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P13637 (AT1A3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 164. Feed History...

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

Names and origin

Protein namesRecommended name:
Sodium/potassium-transporting ATPase subunit alpha-3

Short name=Na(+)/K(+) ATPase alpha-3 subunit
EC=3.6.3.9
Alternative name(s):
Na(+)/K(+) ATPase alpha(III) subunit
Sodium pump subunit alpha-3
Gene names
Name:ATP1A3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1013 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (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 structure

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

Subcellular location

Cell membrane; Multi-pass membrane protein Ref.9.

Involvement in disease

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.11 Ref.12 Ref.13

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.14 Ref.15 Ref.16

ATP1A3 mutations are a cause of cerebellar ataxia, areflexia, pes cavus, optic atrophy and sensorineural hearing loss syndrome (CAPOS) (Ref.17). 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. Ref.17

Sequence similarities

Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IIC subfamily. [View classification]

Ontologies

Keywords
   Biological processIon transport
Potassium transport
Sodium transport
Sodium/potassium transport
Transport
   Cellular componentCell membrane
Membrane
   Coding sequence diversityAlternative splicing
   DiseaseDeafness
Disease mutation
Dystonia
Parkinsonism
   DomainTransmembrane
Transmembrane helix
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
Potassium
Sodium
   Molecular functionHydrolase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processATP biosynthetic process

Inferred from electronic annotation. Source: InterPro

adult locomotory behavior

Inferred from electronic annotation. Source: Ensembl

ion transmembrane transport

Traceable author statement. Source: Reactome

ionotropic glutamate receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

memory

Inferred from electronic annotation. Source: Ensembl

response to drug

Inferred from electronic annotation. Source: Ensembl

sodium ion transmembrane transport

Inferred from mutant phenotype Ref.11. Source: GOC

transmembrane transport

Traceable author statement. Source: Reactome

visual learning

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentGolgi apparatus

Inferred from direct assay Ref.11. Source: UniProtKB

axon

Inferred from electronic annotation. Source: Ensembl

dendritic spine head

Inferred from electronic annotation. Source: Ensembl

dendritic spine neck

Inferred from electronic annotation. Source: Ensembl

endoplasmic reticulum

Inferred from direct assay Ref.11. Source: UniProtKB

integral component of membrane

Non-traceable author statement Ref.11. Source: UniProtKB

myelin sheath

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Inferred from direct assay Ref.11. Source: UniProtKB

sodium:potassium-exchanging ATPase complex

Inferred by curator Ref.11. Source: UniProtKB

synapse

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionATP binding

Non-traceable author statement Ref.11. Source: UniProtKB

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

sodium:potassium-exchanging ATPase activity

Inferred from mutant phenotype Ref.11. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P13637-1)

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.
Isoform 2 (identifier: P13637-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-2: MG → MGGWEEERNRRAT
Isoform 3 (identifier: P13637-3)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10131013Sodium/potassium-transporting ATPase subunit alpha-3
PRO_0000046298

Regions

Topological domain1 – 7777Cytoplasmic Potential
Transmembrane78 – 9821Helical; Potential
Topological domain99 – 12123Extracellular Potential
Transmembrane122 – 14221Helical; Potential
Topological domain143 – 278136Cytoplasmic Potential
Transmembrane279 – 29820Helical; Potential
Topological domain299 – 31012Extracellular Potential
Transmembrane311 – 32818Helical; Potential
Topological domain329 – 762434Cytoplasmic Potential
Transmembrane763 – 78220Helical; Potential
Topological domain783 – 79210Extracellular Potential
Transmembrane793 – 81321Helical; Potential
Topological domain814 – 83320Cytoplasmic Potential
Transmembrane834 – 85623Helical; Potential
Topological domain857 – 90852Extracellular Potential
Transmembrane909 – 92820Helical; Potential
Topological domain929 – 94113Cytoplasmic Potential
Transmembrane942 – 96019Helical; Potential
Topological domain961 – 97515Extracellular Potential
Transmembrane976 – 99621Helical; Potential
Topological domain997 – 101317Cytoplasmic Potential
Region72 – 743Interaction with phosphoinositide-3 kinase By similarity

Sites

Active site36614-aspartylphosphate intermediate By similarity
Metal binding7071Magnesium By similarity
Metal binding7111Magnesium By similarity

Amino acid modifications

Modified residue2651Phosphoserine By similarity
Modified residue5481Phosphotyrosine By similarity
Modified residue9331Phosphoserine; by PKA By similarity

Natural variations

Alternative sequence1 – 22MG → MGGWEEERNRRAT in isoform 2.
VSP_046956
Alternative sequence1 – 22MG → MGSGGSDSYRIATSQ in isoform 3.
VSP_046957
Natural variant1371S → F in AHC2. Ref.15
VAR_068935
Natural variant1371S → Y in AHC2. Ref.15
VAR_068936
Natural variant1401Q → L in AHC2. Ref.15
VAR_068937
Natural variant2201D → N in AHC2. Ref.15
VAR_068938
Natural variant2741I → N in AHC2. Ref.14 Ref.15
VAR_068939
Natural variant2741I → T in DYT12. Ref.11
VAR_026735
Natural variant2771E → K in DYT12. Ref.11
VAR_026736
Natural variant3221V → D in AHC2. Ref.14
VAR_070767
Natural variant3331C → F in AHC2. Ref.15
VAR_068940
Natural variant3711L → P in AHC2. Ref.14
VAR_070768
Natural variant6131T → M in DYT12. Ref.11
VAR_026737
Natural variant7551G → C in AHC2. Ref.14 Ref.16
VAR_070769
Natural variant7551G → S in AHC2. Ref.15
VAR_068941
Natural variant7581I → S in DYT12. Ref.11
VAR_026738
Natural variant7721S → R in AHC2. Ref.14
VAR_070770
Natural variant7731N → I in AHC2. Ref.14
VAR_070771
Natural variant7731N → S in AHC2. Ref.15
VAR_068942
Natural variant7801F → L in DYT12. Ref.11
VAR_026739
Natural variant8011D → N in AHC2; protein levels is similar to wild-type but the enzyme activity is significantly decreased. Ref.14 Ref.15 Ref.16
VAR_068943
Natural variant8011D → Y in DYT12. Ref.11
VAR_026740
Natural variant8061M → R in AHC2. Ref.15
VAR_068944
Natural variant8101I → S in AHC2. Ref.15
VAR_068945
Natural variant8111S → P in AHC2; protein levels is similar to wild-type but the enzyme activity is significantly decreased. Ref.15
VAR_068946
Natural variant8151E → K in AHC2; protein levels is similar to wild-type but the enzyme activity is significantly decreased. Ref.14 Ref.15 Ref.16
VAR_068947
Natural variant8181E → K Probable disease-associated mutation found in patients with CAPOS. Ref.17
VAR_070772
Natural variant9191Missing in AHC2. Ref.15
VAR_068948
Natural variant9231D → N in DYT12. Ref.13
VAR_068949
Natural variant9231D → Y in AHC2. Ref.14
VAR_070773
Natural variant9271C → Y in AHC2.
VAR_070774
Natural variant9471G → R in AHC2. Ref.15
VAR_068950
Natural variant9551A → D in AHC2. Ref.15
VAR_068951
Natural variant9921D → Y in AHC2. Ref.15
VAR_068952
Natural variant10131Y → YY in DYT12; there is a drastic 40-to 50-fold reduction in Na(+) affinity in the mutant protein.
VAR_068953

Experimental info

Sequence conflict1 – 22MG → MEIH in CAA31390. Ref.2
Sequence conflict1441S → R in BAH12387. Ref.3
Sequence conflict3361L → V in AAA51798. Ref.1
Sequence conflict3361L → V in CAA31390. Ref.2
Sequence conflict3361L → V in AAA52285. Ref.6
Sequence conflict3361L → V in AAA58380. Ref.8
Sequence conflict3801H → T in AAA52285. Ref.6
Sequence conflict4211A → P in AAA58380. Ref.8
Sequence conflict4301I → M in CAA31390. Ref.2
Sequence conflict555 – 5573FPK → YPQ in AAA51798. Ref.1
Sequence conflict555 – 5573FPK → YPQ in CAA31390. Ref.2
Sequence conflict555 – 5573FPK → YPQ in AAA52286. Ref.6
Sequence conflict5771G → P in AAA51798. Ref.1
Sequence conflict5831D → G in AAA51798. Ref.1
Sequence conflict5831D → G in CAA31390. Ref.2
Sequence conflict5831D → G in AAA52286. Ref.6
Sequence conflict9191V → A in AAA52286. Ref.6
Sequence conflict9441L → M in AAA52286. Ref.6
Sequence conflict9821F → S in CAA31390. Ref.2
Sequence conflict10061W → S in AAA51798. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 17, 2006. Version 3.
Checksum: BF28CD9F1E11AF48

FASTA1,013111,749
        10         20         30         40         50         60 
MGDKKDDKDS PKKNKGKERR DLDDLKKEVA MTEHKMSVEE VCRKYNTDCV QGLTHSKAQE 

        70         80         90        100        110        120 
ILARDGPNAL TPPPTTPEWV KFCRQLFGGF SILLWIGAIL CFLAYGIQAG TEDDPSGDNL 

       130        140        150        160        170        180 
YLGIVLAAVV IITGCFSYYQ EAKSSKIMES FKNMVPQQAL VIREGEKMQV NAEEVVVGDL 

       190        200        210        220        230        240 
VEIKGGDRVP ADLRIISAHG CKVDNSSLTG ESEPQTRSPD CTHDNPLETR NITFFSTNCV 

       250        260        270        280        290        300 
EGTARGVVVA TGDRTVMGRI ATLASGLEVG KTPIAIEIEH FIQLITGVAV FLGVSFFILS 

       310        320        330        340        350        360 
LILGYTWLEA VIFLIGIIVA NVPEGLLATV TVCLTLTAKR MARKNCLVKN LEAVETLGST 

       370        380        390        400        410        420 
STICSDKTGT LTQNRMTVAH MWFDNQIHEA DTTEDQSGTS FDKSSHTWVA LSHIAGLCNR 

       430        440        450        460        470        480 
AVFKGGQDNI PVLKRDVAGD ASESALLKCI ELSSGSVKLM RERNKKVAEI PFNSTNKYQL 

       490        500        510        520        530        540 
SIHETEDPND NRYLLVMKGA PERILDRCST ILLQGKEQPL DEEMKEAFQN AYLELGGLGE 

       550        560        570        580        590        600 
RVLGFCHYYL PEEQFPKGFA FDCDDVNFTT DNLCFVGLMS MIDPPRAAVP DAVGKCRSAG 

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

       670        680        690        700        710        720 
KDFTSEQIDE ILQNHTEIVF ARTSPQQKLI IVEGCQRQGA IVAVTGDGVN DSPALKKADI 

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

       790        800        810        820        830        840 
LLFIMANIPL PLGTITILCI DLGTDMVPAI SLAYEAAESD IMKRQPRNPR TDKLVNERLI 

       850        860        870        880        890        900 
SMAYGQIGMI QALGGFFSYF VILAENGFLP GNLVGIRLNW DDRTVNDLED SYGQQWTYEQ 

       910        920        930        940        950        960 
RKVVEFTCHT AFFVSIVVVQ WADLIICKTR RNSVFQQGMK NKILIFGLFE ETALAAFLSY 

       970        980        990       1000       1010 
CPGMDVALRM YPLKPSWWFC AFPYSFLIFV YDEIRKLILR RNPGGWVEKE TYY 

« Hide

Isoform 2 [UniParc].

Checksum: D6F4310E7B68C1D1
Show »

FASTA1,024113,134
Isoform 3 [UniParc].

Checksum: 50F72BDBADD90225
Show »

FASTA1,026113,059

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]"The family of human Na+,K+-ATPase genes. A partial nucleotide sequence related to the alpha-subunit."
Ovchinnikov Y.A., Monastyrskaya G.S., Broude N.E., Allikmets R.L., Ushkaryov Y.A., Melkov A.M., Smirnov Y.V., Malyshev I.V., Dulubova I.E., Petrukhin K.E., Gryshin A.V., Sverdlov V.E., Kiyatkin N.I., Kostina M.B., Modyanov N.N., Sverdlov E.D.
FEBS Lett. 213:73-80(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 120-387; 494-538 AND 545-1013.
[7]Erratum
Ovchinnikov Y.A., Monastyrskaya G.S., Broude N.E., Allikmets R.L., Ushkaryov Y.A., Melkov A.M., Smirnov Y.V., Malyshev I.V., Dulubova I.E., Petrukhin K.E., Gryshin A.V., Sverdlov V.E., Kiyatkin N.I., Kostina M.B., Modyanov N.N., Sverdlov E.D.
FEBS Lett. 214:375-375(1987)
[8]"The family of human Na+,K+-ATPase genes. No less than five genes and/or pseudogenes related to the alpha-subunit."
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.
FEBS Lett. 217:275-278(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 243-434.
[9]"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.
[10]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"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.
[12]"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.
[13]"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.
[14]"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.
[15]"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. expand/collapse author list , 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.
[16]"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.
[17]"A novel recurrent mutation in ATP1A3 causes CAPOS syndrome."
Demos M.K., van Karnebeek C.D., Ross C.J., Adam S., Shen Y., Zhan S.H., Shyr C., Horvath G., Suri M., Fryer A., Jones S.J., Friedman J.M.
Orphanet J. Rare Dis. 9:15-15(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN CAPOS, VARIANT LYS-818.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M37457 expand/collapse EMBL AC list , 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 expand/collapse EMBL AC list , 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 expand/collapse EMBL AC list , M28287, M35821, M35822, M28289, M28290, M28291, M28292 Genomic DNA. Translation: AAA52286.1.
M27577, M27570, M27573 Genomic DNA. Translation: AAA58380.1.
CCDSCCDS12594.1. [P13637-1]
CCDS58663.1. [P13637-2]
CCDS58664.1. [P13637-3]
PIRS00801.
RefSeqNP_001243142.1. NM_001256213.1. [P13637-2]
NP_001243143.1. NM_001256214.1. [P13637-3]
NP_689509.1. NM_152296.4. [P13637-1]
UniGeneHs.515427.

3D structure databases

ProteinModelPortalP13637.
SMRP13637. Positions 20-1013.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106968. 4 interactions.
IntActP13637. 4 interactions.
MINTMINT-2857038.
STRING9606.ENSP00000302397.

Chemistry

BindingDBP13637.
ChEMBLCHEMBL2095186.

Protein family/group databases

TCDB3.A.3.1.1. the p-type atpase (p-atpase) superfamily.

PTM databases

PhosphoSiteP13637.

Polymorphism databases

DMDM116241260.

Proteomic databases

MaxQBP13637.
PaxDbP13637.
PRIDEP13637.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000302102; ENSP00000302397; ENSG00000105409. [P13637-1]
ENST00000543770; ENSP00000437577; ENSG00000105409. [P13637-2]
ENST00000545399; ENSP00000444688; ENSG00000105409. [P13637-3]
ENST00000608982; ENSP00000476333; ENSG00000272584. [P13637-2]
ENST00000609321; ENSP00000476705; ENSG00000272584. [P13637-1]
ENST00000609746; ENSP00000476872; ENSG00000272584. [P13637-3]
GeneID478.
KEGGhsa:478.
UCSCuc002osg.4. human. [P13637-1]

Organism-specific databases

CTD478.
GeneCardsGC19M042470.
GeneReviewsATP1A3.
HGNCHGNC:801. ATP1A3.
HPACAB001988.
MIM128235. phenotype.
182350. gene.
614820. phenotype.
neXtProtNX_P13637.
Orphanet2131. Alternating hemiplegia of childhood.
1171. Cerebellar ataxia - areflexia - pes cavus - optic atrophy - sensorineural hearing loss.
71517. Rapid-onset dystonia-parkinsonism.
PharmGKBPA64.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0474.
HOGENOMHOG000265622.
HOVERGENHBG004298.
InParanoidP13637.
KOK01539.
OrthoDBEOG7327N0.
PhylomeDBP13637.
TreeFamTF312838.

Enzyme and pathway databases

ReactomeREACT_15518. Transmembrane transport of small molecules.

Gene expression databases

ArrayExpressP13637.
BgeeP13637.
CleanExHS_ATP1A3.
GenevestigatorP13637.

Family and domain databases

Gene3D1.20.1110.10. 2 hits.
2.70.150.10. 2 hits.
3.40.1110.10. 1 hit.
InterProIPR006068. 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]
PfamPF00689. Cation_ATPase_C. 1 hit.
PF00690. Cation_ATPase_N. 1 hit.
PF00122. E1-E2_ATPase. 1 hit.
PF00702. Hydrolase. 1 hit.
[Graphical view]
PRINTSPR00119. CATATPASE.
SMARTSM00831. Cation_ATPase_N. 1 hit.
[Graphical view]
SUPFAMSSF56784. SSF56784. 3 hits.
SSF81660. SSF81660. 1 hit.
TIGRFAMsTIGR01106. ATPase-IIC_X-K. 1 hit.
TIGR01494. ATPase_P-type. 2 hits.
PROSITEPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSATP1A3. human.
GeneWikiATP1A3.
GenomeRNAi478.
NextBio1981.
PROP13637.
SOURCESearch...

Entry information

Entry nameAT1A3_HUMAN
AccessionPrimary (citable) accession number: P13637
Secondary accession number(s): B7Z2T0 expand/collapse secondary AC list , B7Z401, F5H6J6, Q16732, Q16735, Q969K5
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: October 17, 2006
Last modified: July 9, 2014
This is version 164 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM