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P13637

- AT1A3_HUMAN

UniProt

P13637 - AT1A3_HUMAN

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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

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. chaperone binding Source: BHF-UCL
  3. metal ion binding Source: UniProtKB-KW
  4. sodium:potassium-exchanging ATPase activity Source: UniProtKB
  5. steroid hormone binding Source: BHF-UCL

GO - Biological processi

  1. adult locomotory behavior Source: Ensembl
  2. ATP biosynthetic process Source: InterPro
  3. cell communication by electrical coupling involved in cardiac conduction Source: BHF-UCL
  4. cellular potassium ion homeostasis Source: BHF-UCL
  5. cellular response to steroid hormone stimulus Source: BHF-UCL
  6. cellular sodium ion homeostasis Source: BHF-UCL
  7. ionotropic glutamate receptor signaling pathway Source: Ensembl
  8. ion transmembrane transport Source: Reactome
  9. memory Source: Ensembl
  10. potassium ion import Source: BHF-UCL
  11. response to drug Source: Ensembl
  12. sodium ion export from cell Source: BHF-UCL
  13. transmembrane transport Source: Reactome
  14. visual learning Source: Ensembl
Complete GO annotation...

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
  12. vesicle Source: UniProtKB
Complete GO annotation...

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

BgeeiP13637.
CleanExiHS_ATP1A3.
ExpressionAtlasiP13637. baseline and differential.
GenevestigatoriP13637.

Organism-specific databases

HPAiCAB001988.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi106968. 21 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.
GeneTreeiENSGT00760000119003.
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

        10         20         30         40         50
MGDKKDDKDS PKKNKGKERR DLDDLKKEVA MTEHKMSVEE VCRKYNTDCV
60 70 80 90 100
QGLTHSKAQE ILARDGPNAL TPPPTTPEWV KFCRQLFGGF SILLWIGAIL
110 120 130 140 150
CFLAYGIQAG TEDDPSGDNL YLGIVLAAVV IITGCFSYYQ EAKSSKIMES
160 170 180 190 200
FKNMVPQQAL VIREGEKMQV NAEEVVVGDL VEIKGGDRVP ADLRIISAHG
210 220 230 240 250
CKVDNSSLTG ESEPQTRSPD CTHDNPLETR NITFFSTNCV EGTARGVVVA
260 270 280 290 300
TGDRTVMGRI ATLASGLEVG KTPIAIEIEH FIQLITGVAV FLGVSFFILS
310 320 330 340 350
LILGYTWLEA VIFLIGIIVA NVPEGLLATV TVCLTLTAKR MARKNCLVKN
360 370 380 390 400
LEAVETLGST STICSDKTGT LTQNRMTVAH MWFDNQIHEA DTTEDQSGTS
410 420 430 440 450
FDKSSHTWVA LSHIAGLCNR AVFKGGQDNI PVLKRDVAGD ASESALLKCI
460 470 480 490 500
ELSSGSVKLM RERNKKVAEI PFNSTNKYQL SIHETEDPND NRYLLVMKGA
510 520 530 540 550
PERILDRCST ILLQGKEQPL DEEMKEAFQN AYLELGGLGE RVLGFCHYYL
560 570 580 590 600
PEEQFPKGFA FDCDDVNFTT DNLCFVGLMS MIDPPRAAVP DAVGKCRSAG
610 620 630 640 650
IKVIMVTGDH PITAKAIAKG VGIISEGNET VEDIAARLNI PVSQVNPRDA
660 670 680 690 700
KACVIHGTDL KDFTSEQIDE ILQNHTEIVF ARTSPQQKLI IVEGCQRQGA
710 720 730 740 750
IVAVTGDGVN DSPALKKADI GVAMGIAGSD VSKQAADMIL LDDNFASIVT
760 770 780 790 800
GVEEGRLIFD NLKKSIAYTL TSNIPEITPF LLFIMANIPL PLGTITILCI
810 820 830 840 850
DLGTDMVPAI SLAYEAAESD IMKRQPRNPR TDKLVNERLI SMAYGQIGMI
860 870 880 890 900
QALGGFFSYF VILAENGFLP GNLVGIRLNW DDRTVNDLED SYGQQWTYEQ
910 920 930 940 950
RKVVEFTCHT AFFVSIVVVQ WADLIICKTR RNSVFQQGMK NKILIFGLFE
960 970 980 990 1000
ETALAAFLSY CPGMDVALRM YPLKPSWWFC AFPYSFLIFV YDEIRKLILR
1010
RNPGGWVEKE TYY
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. 21 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.
GeneTreei ENSGT00760000119003.
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

Bgeei P13637.
CleanExi HS_ATP1A3.
ExpressionAtlasi P13637. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 167 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