P13637 (AT1A3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1013 AA.
Sequence status	Complete.
Protein existence	Evidence 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.8.
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.10 Ref.11 Ref.12 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.13
Sequence similarities	Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IIC subfamily. [View classification]

Ontologies

Keywords
Biological process	Ion transport Potassium transport Sodium transport Sodium/potassium transport Transport
Cellular component	Cell membrane Membrane
Disease	Disease mutation Dystonia Parkinsonism
Domain	Transmembrane Transmembrane helix
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding Potassium Sodium
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	ATP biosynthetic process Inferred from electronic annotation. Source: InterPro adult locomotory behavior Inferred from electronic annotation. Source: Compara ionotropic glutamate receptor signaling pathway Inferred from electronic annotation. Source: Compara memory Inferred from electronic annotation. Source: Compara response to drug Inferred from electronic annotation. Source: Compara visual learning Inferred from electronic annotation. Source: Compara
Cellular_component	Golgi apparatus Inferred from direct assay Ref.10. Source: UniProtKB axon Inferred from electronic annotation. Source: Compara endoplasmic reticulum Inferred from direct assay Ref.10. Source: UniProtKB myelin sheath Inferred from electronic annotation. Source: Compara nucleus Inferred from electronic annotation. Source: Compara sodium:potassium-exchanging ATPase complex Inferred by curator Ref.10. Source: UniProtKB synapse Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	ATP binding Non-traceable author statement Ref.10. Source: UniProtKB metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW sodium:potassium-exchanging ATPase activity Inferred from mutant phenotype Ref.10. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1013	1013	Sodium/potassium-transporting ATPase subunit alpha-3		PRO_0000046298
Regions
	Topological domain	1 – 77	77	Cytoplasmic Potential
	Transmembrane	78 – 98	21	Helical; Potential
	Topological domain	99 – 121	23	Extracellular Potential
	Transmembrane	122 – 142	21	Helical; Potential
	Topological domain	143 – 278	136	Cytoplasmic Potential
	Transmembrane	279 – 298	20	Helical; Potential
	Topological domain	299 – 310	12	Extracellular Potential
	Transmembrane	311 – 328	18	Helical; Potential
	Topological domain	329 – 762	434	Cytoplasmic Potential
	Transmembrane	763 – 782	20	Helical; Potential
	Topological domain	783 – 792	10	Extracellular Potential
	Transmembrane	793 – 813	21	Helical; Potential
	Topological domain	814 – 833	20	Cytoplasmic Potential
	Transmembrane	834 – 856	23	Helical; Potential
	Topological domain	857 – 908	52	Extracellular Potential
	Transmembrane	909 – 928	20	Helical; Potential
	Topological domain	929 – 941	13	Cytoplasmic Potential
	Transmembrane	942 – 960	19	Helical; Potential
	Topological domain	961 – 975	15	Extracellular Potential
	Transmembrane	976 – 996	21	Helical; Potential
	Topological domain	997 – 1013	17	Cytoplasmic Potential
	Region	72 – 74	3	Interaction with phosphoinositide-3 kinase By similarity
Sites
	Active site	366	1	4-aspartylphosphate intermediate By similarity
	Metal binding	707	1	Magnesium By similarity
	Metal binding	711	1	Magnesium By similarity
Amino acid modifications
	Modified residue	265	1	Phosphoserine By similarity
	Modified residue	368	1	Phosphothreonine By similarity
	Modified residue	493	1	Phosphotyrosine By similarity
	Modified residue	548	1	Phosphotyrosine By similarity
	Modified residue	549	1	Phosphotyrosine By similarity
	Modified residue	933	1	Phosphoserine; by PKA By similarity
Natural variations
	Natural variant	137	1	S → F in AHC2. Ref.13		VAR_068935
	Natural variant	137	1	S → Y in AHC2. Ref.13		VAR_068936
	Natural variant	140	1	Q → L in AHC2. Ref.13		VAR_068937
	Natural variant	220	1	D → N in AHC2. Ref.13		VAR_068938
	Natural variant	274	1	I → N in AHC2. Ref.13		VAR_068939
	Natural variant	274	1	I → T in DYT12. Ref.10		VAR_026735
	Natural variant	277	1	E → K in DYT12. Ref.10		VAR_026736
	Natural variant	333	1	C → F in AHC2. Ref.13		VAR_068940
	Natural variant	613	1	T → M in DYT12. Ref.10		VAR_026737
	Natural variant	755	1	G → S in AHC2. Ref.13		VAR_068941
	Natural variant	758	1	I → S in DYT12. Ref.10		VAR_026738
	Natural variant	773	1	N → S in AHC2. Ref.13		VAR_068942
	Natural variant	780	1	F → L in DYT12. Ref.10		VAR_026739
	Natural variant	801	1	D → N in AHC2; protein levels is similar to wild-type but the enzyme activity is significantly decreased. Ref.13		VAR_068943
	Natural variant	801	1	D → Y in DYT12. Ref.10		VAR_026740
	Natural variant	806	1	M → R in AHC2. Ref.13		VAR_068944
	Natural variant	810	1	I → S in AHC2. Ref.13		VAR_068945
	Natural variant	811	1	S → P in AHC2; protein levels is similar to wild-type but the enzyme activity is significantly decreased. Ref.13		VAR_068946
	Natural variant	815	1	E → K in AHC2; protein levels is similar to wild-type but the enzyme activity is significantly decreased. Ref.13		VAR_068947
	Natural variant	919	1	Missing in AHC2. Ref.13		VAR_068948
	Natural variant	923	1	D → N in DYT12. Ref.12		VAR_068949
	Natural variant	947	1	G → R in AHC2. Ref.13		VAR_068950
	Natural variant	955	1	A → D in AHC2. Ref.13		VAR_068951
	Natural variant	992	1	D → Y in AHC2. Ref.13		VAR_068952
	Natural variant	1013	1	Y → YY in DYT12; there is a drastic 40-to 50-fold reduction in Na(+) affinity in the mutant protein. Ref.11		VAR_068953
Experimental info
	Sequence conflict	1 – 2	2	MG → MEIH in CAA31390. Ref.2
	Sequence conflict	336	1	L → V in AAA51798. Ref.1
	Sequence conflict	336	1	L → V in CAA31390. Ref.2
	Sequence conflict	336	1	L → V in AAA52285. Ref.5
	Sequence conflict	336	1	L → V in AAA58380. Ref.7
	Sequence conflict	380	1	H → T in AAA52285. Ref.5
	Sequence conflict	421	1	A → P in AAA58380. Ref.7
	Sequence conflict	430	1	I → M in CAA31390. Ref.2
	Sequence conflict	555 – 557	3	FPK → YPQ in AAA51798. Ref.1
	Sequence conflict	555 – 557	3	FPK → YPQ in CAA31390. Ref.2
	Sequence conflict	555 – 557	3	FPK → YPQ in AAA52286. Ref.5
	Sequence conflict	577	1	G → P in AAA51798. Ref.1
	Sequence conflict	583	1	D → G in AAA51798. Ref.1
	Sequence conflict	583	1	D → G in CAA31390. Ref.2
	Sequence conflict	583	1	D → G in AAA52286. Ref.5
	Sequence conflict	919	1	V → A in AAA52286. Ref.5
	Sequence conflict	944	1	L → M in AAA52286. Ref.5
	Sequence conflict	982	1	F → S in CAA31390. Ref.2
	Sequence conflict	1006	1	W → S in AAA51798. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P13637 [UniParc]. Last modified October 17, 2006. Version 3. Checksum: BF28CD9F1E11AF48	FASTA	1,013	111,749
	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

References

	« Hide 'large scale' referencesShow '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].
[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]. Tissue: Brain.
[3]	"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].
[4]	"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]. Tissue: Brain.
[5]	"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.
[6]	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)
[7]	"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.
[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]	"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].
[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 INS, CHARACTERIZATION OF VARIANT DYT12 TYR-1013 INS.
[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]	"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.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases
EMBL GenBank DDBJ	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. 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.
IPI	IPI00302840.
PIR	S00801.
RefSeq	NP_001243142.1. NM_001256213.1. NP_001243143.1. NM_001256214.1. NP_689509.1. NM_152296.4.
UniGene	Hs.515427.
3D structure databases
ProteinModelPortal	P13637.
ModBase	Search...
Protein-protein interaction databases
IntAct	P13637. 3 interactions.
MINT	MINT-2857038.
STRING	9606.ENSP00000302397.
Protein family/group databases
TCDB	3.A.3.1.1. P-type ATPase (P-ATPase) superfamily.
PTM databases
PhosphoSite	P13637.
Polymorphism databases
DMDM	116241260.
Proteomic databases
PaxDb	P13637.
PRIDE	P13637.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000302102; ENSP00000302397; ENSG00000105409.
GeneID	478.
KEGG	hsa:478.
UCSC	uc002osg.3. human.
Organism-specific databases
CTD	478.
GeneCards	GC19M042470.
HGNC	HGNC:801. ATP1A3.
HPA	CAB001988.
MIM	128235. phenotype. 182350. gene. 614820. phenotype.
neXtProt	NX_P13637.
Orphanet	2131. Alternating hemiplegia of childhood. 71517. Rapid-onset dystonia-parkinsonism.
PharmGKB	PA64.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0474.
HOVERGEN	HBG004298.
InParanoid	P13637.
KO	K01539.
OrthoDB	EOG46MBHS.
PhylomeDB	P13637.
Enzyme and pathway databases
Reactome	REACT_15518. Transmembrane transport of small molecules.
Gene expression databases
ArrayExpress	P13637.
Bgee	P13637.
CleanEx	HS_ATP1A3.
Genevestigator	P13637.
GermOnline	ENSG00000105409. Homo sapiens.
Family and domain databases
Gene3D	1.20.1110.10. 2 hits. 2.70.150.10. 2 hits. 3.40.1110.10. 1 hit.
InterPro	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]
PANTHER	PTHR24093. PTHR24093. 1 hit.
Pfam	PF00689. Cation_ATPase_C. 1 hit. PF00690. Cation_ATPase_N. 1 hit. PF00122. E1-E2_ATPase. 1 hit. PF00702. Hydrolase. 1 hit. [Graphical view]
PRINTS	PR00119. CATATPASE.
SMART	SM00831. Cation_ATPase_N. 1 hit. [Graphical view]
SUPFAM	SSF81660. ATPase_cation_domN. 1 hit. SSF56784. HAD-like_dom. 1 hit.
TIGRFAMs	TIGR01106. ATPase-IIC_X-K. 1 hit. TIGR01494. ATPase_P-type. 2 hits.
PROSITE	PS00154. ATPASE_E1_E2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	P13637.
ChEMBL	CHEMBL4052.
ChiTaRS	ATP1A3. human.
GenomeRNAi	478.
NextBio	1981.
SOURCE	Search...

Entry information

Entry name

AT1A3_HUMAN

Accession

Primary (citable) accession number: P13637
Secondary accession number(s): Q16732, Q16735, Q969K5

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	October 17, 2006
Last modified:	May 29, 2013
This is version 151 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.