P50993 (AT1A2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Sodium/potassium-transporting ATPase subunit alpha-2
Short name=Na(+)/K(+) ATPase alpha-2 subunit
EC=3.6.3.9

Alternative name(s):
Sodium pump subunit alpha-2

Gene names

Name:	ATP1A2
Synonyms:	KIAA0778

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	1020 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
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, 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	Membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein Ref.9.
Involvement in disease	Familial hemiplegic migraine 2 (FHM2) [MIM:602481]: A subtype of migraine with aura associated with hemiparesis in some families. Migraine is a disabling symptom complex of periodic headaches, usually temporal and unilateral. Headaches are often accompanied by irritability, nausea, vomiting and photobia, preceded by constriction of the cranial arteries. Migraine with aura is characterized by recurrent attacks of reversible neurological symptoms (aura) that precede or accompany the headache. Aura may include a combination of sensory disturbances, such as blurred vision, hallucinations, vertigo, numbness and difficulty in concentrating and speaking. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.11 Ref.12 Ref.14 Alternating hemiplegia of childhood 1 (AHC1) [MIM:104290]: 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]
Sequence caution	The sequence BAA34498.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Biological process	Ion transport Potassium transport Sodium transport Sodium/potassium transport Transport
Cellular component	Cell membrane Membrane
Disease	Disease mutation
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 ATP hydrolysis coupled proton transport Inferred from electronic annotation. Source: Compara adult locomotory behavior Inferred from electronic annotation. Source: Compara cellular response to mechanical stimulus Inferred from electronic annotation. Source: Compara locomotion Inferred from electronic annotation. Source: Compara negative regulation of heart contraction Inferred from electronic annotation. Source: Compara negative regulation of striated muscle contraction Inferred from electronic annotation. Source: Compara neurotransmitter uptake Inferred from electronic annotation. Source: Compara reduction of cytosolic calcium ion concentration Inferred from electronic annotation. Source: Compara regulation of blood pressure Inferred from electronic annotation. Source: Compara regulation of cardiac muscle cell contraction Inferred from electronic annotation. Source: Compara regulation of respiratory gaseous exchange by neurological system process Inferred from electronic annotation. Source: Compara regulation of smooth muscle contraction Inferred from electronic annotation. Source: Compara regulation of striated muscle contraction Non-traceable author statement PubMed 10642400. Source: UniProtKB regulation of the force of heart contraction Inferred from electronic annotation. Source: Compara regulation of vasoconstriction Inferred from electronic annotation. Source: Compara response to nicotine Inferred from electronic annotation. Source: Compara visual learning Inferred from electronic annotation. Source: Compara
Cellular_component	T-tubule Inferred from electronic annotation. Source: Compara caveola Inferred from electronic annotation. Source: Compara cytoplasm Inferred from direct assay Ref.12. Source: UniProtKB dendritic spine Inferred from electronic annotation. Source: Compara endosome Inferred from electronic annotation. Source: Compara sodium:potassium-exchanging ATPase complex Inferred by curator Ref.12. Source: UniProtKB synapse Inferred from electronic annotation. Source: Compara
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW sodium:potassium-exchanging ATPase activity Inferred from mutant phenotype Ref.12. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Propeptide	1 – 5	5	By similarity		PRO_0000002503
	Chain	6 – 1020	1015	Sodium/potassium-transporting ATPase subunit alpha-2		PRO_0000002504
Regions
	Topological domain	6 – 85	80	Cytoplasmic Potential
	Transmembrane	86 – 106	21	Helical; Potential
	Topological domain	107 – 129	23	Extracellular Potential
	Transmembrane	130 – 150	21	Helical; Potential
	Topological domain	151 – 286	136	Cytoplasmic Potential
	Transmembrane	287 – 306	20	Helical; Potential
	Topological domain	307 – 318	12	Extracellular Potential
	Transmembrane	319 – 336	18	Helical; Potential
	Topological domain	337 – 769	433	Cytoplasmic Potential
	Transmembrane	770 – 789	20	Helical; Potential
	Topological domain	790 – 799	10	Extracellular Potential
	Transmembrane	800 – 820	21	Helical; Potential
	Topological domain	821 – 840	20	Cytoplasmic Potential
	Transmembrane	841 – 863	23	Helical; Potential
	Topological domain	864 – 915	52	Extracellular Potential
	Transmembrane	916 – 935	20	Helical; Potential
	Topological domain	936 – 948	13	Cytoplasmic Potential
	Transmembrane	949 – 967	19	Helical; Potential
	Topological domain	968 – 982	15	Extracellular Potential
	Transmembrane	983 – 1003	21	Helical; Potential
	Topological domain	1004 – 1020	17	Cytoplasmic Potential
	Region	80 – 82	3	Interaction with phosphoinositide-3 kinase By similarity
Sites
	Active site	374	1	4-aspartylphosphate intermediate By similarity
	Metal binding	714	1	Magnesium By similarity
	Metal binding	718	1	Magnesium By similarity
Amino acid modifications
	Modified residue	570	1	Phosphothreonine Ref.10
	Modified residue	587	1	Phosphoserine Ref.10
	Modified residue	650	1	Phosphoserine By similarity
	Modified residue	940	1	Phosphoserine; by PKA By similarity
Natural variations
	Natural variant	378	1	T → N in AHC1. Ref.13 Corresponds to variant rs28934002 [ dbSNP | Ensembl ].		VAR_019934
	Natural variant	689	1	R → Q in FHM2. Ref.11 Corresponds to variant rs28933401 [ dbSNP | Ensembl ].		VAR_019935
	Natural variant	715	1	G → R in FHM2; de novo mutation in a sporadic case. Ref.14		VAR_065685
	Natural variant	731	1	M → T in FHM2. Ref.11 Corresponds to variant rs28933400 [ dbSNP | Ensembl ].		VAR_019936
	Natural variant	764	1	L → P in FHM2; loss of function. Ref.12 Corresponds to variant rs28933398 [ dbSNP | Ensembl ].		VAR_019937
	Natural variant	887	1	W → R in FHM2; loss of function. Ref.12 Corresponds to variant rs28933399 [ dbSNP | Ensembl ].		VAR_019938

Sequences

	Sequence		Length	Mass (Da)
	P50993 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: AFBD8EA94FFB4FC3	FASTA	1,020	112,265
	10 20 30 40 50 60 MGRGAGREYS PAATTAENGG GKKKQKEKEL DELKKEVAMD DHKLSLDELG RKYQVDLSKG 70 80 90 100 110 120 LTNQRAQDVL ARDGPNALTP PPTTPEWVKF CRQLFGGFSI LLWIGAILCF LAYGIQAAME 130 140 150 160 170 180 DEPSNDNLYL GVVLAAVVIV TGCFSYYQEA KSSKIMDSFK NMVPQQALVI REGEKMQINA 190 200 210 220 230 240 EEVVVGDLVE VKGGDRVPAD LRIISSHGCK VDNSSLTGES EPQTRSPEFT HENPLETRNI 250 260 270 280 290 300 CFFSTNCVEG TARGIVIATG DRTVMGRIAT LASGLEVGRT PIAMEIEHFI QLITGVAVFL 310 320 330 340 350 360 GVSFFVLSLI LGYSWLEAVI FLIGIIVANV PEGLLATVTV CLTLTAKRMA RKNCLVKNLE 370 380 390 400 410 420 AVETLGSTST ICSDKTGTLT QNRMTVAHMW FDNQIHEADT TEDQSGATFD KRSPTWTALS 430 440 450 460 470 480 RIAGLCNRAV FKAGQENISV SKRDTAGDAS ESALLKCIEL SCGSVRKMRD RNPKVAEIPF 490 500 510 520 530 540 NSTNKYQLSI HEREDSPQSH VLVMKGAPER ILDRCSTILV QGKEIPLDKE MQDAFQNAYM 550 560 570 580 590 600 ELGGLGERVL GFCQLNLPSG KFPRGFKFDT DELNFPTEKL CFVGLMSMID PPRAAVPDAV 610 620 630 640 650 660 GKCRSAGIKV IMVTGDHPIT AKAIAKGVGI ISEGNETVED IAARLNIPMS QVNPREAKAC 670 680 690 700 710 720 VVHGSDLKDM TSEQLDEILK NHTEIVFART SPQQKLIIVE GCQRQGAIVA VTGDGVNDSP 730 740 750 760 770 780 ALKKADIGIA MGISGSDVSK QAADMILLDD NFASIVTGVE EGRLIFDNLK KSIAYTLTSN 790 800 810 820 830 840 IPEITPFLLF IIANIPLPLG TVTILCIDLG TDMVPAISLA YEAAESDIMK RQPRNSQTDK 850 860 870 880 890 900 LVNERLISMA YGQIGMIQAL GGFFTYFVIL AENGFLPSRL LGIRLDWDDR TMNDLEDSYG 910 920 930 940 950 960 QEWTYEQRKV VEFTCHTAFF ASIVVVQWAD LIICKTRRNS VFQQGMKNKI LIFGLLEETA 970 980 990 1000 1010 1020 LAAFLSYCPG MGVALRMYPL KVTWWFCAFP YSLLIFIYDE VRKLILRRYP GGWVEKETYY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of the human Na,K-ATPase alpha 2 gene and identification of intragenic restriction fragment length polymorphisms." Shull M.M., Pugh D.G., Lingrel J.B. J. Biol. Chem. 264:17532-17543(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Prediction of the coding sequences of unidentified human genes. XI. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro." Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O. DNA Res. 5:277-286(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[3]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases 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]. Tissue: Ovary.
[6]	"Multiple genes encode the human Na+,K+-ATPase catalytic subunit." Shull M.M., Lingrel J.B. Proc. Natl. Acad. Sci. U.S.A. 84:4039-4043(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 211-249. Tissue: Leukocyte.
[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 [MRNA] OF 251-442. Tissue: Brain and Placenta.
[8]	"Family of human Na+,K+-ATPase genes. Structure of the putative regulatory region of the alpha+-gene." Sverdlov E.D., Bessarab D.A., Malyshev I.V., Petrukhin K.E., Smirnov Y.V., Ushkaryov Y.A., Monastyrskaya G.S., Broude N.E., Modyanov N.N. FEBS Lett. 244:481-483(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-4.
[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]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-570 AND SER-587, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"Novel mutations in the Na+, K+-ATPase pump gene ATP1A2 associated with familial hemiplegic migraine and benign familial infantile convulsions." Vanmolkot K.R.J., Kors E.E., Hottenga J.-J., Terwindt G.M., Haan J., Hoefnagels W.A.J., Black D.F., Sandkuijl L.A., Frants R.R., Ferrari M.D., van den Maagdenberg A.M.J.M. Ann. Neurol. 54:360-366(2003) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS FHM2 GLN-689 AND THR-731.
[12]	"Haploinsufficiency of ATP1A2 encoding the Na+/K+ pump alpha2 subunit associated with familial hemiplegic migraine type 2." De Fusco M., Marconi R., Silvestri L., Atorino L., Rampoldi L., Morgante L., Ballabio A., Aridon P., Casari G. Nat. Genet. 33:192-196(2003) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS FHM2 PRO-764 AND ARG-887, CHARACTERIZATION OF VARIANTS FMH2 PRO-764 AND ARG-887.
[13]	"Alternating hemiplegia of childhood or familial hemiplegic migraine? A novel ATP1A2 mutation." Swoboda K.J., Kanavakis E., Xaidara A., Johnson J.E., Leppert M.F., Schlesinger-Massart M.B., Ptacek L.J., Silver K., Youroukos S. Ann. Neurol. 55:884-887(2004) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT AHC1 ASN-378.
[14]	"Prolonged sporadic hemiplegic migraine associated with a novel de novo missense ATP1A2 gene mutation." De Sanctis S., Grieco G.S., Breda L., Casali C., Nozzi M., Del Torto M., Chiarelli F., Verrotti A. Headache 51:447-450(2011) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT FHM2 ARG-715.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases
EMBL GenBank DDBJ	J05096 Genomic DNA. Translation: AAA51797.1. AB018321 mRNA. Translation: BAA34498.2. Different initiation. AL121987 Genomic DNA. Translation: CAI15271.1. CH471121 Genomic DNA. Translation: EAW52740.1. CH471121 Genomic DNA. Translation: EAW52741.1. BC052271 mRNA. Translation: AAH52271.2. M16795 mRNA. Translation: AAA51799.1. M27578, M27571, M27576 Genomic DNA. Translation: AAA35575.1. Y07494 mRNA. Translation: CAA68793.1. Sequence problems.
IPI	IPI00003021.
PIR	A34474.
RefSeq	NP_000693.1. NM_000702.3.
UniGene	Hs.34114.
3D structure databases
ProteinModelPortal	P50993.
ModBase	Search...
Protein-protein interaction databases
IntAct	P50993. 1 interaction.
STRING	9606.ENSP00000354490.
Protein family/group databases
TCDB	3.A.3.1.1. P-type ATPase (P-ATPase) superfamily.
PTM databases
PhosphoSite	P50993.
Polymorphism databases
DMDM	1703467.
Proteomic databases
PaxDb	P50993.
PRIDE	P50993.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000361216; ENSP00000354490; ENSG00000018625.
GeneID	477.
KEGG	hsa:477.
UCSC	uc001fvb.2. human.
Organism-specific databases
CTD	477.
GeneCards	GC01P160085.
HGNC	HGNC:800. ATP1A2.
HPA	CAB022230.
MIM	104290. phenotype. 182340. gene. 602481. phenotype.
neXtProt	NX_P50993.
Orphanet	2131. Alternating hemiplegia of childhood. 569. Familial or sporadic hemiplegic migraine.
PharmGKB	PA30796.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0474.
HOGENOM	HOG000265622.
HOVERGEN	HBG004298.
InParanoid	P50993.
KO	K01539.
OMA	IINIPLP.
OrthoDB	EOG46MBHS.
Enzyme and pathway databases
Reactome	REACT_15518. Transmembrane transport of small molecules.
Gene expression databases
ArrayExpress	P50993.
Bgee	P50993.
CleanEx	HS_ATP1A2.
Genevestigator	P50993.
GermOnline	ENSG00000018625. 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	P50993.
ChEMBL	CHEMBL2715.
ChiTaRS	ATP1A2. human.
GenomeRNAi	477.
NextBio	1977.
SOURCE	Search...

Entry information

Entry name

AT1A2_HUMAN

Accession

Primary (citable) accession number: P50993
Secondary accession number(s): D3DVE4 , Q07059, Q5JW74, Q86UZ5, Q9UQ25

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	May 1, 2013
This is version 138 of the entry and version 1 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.