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Q16720 (AT2B3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 141. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Plasma membrane calcium-transporting ATPase 3

Short name=PMCA3
EC=3.6.3.8
Alternative name(s):
Plasma membrane calcium ATPase isoform 3
Plasma membrane calcium pump isoform 3
Gene names
Name:ATP2B3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1220 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of calcium out of the cell.

Catalytic activity

ATP + H2O + Ca2+(Side 1) = ADP + phosphate + Ca2+(Side 2).

Subunit structure

Interacts with PDZD11. Ref.8

Subcellular location

Cell membrane; Multi-pass membrane protein.

Tissue specificity

Highly expressed in the cerebellum, particulary in the presynaptic terminals of parallel fibers-Purkinje neurons. Isoform XE and isoform XB are the most abundant isoforms and are detected at low levels in brain and fetal skeletal muscle. The other isoforms are only found at lower levels and not in fetal tissues. Ref.9

Involvement in disease

Spinocerebellar ataxia, X-linked 1 (SCAX1) [MIM:302500]: Spinocerebellar ataxia is a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to degeneration of the cerebellum with variable involvement of the brainstem and spinal cord. SCAX1 is characterized by hypotonia at birth, delayed motor development, gait ataxia, difficulty standing, dysarthria, and slow eye movements. Brain MRI shows cerebellar ataxia.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.9

Sequence similarities

Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IIB subfamily. [View classification]

Alternative products

This entry describes 8 isoforms produced by alternative splicing. [Align] [Select]

Note: There is a combination of two alternatively spliced domains at N-terminal site A (X and Z) and at C-terminal site C (A, B, E and G). The splice sites have mostly been studied independently. Full isoforms so far detected are isoform XA and isoform XB. Experimental confirmation may be lacking for some isoforms.
Isoform XB (identifier: Q16720-1)

Also known as: AIICI;

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.
Isoform XA (identifier: Q16720-2)

Also known as: AIICII;

The sequence of this isoform differs from the canonical sequence as follows:
     1115-1220: IRVVKAFRSS...SPLHSVETSL → MEVVSTFKRS...AGNPGGESVP
Isoform ZA (identifier: Q16720-3)

Also known as: AICII;

The sequence of this isoform differs from the canonical sequence as follows:
     306-319: Missing.
     1115-1220: IRVVKAFRSS...SPLHSVETSL → MEVVSTFKRS...AGNPGGESVP
Isoform ZB (identifier: Q16720-4)

Also known as: AICI;

The sequence of this isoform differs from the canonical sequence as follows:
     306-319: Missing.
Isoform XE (identifier: Q16720-5)

Also known as: AIICV;

The sequence of this isoform differs from the canonical sequence as follows:
     1115-1220: IRVVKAFRSS...SPLHSVETSL → MEVVSTFKRS...NPTSAAGSES
Isoform ZE (identifier: Q16720-6)

Also known as: AICV;

The sequence of this isoform differs from the canonical sequence as follows:
     306-319: Missing.
     1115-1220: IRVVKAFRSS...SPLHSVETSL → MEVVSTFKRS...NPTSAAGSES
Isoform XG (identifier: Q16720-7)

Also known as: AIICVII;

The sequence of this isoform differs from the canonical sequence as follows:
     1115-1220: IRVVKAFRSS...SPLHSVETSL → VCWDGKKMLRTTEVG
Isoform ZG (identifier: Q16720-8)

Also known as: AICVII;

The sequence of this isoform differs from the canonical sequence as follows:
     306-319: Missing.
     1115-1220: IRVVKAFRSS...SPLHSVETSL → VCWDGKKMLRTTEVG

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12201220Plasma membrane calcium-transporting ATPase 3
PRO_0000046218

Regions

Topological domain1 – 9797Cytoplasmic Potential
Transmembrane98 – 11821Helical; Potential
Topological domain119 – 15537Extracellular Potential
Transmembrane156 – 17621Helical; Potential
Topological domain177 – 364188Cytoplasmic Potential
Transmembrane365 – 38420Helical; Potential
Topological domain385 – 41733Extracellular Potential
Transmembrane418 – 43518Helical; Potential
Topological domain436 – 849414Cytoplasmic Potential
Transmembrane850 – 86920Helical; Potential
Topological domain870 – 87910Extracellular Potential
Transmembrane880 – 90021Helical; Potential
Topological domain901 – 92020Cytoplasmic Potential
Transmembrane921 – 94323Helical; Potential
Topological domain944 – 96118Extracellular Potential
Transmembrane962 – 98322Helical; Potential
Topological domain984 – 100219Cytoplasmic Potential
Transmembrane1003 – 102422Helical; Potential
Topological domain1025 – 103410Extracellular Potential
Transmembrane1035 – 105622Helical; Potential
Topological domain1057 – 1220164Cytoplasmic Potential
Region1097 – 111418Calmodulin-binding subdomain A By similarity
Region1115 – 112410Calmodulin-binding subdomain B By similarity
Compositional bias297 – 3004Poly-Glu
Compositional bias1174 – 11796Poly-Pro

Sites

Active site47314-aspartylphosphate intermediate By similarity
Metal binding7941Magnesium By similarity
Metal binding7981Magnesium By similarity

Amino acid modifications

Modified residue11131Phosphothreonine; by PKC By similarity

Natural variations

Alternative sequence306 – 31914Missing in isoform ZA, isoform ZB, isoform ZE and isoform ZG.
VSP_000392
Alternative sequence1115 – 1220106IRVVK…VETSL → MEVVSTFKRSGSVQGAVRRR SSVLSQLHDVTNLSTPTHAI LSAANPTSAAGNPGGESVP in isoform XA and isoform ZA.
VSP_000393
Alternative sequence1115 – 1220106IRVVK…VETSL → MEVVSTFKRSGSVQGAVRRR SSVLSQLHDVTNLSTPTHAI LSAANPTSAAGSES in isoform XE and isoform ZE.
VSP_000394
Alternative sequence1115 – 1220106IRVVK…VETSL → VCWDGKKMLRTTEVG in isoform XG and isoform ZG.
VSP_000395
Natural variant1981I → M.
Corresponds to variant rs2269409 [ dbSNP | Ensembl ].
VAR_027928
Natural variant11071G → D in SCAX1; the mutant protein is expressed at the plasma membrane but shows impaired extrusion of intracellular calcium with prolonged retention of cytoplasmic calcium compared to wild-type under physiologic conditions. Ref.9
VAR_069308

Experimental info

Sequence conflict5871I → V in AAB09762. Ref.1
Sequence conflict5871I → V in AAB38530. Ref.1
Sequence conflict6541S → Y in AAB09762. Ref.1
Sequence conflict6541S → Y in AAB38530. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform XB (AIICI) [UniParc].

Last modified October 17, 2006. Version 3.
Checksum: 03B2BA8A0A33B193

FASTA1,220134,197
        10         20         30         40         50         60 
MGDMANSSIE FHPKPQQQRD VPQAGGFGCT LAELRTLMEL RGAEALQKIE EAYGDVSGLC 

        70         80         90        100        110        120 
RRLKTSPTEG LADNTNDLEK RRQIYGQNFI PPKQPKTFLQ LVWEALQDVT LIILEVAAIV 

       130        140        150        160        170        180 
SLGLSFYAPP GEESEACGNV SGGAEDEGEA EAGWIEGAAI LLSVICVVLV TAFNDWSKEK 

       190        200        210        220        230        240 
QFRGLQSRIE QEQKFTVIRN GQLLQVPVAA LVVGDIAQVK YGDLLPADGV LIQANDLKID 

       250        260        270        280        290        300 
ESSLTGESDH VRKSADKDPM LLSGTHVMEG SGRMVVTAVG VNSQTGIIFT LLGAGGEEEE 

       310        320        330        340        350        360 
KKDKKGKQQD GAMESSQTKA KKQDGAVAME MQPLKSAEGG EMEEREKKKA NAPKKEKSVL 

       370        380        390        400        410        420 
QGKLTKLAVQ IGKAGLVMSA ITVIILVLYF VIETFVVEGR TWLAECTPVY VQYFVKFFII 

       430        440        450        460        470        480 
GVTVLVVAVP EGLPLAVTIS LAYSVKKMMK DNNLVRHLDA CETMGNATAI CSDKTGTLTT 

       490        500        510        520        530        540 
NRMTVVQSYL GDTHYKEIPA PSALTPKILD LLVHAISINS AYTTKILPPE KEGALPRQVG 

       550        560        570        580        590        600 
NKTECALLGF VLDLKRDFQP VREQIPEDKL YKVYTFNSVR KSMSTVIRMP DGGFRLFSKG 

       610        620        630        640        650        660 
ASEILLKKCT NILNSNGELR GFRPRDRDDM VRKIIEPMAC DGLRTICIAY RDFSAGQEPD 

       670        680        690        700        710        720 
WDNENEVVGD LTCIAVVGIE DPVRPEVPEA IRKCQRAGIT VRMVTGDNIN TARAIAAKCG 

       730        740        750        760        770        780 
IIQPGEDFLC LEGKEFNRRI RNEKGEIEQE RLDKVWPKLR VLARSSPTDK HTLVKGIIDS 

       790        800        810        820        830        840 
TTGEQRQVVA VTGDGTNDGP ALKKADVGFA MGIAGTDVAK EASDIILTDD NFTSIVKAVM 

       850        860        870        880        890        900 
WGRNVYDSIS KFLQFQLTVN VVAVIVAFTG ACITQDSPLK AVQMLWVNLI MDTFASLALA 

       910        920        930        940        950        960 
TEPPTESLLL RKPYGRDKPL ISRTMMKNIL GHAVYQLAII FTLLFVGELF FDIDSGRNAP 

       970        980        990       1000       1010       1020 
LHSPPSEHYT IIFNTFVMMQ LFNEINARKI HGERNVFDGI FSNPIFCTIV LGTFGIQIVI 

      1030       1040       1050       1060       1070       1080 
VQFGGKPFSC SPLSTEQWLW CLFVGVGELV WGQVIATIPT SQLKCLKEAG HGPGKDEMTD 

      1090       1100       1110       1120       1130       1140 
EELAEGEEEI DHAERELRRG QILWFRGLNR IQTQIRVVKA FRSSLYEGLE KPESKTSIHN 

      1150       1160       1170       1180       1190       1200 
FMATPEFLIN DYTHNIPLID DTDVDENEER LRAPPPPSPN QNNNAIDSGI YLTTHVTKSA 

      1210       1220 
TSSVFSSSPG SPLHSVETSL 

« Hide

Isoform XA (AIICII) [UniParc].

Checksum: EF3ACDF02DF40B8C
Show »

FASTA1,173128,545
Isoform ZA (AICII) [UniParc].

Checksum: D092487DFC13E8A3
Show »

FASTA1,159127,068
Isoform ZB (AICI) [UniParc].

Checksum: 2366490D5E398C08
Show »

FASTA1,206132,721
Isoform XE (AIICV) [UniParc].

Checksum: 79D7ED01B8F1BA88
Show »

FASTA1,168128,110
Isoform ZE (AICV) [UniParc].

Checksum: 6E34C22E92BEAE95
Show »

FASTA1,154126,634
Isoform XG (AIICVII) [UniParc].

Checksum: 17805052F1230AEF
Show »

FASTA1,129124,236
Isoform ZG (AICVII) [UniParc].

Checksum: 46F7F01999CFA318
Show »

FASTA1,115122,760

References

« Hide 'large scale' references
[1]"Primary structure of human plasma membrane Ca(2+)-ATPase isoform 3."
Brown B., Hilfiker H., Demarco S.J., Zacharias D.A., Greenwood T.M., Carafoli E., Strehler E.E.
Biochim. Biophys. Acta 1283:10-13(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS XA AND XB).
Tissue: Brain.
[2]"The DNA sequence of the human X chromosome."
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. expand/collapse author list , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]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].
[4]"Localization of two genes encoding plasma membrane Ca2+ ATPases isoforms 2 (ATP2B2) and 3 (ATP2B3) to human chromosomes 3p26-->p25 and Xq28, respectively."
Wang M.G., Yi H., Hilfiker H., Carafoli E., Strehler E.E., McBride O.W.
Cytogenet. Cell Genet. 67:41-45(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-319, ALTERNATIVE SPLICING (ISOFORMS XB/XA/XE/XG).
[5]"Comparative genome sequence analysis of the Bpa/Str region in mouse and man."
Mallon A.-M., Platzer M., Bate R., Gloeckner G., Botcherby M.R.M., Nordsiek G., Strivens M.A., Kioschis P., Dangel A., Cunningham D., Straw R.N.A., Weston P., Gilbert M., Fernando S., Goodall K., Hunter G., Greystrong J.S., Clarke D. expand/collapse author list , Kimberley C., Goerdes M., Blechschmidt K., Rump A., Hinzmann B., Mundy C.R., Miller W., Poustka A., Herman G.E., Rhodes M., Denny P., Rosenthal A., Brown S.D.M.
Genome Res. 10:758-775(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-1053, ALTERNATIVE SPLICING (ISOFORMS XB/XA/XE/XG).
[6]"Quantitative analysis of alternative splicing options of human plasma membrane calcium pump genes."
Stauffer T.P., Hilfiker H., Carafoli E., Strehler E.E.
J. Biol. Chem. 268:25993-26003(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS XG/ZG AND XA/ZA), ALTERNATIVE SPLICING.
Tissue: Brain cortex.
[7]Erratum
Stauffer T.P., Hilfiker H., Carafoli E., Strehler E.E.
J. Biol. Chem. 269:32022-32022(1994) [PubMed] [Europe PMC] [Abstract]
[8]"Characterization of PISP, a novel single-PDZ protein that binds to all plasma membrane Ca2+-ATPase b-splice variants."
Goellner G.M., DeMarco S.J., Strehler E.E.
Ann. N. Y. Acad. Sci. 986:461-471(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PDZD11.
[9]"Mutation of plasma membrane Ca2+ ATPase isoform 3 in a family with X-linked congenital cerebellar ataxia impairs Ca2+ homeostasis."
Zanni G., Cali T., Kalscheuer V.M., Ottolini D., Barresi S., Lebrun N., Montecchi-Palazzi L., Hu H., Chelly J., Bertini E., Brini M., Carafoli E.
Proc. Natl. Acad. Sci. U.S.A. 109:14514-14519(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, VARIANT SCAX1 ASP-1107, CHARACTERIZATION OF VARIANT SCAX1 ASP-1107.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U57971 mRNA. Translation: AAB09762.1.
U60414 mRNA. Translation: AAB38530.1.
AH006061 Genomic DNA. Translation: AAC15078.1.
CH471172 Genomic DNA. Translation: EAW72859.1.
U82695 Genomic DNA. No translation available.
U15689 mRNA. Translation: AAA60986.1.
U15690 mRNA. Translation: AAA60987.1.
CCDSCCDS14722.1. [Q16720-2]
CCDS35440.1. [Q16720-1]
RefSeqNP_001001344.1. NM_001001344.2. [Q16720-1]
NP_068768.2. NM_021949.3. [Q16720-2]
XP_005274747.1. XM_005274690.1. [Q16720-1]
XP_005274748.1. XM_005274691.1. [Q16720-4]
XP_005274749.1. XM_005274692.1. [Q16720-2]
XP_005274750.1. XM_005274693.1. [Q16720-3]
UniGeneHs.533956.
Hs.658008.

3D structure databases

ProteinModelPortalQ16720.
SMRQ16720. Positions 66-943, 1097-1124.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106982. 3 interactions.
IntActQ16720. 1 interaction.
MINTMINT-2807671.
STRING9606.ENSP00000263519.

PTM databases

PhosphoSiteQ16720.

Polymorphism databases

DMDM116241261.

Proteomic databases

MaxQBQ16720.
PaxDbQ16720.
PRIDEQ16720.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000263519; ENSP00000263519; ENSG00000067842. [Q16720-1]
ENST00000349466; ENSP00000343886; ENSG00000067842. [Q16720-1]
ENST00000359149; ENSP00000352062; ENSG00000067842. [Q16720-2]
ENST00000370181; ENSP00000359200; ENSG00000067842. [Q16720-3]
ENST00000370186; ENSP00000359205; ENSG00000067842. [Q16720-3]
ENST00000393842; ENSP00000377425; ENSG00000067842. [Q16720-6]
ENST00000571862; ENSP00000460932; ENSG00000263148. [Q16720-6]
ENST00000571969; ENSP00000461370; ENSG00000263148. [Q16720-1]
ENST00000572057; ENSP00000458650; ENSG00000263148. [Q16720-2]
ENST00000575463; ENSP00000460886; ENSG00000263148. [Q16720-3]
ENST00000601388; ENSP00000471537; ENSG00000263148. [Q16720-3]
ENST00000602058; ENSP00000468854; ENSG00000263148. [Q16720-1]
GeneID492.
KEGGhsa:492.
UCSCuc004fhs.1. human. [Q16720-2]
uc004fht.1. human. [Q16720-1]

Organism-specific databases

CTD492.
GeneCardsGC0XP152783.
H-InvDBHIX0017131.
HGNCHGNC:816. ATP2B3.
HPACAB005607.
HPA001583.
MIM300014. gene.
302500. phenotype.
neXtProtNX_Q16720.
Orphanet85142. Aldosterone-producing adenoma.
314978. X-linked non progressive cerebellar ataxia.
PharmGKBPA25109.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0474.
HOGENOMHOG000265623.
HOVERGENHBG061286.
InParanoidQ16720.
KOK05850.
OMAMGDVANS.
OrthoDBEOG7SN8BN.
PhylomeDBQ16720.
TreeFamTF300330.

Enzyme and pathway databases

ReactomeREACT_15518. Transmembrane transport of small molecules.
REACT_604. Hemostasis.

Gene expression databases

ArrayExpressQ16720.
BgeeQ16720.
CleanExHS_ATP2B3.
GenevestigatorQ16720.

Family and domain databases

Gene3D1.20.1110.10. 3 hits.
InterProIPR022141. ATP_Ca_trans_C.
IPR006408. ATPase_P-typ_Ca-transp_plasma.
IPR006068. ATPase_P-typ_cation-transptr_C.
IPR004014. ATPase_P-typ_cation-transptr_N.
IPR023299. ATPase_P-typ_cyto_domN.
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]
PfamPF12424. ATP_Ca_trans_C. 1 hit.
PF00689. 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.
TIGRFAMsTIGR01517. ATPase-IIB_Ca. 1 hit.
TIGR01494. ATPase_P-type. 3 hits.
PROSITEPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]
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Other

GeneWikiATP2B3.
GenomeRNAi492.
NextBio2065.
PROQ16720.
SOURCESearch...

Entry information

Entry nameAT2B3_HUMAN
AccessionPrimary (citable) accession number: Q16720
Secondary accession number(s): B7WNR8 expand/collapse secondary AC list , B7WNY5, Q12995, Q16858
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: October 17, 2006
Last modified: July 9, 2014
This is version 141 of the entry and version 3 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 X

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