ATP2B2
entrez
491
canonical
uniprot
Q01814
canonical
ensembl
ENSG00000157087
resolver
ensp
ENSP00000324172
resolver
ensp
ENSP00000353414
resolver
ensp
ENSP00000380267
resolver
ensp
ENSP00000414854
resolver
ensp
ENSP00000492732
resolver
ensp
ENSP00000494381
resolver
ensp
ENSP00000494716
resolver
ensp
ENSP00000495228
resolver
enst
ENST00000638646
resolver
genesymbol
ATP2B2
resolver
genesymbol_syn
PMCA2
resolver
hgnc
HGNC:815
resolver
uniprot
A0A2U3U055
resolver
uniprot
O00766
resolver
uniprot
Q12994
resolver
uniprot
Q16818
resolver
uniprot_entry
A0A2U3U055_HUMAN
resolver
uniprot_entry
AT2B2_HUMAN
resolver
uniprot_sec
O00766
resolver
uniprot_sec
Q12994
resolver
uniprot_sec
Q16818
resolver
activity_regulation
ACTIVITY REGULATION: Up-regulated by calmodulin which increases the affinity of the pump for Ca(2+) ions (PubMed:15829536). Regulated by phospholipids such as phosphatidylinositol 4,5-bisphosphate; this interaction is essential for optimal activity (By similarity). {ECO:0000250|UniProtKB:Q9R0K7, ECO:0000269|PubMed:15829536}.
uniprot
proteins
amino_acid_sequence
MGDMTNSDFYSKNQRNESSHGGEFGCTMEELRSLMELRGTEAVVKIKETYGDTEAICRRLKTSPVEGLPGTAPDLEKRKQIFGQNFIPPKKPKTFLQLVWEALQDVTLIILEIAAIISLGLSFYHPPGEGNEGCATAQGGAEDEGEAEAGWIEGAAILLSVICVVLVTAFNDWSKEKQFRGLQSRIEQEQKFTVVRAGQVVQIPVAEIVVGDIAQVKYGDLLPADGLFIQGNDLKIDESSLTGESDQVRKSVDKDPMLLSGTHVMEGSGRMLVTAVGVNSQTGIIFTLLGAGGEEEEKKDKKGVKKGDGLQLPAADGAAASNAADSANASLVNGKMQDGNVDASQSKAKQQDGAAAMEMQPLKSAEGGDADDRKKASMHKKEKSVLQGKLTKLAVQIGKAGLVMSAITVIILVLYFTVDTFVVNKKPWLPECTPVYVQYFVKFFIIGVTVLVVAVPEGLPLAVTISLAYSVKKMMKDNNLVRHLDACETMGNATAICSDKTGTLTTNRMTVVQAYVGDVHYKEIPDPSSINTKTMELLINAIAINSAYTTKILPPEKEGALPRQVGNKTECGLLGFVLDLKQDYEPVRSQMPEEKLYKVYTFNSVRKSMSTVIKLPDESFRMYSKGASEIVLKKCCKILNGAGEPRVFRPRDRDEMVKKVIEPMACDGLRTICVAYRDFPSSPEPDWDNENDILNELTCICVVGIEDPVRPEVPEAIRKCQRAGITVRMVTGDNINTARAIAIKCGIIHPGEDFLCLEGKEFNRRIRNEKGEIEQERIDKIWPKLRVLARSSPTDKHTLVKGIIDSTHTEQRQVVAVTGDGTNDGPALKKADVGFAMGIAGTDVAKEASDIILTDDNFSSIVKAVMWGRNVYDSISKFLQFQLTVNVVAVIVAFTGACITQDSPLKAVQMLWVNLIMDTFASLALATEPPTETLLLRKPYGRNKPLISRTMMKNILGHAVYQLALIFTLLFVGEKMFQIDSGRNAPLHSPPSEHYTIIFNTFVMMQLFNEINARKIHGERNVFDGIFRNPIFCTIVLGTFAIQIVIVQFGGKPFSCSPLQLDQWMWCIFIGLGELVWGQVIATIPTSRLKFLKEAGRLTQKEEIPEEELNEDVEEIDHAERELRRGQILWFRGLNRIQTQIRVVKAFRSSLYEGLEKPESRTSIHNFMAHPEFRIEDSQPHIPLIDDTDLEEDAALKQNSSPPSSLNKNNSAIDSGINLTTDTSKSATSSSPGSPIHSLETSL
uniprot
proteins
disease_involvement
DISEASE: Note=May act as a disease modifier. ATP2B2 variants may exacerbate the severity of non-syndromic sensorineural hearing loss in patients carrying causative variants in the CDH23 gene. Sensorineural deafness results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information. {ECO:0000269|PubMed:15829536, ECO:0000269|PubMed:17234811}.; DISEASE: Deafness, autosomal dominant, 82 (DFNA82) [MIM:619804]: A form of non-syndromic, sensorineural hearing loss. Sensorineural hearing loss results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information. DNFA82 is characterized by onset of rapidly progressive bilateral sensorineural hearing loss usually early in the first decade. {ECO:0000269|PubMed:30535804}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
7.2.2.10
uniprot
proteins
function
FUNCTION: ATP-driven Ca(2+) ion pump involved in the maintenance of basal intracellular Ca(2+) levels in specialized cells of cerebellar circuit and vestibular and cochlear systems (PubMed:15829536, PubMed:17234811). Uses ATP as an energy source to transport cytosolic Ca(2+) ions across the plasma membrane to the extracellular compartment (PubMed:15829536, PubMed:17234811). Has fast activation and Ca(2+) clearance rate suited to control fast neuronal Ca(2+) dynamics. At parallel fiber to Purkinje neuron synapse, mediates presynaptic Ca(2+) efflux in response to climbing fiber-induced Ca(2+) rise. Provides for fast return of Ca(2+) concentrations back to their resting levels, ultimately contributing to long-term depression induction and motor learning (By similarity). Plays an essential role in hearing and balance (PubMed:15829536, PubMed:17234811). In cochlear hair cells, shuttles Ca(2+) ions from stereocilia to the endolymph and dissipates Ca(2+) transients generated by the opening of the mechanoelectrical transduction channels. Regulates Ca(2+) levels in the vestibular system, where it contributes to the formation of otoconia (PubMed:15829536, PubMed:17234811). In non-excitable cells, regulates Ca(2+) signaling through spatial control of Ca(2+) ions extrusion and dissipation of Ca(2+) transients generated by store-operated channels (PubMed:25690014). In lactating mammary gland, allows for the high content of Ca(2+) ions in the milk (By similarity). {ECO:0000250|UniProtKB:Q9R0K7, ECO:0000269|PubMed:15829536, ECO:0000269|PubMed:17234811, ECO:0000269|PubMed:25690014}.
uniprot
proteins
mass_dalton
136876
uniprot
proteins
protein_family
Cation transport ATPase (P-type) (TC 3.A.3) family
uniprot
proteins
protein_family
Type IIB subfamily
uniprot
proteins
pubmed
12624087
uniprot
proteins
pubmed
12763866
uniprot
proteins
pubmed
1313367
uniprot
proteins
pubmed
1427863
uniprot
proteins
pubmed
15829536
uniprot
proteins
pubmed
16641997
uniprot
proteins
pubmed
17234811
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25690014
uniprot
proteins
pubmed
30535804
uniprot
proteins
pubmed
7989379
uniprot
proteins
pubmed
8245032
uniprot
proteins
pubmed
8428366
uniprot
proteins
sequence_length
1243
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17234811}; Multi-pass membrane protein {ECO:0000255}. Synapse {ECO:0000250|UniProtKB:Q9R0K7}.; SUBCELLULAR LOCATION: [Isoform WA]: Apical cell membrane {ECO:0000269|PubMed:12624087}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9R0K7}. Basolateral cell membrane {ECO:0000269|PubMed:12624087}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9R0K7}.; SUBCELLULAR LOCATION: [Isoform WB]: Apical cell membrane {ECO:0000269|PubMed:12624087}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9R0K7}. Basolateral cell membrane {ECO:0000269|PubMed:12624087}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9R0K7}.; SUBCELLULAR LOCATION: [Isoform XB]: Basolateral cell membrane {ECO:0000269|PubMed:12624087}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9R0K7}.; SUBCELLULAR LOCATION: [Isoform ZA]: Basolateral cell membrane {ECO:0000269|PubMed:12624087}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9R0K7}.; SUBCELLULAR LOCATION: [Isoform ZB]: Basolateral cell membrane {ECO:0000269|PubMed:12624087}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9R0K7}.
uniprot
proteins
transmembrane_region
TRANSMEM 95..115; /note="Helical; Name=1"; /evidence="ECO:0000250|UniProtKB:Q9R0K7"; TRANSMEM 153..173; /note="Helical; Name=2"; /evidence="ECO:0000250|UniProtKB:Q9R0K7"; TRANSMEM 391..410; /note="Helical; Name=3"; /evidence="ECO:0000250|UniProtKB:Q9R0K7"; TRANSMEM 444..461; /note="Helical; Name=4"; /evidence="ECO:0000250|UniProtKB:Q9R0K7"; TRANSMEM 876..895; /note="Helical; Name=5"; /evidence="ECO:0000250|UniProtKB:Q9R0K7"; TRANSMEM 906..926; /note="Helical; Name=6"; /evidence="ECO:0000250|UniProtKB:Q9R0K7"; TRANSMEM 947..969; /note="Helical; Name=7"; /evidence="ECO:0000250|UniProtKB:Q9R0K7"; TRANSMEM 988..1009; /note="Helical; Name=8"; /evidence="ECO:0000250|UniProtKB:Q9R0K7"; TRANSMEM 1029..1050; /note="Helical; Name=9"; /evidence="ECO:0000250|UniProtKB:Q9R0K7"; TRANSMEM 1061..1082; /note="Helical; Name=10"; /evidence="ECO:0000250|UniProtKB:Q9R0K7
uniprot
proteins