Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P50993 (AT1A2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 147. 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·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1020 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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, 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

Migraine, familial hemiplegic, 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 photophobia, 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 Ref.15 Ref.16

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 processIon transport
Potassium transport
Sodium transport
Sodium/potassium transport
Transport
   Cellular componentCell membrane
Membrane
   DiseaseDisease mutation
   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

ATP hydrolysis coupled proton transport

Inferred from electronic annotation. Source: Ensembl

adult locomotory behavior

Inferred from electronic annotation. Source: Ensembl

cellular response to mechanical stimulus

Inferred from electronic annotation. Source: Ensembl

ion transmembrane transport

Traceable author statement. Source: Reactome

locomotion

Inferred from electronic annotation. Source: Ensembl

negative regulation of cytosolic calcium ion concentration

Inferred from electronic annotation. Source: Ensembl

negative regulation of heart contraction

Inferred from electronic annotation. Source: Ensembl

negative regulation of striated muscle contraction

Inferred from electronic annotation. Source: Ensembl

neurotransmitter uptake

Inferred from electronic annotation. Source: Ensembl

potassium ion transport

Non-traceable author statement PubMed 10642400. Source: UniProtKB

regulation of blood pressure

Inferred from electronic annotation. Source: Ensembl

regulation of cardiac muscle cell contraction

Inferred from electronic annotation. Source: Ensembl

regulation of respiratory gaseous exchange by neurological system process

Inferred from electronic annotation. Source: Ensembl

regulation of smooth muscle contraction

Inferred from electronic annotation. Source: Ensembl

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: Ensembl

regulation of vasoconstriction

Inferred from electronic annotation. Source: Ensembl

response to nicotine

Inferred from electronic annotation. Source: Ensembl

sodium ion transmembrane transport

Inferred from mutant phenotype Ref.12. Source: GOC

sodium ion transport

Non-traceable author statement PubMed 10642400. Source: UniProtKB

transmembrane transport

Traceable author statement. Source: Reactome

visual learning

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentT-tubule

Inferred from electronic annotation. Source: Ensembl

caveola

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from direct assay Ref.12. Source: UniProtKB

dendritic spine

Inferred from electronic annotation. Source: Ensembl

endosome

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Inferred from direct assay Ref.12. Source: UniProtKB

sodium:potassium-exchanging ATPase complex

Inferred by curator Ref.12. Source: UniProtKB

synapse

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionATP 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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide1 – 55 By similarity
PRO_0000002503
Chain6 – 10201015Sodium/potassium-transporting ATPase subunit alpha-2
PRO_0000002504

Regions

Topological domain6 – 8580Cytoplasmic Potential
Transmembrane86 – 10621Helical; Potential
Topological domain107 – 12923Extracellular Potential
Transmembrane130 – 15021Helical; Potential
Topological domain151 – 286136Cytoplasmic Potential
Transmembrane287 – 30620Helical; Potential
Topological domain307 – 31812Extracellular Potential
Transmembrane319 – 33618Helical; Potential
Topological domain337 – 769433Cytoplasmic Potential
Transmembrane770 – 78920Helical; Potential
Topological domain790 – 79910Extracellular Potential
Transmembrane800 – 82021Helical; Potential
Topological domain821 – 84020Cytoplasmic Potential
Transmembrane841 – 86323Helical; Potential
Topological domain864 – 91552Extracellular Potential
Transmembrane916 – 93520Helical; Potential
Topological domain936 – 94813Cytoplasmic Potential
Transmembrane949 – 96719Helical; Potential
Topological domain968 – 98215Extracellular Potential
Transmembrane983 – 100321Helical; Potential
Topological domain1004 – 102017Cytoplasmic Potential
Region80 – 823Interaction with phosphoinositide-3 kinase By similarity

Sites

Active site37414-aspartylphosphate intermediate By similarity
Metal binding7141Magnesium By similarity
Metal binding7181Magnesium By similarity

Amino acid modifications

Modified residue5701Phosphothreonine Ref.10
Modified residue5871Phosphoserine Ref.10
Modified residue9401Phosphoserine; by PKA By similarity

Natural variations

Natural variant3781T → N in AHC1. Ref.13
Corresponds to variant rs28934002 [ dbSNP | Ensembl ].
VAR_019934
Natural variant6891R → Q in FHM2. Ref.11
Corresponds to variant rs28933401 [ dbSNP | Ensembl ].
VAR_019935
Natural variant7151G → R in FHM2; de novo mutation in a sporadic case. Ref.14
VAR_065685
Natural variant7311M → T in FHM2. Ref.11
Corresponds to variant rs28933400 [ dbSNP | Ensembl ].
VAR_019936
Natural variant7641L → P in FHM2; loss of function. Ref.12
Corresponds to variant rs28933398 [ dbSNP | Ensembl ].
VAR_019937
Natural variant8741G → S in FHM2; some patients exhibit a clinical overlap between migraine and epilepsy. Ref.16
VAR_069991
Natural variant8871W → R in FHM2; loss of function. Ref.12
Corresponds to variant rs28933399 [ dbSNP | Ensembl ].
VAR_019938
Natural variant10071R → W in FHM2; some patients exhibit a clinical overlap between migraine and epilepsy. Ref.15
VAR_069992

Sequences

Sequence LengthMass (Da)Tools
P50993 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: AFBD8EA94FFB4FC3

FASTA1,020112,265
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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.
[15]"Functional characterization of a novel C-terminal ATP1A2 mutation causing hemiplegic migraine and epilepsy."
Pisano T., Spiller S., Mei D., Guerrini R., Cianchetti C., Friedrich T., Pruna D.
Cephalalgia 33:1302-1310(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FHM2 TRP-1007.
[16]"A novel ATP1A2 gene mutation in familial hemiplegic migraine and epilepsy."
Costa C., Prontera P., Sarchielli P., Tonelli A., Bassi M.T., Cupini L.M., Caproni S., Siliquini S., Donti E., Calabresi P.
Cephalalgia 34:68-72(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FHM2 SER-874.
+Additional computationally mapped references.

Web resources

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.
PIRA34474.
RefSeqNP_000693.1. NM_000702.3.
UniGeneHs.34114.

3D structure databases

ProteinModelPortalP50993.
SMRP50993. Positions 28-1020.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106967. 6 interactions.
IntActP50993. 1 interaction.
STRING9606.ENSP00000354490.

Chemistry

BindingDBP50993.
ChEMBLCHEMBL2095186.

Protein family/group databases

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

PTM databases

PhosphoSiteP50993.

Polymorphism databases

DMDM1703467.

Proteomic databases

PaxDbP50993.
PRIDEP50993.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000361216; ENSP00000354490; ENSG00000018625.
GeneID477.
KEGGhsa:477.
UCSCuc001fvb.2. human.

Organism-specific databases

CTD477.
GeneCardsGC01P160085.
HGNCHGNC:800. ATP1A2.
HPACAB022230.
MIM104290. phenotype.
182340. gene.
602481. phenotype.
neXtProtNX_P50993.
Orphanet2131. Alternating hemiplegia of childhood.
569. Familial or sporadic hemiplegic migraine.
PharmGKBPA30796.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0474.
HOGENOMHOG000265622.
HOVERGENHBG004298.
InParanoidP50993.
KOK01539.
OMAIINIPLP.
OrthoDBEOG7327N0.
PhylomeDBP50993.
TreeFamTF312838.

Enzyme and pathway databases

ReactomeREACT_15518. Transmembrane transport of small molecules.

Gene expression databases

ArrayExpressP50993.
BgeeP50993.
CleanExHS_ATP1A2.
GenevestigatorP50993.

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. 2 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

ChiTaRSATP1A2. human.
GeneWikiATP1A2.
GenomeRNAi477.
NextBio1977.
PROP50993.
SOURCESearch...

Entry information

Entry nameAT1A2_HUMAN
AccessionPrimary (citable) accession number: P50993
Secondary accession number(s): D3DVE4 expand/collapse secondary AC list , Q07059, Q5JW74, Q86UZ5, Q9UQ25
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: April 16, 2014
This is version 147 of the entry and version 1 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 1

Human chromosome 1: entries, gene names and cross-references to MIM