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P13637

- AT1A3_HUMAN

UniProt

P13637 - AT1A3_HUMAN

Protein

Sodium/potassium-transporting ATPase subunit alpha-3

Gene

ATP1A3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 166 (01 Oct 2014)
      Sequence version 3 (17 Oct 2006)
      Previous versions | rss
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    Functioni

    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 activityi

    ATP + H2O + Na+(In) + K+(Out) = ADP + phosphate + Na+(Out) + K+(In).

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei366 – 36614-aspartylphosphate intermediateBy similarity
    Metal bindingi707 – 7071MagnesiumBy similarity
    Metal bindingi711 – 7111MagnesiumBy similarity

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB
    2. metal ion binding Source: UniProtKB-KW
    3. sodium:potassium-exchanging ATPase activity Source: UniProtKB

    GO - Biological processi

    1. adult locomotory behavior Source: Ensembl
    2. ATP biosynthetic process Source: InterPro
    3. ionotropic glutamate receptor signaling pathway Source: Ensembl
    4. ion transmembrane transport Source: Reactome
    5. memory Source: Ensembl
    6. response to drug Source: Ensembl
    7. sodium ion transmembrane transport Source: GOC
    8. transmembrane transport Source: Reactome
    9. visual learning Source: Ensembl

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Ion transport, Potassium transport, Sodium transport, Sodium/potassium transport, Transport

    Keywords - Ligandi

    ATP-binding, Magnesium, Metal-binding, Nucleotide-binding, Potassium, Sodium

    Enzyme and pathway databases

    ReactomeiREACT_25149. Ion transport by P-type ATPases.

    Protein family/group databases

    TCDBi3.A.3.1.1. the p-type atpase (p-atpase) superfamily.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Sodium/potassium-transporting ATPase subunit alpha-3 (EC:3.6.3.9)
    Short name:
    Na(+)/K(+) ATPase alpha-3 subunit
    Alternative name(s):
    Na(+)/K(+) ATPase alpha(III) subunit
    Sodium pump subunit alpha-3
    Gene namesi
    Name:ATP1A3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:801. ATP1A3.

    Subcellular locationi

    Cell membrane 1 Publication; Multi-pass membrane protein 1 Publication

    GO - Cellular componenti

    1. axon Source: Ensembl
    2. dendritic spine head Source: Ensembl
    3. dendritic spine neck Source: Ensembl
    4. endoplasmic reticulum Source: UniProtKB
    5. Golgi apparatus Source: UniProtKB
    6. integral component of membrane Source: UniProtKB
    7. myelin sheath Source: Ensembl
    8. nucleus Source: Ensembl
    9. plasma membrane Source: UniProtKB
    10. sodium:potassium-exchanging ATPase complex Source: UniProtKB
    11. synapse Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Dystonia 12 (DYT12) [MIM:128235]: An autosomal dominant dystonia-parkinsonism disorder. Dystonia is defined by the presence of sustained involuntary muscle contractions, often leading to abnormal postures. DYT12 patients develop dystonia and parkinsonism between 15 and 45 years of age. The disease is characterized by an unusually rapid evolution of signs and symptoms. The sudden onset of symptoms over hours to a few weeks, often associated with physical or emotional stress, suggests a trigger initiating a nervous system insult resulting in permanent neurologic disability.3 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti274 – 2741I → T in DYT12. 1 Publication
    VAR_026735
    Natural varianti277 – 2771E → K in DYT12. 1 Publication
    VAR_026736
    Natural varianti613 – 6131T → M in DYT12. 1 Publication
    VAR_026737
    Natural varianti758 – 7581I → S in DYT12. 1 Publication
    VAR_026738
    Natural varianti780 – 7801F → L in DYT12. 1 Publication
    VAR_026739
    Natural varianti801 – 8011D → Y in DYT12. 1 Publication
    VAR_026740
    Natural varianti923 – 9231D → N in DYT12. 1 Publication
    VAR_068949
    Natural varianti1013 – 10131Y → YY in DYT12; there is a drastic 40-to 50-fold reduction in Na(+) affinity in the mutant protein.
    VAR_068953
    Alternating hemiplegia of childhood 2 (AHC2) [MIM:614820]: A rare syndrome of episodic hemi- or quadriplegia lasting minutes to days. Most cases are accompanied by dystonic posturing, choreoathetoid movements, nystagmus, other ocular motor abnormalities, autonomic disturbances, and progressive cognitive impairment. It is typically distinguished from familial hemiplegic migraine by infantile onset and high prevalence of associated neurological deficits that become increasingly obvious with age.3 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti137 – 1371S → F in AHC2. 1 Publication
    VAR_068935
    Natural varianti137 – 1371S → Y in AHC2. 1 Publication
    VAR_068936
    Natural varianti140 – 1401Q → L in AHC2. 1 Publication
    VAR_068937
    Natural varianti220 – 2201D → N in AHC2. 1 Publication
    VAR_068938
    Natural varianti274 – 2741I → N in AHC2. 2 Publications
    VAR_068939
    Natural varianti322 – 3221V → D in AHC2. 1 Publication
    VAR_070767
    Natural varianti333 – 3331C → F in AHC2. 1 Publication
    VAR_068940
    Natural varianti371 – 3711L → P in AHC2. 1 Publication
    VAR_070768
    Natural varianti755 – 7551G → C in AHC2. 2 Publications
    VAR_070769
    Natural varianti755 – 7551G → S in AHC2. 1 Publication
    VAR_068941
    Natural varianti772 – 7721S → R in AHC2. 1 Publication
    VAR_070770
    Natural varianti773 – 7731N → I in AHC2. 1 Publication
    VAR_070771
    Natural varianti773 – 7731N → S in AHC2. 1 Publication
    VAR_068942
    Natural varianti801 – 8011D → N in AHC2; protein levels is similar to wild-type but the enzyme activity is significantly decreased. 3 Publications
    VAR_068943
    Natural varianti806 – 8061M → R in AHC2. 1 Publication
    VAR_068944
    Natural varianti810 – 8101I → S in AHC2. 1 Publication
    VAR_068945
    Natural varianti811 – 8111S → P in AHC2; protein levels is similar to wild-type but the enzyme activity is significantly decreased. 1 Publication
    VAR_068946
    Natural varianti815 – 8151E → K in AHC2; protein levels is similar to wild-type but the enzyme activity is significantly decreased. 3 Publications
    VAR_068947
    Natural varianti919 – 9191Missing in AHC2. 1 Publication
    VAR_068948
    Natural varianti923 – 9231D → Y in AHC2. 1 Publication
    VAR_070773
    Natural varianti927 – 9271C → Y in AHC2.
    VAR_070774
    Natural varianti947 – 9471G → R in AHC2. 1 Publication
    VAR_068950
    Natural varianti955 – 9551A → D in AHC2. 1 Publication
    VAR_068951
    Natural varianti992 – 9921D → Y in AHC2. 1 Publication
    VAR_068952
    ATP1A3 mutations are a cause of cerebellar ataxia, areflexia, pes cavus, optic atrophy and sensorineural hearing loss syndrome (CAPOS) (PubMed:24468074). Patients present with a relapsing and partially remitting, early-onset cerebellar ataxia following a febrile illness. Other features include progressive optic atrophy and sensorineural hearing loss, generalized hypotonia, areflexia and pes cavus without evidence of a peripheral neuropathy on neurophysiological studies.1 Publication

    Keywords - Diseasei

    Deafness, Disease mutation, Dystonia, Parkinsonism

    Organism-specific databases

    MIMi128235. phenotype.
    614820. phenotype.
    Orphaneti2131. Alternating hemiplegia of childhood.
    1171. Cerebellar ataxia - areflexia - pes cavus - optic atrophy - sensorineural hearing loss.
    71517. Rapid-onset dystonia-parkinsonism.
    PharmGKBiPA64.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10131013Sodium/potassium-transporting ATPase subunit alpha-3PRO_0000046298Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei265 – 2651PhosphoserineBy similarity
    Modified residuei548 – 5481PhosphotyrosineBy similarity
    Modified residuei933 – 9331Phosphoserine; by PKABy similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP13637.
    PaxDbiP13637.
    PRIDEiP13637.

    PTM databases

    PhosphoSiteiP13637.

    Expressioni

    Gene expression databases

    ArrayExpressiP13637.
    BgeeiP13637.
    CleanExiHS_ATP1A3.
    GenevestigatoriP13637.

    Organism-specific databases

    HPAiCAB001988.

    Interactioni

    Subunit structurei

    Composed of three subunits: alpha (catalytic), beta and gamma.

    Protein-protein interaction databases

    BioGridi106968. 4 interactions.
    IntActiP13637. 4 interactions.
    MINTiMINT-2857038.
    STRINGi9606.ENSP00000302397.

    Structurei

    3D structure databases

    ProteinModelPortaliP13637.
    SMRiP13637. Positions 20-1013.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 7777CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini99 – 12123ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini143 – 278136CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini299 – 31012ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini329 – 762434CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini783 – 79210ExtracellularSequence Analysis
    Topological domaini814 – 83320CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini857 – 90852ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini929 – 94113CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini961 – 97515ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini997 – 101317CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei78 – 9821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei122 – 14221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei279 – 29820HelicalSequence AnalysisAdd
    BLAST
    Transmembranei311 – 32818HelicalSequence AnalysisAdd
    BLAST
    Transmembranei763 – 78220HelicalSequence AnalysisAdd
    BLAST
    Transmembranei793 – 81321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei834 – 85623HelicalSequence AnalysisAdd
    BLAST
    Transmembranei909 – 92820HelicalSequence AnalysisAdd
    BLAST
    Transmembranei942 – 96019HelicalSequence AnalysisAdd
    BLAST
    Transmembranei976 – 99621HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni72 – 743Interaction with phosphoinositide-3 kinaseBy similarity

    Sequence similaritiesi

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0474.
    HOGENOMiHOG000265622.
    HOVERGENiHBG004298.
    InParanoidiP13637.
    KOiK01539.
    OrthoDBiEOG7327N0.
    PhylomeDBiP13637.
    TreeFamiTF312838.

    Family and domain databases

    Gene3Di1.20.1110.10. 2 hits.
    2.70.150.10. 2 hits.
    3.40.1110.10. 1 hit.
    InterProiIPR006068. ATPase_P-typ_cation-transptr_C.
    IPR004014. ATPase_P-typ_cation-transptr_N.
    IPR023299. ATPase_P-typ_cyto_domN.
    IPR005775. ATPase_P-typ_Na/K_IIC.
    IPR018303. ATPase_P-typ_P_site.
    IPR023298. ATPase_P-typ_TM_dom.
    IPR008250. ATPase_P-typ_transduc_dom_A.
    IPR001757. Cation_transp_P_typ_ATPase.
    IPR023214. HAD-like_dom.
    [Graphical view]
    PfamiPF00689. Cation_ATPase_C. 1 hit.
    PF00690. Cation_ATPase_N. 1 hit.
    PF00122. E1-E2_ATPase. 1 hit.
    PF00702. Hydrolase. 1 hit.
    [Graphical view]
    PRINTSiPR00119. CATATPASE.
    SMARTiSM00831. Cation_ATPase_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF56784. SSF56784. 3 hits.
    SSF81660. SSF81660. 1 hit.
    TIGRFAMsiTIGR01106. ATPase-IIC_X-K. 1 hit.
    TIGR01494. ATPase_P-type. 2 hits.
    PROSITEiPS00154. ATPASE_E1_E2. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P13637-1) [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

    MGDKKDDKDS PKKNKGKERR DLDDLKKEVA MTEHKMSVEE VCRKYNTDCV     50
    QGLTHSKAQE ILARDGPNAL TPPPTTPEWV KFCRQLFGGF SILLWIGAIL 100
    CFLAYGIQAG TEDDPSGDNL YLGIVLAAVV IITGCFSYYQ EAKSSKIMES 150
    FKNMVPQQAL VIREGEKMQV NAEEVVVGDL VEIKGGDRVP ADLRIISAHG 200
    CKVDNSSLTG ESEPQTRSPD CTHDNPLETR NITFFSTNCV EGTARGVVVA 250
    TGDRTVMGRI ATLASGLEVG KTPIAIEIEH FIQLITGVAV FLGVSFFILS 300
    LILGYTWLEA VIFLIGIIVA NVPEGLLATV TVCLTLTAKR MARKNCLVKN 350
    LEAVETLGST STICSDKTGT LTQNRMTVAH MWFDNQIHEA DTTEDQSGTS 400
    FDKSSHTWVA LSHIAGLCNR AVFKGGQDNI PVLKRDVAGD ASESALLKCI 450
    ELSSGSVKLM RERNKKVAEI PFNSTNKYQL SIHETEDPND NRYLLVMKGA 500
    PERILDRCST ILLQGKEQPL DEEMKEAFQN AYLELGGLGE RVLGFCHYYL 550
    PEEQFPKGFA FDCDDVNFTT DNLCFVGLMS MIDPPRAAVP DAVGKCRSAG 600
    IKVIMVTGDH PITAKAIAKG VGIISEGNET VEDIAARLNI PVSQVNPRDA 650
    KACVIHGTDL KDFTSEQIDE ILQNHTEIVF ARTSPQQKLI IVEGCQRQGA 700
    IVAVTGDGVN DSPALKKADI GVAMGIAGSD VSKQAADMIL LDDNFASIVT 750
    GVEEGRLIFD NLKKSIAYTL TSNIPEITPF LLFIMANIPL PLGTITILCI 800
    DLGTDMVPAI SLAYEAAESD IMKRQPRNPR TDKLVNERLI SMAYGQIGMI 850
    QALGGFFSYF VILAENGFLP GNLVGIRLNW DDRTVNDLED SYGQQWTYEQ 900
    RKVVEFTCHT AFFVSIVVVQ WADLIICKTR RNSVFQQGMK NKILIFGLFE 950
    ETALAAFLSY CPGMDVALRM YPLKPSWWFC AFPYSFLIFV YDEIRKLILR 1000
    RNPGGWVEKE TYY 1013
    Length:1,013
    Mass (Da):111,749
    Last modified:October 17, 2006 - v3
    Checksum:iBF28CD9F1E11AF48
    GO
    Isoform 2 (identifier: P13637-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-2: MG → MGGWEEERNRRAT

    Show »
    Length:1,024
    Mass (Da):113,134
    Checksum:iD6F4310E7B68C1D1
    GO
    Isoform 3 (identifier: P13637-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-2: MG → MGSGGSDSYRIATSQ

    Show »
    Length:1,026
    Mass (Da):113,059
    Checksum:i50F72BDBADD90225
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti1 – 22MG → MEIH in CAA31390. (PubMed:2834163)Curated
    Sequence conflicti144 – 1441S → R in BAH12387. (PubMed:14702039)Curated
    Sequence conflicti336 – 3361L → V in AAA51798. (PubMed:2838329)Curated
    Sequence conflicti336 – 3361L → V in CAA31390. (PubMed:2834163)Curated
    Sequence conflicti336 – 3361L → V in AAA52285. (PubMed:3030810)Curated
    Sequence conflicti336 – 3361L → V in AAA58380. (PubMed:3036582)Curated
    Sequence conflicti380 – 3801H → T in AAA52285. (PubMed:3030810)Curated
    Sequence conflicti421 – 4211A → P in AAA58380. (PubMed:3036582)Curated
    Sequence conflicti430 – 4301I → M in CAA31390. (PubMed:2834163)Curated
    Sequence conflicti555 – 5573FPK → YPQ in AAA51798. (PubMed:2838329)Curated
    Sequence conflicti555 – 5573FPK → YPQ in CAA31390. (PubMed:2834163)Curated
    Sequence conflicti555 – 5573FPK → YPQ in AAA52286. (PubMed:3030810)Curated
    Sequence conflicti577 – 5771G → P in AAA51798. (PubMed:2838329)Curated
    Sequence conflicti583 – 5831D → G in AAA51798. (PubMed:2838329)Curated
    Sequence conflicti583 – 5831D → G in CAA31390. (PubMed:2834163)Curated
    Sequence conflicti583 – 5831D → G in AAA52286. (PubMed:3030810)Curated
    Sequence conflicti919 – 9191V → A in AAA52286. (PubMed:3030810)Curated
    Sequence conflicti944 – 9441L → M in AAA52286. (PubMed:3030810)Curated
    Sequence conflicti982 – 9821F → S in CAA31390. (PubMed:2834163)Curated
    Sequence conflicti1006 – 10061W → S in AAA51798. (PubMed:2838329)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti137 – 1371S → F in AHC2. 1 Publication
    VAR_068935
    Natural varianti137 – 1371S → Y in AHC2. 1 Publication
    VAR_068936
    Natural varianti140 – 1401Q → L in AHC2. 1 Publication
    VAR_068937
    Natural varianti220 – 2201D → N in AHC2. 1 Publication
    VAR_068938
    Natural varianti274 – 2741I → N in AHC2. 2 Publications
    VAR_068939
    Natural varianti274 – 2741I → T in DYT12. 1 Publication
    VAR_026735
    Natural varianti277 – 2771E → K in DYT12. 1 Publication
    VAR_026736
    Natural varianti322 – 3221V → D in AHC2. 1 Publication
    VAR_070767
    Natural varianti333 – 3331C → F in AHC2. 1 Publication
    VAR_068940
    Natural varianti371 – 3711L → P in AHC2. 1 Publication
    VAR_070768
    Natural varianti613 – 6131T → M in DYT12. 1 Publication
    VAR_026737
    Natural varianti755 – 7551G → C in AHC2. 2 Publications
    VAR_070769
    Natural varianti755 – 7551G → S in AHC2. 1 Publication
    VAR_068941
    Natural varianti758 – 7581I → S in DYT12. 1 Publication
    VAR_026738
    Natural varianti772 – 7721S → R in AHC2. 1 Publication
    VAR_070770
    Natural varianti773 – 7731N → I in AHC2. 1 Publication
    VAR_070771
    Natural varianti773 – 7731N → S in AHC2. 1 Publication
    VAR_068942
    Natural varianti780 – 7801F → L in DYT12. 1 Publication
    VAR_026739
    Natural varianti801 – 8011D → N in AHC2; protein levels is similar to wild-type but the enzyme activity is significantly decreased. 3 Publications
    VAR_068943
    Natural varianti801 – 8011D → Y in DYT12. 1 Publication
    VAR_026740
    Natural varianti806 – 8061M → R in AHC2. 1 Publication
    VAR_068944
    Natural varianti810 – 8101I → S in AHC2. 1 Publication
    VAR_068945
    Natural varianti811 – 8111S → P in AHC2; protein levels is similar to wild-type but the enzyme activity is significantly decreased. 1 Publication
    VAR_068946
    Natural varianti815 – 8151E → K in AHC2; protein levels is similar to wild-type but the enzyme activity is significantly decreased. 3 Publications
    VAR_068947
    Natural varianti818 – 8181E → K Probable disease-associated mutation found in patients with CAPOS. 1 Publication
    VAR_070772
    Natural varianti919 – 9191Missing in AHC2. 1 Publication
    VAR_068948
    Natural varianti923 – 9231D → N in DYT12. 1 Publication
    VAR_068949
    Natural varianti923 – 9231D → Y in AHC2. 1 Publication
    VAR_070773
    Natural varianti927 – 9271C → Y in AHC2.
    VAR_070774
    Natural varianti947 – 9471G → R in AHC2. 1 Publication
    VAR_068950
    Natural varianti955 – 9551A → D in AHC2. 1 Publication
    VAR_068951
    Natural varianti992 – 9921D → Y in AHC2. 1 Publication
    VAR_068952
    Natural varianti1013 – 10131Y → YY in DYT12; there is a drastic 40-to 50-fold reduction in Na(+) affinity in the mutant protein.
    VAR_068953

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 22MG → MGGWEEERNRRAT in isoform 2. 1 PublicationVSP_046956
    Alternative sequencei1 – 22MG → MGSGGSDSYRIATSQ in isoform 3. 1 PublicationVSP_046957

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M37457
    , M37436, M37437, M37438, M37462, M37439, M37440, M37441, M37442, M37443, M37444, M37445, M37447, M37448, M37449, M37450, M37451, M37452, M37453, M37454, M37455, M37456 Genomic DNA. Translation: AAA51798.1.
    X12910
    , X12911, X12912, X12913, X12914, X12915, X12916, X12917, X12919, X12920, X12921, X12922, X12923 Genomic DNA. Translation: CAA31390.1.
    AK295078 mRNA. Translation: BAH11966.1.
    AK296557 mRNA. Translation: BAH12387.1.
    AC010616 Genomic DNA. No translation available.
    BC009282 mRNA. Translation: AAH09282.1.
    BC009394 mRNA. Translation: AAH09394.1.
    BC015566 mRNA. Translation: AAH15566.1.
    M28286, M28284, M28285 Genomic DNA. Translation: AAA52285.1.
    M28293
    , M28287, M35821, M35822, M28289, M28290, M28291, M28292 Genomic DNA. Translation: AAA52286.1.
    M27577, M27570, M27573 Genomic DNA. Translation: AAA58380.1.
    CCDSiCCDS12594.1. [P13637-1]
    CCDS58663.1. [P13637-2]
    CCDS58664.1. [P13637-3]
    PIRiS00801.
    RefSeqiNP_001243142.1. NM_001256213.1. [P13637-2]
    NP_001243143.1. NM_001256214.1. [P13637-3]
    NP_689509.1. NM_152296.4. [P13637-1]
    UniGeneiHs.515427.

    Genome annotation databases

    EnsembliENST00000302102; ENSP00000302397; ENSG00000105409. [P13637-1]
    ENST00000543770; ENSP00000437577; ENSG00000105409. [P13637-2]
    ENST00000545399; ENSP00000444688; ENSG00000105409. [P13637-3]
    GeneIDi478.
    KEGGihsa:478.
    UCSCiuc002osg.4. human. [P13637-1]

    Polymorphism databases

    DMDMi116241260.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M37457
    , M37436 , M37437 , M37438 , M37462 , M37439 , M37440 , M37441 , M37442 , M37443 , M37444 , M37445 , M37447 , M37448 , M37449 , M37450 , M37451 , M37452 , M37453 , M37454 , M37455 , M37456 Genomic DNA. Translation: AAA51798.1 .
    X12910
    , X12911 , X12912 , X12913 , X12914 , X12915 , X12916 , X12917 , X12919 , X12920 , X12921 , X12922 , X12923 Genomic DNA. Translation: CAA31390.1 .
    AK295078 mRNA. Translation: BAH11966.1 .
    AK296557 mRNA. Translation: BAH12387.1 .
    AC010616 Genomic DNA. No translation available.
    BC009282 mRNA. Translation: AAH09282.1 .
    BC009394 mRNA. Translation: AAH09394.1 .
    BC015566 mRNA. Translation: AAH15566.1 .
    M28286 , M28284 , M28285 Genomic DNA. Translation: AAA52285.1 .
    M28293
    , M28287 , M35821 , M35822 , M28289 , M28290 , M28291 , M28292 Genomic DNA. Translation: AAA52286.1 .
    M27577 , M27570 , M27573 Genomic DNA. Translation: AAA58380.1 .
    CCDSi CCDS12594.1. [P13637-1 ]
    CCDS58663.1. [P13637-2 ]
    CCDS58664.1. [P13637-3 ]
    PIRi S00801.
    RefSeqi NP_001243142.1. NM_001256213.1. [P13637-2 ]
    NP_001243143.1. NM_001256214.1. [P13637-3 ]
    NP_689509.1. NM_152296.4. [P13637-1 ]
    UniGenei Hs.515427.

    3D structure databases

    ProteinModelPortali P13637.
    SMRi P13637. Positions 20-1013.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106968. 4 interactions.
    IntActi P13637. 4 interactions.
    MINTi MINT-2857038.
    STRINGi 9606.ENSP00000302397.

    Chemistry

    BindingDBi P13637.
    ChEMBLi CHEMBL2095186.

    Protein family/group databases

    TCDBi 3.A.3.1.1. the p-type atpase (p-atpase) superfamily.

    PTM databases

    PhosphoSitei P13637.

    Polymorphism databases

    DMDMi 116241260.

    Proteomic databases

    MaxQBi P13637.
    PaxDbi P13637.
    PRIDEi P13637.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000302102 ; ENSP00000302397 ; ENSG00000105409 . [P13637-1 ]
    ENST00000543770 ; ENSP00000437577 ; ENSG00000105409 . [P13637-2 ]
    ENST00000545399 ; ENSP00000444688 ; ENSG00000105409 . [P13637-3 ]
    GeneIDi 478.
    KEGGi hsa:478.
    UCSCi uc002osg.4. human. [P13637-1 ]

    Organism-specific databases

    CTDi 478.
    GeneCardsi GC19M042470.
    GeneReviewsi ATP1A3.
    HGNCi HGNC:801. ATP1A3.
    HPAi CAB001988.
    MIMi 128235. phenotype.
    182350. gene.
    614820. phenotype.
    neXtProti NX_P13637.
    Orphaneti 2131. Alternating hemiplegia of childhood.
    1171. Cerebellar ataxia - areflexia - pes cavus - optic atrophy - sensorineural hearing loss.
    71517. Rapid-onset dystonia-parkinsonism.
    PharmGKBi PA64.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0474.
    HOGENOMi HOG000265622.
    HOVERGENi HBG004298.
    InParanoidi P13637.
    KOi K01539.
    OrthoDBi EOG7327N0.
    PhylomeDBi P13637.
    TreeFami TF312838.

    Enzyme and pathway databases

    Reactomei REACT_25149. Ion transport by P-type ATPases.

    Miscellaneous databases

    ChiTaRSi ATP1A3. human.
    GeneWikii ATP1A3.
    GenomeRNAii 478.
    NextBioi 1981.
    PROi P13637.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P13637.
    Bgeei P13637.
    CleanExi HS_ATP1A3.
    Genevestigatori P13637.

    Family and domain databases

    Gene3Di 1.20.1110.10. 2 hits.
    2.70.150.10. 2 hits.
    3.40.1110.10. 1 hit.
    InterProi IPR006068. ATPase_P-typ_cation-transptr_C.
    IPR004014. ATPase_P-typ_cation-transptr_N.
    IPR023299. ATPase_P-typ_cyto_domN.
    IPR005775. ATPase_P-typ_Na/K_IIC.
    IPR018303. ATPase_P-typ_P_site.
    IPR023298. ATPase_P-typ_TM_dom.
    IPR008250. ATPase_P-typ_transduc_dom_A.
    IPR001757. Cation_transp_P_typ_ATPase.
    IPR023214. HAD-like_dom.
    [Graphical view ]
    Pfami PF00689. Cation_ATPase_C. 1 hit.
    PF00690. Cation_ATPase_N. 1 hit.
    PF00122. E1-E2_ATPase. 1 hit.
    PF00702. Hydrolase. 1 hit.
    [Graphical view ]
    PRINTSi PR00119. CATATPASE.
    SMARTi SM00831. Cation_ATPase_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56784. SSF56784. 3 hits.
    SSF81660. SSF81660. 1 hit.
    TIGRFAMsi TIGR01106. ATPase-IIC_X-K. 1 hit.
    TIGR01494. ATPase_P-type. 2 hits.
    PROSITEi PS00154. ATPASE_E1_E2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Family of human Na+, K+-ATPase genes. Structure of the gene for the catalytic subunit (alpha III-form) and its relationship with structural features of the protein."
      Ovchinnikov Y.A., Monastyrskaya G.S., Broude N.E., Ushkaryov Y.A., Melkov A.M., Smirnov Y.V., Malyshev I.V., Allikmets R.L., Kostina M.B., Dulubova I.E., Kiyatkin N.I., Grishin A.V., Modyanov N.N., Sverdlov E.D.
      FEBS Lett. 233:87-94(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
    2. "Family of human Na(+),K(+)-ATPase genes. Structure of the gene of isoform alpha-III."
      Sverdlov E.D., Monastyrskaya G.S., Broude N.E., Ushkarev Y.A., Melkov A.M., Smirnov Y.V., Malyshev I.V., Allikmets R.L., Kostina M.B., Dulubova I.E., Kiyatkin N.I., Grishin A.V., Modyanov N.N., Ovchinnikov Y.A.
      Dokl. Akad. Nauk SSSR 297:1488-1494(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
      Tissue: Brain.
    3. "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] (ISOFORMS 2 AND 3).
      Tissue: Brain and Thalamus.
    4. "The DNA sequence and biology of human chromosome 19."
      Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
      , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
      Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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.
    6. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 120-387; 494-538 AND 545-1013.
    7. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 243-434.
    8. "Subcellular distribution and immunocytochemical localization of Na,K-ATPase subunit isoforms in human skeletal muscle."
      Hundal H.S., Maxwell D.L., Ahmed A., Darakhshan F., Mitsumoto Y., Klip A.
      Mol. Membr. Biol. 11:255-262(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "Mutations in the Na(+)/K(+)-ATPase alpha-3 gene ATP1A3 are associated with rapid-onset dystonia parkinsonism."
      de Carvalho Aguiar P., Sweadner K.J., Penniston J.T., Zaremba J., Liu L., Caton M., Linazasoro G., Borg M., Tijssen M.A.J., Bressman S.B., Dobyns W.B., Brashear A., Ozelius L.J.
      Neuron 43:169-175(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS DYT12 THR-274; LYS-277; MET-613; SER-758; LEU-780 AND TYR-801.
    11. "A C-terminal mutation of ATP1A3 underscores the crucial role of sodium affinity in the pathophysiology of rapid-onset dystonia-parkinsonism."
      Blanco-Arias P., Einholm A.P., Mamsa H., Concheiro C., Gutierrez-de-Teran H., Romero J., Toustrup-Jensen M.S., Carracedo A., Jen J.C., Vilsen B., Sobrido M.J.
      Hum. Mol. Genet. 18:2370-2377(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT DYT12 TYR-1013 EXT, CHARACTERIZATION OF VARIANT DYT12 TYR-1013 EXT.
    12. "Rapid-onset dystonia-parkinsonism in a child with a novel atp1a3 gene mutation."
      Anselm I.A., Sweadner K.J., Gollamudi S., Ozelius L.J., Darras B.T.
      Neurology 73:400-401(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT DYT12 ASN-923.
    13. "Heterozygous de-novo mutations in ATP1A3 in patients with alternating hemiplegia of childhood: a whole-exome sequencing gene-identification study."
      Rosewich H., Thiele H., Ohlenbusch A., Maschke U., Altmuller J., Frommolt P., Zirn B., Ebinger F., Siemes H., Nurnberg P., Brockmann K., Gartner J.
      Lancet Neurol. 11:764-773(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS AHC2 ASN-274; ASP-322; PRO-371; CYS-755; ARG-772; ILE-773; ASN-801; LYS-815 AND TYR-923.
    14. "De novo mutations in ATP1A3 cause alternating hemiplegia of childhood."
      Heinzen E.L., Swoboda K.J., Hitomi Y., Gurrieri F., Nicole S., de Vries B., Tiziano F.D., Fontaine B., Walley N.M., Heavin S., Panagiotakaki E., Neri G., Koelewijn S., Kamphorst J., Geilenkirchen M., Pelzer N., Laan L., Haan J.
      , Ferrari M., van den Maagdenberg A.M., Zucca C., Bassi M.T., Franchini F., Vavassori R., Giannotta M., Gobbi G., Granata T., Nardocci N., De Grandis E., Veneselli E., Stagnaro M., Vigevano F., Oechsler C., Arzimanoglou A., Ninan M., Neville B., Ebinger F., Fons C., Campistol J., Kemlink D., Nevsimalova S., Peeters-Scholte C., Casaer P., Casari G., Sange G., Spiel G., Martinelli Boneschi F., Schyns T., Crawley F., Poncelin D., Fiori S., Abiusi E., Di Pietro L., Sweney M.T., Newcomb T.M., Viollet L., Huff C., Jorde L.B., Reyna S.P., Murphy K.J., Shianna K.V., Gumbs C.E., Little L., Silver K., Ptacek L.J., Ferrari M.D., Bye A.M., Herkes G.K., Whitelaw C.M., Webb D., Lynch B.J., Uldall P., King M.D., Scheffer I.E., Sisodiya S.M., Mikati M.A., Goldstein D.B.
      Nat. Genet. 44:1030-1034(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS AHC2 TYR-137; PHE-137; LEU-140; ASN-220; ASN-274; PHE-333; SER-755; SER-773; ASN-801; ARG-806; SER-810; PRO-811; LYS-815; VAL-919 DEL; ARG-947; ASP-955 AND TYR-992, CHARACTERIZATION OF VARIANTS AHC2 ASN-801; PRO-811 AND LYS-815.
    15. "Identification of ATP1A3 mutations by exome sequencing as the cause of alternating hemiplegia of childhood in Japanese patients."
      Ishii A., Saito Y., Mitsui J., Ishiura H., Yoshimura J., Arai H., Yamashita S., Kimura S., Oguni H., Morishita S., Tsuji S., Sasaki M., Hirose S.
      PLoS ONE 8:E56120-E56120(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS AHC2 CYS-755; ASN-801 AND LYS-815.
    16. Cited for: INVOLVEMENT IN CAPOS, VARIANT LYS-818.

    Entry informationi

    Entry nameiAT1A3_HUMAN
    AccessioniPrimary (citable) accession number: P13637
    Secondary accession number(s): B7Z2T0
    , B7Z401, F5H6J6, Q16732, Q16735, Q969K5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1990
    Last sequence update: October 17, 2006
    Last modified: October 1, 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

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 19
      Human chromosome 19: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3