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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 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
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

GO - Cellular componenti

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

BgeeiQ16720.
CleanExiHS_ATP2B3.
ExpressionAtlasiQ16720. baseline and differential.
GenevestigatoriQ16720.

Organism-specific databases

HPAiCAB005607.
HPA001583.

Interactioni

Subunit structurei

Interacts with PDZD11.1 Publication

Protein-protein interaction databases

BioGridi106982. 19 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.
GeneTreeiENSGT00510000046331.
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

        10         20         30         40         50
MGDMANSSIE FHPKPQQQRD VPQAGGFGCT LAELRTLMEL RGAEALQKIE
60 70 80 90 100
EAYGDVSGLC RRLKTSPTEG LADNTNDLEK RRQIYGQNFI PPKQPKTFLQ
110 120 130 140 150
LVWEALQDVT LIILEVAAIV SLGLSFYAPP GEESEACGNV SGGAEDEGEA
160 170 180 190 200
EAGWIEGAAI LLSVICVVLV TAFNDWSKEK QFRGLQSRIE QEQKFTVIRN
210 220 230 240 250
GQLLQVPVAA LVVGDIAQVK YGDLLPADGV LIQANDLKID ESSLTGESDH
260 270 280 290 300
VRKSADKDPM LLSGTHVMEG SGRMVVTAVG VNSQTGIIFT LLGAGGEEEE
310 320 330 340 350
KKDKKGKQQD GAMESSQTKA KKQDGAVAME MQPLKSAEGG EMEEREKKKA
360 370 380 390 400
NAPKKEKSVL QGKLTKLAVQ IGKAGLVMSA ITVIILVLYF VIETFVVEGR
410 420 430 440 450
TWLAECTPVY VQYFVKFFII GVTVLVVAVP EGLPLAVTIS LAYSVKKMMK
460 470 480 490 500
DNNLVRHLDA CETMGNATAI CSDKTGTLTT NRMTVVQSYL GDTHYKEIPA
510 520 530 540 550
PSALTPKILD LLVHAISINS AYTTKILPPE KEGALPRQVG NKTECALLGF
560 570 580 590 600
VLDLKRDFQP VREQIPEDKL YKVYTFNSVR KSMSTVIRMP DGGFRLFSKG
610 620 630 640 650
ASEILLKKCT NILNSNGELR GFRPRDRDDM VRKIIEPMAC DGLRTICIAY
660 670 680 690 700
RDFSAGQEPD WDNENEVVGD LTCIAVVGIE DPVRPEVPEA IRKCQRAGIT
710 720 730 740 750
VRMVTGDNIN TARAIAAKCG IIQPGEDFLC LEGKEFNRRI RNEKGEIEQE
760 770 780 790 800
RLDKVWPKLR VLARSSPTDK HTLVKGIIDS TTGEQRQVVA VTGDGTNDGP
810 820 830 840 850
ALKKADVGFA MGIAGTDVAK EASDIILTDD NFTSIVKAVM WGRNVYDSIS
860 870 880 890 900
KFLQFQLTVN VVAVIVAFTG ACITQDSPLK AVQMLWVNLI MDTFASLALA
910 920 930 940 950
TEPPTESLLL RKPYGRDKPL ISRTMMKNIL GHAVYQLAII FTLLFVGELF
960 970 980 990 1000
FDIDSGRNAP LHSPPSEHYT IIFNTFVMMQ LFNEINARKI HGERNVFDGI
1010 1020 1030 1040 1050
FSNPIFCTIV LGTFGIQIVI VQFGGKPFSC SPLSTEQWLW CLFVGVGELV
1060 1070 1080 1090 1100
WGQVIATIPT SQLKCLKEAG HGPGKDEMTD EELAEGEEEI DHAERELRRG
1110 1120 1130 1140 1150
QILWFRGLNR IQTQIRVVKA FRSSLYEGLE KPESKTSIHN FMATPEFLIN
1160 1170 1180 1190 1200
DYTHNIPLID DTDVDENEER LRAPPPPSPN QNNNAIDSGI YLTTHVTKSA
1210 1220
TSSVFSSSPG SPLHSVETSL
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. 19 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.
GeneTreei ENSGT00510000046331.
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

Bgeei Q16720.
CleanExi HS_ATP2B3.
ExpressionAtlasi Q16720. baseline and differential.
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: October 29, 2014
This is version 144 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