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Protein

Plasma membrane calcium-transporting ATPase 4

Gene

ATP2B4

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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 sitei465 – 46514-aspartylphosphate intermediateBy similarity
Metal bindingi785 – 7851MagnesiumBy similarity
Metal bindingi789 – 7891MagnesiumBy similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. calcium-transporting ATPase activity Source: BHF-UCL
  3. calmodulin binding Source: BHF-UCL
  4. metal ion binding Source: UniProtKB-KW
  5. nitric-oxide synthase binding Source: BHF-UCL
  6. nitric-oxide synthase inhibitor activity Source: BHF-UCL
  7. protein phosphatase 2B binding Source: BHF-UCL
  8. scaffold protein binding Source: BHF-UCL

GO - Biological processi

  1. blood coagulation Source: Reactome
  2. calcium ion homeostasis Source: BHF-UCL
  3. calcium ion import across plasma membrane Source: BHF-UCL
  4. calcium ion transmembrane transport Source: BHF-UCL
  5. cellular calcium ion homeostasis Source: BHF-UCL
  6. cellular response to epinephrine stimulus Source: BHF-UCL
  7. ion transmembrane transport Source: Reactome
  8. negative regulation of adrenergic receptor signaling pathway involved in heart process Source: BHF-UCL
  9. negative regulation of arginine catabolic process Source: BHF-UCL
  10. negative regulation of calcineurin-NFAT signaling cascade Source: BHF-UCL
  11. negative regulation of cardiac muscle hypertrophy in response to stress Source: BHF-UCL
  12. negative regulation of citrulline biosynthetic process Source: BHF-UCL
  13. negative regulation of nitric oxide biosynthetic process Source: BHF-UCL
  14. negative regulation of nitric oxide mediated signal transduction Source: BHF-UCL
  15. negative regulation of nitric-oxide synthase activity Source: BHF-UCL
  16. negative regulation of peptidyl-cysteine S-nitrosylation Source: BHF-UCL
  17. negative regulation of the force of heart contraction Source: BHF-UCL
  18. positive regulation of cAMP-dependent protein kinase activity Source: BHF-UCL
  19. positive regulation of peptidyl-serine phosphorylation Source: BHF-UCL
  20. regulation of sodium ion transmembrane transport Source: BHF-UCL
  21. regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  22. response to hydrostatic pressure Source: BHF-UCL
  23. transmembrane transport Source: Reactome
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.

Protein family/group databases

TCDBi3.A.3.2.1. the p-type atpase (p-atpase) superfamily.

Names & Taxonomyi

Protein namesi
Recommended name:
Plasma membrane calcium-transporting ATPase 4 (EC:3.6.3.8)
Short name:
PMCA4
Alternative name(s):
Matrix-remodeling-associated protein 1
Plasma membrane calcium ATPase isoform 4
Plasma membrane calcium pump isoform 4
Gene namesi
Name:ATP2B4
Synonyms:ATP2B2, MXRA1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:817. ATP2B4.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 9291CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei93 – 11321HelicalSequence AnalysisAdd
BLAST
Topological domaini114 – 15037ExtracellularSequence AnalysisAdd
BLAST
Transmembranei151 – 17121HelicalSequence AnalysisAdd
BLAST
Topological domaini172 – 356185CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei357 – 37620HelicalSequence AnalysisAdd
BLAST
Topological domaini377 – 40933ExtracellularSequence AnalysisAdd
BLAST
Transmembranei410 – 42718HelicalSequence AnalysisAdd
BLAST
Topological domaini428 – 840413CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei841 – 86020HelicalSequence AnalysisAdd
BLAST
Topological domaini861 – 87010ExtracellularSequence Analysis
Transmembranei871 – 89121HelicalSequence AnalysisAdd
BLAST
Topological domaini892 – 91120CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei912 – 93423HelicalSequence AnalysisAdd
BLAST
Topological domaini935 – 95218ExtracellularSequence AnalysisAdd
BLAST
Transmembranei953 – 97422HelicalSequence AnalysisAdd
BLAST
Topological domaini975 – 99319CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei994 – 101522HelicalSequence AnalysisAdd
BLAST
Topological domaini1016 – 102510ExtracellularSequence Analysis
Transmembranei1026 – 104722HelicalSequence AnalysisAdd
BLAST
Topological domaini1048 – 1241194CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. caveola Source: BHF-UCL
  2. integral component of plasma membrane Source: ProtInc
  3. membrane Source: UniProtKB
  4. plasma membrane Source: HPA
  5. protein complex Source: BHF-UCL
  6. T-tubule Source: BHF-UCL
  7. Z disc Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA25110.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 12411240Plasma membrane calcium-transporting ATPase 4PRO_0000046220Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei13 – 131Phosphoserine1 Publication
Modified residuei328 – 3281PhosphoserineBy similarity
Modified residuei1102 – 11021Phosphothreonine; by PKCBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP23634.
PaxDbiP23634.
PRIDEiP23634.

PTM databases

PhosphoSiteiP23634.

Expressioni

Tissue specificityi

Isoform XB is the most abundant isoform and is expressed ubiquitously. Isoforms containing segment Z have only been detected in heart, while isoforms containing segment a have been found in heart, stomach and brain cortex.

Gene expression databases

BgeeiP23634.
CleanExiHS_ATP2B2.
HS_ATP2B4.
ExpressionAtlasiP23634. baseline and differential.
GenevestigatoriP23634.

Organism-specific databases

HPAiCAB016118.
HPA040431.

Interactioni

Subunit structurei

Interacts with PDZD11. Interacts with SLC35G1 and STIM1.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CALCAP012582EBI-1174388,EBI-1018474
Dlg2Q636222EBI-1174437,EBI-396947From a different organism.
Dlg3Q629362EBI-1174437,EBI-349596From a different organism.

Protein-protein interaction databases

BioGridi106983. 26 interactions.
DIPiDIP-6128N.
IntActiP23634. 11 interactions.
MINTiMINT-219327.
STRINGi9606.ENSP00000350310.

Structurei

Secondary structure

1
1241
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni1087 – 10893Combined sources
Turni1090 – 10923Combined sources
Helixi1093 – 110210Combined sources
Helixi1141 – 11477Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CFFNMR-B1086-1104[»]
2KNENMR-B1086-1149[»]
ProteinModelPortaliP23634.
SMRiP23634. Positions 47-945.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP23634.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1086 – 110318Calmodulin-binding subdomain AAdd
BLAST
Regioni1104 – 111310Calmodulin-binding subdomain BBy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi297 – 3037Poly-Lys
Compositional biasi1186 – 11905Poly-Glu

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0474.
GeneTreeiENSGT00510000046331.
HOVERGENiHBG061286.
InParanoidiP23634.
KOiK05850.
OMAiEPVMVNA.
OrthoDBiEOG7SN8BN.
PhylomeDBiP23634.
TreeFamiTF300330.

Family and domain databases

Gene3Di1.20.1110.10. 3 hits.
InterProiIPR030319. ATP2B4.
IPR022141. ATP_Ca_trans_C.
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.
IPR023214. HAD-like_dom.
IPR006408. P-type_ATPase_IIB.
IPR001757. P_typ_ATPase.
[Graphical view]
PANTHERiPTHR24093:SF276. PTHR24093:SF276. 1 hit.
PfamiPF12424. ATP_Ca_trans_C. 2 hits.
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.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 8 isoformsi produced by alternative splicing. AlignAdd to basket

Note: There is a combination of two alternatively spliced domains at N-terminal site A (X and Z) and at C-terminal site B/C (A, B, D and K). 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 XD (identifier: P23634-1) [UniParc]FASTAAdd to basket

Also known as: AIICIV

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
MTNPSDRVLP ANSMAESREG DFGCTVMELR KLMELRSRDA LTQINVHYGG
60 70 80 90 100
VQNLCSRLKT SPVEGLSGNP ADLEKRRQVF GHNVIPPKKP KTFLELVWEA
110 120 130 140 150
LQDVTLIILE IAAIISLVLS FYRPAGEENE LCGQVATTPE DENEAQAGWI
160 170 180 190 200
EGAAILFSVI IVVLVTAFND WSKEKQFRGL QCRIEQEQKF SIIRNGQLIQ
210 220 230 240 250
LPVAEIVVGD IAQVKYGDLL PADGILIQGN DLKIDESSLT GESDHVKKSL
260 270 280 290 300
DKDPMLLSGT HVMEGSGRMV VTAVGVNSQT GIILTLLGVN EDDEGEKKKK
310 320 330 340 350
GKKQGVPENR NKAKTQDGVA LEIQPLNSQE GIDNEEKDKK AVKVPKKEKS
360 370 380 390 400
VLQGKLTRLA VQIGKAGLLM SALTVFILIL YFVIDNFVIN RRPWLPECTP
410 420 430 440 450
IYIQYFVKFF IIGITVLVVA VPEGLPLAVT ISLAYSVKKM MKDNNLVRHL
460 470 480 490 500
DACETMGNAT AICSDKTGTL TMNRMTVVQA YIGGIHYRQI PSPDVFLPKV
510 520 530 540 550
LDLIVNGISI NSAYTSKILP PEKEGGLPRQ VGNKTECALL GFVTDLKQDY
560 570 580 590 600
QAVRNEVPEE KLYKVYTFNS VRKSMSTVIR NPNGGFRMYS KGASEIILRK
610 620 630 640 650
CNRILDRKGE AVPFKNKDRD DMVRTVIEPM ACDGLRTICI AYRDFDDTEP
660 670 680 690 700
SWDNENEILT ELTCIAVVGI EDPVRPEVPD AIAKCKQAGI TVRMVTGDNI
710 720 730 740 750
NTARAIATKC GILTPGDDFL CLEGKEFNRL IRNEKGEVEQ EKLDKIWPKL
760 770 780 790 800
RVLARSSPTD KHTLVKGIID STVGEHRQVV AVTGDGTNDG PALKKADVGF
810 820 830 840 850
AMGIAGTDVA KEASDIILTD DNFTSIVKAV MWGRNVYDSI SKFLQFQLTV
860 870 880 890 900
NVVAVIVAFT GACITQDSPL KAVQMLWVNL IMDTFASLAL ATEPPTESLL
910 920 930 940 950
KRRPYGRNKP LISRTMMKNI LGHAFYQLIV IFILVFAGEK FFDIDSGRKA
960 970 980 990 1000
PLHSPPSQHY TIVFNTFVLM QLFNEINSRK IHGEKNVFSG IYRNIIFCSV
1010 1020 1030 1040 1050
VLGTFICQIF IVEFGGKPFS CTSLSLSQWL WCLFIGIGEL LWGQFISAIP
1060 1070 1080 1090 1100
TRSLKFLKEA GHGTTKEEIT KDAEGLDEID HAEMELRRGQ ILWFRGLNRI
1110 1120 1130 1140 1150
QTQIDVINTF QTGASFKGVL RRQNMGQHLD VKLVPSSSYI KVVKAFHSSL
1160 1170 1180 1190 1200
HESIQKPYNQ KSIHSFMTHP EFAIEEELPR TPLLDEEEEE NPDKASKFGT
1210 1220 1230 1240
RVLLLDGEVT PYANTNNNAV DCNQVQLPQS DSSLQSLETS V
Length:1,241
Mass (Da):137,920
Last modified:June 1, 2001 - v2
Checksum:i568544103CD5F494
GO
Isoform XA (identifier: P23634-2) [UniParc]FASTAAdd to basket

Also known as: AIICII

The sequence of this isoform differs from the canonical sequence as follows:
     1140-1241: IKVVKAFHSS...SSLQSLETSV → VAVAPVKSSPTTSVPAVSSPPMGNQSGQSVP

Show »
Length:1,170
Mass (Da):129,403
Checksum:iC4ED2E2EFE1BB043
GO
Isoform ZA (identifier: P23634-3) [UniParc]FASTAAdd to basket

Also known as: AICII

The sequence of this isoform differs from the canonical sequence as follows:
     301-312: Missing.
     1140-1241: IKVVKAFHSS...SSLQSLETSV → VAVAPVKSSPTTSVPAVSSPPMGNQSGQSVP

Show »
Length:1,158
Mass (Da):128,066
Checksum:iE7AA8CC9C25E0727
GO
Isoform XK (identifier: P23634-4) [UniParc]FASTAAdd to basket

Also known as: XG

The sequence of this isoform differs from the canonical sequence as follows:
     1009-1044: Missing.
     1140-1241: IKVVKAFHSS...SSLQSLETSV → VAVAPVKSSPTTSVPAVSSPPMGNQSGQSVP

Show »
Length:1,134
Mass (Da):125,344
Checksum:i088F8CB994D46238
GO
Isoform ZK (identifier: P23634-5) [UniParc]FASTAAdd to basket

Also known as: ZG

The sequence of this isoform differs from the canonical sequence as follows:
     301-312: Missing.
     1009-1044: Missing.
     1140-1241: IKVVKAFHSS...SSLQSLETSV → VAVAPVKSSPTTSVPAVSSPPMGNQSGQSVP

Show »
Length:1,122
Mass (Da):124,007
Checksum:i4AD4378ED226853B
GO
Isoform XB (identifier: P23634-6) [UniParc]FASTAAdd to basket

Also known as: AIICI

The sequence of this isoform differs from the canonical sequence as follows:
     1104-1139: Missing.

Show »
Length:1,205
Mass (Da):133,931
Checksum:i76CE806974035974
GO
Isoform ZB (identifier: P23634-7) [UniParc]FASTAAdd to basket

Also known as: AICI

The sequence of this isoform differs from the canonical sequence as follows:
     301-312: Missing.
     1104-1139: Missing.

Show »
Length:1,193
Mass (Da):132,594
Checksum:i6AA34BD1850CADB7
GO
Isoform ZD (identifier: P23634-8) [UniParc]FASTAAdd to basket

Also known as: AICIV

The sequence of this isoform differs from the canonical sequence as follows:
     301-312: Missing.

Show »
Length:1,229
Mass (Da):136,584
Checksum:i5E9E48B86464E926
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti492 – 4921S → C in CAD97686 (PubMed:17974005).Curated
Sequence conflicti1144 – 11441K → N AA sequence (PubMed:2963820).Curated
Sequence conflicti1147 – 11471H → S AA sequence (PubMed:2963820).Curated
Sequence conflicti1153 – 11531S → F AA sequence (PubMed:2963820).Curated
Sequence conflicti1178 – 11781L → Q AA sequence (PubMed:2966397).Curated
Sequence conflicti1187 – 11871E → Q AA sequence (PubMed:2966397).Curated
Sequence conflicti1190 – 11901E → G in CAD97686 (PubMed:17974005).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei301 – 31212Missing in isoform ZA, isoform ZK, isoform ZB and isoform ZD. CuratedVSP_000402Add
BLAST
Alternative sequencei1009 – 104436Missing in isoform XK and isoform ZK. CuratedVSP_000403Add
BLAST
Alternative sequencei1104 – 113936Missing in isoform XB and isoform ZB. 2 PublicationsVSP_000404Add
BLAST
Alternative sequencei1140 – 1241102IKVVK…LETSV → VAVAPVKSSPTTSVPAVSSP PMGNQSGQSVP in isoform XA, isoform XK, isoform ZA and isoform ZK. 2 PublicationsVSP_000405Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M25874 mRNA. Translation: AAA50819.1.
M83363 mRNA. Translation: AAA36455.1.
BX537444 mRNA. Translation: CAD97686.1.
U42026 mRNA. Translation: AAB17577.1.
U42061 mRNA. Translation: AAB17578.1.
U42062 mRNA. Translation: AAB17579.1.
U42378 mRNA. Translation: AAB17580.1.
AL513343, AC114402 Genomic DNA. Translation: CAI17025.1.
AL513343, AC114402 Genomic DNA. Translation: CAI17026.1.
CH471067 Genomic DNA. Translation: EAW91483.1.
CH471067 Genomic DNA. Translation: EAW91486.1.
BC140774 mRNA. Translation: AAI40775.1.
CCDSiCCDS1440.1. [P23634-6]
CCDS30977.1. [P23634-2]
PIRiA35547.
RefSeqiNP_001001396.1. NM_001001396.2. [P23634-2]
NP_001675.3. NM_001684.4. [P23634-6]
UniGeneiHs.343522.
Hs.733333.

Genome annotation databases

EnsembliENST00000341360; ENSP00000340930; ENSG00000058668. [P23634-2]
ENST00000357681; ENSP00000350310; ENSG00000058668. [P23634-6]
ENST00000367218; ENSP00000356187; ENSG00000058668. [P23634-2]
GeneIDi493.
KEGGihsa:493.
UCSCiuc001gzv.3. human. [P23634-2]
uc001gzw.3. human. [P23634-6]

Polymorphism databases

DMDMi14286105.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M25874 mRNA. Translation: AAA50819.1.
M83363 mRNA. Translation: AAA36455.1.
BX537444 mRNA. Translation: CAD97686.1.
U42026 mRNA. Translation: AAB17577.1.
U42061 mRNA. Translation: AAB17578.1.
U42062 mRNA. Translation: AAB17579.1.
U42378 mRNA. Translation: AAB17580.1.
AL513343, AC114402 Genomic DNA. Translation: CAI17025.1.
AL513343, AC114402 Genomic DNA. Translation: CAI17026.1.
CH471067 Genomic DNA. Translation: EAW91483.1.
CH471067 Genomic DNA. Translation: EAW91486.1.
BC140774 mRNA. Translation: AAI40775.1.
CCDSiCCDS1440.1. [P23634-6]
CCDS30977.1. [P23634-2]
PIRiA35547.
RefSeqiNP_001001396.1. NM_001001396.2. [P23634-2]
NP_001675.3. NM_001684.4. [P23634-6]
UniGeneiHs.343522.
Hs.733333.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CFFNMR-B1086-1104[»]
2KNENMR-B1086-1149[»]
ProteinModelPortaliP23634.
SMRiP23634. Positions 47-945.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106983. 26 interactions.
DIPiDIP-6128N.
IntActiP23634. 11 interactions.
MINTiMINT-219327.
STRINGi9606.ENSP00000350310.

Protein family/group databases

TCDBi3.A.3.2.1. the p-type atpase (p-atpase) superfamily.

PTM databases

PhosphoSiteiP23634.

Polymorphism databases

DMDMi14286105.

Proteomic databases

MaxQBiP23634.
PaxDbiP23634.
PRIDEiP23634.

Protocols and materials databases

DNASUi493.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000341360; ENSP00000340930; ENSG00000058668. [P23634-2]
ENST00000357681; ENSP00000350310; ENSG00000058668. [P23634-6]
ENST00000367218; ENSP00000356187; ENSG00000058668. [P23634-2]
GeneIDi493.
KEGGihsa:493.
UCSCiuc001gzv.3. human. [P23634-2]
uc001gzw.3. human. [P23634-6]

Organism-specific databases

CTDi493.
GeneCardsiGC01P203595.
HGNCiHGNC:817. ATP2B4.
HPAiCAB016118.
HPA040431.
MIMi108732. gene.
neXtProtiNX_P23634.
PharmGKBiPA25110.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0474.
GeneTreeiENSGT00510000046331.
HOVERGENiHBG061286.
InParanoidiP23634.
KOiK05850.
OMAiEPVMVNA.
OrthoDBiEOG7SN8BN.
PhylomeDBiP23634.
TreeFamiTF300330.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSiATP2B4. human.
EvolutionaryTraceiP23634.
GeneWikiiATP2B4.
GenomeRNAii493.
NextBioi2071.
PROiP23634.
SOURCEiSearch...

Gene expression databases

BgeeiP23634.
CleanExiHS_ATP2B2.
HS_ATP2B4.
ExpressionAtlasiP23634. baseline and differential.
GenevestigatoriP23634.

Family and domain databases

Gene3Di1.20.1110.10. 3 hits.
InterProiIPR030319. ATP2B4.
IPR022141. ATP_Ca_trans_C.
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.
IPR023214. HAD-like_dom.
IPR006408. P-type_ATPase_IIB.
IPR001757. P_typ_ATPase.
[Graphical view]
PANTHERiPTHR24093:SF276. PTHR24093:SF276. 1 hit.
PfamiPF12424. ATP_Ca_trans_C. 2 hits.
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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Peptide sequence analysis and molecular cloning reveal two calcium pump isoforms in the human erythrocyte membrane."
    Strehler E.E., James P., Fischer R., Heim R., Vorherr T.E., Filoteo A.G., Penniston J.T., Carafoli E.
    J. Biol. Chem. 265:2835-2842(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM XB), PARTIAL PROTEIN SEQUENCE.
    Tissue: Erythrocyte.
  2. "Analysis of the tissue-specific distribution of mRNAs encoding the plasma membrane calcium-pumping ATPases and characterization of an alternately spliced form of PMCA4 at the cDNA and genomic levels."
    Brandt P., Neve R.L., Kammesheidt A., Rhoads R.E., Vanaman T.C.
    J. Biol. Chem. 267:4376-4385(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM XA).
    Tissue: Fetal brain.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM XB).
    Tissue: Fetal kidney.
  4. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM XA).
    Tissue: Brain.
  7. "Analysis of mRNA expression and cloning of a novel plasma membrane Ca(2+)-ATPase splice variant in human heart."
    Santiago-Garcia J., Mas-Oliva J., Saavedra D., Zarain-Herzberg A.
    Mol. Cell. Biochem. 155:173-182(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS XA; XB; XK; ZA; ZB AND ZK).
    Tissue: Heart muscle.
  8. "Identification and primary structure of a calmodulin binding domain of the Ca2+ pump of human erythrocytes."
    James P., Maeda M., Fischer R., Verma A.K., Krebs J., Penniston J.T., Carafoli E.
    J. Biol. Chem. 263:2905-2910(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1085-1153 (ISOFORMS XB/ZB), CALMODULIN-BINDING SUBDOMAIN A.
  9. "A C-terminal, calmodulin-like regulatory domain from the plasma membrane Ca2+-pumping ATPase."
    Brandt P., Zurini M., Neve R.L., Rhoads R.E., Vanaman T.C.
    Proc. Natl. Acad. Sci. U.S.A. 85:2914-2918(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1177-1190.
  10. "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(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE SPLICING (ISOFORMS X AND Z).
    Tissue: Heart.
  11. Erratum
    Stauffer T.P., Hilfiker H., Carafoli E., Strehler E.E.
    J. Biol. Chem. 269:32022-32022(1993) [PubMed] [Europe PMC] [Abstract]
  12. "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(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PDZD11.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "POST, partner of stromal interaction molecule 1 (STIM1), targets STIM1 to multiple transporters."
    Krapivinsky G., Krapivinsky L., Stotz S.C., Manasian Y., Clapham D.E.
    Proc. Natl. Acad. Sci. U.S.A. 108:19234-19239(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SLC35G1 AND STIM1.
  15. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  16. "NMR solution structure of a complex of calmodulin with a binding peptide of the Ca(2+) pump."
    Elshorst B., Hennig M., Foersterling H., Diener A., Maurer M., Schulte P., Schwalbe H., Griesinger C., Krebs J., Schmid H., Vorherr T.E., Carafoli E.
    Biochemistry 38:12320-12332(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 1086-1104 IN COMPLEX WITH CALMODULIN.

Entry informationi

Entry nameiAT2B4_HUMAN
AccessioniPrimary (citable) accession number: P23634
Secondary accession number(s): B1APW5
, B1APW6, Q13450, Q13452, Q13455, Q16817, Q7Z3S1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: June 1, 2001
Last modified: March 4, 2015
This is version 162 of the entry and version 2 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.