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Q16720

- AT2B3_HUMAN

UniProt

Q16720 - AT2B3_HUMAN

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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

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 intermediate By similarity
Metal bindingi794 – 7941Magnesium By similarity
Metal bindingi798 – 7981Magnesium By 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
Complete GO annotation...

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 9797Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei98 – 11821Helical; Reviewed prediction
Add
BLAST
Topological domaini119 – 15537Extracellular Reviewed prediction
Add
BLAST
Transmembranei156 – 17621Helical; Reviewed prediction
Add
BLAST
Topological domaini177 – 364188Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei365 – 38420Helical; Reviewed prediction
Add
BLAST
Topological domaini385 – 41733Extracellular Reviewed prediction
Add
BLAST
Transmembranei418 – 43518Helical; Reviewed prediction
Add
BLAST
Topological domaini436 – 849414Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei850 – 86920Helical; Reviewed prediction
Add
BLAST
Topological domaini870 – 87910Extracellular Reviewed prediction
Transmembranei880 – 90021Helical; Reviewed prediction
Add
BLAST
Topological domaini901 – 92020Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei921 – 94323Helical; Reviewed prediction
Add
BLAST
Topological domaini944 – 96118Extracellular Reviewed prediction
Add
BLAST
Transmembranei962 – 98322Helical; Reviewed prediction
Add
BLAST
Topological domaini984 – 100219Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei1003 – 102422Helical; Reviewed prediction
Add
BLAST
Topological domaini1025 – 103410Extracellular Reviewed prediction
Transmembranei1035 – 105622Helical; Reviewed prediction
Add
BLAST
Topological domaini1057 – 1220164Cytoplasmic Reviewed prediction
Add
BLAST

GO - Cellular componenti

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

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.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
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 3
PRO_0000046218Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1113 – 11131Phosphothreonine; by PKC By 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.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1097 – 111418Calmodulin-binding subdomain A By similarity
Add
BLAST
Regioni1115 – 112410Calmodulin-binding subdomain B By 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

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.
VSP_000392Add
BLAST
Alternative sequencei1115 – 1220106IRVVK…VETSL → MEVVSTFKRSGSVQGAVRRR SSVLSQLHDVTNLSTPTHAI LSAANPTSAAGNPGGESVP in isoform XA and isoform ZA.
VSP_000393Add
BLAST
Alternative sequencei1115 – 1220106IRVVK…VETSL → MEVVSTFKRSGSVQGAVRRR SSVLSQLHDVTNLSTPTHAI LSAANPTSAAGSES in isoform XE and isoform ZE.
VSP_000394Add
BLAST
Alternative sequencei1115 – 1220106IRVVK…VETSL → VCWDGKKMLRTTEVG in isoform XG and isoform ZG.
VSP_000395Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti587 – 5871I → V in AAB09762. 1 Publication
Sequence conflicti587 – 5871I → V in AAB38530. 1 Publication
Sequence conflicti654 – 6541S → Y in AAB09762. 1 Publication
Sequence conflicti654 – 6541S → Y in AAB38530. 1 Publication

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]
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]
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 ]
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 ]
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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 142 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

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