated mutation."
    Stoica A., Larsen B.R., Assentoft M., Holm R., Holt L.M., Vilhardt F., Vilsen B., Lykke-Hartmann K., Olsen M.L., MacAulay N.
    Glia 65:1777-1793(2017) [PubMed] [Europe PMC] [Abstract]
• protein kinase binding Source: UniProtKBInferred from physical interactionⁱ
  • Ref.15

    "SIK1 is part of a cell sodium-sensing network that regulates active sodium transport through a calcium-dependent process."
    Sjostrom M., Stenstrom K., Eneling K., Zwiller J., Katz A.I., Takemori H., Bertorello A.M.
    Proc. Natl. Acad. Sci. U.S.A. 104:16922-16927(2007) [PubMed] [Europe PMC] [Abstract]

    Cited for: PHOSPHORYLATION, DEPHOSPHORYLATION, INTERACTION WITH SIK1.

Protein-protein interaction databases

Chemistry databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structureⁱ

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsⁱ

Region

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesⁱ

Keywords - Domainⁱ

Phylogenomic databases

Family and domain databases

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequenceⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusⁱ: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingⁱ: The displayed sequence is further processed into a mature form.

        10         20         30         40         50
MGKGVGRDKY EPAAVSEHGD KKSKKAKKER DMDELKKEVS MDDHKLSLDE 
        60         70         80         90        100
LHRKYGTDLS RGLTPARAAE ILARDGPNAL TPPPTTPEWV KFCRQLFGGF 
       110        120        130        140        150
SMLLWIGAIL CFLAYGIRSA TEEEPPNDDL YLGVVLSAVV IITGCFSYYQ 
       160        170        180        190        200
EAKSSKIMES FKNMVPQQAL VIRNGEKMSI NAEDVVVGDL VEVKGGDRIP 
       210        220        230        240        250
ADLRIISANG CKVDNSSLTG ESEPQTRSPD FTNENPLETR NIAFFSTNCV 
       260        270        280        290        300
EGTARGIVVY TGDRTVMGRI ATLASGLEGG QTPIAEEIEH FIHLITGVAV 
       310        320        330        340        350
FLGVSFFILS LILEYTWLEA VIFLIGIIVA NVPEGLLATV TVCLTLTAKR 
       360        370        380        390        400
MARKNCLVKN LEAVETLGST STICSDKTGT LTQNRMTVAH MWFDNQIHEA 
       410        420        430        440        450
DTTENQSGVS FDKTSATWFA LSRIAGLCNR AVFQANQENL PILKRAVAGD 
       460        470        480        490        500
ASESALLKCI EVCCGSVMEM REKYTKIVEI PFNSTNKYQL SIHKNPNASE 
       510        520        530        540        550
PKHLLVMKGA PERILDRCSS ILLHGKEQPL DEELKDAFQN AYLELGGLGE 
       560        570        580        590        600
RVLGFCHLLL PDEQFPEGFQ FDTDEVNFPV DNLCFVGLIS MIDPPRAAVP 
       610        620        630        640        650
DAVGKCRSAG IKVIMVTGDH PITAKAIAKG VGIISEGNET VEDIAARLNI 
       660        670        680        690        700
PVNQVNPRDA KACVVHGSDL KDMTSEELDD ILRYHTEIVF ARTSPQQKLI 
       710        720        730        740        750
IVEGCQRQGA IVAVTGDGVN DSPALKKADI GVAMGIVGSD VSKQAADMIL 
       760        770        780        790        800
LDDNFASIVT GVEEGRLIFD NLKKSIAYTL TSNIPEITPF LIFIIANIPL 
       810        820        830        840        850
PLGTVTILCI DLGTDMVPAI SLAYEQAESD IMKRQPRNPK TDKLVNERLI 
       860        870        880        890        900
SMAYGQIGMI QALGGFFTYF VILAENGFLP FHLLGIRETW DDRWINDVED 
       910        920        930        940        950
SYGQQWTYEQ RKIVEFTCHT AFFVSIVVVQ WADLVICKTR RNSVFQQGMK 
       960        970        980        990       1000
NKILIFGLFE ETALAAFLSY CPGMGAALRM YPLKPTWWFC AFPYSLLIFV 
      1010       1020 
YDEVRKLIIR RRPGGWVEKE TYY                              

Experimental Info

Sequence databases

Genome annotation databases

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsⁱ

• 90% Identity
• 50% Identity

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesⁱ

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

PTM databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationⁱ

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousⁱ

Keywords - Technical termⁱ

Documents

1. PDB cross-references
   Index of Protein Data Bank (PDB) cross-references
2. SIMILARITY comments
   Index of protein domains and families