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Q16720

- AT2B3_HUMAN

UniProt

Q16720 - AT2B3_HUMAN

Protein

Plasma membrane calcium-transporting ATPase 3

Gene

ATP2B3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 143 (01 Oct 2014)
      Sequence version 3 (17 Oct 2006)
      Previous versions | rss
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    Functioni

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

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei473 – 47314-aspartylphosphate intermediateBy similarity
    Metal bindingi794 – 7941MagnesiumBy similarity
    Metal bindingi798 – 7981MagnesiumBy similarity

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. calcium-transporting ATPase activity Source: ProtInc
    3. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. blood coagulation Source: Reactome
    2. cell death Source: UniProtKB-KW
    3. ion transmembrane transport Source: Reactome
    4. transmembrane transport Source: Reactome
    5. transport Source: ProtInc

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Calcium transport, Ion transport, Transport

    Keywords - Ligandi

    ATP-binding, Calcium, Calmodulin-binding, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_23765. Reduction of cytosolic Ca++ levels.
    REACT_25149. Ion transport by P-type ATPases.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Plasma membrane calcium-transporting ATPase 3 (EC:3.6.3.8)
    Short name:
    PMCA3
    Alternative name(s):
    Plasma membrane calcium ATPase isoform 3
    Plasma membrane calcium pump isoform 3
    Gene namesi
    Name:ATP2B3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:816. ATP2B3.

    Subcellular locationi

    GO - Cellular componenti

    1. Golgi apparatus Source: HPA
    2. integral component of membrane Source: UniProtKB-KW
    3. plasma membrane Source: HPA

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti1107 – 11071G → 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. 1 Publication
    VAR_069308

    Keywords - Diseasei

    Disease mutation, Neurodegeneration

    Organism-specific databases

    MIMi302500. phenotype.
    Orphaneti85142. Aldosterone-producing adenoma.
    314978. X-linked non progressive cerebellar ataxia.
    PharmGKBiPA25109.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 12201220Plasma membrane calcium-transporting ATPase 3PRO_0000046218Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1113 – 11131Phosphothreonine; by PKCBy similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ16720.
    PaxDbiQ16720.
    PRIDEiQ16720.

    PTM databases

    PhosphoSiteiQ16720.

    Expressioni

    Tissue specificityi

    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.1 Publication

    Gene expression databases

    ArrayExpressiQ16720.
    BgeeiQ16720.
    CleanExiHS_ATP2B3.
    GenevestigatoriQ16720.

    Organism-specific databases

    HPAiCAB005607.
    HPA001583.

    Interactioni

    Subunit structurei

    Interacts with PDZD11.1 Publication

    Protein-protein interaction databases

    BioGridi106982. 4 interactions.
    IntActiQ16720. 1 interaction.
    MINTiMINT-2807671.
    STRINGi9606.ENSP00000263519.

    Structurei

    3D structure databases

    ProteinModelPortaliQ16720.
    SMRiQ16720. Positions 66-943, 1097-1124.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 9797CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini119 – 15537ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini177 – 364188CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini385 – 41733ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini436 – 849414CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini870 – 87910ExtracellularSequence Analysis
    Topological domaini901 – 92020CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini944 – 96118ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini984 – 100219CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini1025 – 103410ExtracellularSequence Analysis
    Topological domaini1057 – 1220164CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei98 – 11821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei156 – 17621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei365 – 38420HelicalSequence AnalysisAdd
    BLAST
    Transmembranei418 – 43518HelicalSequence AnalysisAdd
    BLAST
    Transmembranei850 – 86920HelicalSequence AnalysisAdd
    BLAST
    Transmembranei880 – 90021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei921 – 94323HelicalSequence AnalysisAdd
    BLAST
    Transmembranei962 – 98322HelicalSequence AnalysisAdd
    BLAST
    Transmembranei1003 – 102422HelicalSequence AnalysisAdd
    BLAST
    Transmembranei1035 – 105622HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1097 – 111418Calmodulin-binding subdomain ABy similarityAdd
    BLAST
    Regioni1115 – 112410Calmodulin-binding subdomain BBy similarity

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi297 – 3004Poly-Glu
    Compositional biasi1174 – 11796Poly-Pro

    Sequence similaritiesi

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0474.
    HOGENOMiHOG000265623.
    HOVERGENiHBG061286.
    InParanoidiQ16720.
    KOiK05850.
    OMAiMGDVANS.
    OrthoDBiEOG7SN8BN.
    PhylomeDBiQ16720.
    TreeFamiTF300330.

    Family and domain databases

    Gene3Di1.20.1110.10. 3 hits.
    InterProiIPR022141. 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]
    PfamiPF12424. 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]
    PRINTSiPR00119. CATATPASE.
    SMARTiSM00831. Cation_ATPase_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF56784. SSF56784. 2 hits.
    SSF81660. SSF81660. 1 hit.
    TIGRFAMsiTIGR01517. ATPase-IIB_Ca. 1 hit.
    TIGR01494. ATPase_P-type. 3 hits.
    PROSITEiPS00154. ATPASE_E1_E2. 1 hit.
    [Graphical view]

    Sequences (8)i

    Sequence statusi: Complete.

    This entry describes 8 isoformsi produced by alternative splicing. Align

    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) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MGDMANSSIE FHPKPQQQRD VPQAGGFGCT LAELRTLMEL RGAEALQKIE     50
    EAYGDVSGLC RRLKTSPTEG LADNTNDLEK RRQIYGQNFI PPKQPKTFLQ 100
    LVWEALQDVT LIILEVAAIV SLGLSFYAPP GEESEACGNV SGGAEDEGEA 150
    EAGWIEGAAI LLSVICVVLV TAFNDWSKEK QFRGLQSRIE QEQKFTVIRN 200
    GQLLQVPVAA LVVGDIAQVK YGDLLPADGV LIQANDLKID ESSLTGESDH 250
    VRKSADKDPM LLSGTHVMEG SGRMVVTAVG VNSQTGIIFT LLGAGGEEEE 300
    KKDKKGKQQD GAMESSQTKA KKQDGAVAME MQPLKSAEGG EMEEREKKKA 350
    NAPKKEKSVL QGKLTKLAVQ IGKAGLVMSA ITVIILVLYF VIETFVVEGR 400
    TWLAECTPVY VQYFVKFFII GVTVLVVAVP EGLPLAVTIS LAYSVKKMMK 450
    DNNLVRHLDA CETMGNATAI CSDKTGTLTT NRMTVVQSYL GDTHYKEIPA 500
    PSALTPKILD LLVHAISINS AYTTKILPPE KEGALPRQVG NKTECALLGF 550
    VLDLKRDFQP VREQIPEDKL YKVYTFNSVR KSMSTVIRMP DGGFRLFSKG 600
    ASEILLKKCT NILNSNGELR GFRPRDRDDM VRKIIEPMAC DGLRTICIAY 650
    RDFSAGQEPD WDNENEVVGD LTCIAVVGIE DPVRPEVPEA IRKCQRAGIT 700
    VRMVTGDNIN TARAIAAKCG IIQPGEDFLC LEGKEFNRRI RNEKGEIEQE 750
    RLDKVWPKLR VLARSSPTDK HTLVKGIIDS TTGEQRQVVA VTGDGTNDGP 800
    ALKKADVGFA MGIAGTDVAK EASDIILTDD NFTSIVKAVM WGRNVYDSIS 850
    KFLQFQLTVN VVAVIVAFTG ACITQDSPLK AVQMLWVNLI MDTFASLALA 900
    TEPPTESLLL RKPYGRDKPL ISRTMMKNIL GHAVYQLAII FTLLFVGELF 950
    FDIDSGRNAP LHSPPSEHYT IIFNTFVMMQ LFNEINARKI HGERNVFDGI 1000
    FSNPIFCTIV LGTFGIQIVI VQFGGKPFSC SPLSTEQWLW CLFVGVGELV 1050
    WGQVIATIPT SQLKCLKEAG HGPGKDEMTD EELAEGEEEI DHAERELRRG 1100
    QILWFRGLNR IQTQIRVVKA FRSSLYEGLE KPESKTSIHN FMATPEFLIN 1150
    DYTHNIPLID DTDVDENEER LRAPPPPSPN QNNNAIDSGI YLTTHVTKSA 1200
    TSSVFSSSPG SPLHSVETSL 1220
    Length:1,220
    Mass (Da):134,197
    Last modified:October 17, 2006 - v3
    Checksum:i03B2BA8A0A33B193
    GO
    Isoform XA (identifier: Q16720-2) [UniParc]FASTAAdd to Basket

    Also known as: AIICII

    The sequence of this isoform differs from the canonical sequence as follows:
         1115-1220: IRVVKAFRSS...SPLHSVETSL → MEVVSTFKRS...AGNPGGESVP

    Show »
    Length:1,173
    Mass (Da):128,545
    Checksum:iEF3ACDF02DF40B8C
    GO
    Isoform ZA (identifier: Q16720-3) [UniParc]FASTAAdd to Basket

    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

    Show »
    Length:1,159
    Mass (Da):127,068
    Checksum:iD092487DFC13E8A3
    GO
    Isoform ZB (identifier: Q16720-4) [UniParc]FASTAAdd to Basket

    Also known as: AICI

    The sequence of this isoform differs from the canonical sequence as follows:
         306-319: Missing.

    Show »
    Length:1,206
    Mass (Da):132,721
    Checksum:i2366490D5E398C08
    GO
    Isoform XE (identifier: Q16720-5) [UniParc]FASTAAdd to Basket

    Also known as: AIICV

    The sequence of this isoform differs from the canonical sequence as follows:
         1115-1220: IRVVKAFRSS...SPLHSVETSL → MEVVSTFKRS...NPTSAAGSES

    Show »
    Length:1,168
    Mass (Da):128,110
    Checksum:i79D7ED01B8F1BA88
    GO
    Isoform ZE (identifier: Q16720-6) [UniParc]FASTAAdd to Basket

    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

    Show »
    Length:1,154
    Mass (Da):126,634
    Checksum:i6E34C22E92BEAE95
    GO
    Isoform XG (identifier: Q16720-7) [UniParc]FASTAAdd to Basket

    Also known as: AIICVII

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

    Show »
    Length:1,129
    Mass (Da):124,236
    Checksum:i17805052F1230AEF
    GO
    Isoform ZG (identifier: Q16720-8) [UniParc]FASTAAdd to Basket

    Also known as: AICVII

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

    Show »
    Length:1,115
    Mass (Da):122,760
    Checksum:i46F7F01999CFA318
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti587 – 5871I → V in AAB09762. (PubMed:8765088)Curated
    Sequence conflicti587 – 5871I → V in AAB38530. (PubMed:8765088)Curated
    Sequence conflicti654 – 6541S → Y in AAB09762. (PubMed:8765088)Curated
    Sequence conflicti654 – 6541S → Y in AAB38530. (PubMed:8765088)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti198 – 1981I → M.
    Corresponds to variant rs2269409 [ dbSNP | Ensembl ].
    VAR_027928
    Natural varianti1107 – 11071G → 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. 1 Publication
    VAR_069308

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei306 – 31914Missing in isoform ZA, isoform ZB, isoform ZE and isoform ZG. CuratedVSP_000392Add
    BLAST
    Alternative sequencei1115 – 1220106IRVVK…VETSL → MEVVSTFKRSGSVQGAVRRR SSVLSQLHDVTNLSTPTHAI LSAANPTSAAGNPGGESVP in isoform XA and isoform ZA. 1 PublicationVSP_000393Add
    BLAST
    Alternative sequencei1115 – 1220106IRVVK…VETSL → MEVVSTFKRSGSVQGAVRRR SSVLSQLHDVTNLSTPTHAI LSAANPTSAAGSES in isoform XE and isoform ZE. CuratedVSP_000394Add
    BLAST
    Alternative sequencei1115 – 1220106IRVVK…VETSL → VCWDGKKMLRTTEVG in isoform XG and isoform ZG. CuratedVSP_000395Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS14722.1. [Q16720-2]
    CCDS35440.1. [Q16720-1]
    RefSeqiNP_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]
    UniGeneiHs.533956.
    Hs.658008.

    Genome annotation databases

    EnsembliENST00000263519; ENSP00000263519; ENSG00000067842. [Q16720-1]
    ENST00000349466; ENSP00000343886; ENSG00000067842. [Q16720-1]
    ENST00000359149; ENSP00000352062; ENSG00000067842. [Q16720-2]
    ENST00000370186; ENSP00000359205; ENSG00000067842. [Q16720-3]
    ENST00000393842; ENSP00000377425; ENSG00000067842. [Q16720-6]
    GeneIDi492.
    KEGGihsa:492.
    UCSCiuc004fhs.1. human. [Q16720-2]
    uc004fht.1. human. [Q16720-1]

    Polymorphism databases

    DMDMi116241261.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS14722.1. [Q16720-2 ]
    CCDS35440.1. [Q16720-1 ]
    RefSeqi NP_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 ]
    UniGenei Hs.533956.
    Hs.658008.

    3D structure databases

    ProteinModelPortali Q16720.
    SMRi Q16720. Positions 66-943, 1097-1124.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106982. 4 interactions.
    IntActi Q16720. 1 interaction.
    MINTi MINT-2807671.
    STRINGi 9606.ENSP00000263519.

    PTM databases

    PhosphoSitei Q16720.

    Polymorphism databases

    DMDMi 116241261.

    Proteomic databases

    MaxQBi Q16720.
    PaxDbi Q16720.
    PRIDEi Q16720.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000263519 ; ENSP00000263519 ; ENSG00000067842 . [Q16720-1 ]
    ENST00000349466 ; ENSP00000343886 ; ENSG00000067842 . [Q16720-1 ]
    ENST00000359149 ; ENSP00000352062 ; ENSG00000067842 . [Q16720-2 ]
    ENST00000370186 ; ENSP00000359205 ; ENSG00000067842 . [Q16720-3 ]
    ENST00000393842 ; ENSP00000377425 ; ENSG00000067842 . [Q16720-6 ]
    GeneIDi 492.
    KEGGi hsa:492.
    UCSCi uc004fhs.1. human. [Q16720-2 ]
    uc004fht.1. human. [Q16720-1 ]

    Organism-specific databases

    CTDi 492.
    GeneCardsi GC0XP152783.
    H-InvDB HIX0017131.
    HGNCi HGNC:816. ATP2B3.
    HPAi CAB005607.
    HPA001583.
    MIMi 300014. gene.
    302500. phenotype.
    neXtProti NX_Q16720.
    Orphaneti 85142. Aldosterone-producing adenoma.
    314978. X-linked non progressive cerebellar ataxia.
    PharmGKBi PA25109.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0474.
    HOGENOMi HOG000265623.
    HOVERGENi HBG061286.
    InParanoidi Q16720.
    KOi K05850.
    OMAi MGDVANS.
    OrthoDBi EOG7SN8BN.
    PhylomeDBi Q16720.
    TreeFami TF300330.

    Enzyme and pathway databases

    Reactomei REACT_23765. Reduction of cytosolic Ca++ levels.
    REACT_25149. Ion transport by P-type ATPases.

    Miscellaneous databases

    GeneWikii ATP2B3.
    GenomeRNAii 492.
    NextBioi 2065.
    PROi Q16720.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q16720.
    Bgeei Q16720.
    CleanExi HS_ATP2B3.
    Genevestigatori Q16720.

    Family and domain databases

    Gene3Di 1.20.1110.10. 3 hits.
    InterProi IPR022141. 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 ]
    Pfami PF12424. 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 ]
    PRINTSi PR00119. CATATPASE.
    SMARTi SM00831. Cation_ATPase_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56784. SSF56784. 2 hits.
    SSF81660. SSF81660. 1 hit.
    TIGRFAMsi TIGR01517. ATPase-IIB_Ca. 1 hit.
    TIGR01494. ATPase_P-type. 3 hits.
    PROSITEi PS00154. ATPASE_E1_E2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. 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.
      , 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. 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. 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.

    Entry informationi

    Entry nameiAT2B3_HUMAN
    AccessioniPrimary (citable) accession number: Q16720
    Secondary accession number(s): B7WNR8
    , B7WNY5, Q12995, Q16858
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: October 17, 2006
    Last modified: October 1, 2014
    This is version 143 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome X
      Human chromosome X: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3