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Entry version 228 (18 Sep 2019)
Sequence version 1 (01 Aug 1990)
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Protein

Sarcoplasmic/endoplasmic reticulum calcium ATPase 2

Gene

ATP2A2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol to the sarcoplasmic reticulum lumen. Isoform 2 is involved in the regulation of the contraction/relaxation cycle (PubMed:16402920). Acts as a regulator of TNFSF11-mediated Ca2+ signaling pathways via its interaction with TMEM64 which is critical for the TNFSF11-induced CREB1 activation and mitochondrial ROS generation necessary for proper osteoclast generation. Association between TMEM64 and SERCA2 in the ER leads to cytosolic Ca (2+) spiking for activation of NFATC1 and production of mitochondrial ROS, thereby triggering Ca (2+) signaling cascades that promote osteoclast differentiation and activation (By similarity).By similarity1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Reversibly inhibited by phospholamban (PLN) at low calcium concentrations (By similarity). Inhibited by sarcolipin (SLN) and myoregulin (MRLN) (By similarity). Enhanced by DWORF; DWORF increases activity by displacing sarcolipin (SLN), phospholamban (PLN) and myoregulin (MRLN) (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi304Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi305Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi307Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi309Calcium 1By similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei3514-aspartylphosphate intermediateBy similarity1
Metal bindingi351MagnesiumBy similarity1
Metal bindingi353Magnesium; via carbonyl oxygenBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei353ATPBy similarity1
Binding sitei442ATPBy similarity1
Binding sitei489ATPBy similarity1
Binding sitei514ATPBy similarity1
Binding sitei559ATPBy similarity1
Binding sitei677ATPBy similarity1
Binding sitei683ATPBy similarity1
Metal bindingi702MagnesiumBy similarity1
Binding sitei705ATPBy similarity1
Metal bindingi767Calcium 2By similarity1
Metal bindingi770Calcium 2By similarity1
Metal bindingi795Calcium 1By similarity1
Metal bindingi798Calcium 2By similarity1
Metal bindingi799Calcium 1By similarity1
Metal bindingi799Calcium 2By similarity1
Metal bindingi907Calcium 2By similarity1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionTranslocase
Biological processCalcium transport, Ion transport, Transport
LigandATP-binding, Calcium, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-1912420 Pre-NOTCH Processing in Golgi
R-HSA-418359 Reduction of cytosolic Ca++ levels
R-HSA-5578775 Ion homeostasis
R-HSA-936837 Ion transport by P-type ATPases

SignaLink: a signaling pathway resource with multi-layered regulatory networks

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SignaLinki
P16615

SIGNOR Signaling Network Open Resource

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SIGNORi
P16615

Protein family/group databases

Transport Classification Database

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TCDBi
3.A.3.2.7 the p-type atpase (p-atpase) superfamily

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Sarcoplasmic/endoplasmic reticulum calcium ATPase 2 (EC:7.2.2.10)
Short name:
SERCA2
Short name:
SR Ca(2+)-ATPase 2
Alternative name(s):
Calcium pump 2
Calcium-transporting ATPase sarcoplasmic reticulum type, slow twitch skeletal muscle isoform
Endoplasmic reticulum class 1/2 Ca(2+) ATPase
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:ATP2A2
Synonyms:ATP2B
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 12

Organism-specific databases

Human Gene Nomenclature Database

More...
HGNCi
HGNC:812 ATP2A2

Online Mendelian Inheritance in Man (OMIM)

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MIMi
108740 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_P16615

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini1 – 48CytoplasmicCuratedAdd BLAST48
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei49 – 69Helical; Name=1By similarityAdd BLAST21
Topological domaini70 – 89LumenalCuratedAdd BLAST20
Transmembranei90 – 110Helical; Name=2By similarityAdd BLAST21
Topological domaini111 – 253CytoplasmicCuratedAdd BLAST143
Transmembranei254 – 273Helical; Name=3By similarityAdd BLAST20
Topological domaini274 – 295LumenalCuratedAdd BLAST22
Transmembranei296 – 313Helical; Name=4By similarityAdd BLAST18
Topological domaini314 – 756CytoplasmicCuratedAdd BLAST443
Transmembranei757 – 776Helical; Name=5By similarityAdd BLAST20
Topological domaini777 – 786LumenalCurated10
Transmembranei787 – 807Helical; Name=6By similarityAdd BLAST21
Topological domaini808 – 827CytoplasmicCuratedAdd BLAST20
Transmembranei828 – 850Helical; Name=7By similarityAdd BLAST23
Topological domaini851 – 896LumenalCuratedAdd BLAST46
Transmembranei897 – 916Helical; Name=8By similarityAdd BLAST20
Topological domaini917 – 929CytoplasmicCuratedAdd BLAST13
Transmembranei930 – 948Helical; Name=9By similarityAdd BLAST19
Topological domaini949 – 963LumenalCuratedAdd BLAST15
Transmembranei964 – 984Helical; Name=10By similarityAdd BLAST21
Topological domaini985 – 1042CytoplasmicCuratedAdd BLAST58

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Sarcoplasmic reticulum

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Acrokeratosis verruciformis (AKV)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA localized disorder of keratinization, which is inherited as an autosomal dominant trait. Its onset is early in life with multiple flat-topped, flesh-colored papules on the hands and feet, punctate keratoses on the palms and soles, with varying degrees of nail involvement. The histopathology shows a distinctive pattern of epidermal features with hyperkeratosis, hypergranulosis and acanthosis together with papillomatosis. These changes are frequently associated with circumscribed elevations of the epidermis that are said to resemble church spires. There are no features of dyskeratosis or acantholysis, the typical findings in lesions of Darier disease.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_017532602P → L in AKV; loss of activity. 1 PublicationCorresponds to variant dbSNP:rs121912737EnsemblClinVar.1
Darier disease (DD)6 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA skin disorder characterized by warty papules and plaques in seborrheic areas (central trunk, flexures, scalp and forehead), palmoplantar pits and distinctive nail abnormalities. It is due to loss of adhesion between epidermal cells (acantholysis) and abnormal keratinization. Patients with mild disease may have no more than a few scattered keratotic papules or subtle nail changes, whereas those with severe disease are handicapped by widespread malodorous keratotic plaques. Some patients present with hemorrhage into acantholytic vesicles on the palms and dorsal aspects of the fingers which gives rise to black macules. In a few families affected by Darier disease, neuropsychiatric abnormalities such as mild mental retardation, schizophrenia, bipolar disorder and epilepsy have been reported. Stress, UV exposure, heat, sweat, friction and oral contraception exacerbate disease symptoms. Clinical variants of Darier disease include hypertrophic, vesicobullous, hypopigmented, cornifying, zosteriform or linear, acute and comedonal subtypes. Comedonal Darier disease is characterized by the coexistence of acne-like comedonal lesions with typical Darier hyperkeratotic papules on light-exposed areas. At histopathologic level, comedonal Darier disease differs from classic Darier disease in the prominent follicular involvement and the presence of greatly elongated dermal villi.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_00860823G → E in DD. 1 PublicationCorresponds to variant dbSNP:rs28929478EnsemblClinVar.1
Natural variantiVAR_00860939N → T in DD. 1 Publication1
Natural variantiVAR_06339841Missing in DD; comedonal type. 1 Publication1
Natural variantiVAR_00861047K → KMFLTGK in DD. 1
Natural variantiVAR_00861165L → S in DD; severe form. 1
Natural variantiVAR_07968574 – 108Missing in DD. 1 PublicationAdd BLAST35
Natural variantiVAR_079686101N → S in DD. 1 Publication1
Natural variantiVAR_008612131R → Q in DD. 1 PublicationCorresponds to variant dbSNP:rs121912738EnsemblClinVar.1
Natural variantiVAR_008613160P → L in DD. 1
Natural variantiVAR_008614186S → P in DD. 1
Natural variantiVAR_079687194 – 197Missing in DD. 1 Publication4
Natural variantiVAR_008615211G → D in DD; severe form. 1
Natural variantiVAR_008616223V → M in DD. 1
Natural variantiVAR_008617268C → F in DD; haemorrhagic lesions. Corresponds to variant dbSNP:rs121912733EnsemblClinVar.1
Natural variantiVAR_008618310G → V in DD. 1
Natural variantiVAR_008619318C → R in DD; severe form. 1
Natural variantiVAR_008620348I → T in DD. 1
Natural variantiVAR_009508357T → K in DD. 1 Publication1
Natural variantiVAR_008621412E → G in DD. 1
Natural variantiVAR_008622495S → F in DD. 1 Publication1
Natural variantiVAR_008623560C → R in DD; neuropsychiatric phenotype. 1 PublicationCorresponds to variant dbSNP:rs121912734EnsemblClinVar.1
Natural variantiVAR_079688590L → P in DD. 1 Publication1
Natural variantiVAR_079689625G → A in DD. 1 Publication1
Natural variantiVAR_079690626D → E in DD. 1 Publication1
Natural variantiVAR_079691666 – 1042Missing in DD. 1 PublicationAdd BLAST377
Natural variantiVAR_079692672A → P in DD. 1 Publication1
Natural variantiVAR_008624675F → S in DD; multiple neuropsychiatric features. 1
Natural variantiVAR_008625683K → E in DD; depression. 1
Natural variantiVAR_079693691Q → P in DD. 1 Publication1
Natural variantiVAR_008626702D → N in DD; moderate form. 1
Natural variantiVAR_008627745A → D in DD; moderate form. 1
Natural variantiVAR_009509749G → R in DD. 1 Publication1
Natural variantiVAR_079694750R → W in DD. 1 Publication1
Natural variantiVAR_008628754Missing in DD. 1
Natural variantiVAR_008629765S → L in DD. 1 Publication1
Natural variantiVAR_079695765S → W in DD. 1 Publication1
Natural variantiVAR_008630767N → S in DD; haemorrhagic lesions and neuropsychiatric phenotype. Corresponds to variant dbSNP:rs121912732EnsemblClinVar.1
Natural variantiVAR_008631769G → R in DD. Corresponds to variant dbSNP:rs121912736EnsemblClinVar.1
Natural variantiVAR_008632803A → T in DD; mild/moderate form. 1
Natural variantiVAR_008633838A → P in DD; severe form; petit mal epilepsy. 1
Natural variantiVAR_008634843V → F in DD; depression. 1
Natural variantiVAR_079696849G → GG in DD. 1 Publication1
Natural variantiVAR_008635875C → G in DD; retinitis pigmentosa. 1
Natural variantiVAR_079697900L → P in DD. 1 Publication1
Natural variantiVAR_008636920S → Y in DD; mild/moderate/severe form; one patient with epilepsy. 1
Natural variantiVAR_008637943H → R in DD; learning difficulties. 1 Publication1
Natural variantiVAR_008638975P → R in DD. 1

Keywords - Diseasei

Disease mutation, Epilepsy

Organism-specific databases

DisGeNET

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DisGeNETi
488

MalaCards human disease database

More...
MalaCardsi
ATP2A2
MIMi101900 phenotype
124200 phenotype

Open Targets

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OpenTargetsi
ENSG00000174437

Orphanet; a database dedicated to information on rare diseases and orphan drugs

More...
Orphaneti
79151 Acrokeratosis verruciformis of Hopf
218 Darier disease

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA71

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL3901

Drug and drug target database

More...
DrugBanki
DB06157 Istaroxime

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
ATP2A2

Domain mapping of disease mutations (DMDM)

More...
DMDMi
114312

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000461961 – 1042Sarcoplasmic/endoplasmic reticulum calcium ATPase 2Add BLAST1042

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei38PhosphoserineBy similarity1
Modified residuei294Nitrated tyrosine1 Publication1
Modified residuei295Nitrated tyrosine1 Publication1
Modified residuei441PhosphothreonineBy similarity1
Modified residuei531PhosphoserineBy similarity1
Modified residuei580PhosphoserineCombined sources1
Modified residuei663PhosphoserineCombined sources1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi875 ↔ 887By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Nitrated under oxidative stress. Nitration on the two tyrosine residues inhibits catalytic activity.1 Publication

Keywords - PTMi

Disulfide bond, Nitration, Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P16615

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P16615

MassIVE - Mass Spectrometry Interactive Virtual Environment

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MassIVEi
P16615

MaxQB - The MaxQuant DataBase

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MaxQBi
P16615

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
P16615

PeptideAtlas

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PeptideAtlasi
P16615

PRoteomics IDEntifications database

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PRIDEi
P16615

ProteomicsDB human proteome resource

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ProteomicsDBi
53385 [P16615-1]
53386 [P16615-2]
53387 [P16615-3]
53388 [P16615-4]
53389 [P16615-5]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P16615

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
P16615

SwissPalm database of S-palmitoylation events

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SwissPalmi
P16615

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Isoform 1 is widely expressed in smooth muscle and nonmuscle tissues such as in adult skin epidermis, with highest expression in liver, pancreas and lung, and intermediate expression in brain, kidney and placenta. Also expressed at lower levels in heart and skeletal muscle. Isoforms 2 and 3 are highly expressed in the heart and slow twitch skeletal muscle. Expression of isoform 3 is predominantly restricted to cardiomyocytes and in close proximity to the sarcolemma. Both isoforms are mildly expressed in lung, kidney, liver, pancreas and placenta. Expression of isoform 3 is amplified during monocytic differentiation and also observed in the fetal heart.3 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000174437 Expressed in 244 organ(s), highest expression level in heart

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P16615 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P16615 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
HPA062605
HPA067892

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Interacts with sarcolipin (SLN) (By similarity).

Interacts with phospholamban (PLN) (By similarity).

Interacts with myoregulin (MRLN) (By similarity).

Interacts with DWORF (By similarity).

Isoform 1 interacts with TRAM2 (via C-terminus) (PubMed:14749390).

Interacts with HAX1 (PubMed:18971376).

Interacts with S100A8 and S100A9 (By similarity).

Interacts with SLC35G1 and STIM1 (PubMed:22084111).

Interacts with TMEM203 (PubMed:25996873).

Interacts with TMEM64 and PDIA3 (By similarity).

By similarity4 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
106978, 120 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
P16615

Database of interacting proteins

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DIPi
DIP-33868N

Protein interaction database and analysis system

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IntActi
P16615, 99 interactors

Molecular INTeraction database

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MINTi
P16615

STRING: functional protein association networks

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STRINGi
9606.ENSP00000440045

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

11042
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P16615

Database of comparative protein structure models

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ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni575 – 594Interaction with HAX11 PublicationAdd BLAST20
Regioni787 – 807Interaction with PLNBy similarityAdd BLAST21
Regioni788 – 1042Interaction with TMEM64 and PDIA3By similarityAdd BLAST255
Regioni931 – 942Interaction with PLNBy similarityAdd BLAST12

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

Ca2+ and ATP binding cause major rearrangements of the cytoplasmic and transmembrane domains. According to the E1-E2 model, Ca2+ binding to the cytosolic domain of the pump in the high-affinity E1 conformation is followed by the ATP-dependent phosphorylation of the active site Asp, giving rise to E1P. A conformational change of the phosphoenzyme gives rise to the low-affinity E2P state that exposes the Ca2+ ions to the lumenal side and promotes Ca2+ release. Dephosphorylation of the active site Asp mediates the subsequent return to the E1 conformation.By similarity
PLN and SLN both have a single transmembrane helix; both occupy a similar binding site that is situated between the ATP2A2 transmembrane helices.By similarity

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG0202 Eukaryota
COG0474 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000159986

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000265621

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P16615

KEGG Orthology (KO)

More...
KOi
K05853

Identification of Orthologs from Complete Genome Data

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OMAi
DPPTPLW

Database of Orthologous Groups

More...
OrthoDBi
100699at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P16615

TreeFam database of animal gene trees

More...
TreeFami
TF300651

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.40.1110.10, 1 hit
3.40.50.1000, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR006068 ATPase_P-typ_cation-transptr_C
IPR004014 ATPase_P-typ_cation-transptr_N
IPR023299 ATPase_P-typ_cyto_dom_N
IPR018303 ATPase_P-typ_P_site
IPR023298 ATPase_P-typ_TM_dom_sf
IPR008250 ATPase_P-typ_transduc_dom_A_sf
IPR036412 HAD-like_sf
IPR023214 HAD_sf
IPR005782 P-type_ATPase_IIA
IPR001757 P_typ_ATPase
IPR030332 SERCA1/2

The PANTHER Classification System

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PANTHERi
PTHR42861:SF18 PTHR42861:SF18, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00689 Cation_ATPase_C, 1 hit
PF00690 Cation_ATPase_N, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00120 HATPASE

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00831 Cation_ATPase_N, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF56784 SSF56784, 1 hit
SSF81653 SSF81653, 1 hit
SSF81660 SSF81660, 1 hit
SSF81665 SSF81665, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR01116 ATPase-IIA1_Ca, 1 hit
TIGR01494 ATPase_P-type, 2 hits

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00154 ATPASE_E1_E2, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (5+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry describes 5 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket
Note: SERCA2 transcripts differ only in their 3'-UTR region and are expressed in a tissue-specific manner.

This entry has 5 described isoforms and 4 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: P16615-1) [UniParc]FASTAAdd to basket
Also known as: ATP2A2B, Class 2-4, HK1, SERCA2b

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali 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
MENAHTKTVE EVLGHFGVNE STGLSLEQVK KLKERWGSNE LPAEEGKTLL
60 70 80 90 100
ELVIEQFEDL LVRILLLAAC ISFVLAWFEE GEETITAFVE PFVILLILVA
110 120 130 140 150
NAIVGVWQER NAENAIEALK EYEPEMGKVY RQDRKSVQRI KAKDIVPGDI
160 170 180 190 200
VEIAVGDKVP ADIRLTSIKS TTLRVDQSIL TGESVSVIKH TDPVPDPRAV
210 220 230 240 250
NQDKKNMLFS GTNIAAGKAM GVVVATGVNT EIGKIRDEMV ATEQERTPLQ
260 270 280 290 300
QKLDEFGEQL SKVISLICIA VWIINIGHFN DPVHGGSWIR GAIYYFKIAV
310 320 330 340 350
ALAVAAIPEG LPAVITTCLA LGTRRMAKKN AIVRSLPSVE TLGCTSVICS
360 370 380 390 400
DKTGTLTTNQ MSVCRMFILD RVEGDTCSLN EFTITGSTYA PIGEVHKDDK
410 420 430 440 450
PVNCHQYDGL VELATICALC NDSALDYNEA KGVYEKVGEA TETALTCLVE
460 470 480 490 500
KMNVFDTELK GLSKIERANA CNSVIKQLMK KEFTLEFSRD RKSMSVYCTP
510 520 530 540 550
NKPSRTSMSK MFVKGAPEGV IDRCTHIRVG STKVPMTSGV KQKIMSVIRE
560 570 580 590 600
WGSGSDTLRC LALATHDNPL RREEMHLEDS ANFIKYETNL TFVGCVGMLD
610 620 630 640 650
PPRIEVASSV KLCRQAGIRV IMITGDNKGT AVAICRRIGI FGQDEDVTSK
660 670 680 690 700
AFTGREFDEL NPSAQRDACL NARCFARVEP SHKSKIVEFL QSFDEITAMT
710 720 730 740 750
GDGVNDAPAL KKAEIGIAMG SGTAVAKTAS EMVLADDNFS TIVAAVEEGR
760 770 780 790 800
AIYNNMKQFI RYLISSNVGE VVCIFLTAAL GFPEALIPVQ LLWVNLVTDG
810 820 830 840 850
LPATALGFNP PDLDIMNKPP RNPKEPLISG WLFFRYLAIG CYVGAATVGA
860 870 880 890 900
AAWWFIAADG GPRVSFYQLS HFLQCKEDNP DFEGVDCAIF ESPYPMTMAL
910 920 930 940 950
SVLVTIEMCN ALNSLSENQS LLRMPPWENI WLVGSICLSM SLHFLILYVE
960 970 980 990 1000
PLPLIFQITP LNVTQWLMVL KISLPVILMD ETLKFVARNY LEPGKECVQP
1010 1020 1030 1040
ATKSCSFSAC TDGISWPFVL LIMPLVIWVY STDTNFSDMF WS
Note: Ubiquitous housekeeping isoform.
Length:1,042
Mass (Da):114,757
Last modified:August 1, 1990 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i5462FF2DA7FB630A
GO
Isoform 2 (identifier: P16615-2) [UniParc]FASTAAdd to basket
Also known as: ATP2A2A, Class 1, HK2, SERCA2a

The sequence of this isoform differs from the canonical sequence as follows:
     994-1042: GKECVQPATKSCSFSACTDGISWPFVLLIMPLVIWVYSTDTNFSDMFWS → AILE

Note: Cardiac/slow twitch, muscle specific isoform. Has a lower affinity for calcium and a higher catalytic turnover rate.
Show »
Length:997
Mass (Da):109,691
Checksum:iDD57D12A2B24FEC1
GO
Isoform 3 (identifier: P16615-3) [UniParc]FASTAAdd to basket
Also known as: SERCA2C

The sequence of this isoform differs from the canonical sequence as follows:
     994-1042: GKECVQPATKSCSFSACTDGISWPFVLLIMPLVIWVYSTDTNFSDMFWS → VLSSEL

Note: May be due to intron retention. Shows a lower apparent affinity for cytosolic calcium than isoform 2 and a catalytic turnover rate similar to isoform 1.
Show »
Length:999
Mass (Da):109,893
Checksum:iF6BE03E546453B24
GO
Isoform 4 (identifier: P16615-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     155-181: Missing.

Note: No experimental confirmation available.
Show »
Length:1,015
Mass (Da):111,847
Checksum:i6C99B5C382834A63
GO
Isoform 5 (identifier: P16615-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     994-1042: GKECVQPATKSCSFSACTDGISWPFVLLIMPLVIWVYSTDTNFSDMFWS → DIIK

Note: No experimental confirmation available.
Show »
Length:997
Mass (Da):109,734
Checksum:iD570A12D5B24FEC1
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 4 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
H7C5W9H7C5W9_HUMAN
Sarcoplasmic/endoplasmic reticulum ...
ATP2A2
933Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
J3QSY6J3QSY6_HUMAN
Sarcoplasmic/endoplasmic reticulum ...
ATP2A2
50Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A0C4DH86A0A0C4DH86_HUMAN
Sarcoplasmic/endoplasmic reticulum ...
ATP2A2
46Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
F8W1Z7F8W1Z7_HUMAN
Sarcoplasmic/endoplasmic reticulum ...
ATP2A2
44Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence BAG57266 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_00860823G → E in DD. 1 PublicationCorresponds to variant dbSNP:rs28929478EnsemblClinVar.1
Natural variantiVAR_00860939N → T in DD. 1 Publication1
Natural variantiVAR_06339841Missing in DD; comedonal type. 1 Publication1
Natural variantiVAR_00861047K → KMFLTGK in DD. 1
Natural variantiVAR_00861165L → S in DD; severe form. 1
Natural variantiVAR_07968574 – 108Missing in DD. 1 PublicationAdd BLAST35
Natural variantiVAR_079686101N → S in DD. 1 Publication1
Natural variantiVAR_008612131R → Q in DD. 1 PublicationCorresponds to variant dbSNP:rs121912738EnsemblClinVar.1
Natural variantiVAR_008613160P → L in DD. 1
Natural variantiVAR_008614186S → P in DD. 1
Natural variantiVAR_079687194 – 197Missing in DD. 1 Publication4
Natural variantiVAR_008615211G → D in DD; severe form. 1
Natural variantiVAR_008616223V → M in DD. 1
Natural variantiVAR_008617268C → F in DD; haemorrhagic lesions. Corresponds to variant dbSNP:rs121912733EnsemblClinVar.1
Natural variantiVAR_008618310G → V in DD. 1
Natural variantiVAR_008619318C → R in DD; severe form. 1
Natural variantiVAR_008620348I → T in DD. 1
Natural variantiVAR_009508357T → K in DD. 1 Publication1
Natural variantiVAR_008621412E → G in DD. 1
Natural variantiVAR_008622495S → F in DD. 1 Publication1
Natural variantiVAR_008623560C → R in DD; neuropsychiatric phenotype. 1 PublicationCorresponds to variant dbSNP:rs121912734EnsemblClinVar.1
Natural variantiVAR_079688590L → P in DD. 1 Publication1
Natural variantiVAR_017532602P → L in AKV; loss of activity. 1 PublicationCorresponds to variant dbSNP:rs121912737EnsemblClinVar.1
Natural variantiVAR_079689625G → A in DD. 1 Publication1
Natural variantiVAR_079690626D → E in DD. 1 Publication1
Natural variantiVAR_079691666 – 1042Missing in DD. 1 PublicationAdd BLAST377
Natural variantiVAR_079692672A → P in DD. 1 Publication1
Natural variantiVAR_008624675F → S in DD; multiple neuropsychiatric features. 1
Natural variantiVAR_008625683K → E in DD; depression. 1
Natural variantiVAR_079693691Q → P in DD. 1 Publication1
Natural variantiVAR_008626702D → N in DD; moderate form. 1
Natural variantiVAR_008627745A → D in DD; moderate form. 1
Natural variantiVAR_009509749G → R in DD. 1 Publication1
Natural variantiVAR_079694750R → W in DD. 1 Publication1
Natural variantiVAR_008628754Missing in DD. 1
Natural variantiVAR_008629765S → L in DD. 1 Publication1
Natural variantiVAR_079695765S → W in DD. 1 Publication1
Natural variantiVAR_008630767N → S in DD; haemorrhagic lesions and neuropsychiatric phenotype. Corresponds to variant dbSNP:rs121912732EnsemblClinVar.1
Natural variantiVAR_008631769G → R in DD. Corresponds to variant dbSNP:rs121912736EnsemblClinVar.1
Natural variantiVAR_008632803A → T in DD; mild/moderate form. 1
Natural variantiVAR_008633838A → P in DD; severe form; petit mal epilepsy. 1
Natural variantiVAR_008634843V → F in DD; depression. 1
Natural variantiVAR_079696849G → GG in DD. 1 Publication1
Natural variantiVAR_008635875C → G in DD; retinitis pigmentosa. 1
Natural variantiVAR_079697900L → P in DD. 1 Publication1
Natural variantiVAR_008636920S → Y in DD; mild/moderate/severe form; one patient with epilepsy. 1
Natural variantiVAR_008637943H → R in DD; learning difficulties. 1 Publication1
Natural variantiVAR_008638975P → R in DD. 1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_039392155 – 181Missing in isoform 4. 1 PublicationAdd BLAST27
Alternative sequenceiVSP_000358994 – 1042GKECV…DMFWS → AILE in isoform 2. 1 PublicationAdd BLAST49
Alternative sequenceiVSP_039393994 – 1042GKECV…DMFWS → VLSSEL in isoform 3. 1 PublicationAdd BLAST49
Alternative sequenceiVSP_039394994 – 1042GKECV…DMFWS → DIIK in isoform 5. CuratedAdd BLAST49

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
M23114 mRNA Translation: AAA53193.1
M23116 Genomic DNA Translation: AAA52757.1
M23115 mRNA Translation: AAA53194.1
M23278, M23116 Genomic DNA Translation: AAA52758.1
AC006088 Genomic DNA No translation available.
BC035588 mRNA Translation: AAH35588.1
AK293877 mRNA Translation: BAG57266.1 Different initiation.
AY186578 mRNA Translation: AAO47398.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS9143.1 [P16615-2]
CCDS9144.1 [P16615-1]

Protein sequence database of the Protein Information Resource

More...
PIRi
A31981
B31981

NCBI Reference Sequences

More...
RefSeqi
NP_001672.1, NM_001681.3 [P16615-2]
NP_733765.1, NM_170665.3 [P16615-1]
XP_005253945.1, XM_005253888.2 [P16615-3]
XP_011536704.1, XM_011538402.2 [P16615-3]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000308664; ENSP00000311186; ENSG00000174437 [P16615-2]
ENST00000539276; ENSP00000440045; ENSG00000174437 [P16615-1]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
488

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:488

UCSC genome browser

More...
UCSCi
uc001tqk.5 human [P16615-1]

Keywords - Coding sequence diversityi

Alternative splicing

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M23114 mRNA Translation: AAA53193.1
M23116 Genomic DNA Translation: AAA52757.1
M23115 mRNA Translation: AAA53194.1
M23278, M23116 Genomic DNA Translation: AAA52758.1
AC006088 Genomic DNA No translation available.
BC035588 mRNA Translation: AAH35588.1
AK293877 mRNA Translation: BAG57266.1 Different initiation.
AY186578 mRNA Translation: AAO47398.1
CCDSiCCDS9143.1 [P16615-2]
CCDS9144.1 [P16615-1]
PIRiA31981
B31981
RefSeqiNP_001672.1, NM_001681.3 [P16615-2]
NP_733765.1, NM_170665.3 [P16615-1]
XP_005253945.1, XM_005253888.2 [P16615-3]
XP_011536704.1, XM_011538402.2 [P16615-3]

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5ZTFX-ray3.45A1-1042[»]
6JJUX-ray3.20A1-993[»]
SMRiP16615
ModBaseiSearch...

Protein-protein interaction databases

BioGridi106978, 120 interactors
CORUMiP16615
DIPiDIP-33868N
IntActiP16615, 99 interactors
MINTiP16615
STRINGi9606.ENSP00000440045

Chemistry databases

ChEMBLiCHEMBL3901
DrugBankiDB06157 Istaroxime

Protein family/group databases

TCDBi3.A.3.2.7 the p-type atpase (p-atpase) superfamily

PTM databases

iPTMnetiP16615
PhosphoSitePlusiP16615
SwissPalmiP16615

Polymorphism and mutation databases

BioMutaiATP2A2
DMDMi114312

Proteomic databases

EPDiP16615
jPOSTiP16615
MassIVEiP16615
MaxQBiP16615
PaxDbiP16615
PeptideAtlasiP16615
PRIDEiP16615
ProteomicsDBi53385 [P16615-1]
53386 [P16615-2]
53387 [P16615-3]
53388 [P16615-4]
53389 [P16615-5]

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000308664; ENSP00000311186; ENSG00000174437 [P16615-2]
ENST00000539276; ENSP00000440045; ENSG00000174437 [P16615-1]
GeneIDi488
KEGGihsa:488
UCSCiuc001tqk.5 human [P16615-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
488
DisGeNETi488

GeneCards: human genes, protein and diseases

More...
GeneCardsi
ATP2A2
HGNCiHGNC:812 ATP2A2
HPAiHPA062605
HPA067892
MalaCardsiATP2A2
MIMi101900 phenotype
108740 gene
124200 phenotype
neXtProtiNX_P16615
OpenTargetsiENSG00000174437
Orphaneti79151 Acrokeratosis verruciformis of Hopf
218 Darier disease
PharmGKBiPA71

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG0202 Eukaryota
COG0474 LUCA
GeneTreeiENSGT00940000159986
HOGENOMiHOG000265621
InParanoidiP16615
KOiK05853
OMAiDPPTPLW
OrthoDBi100699at2759
PhylomeDBiP16615
TreeFamiTF300651

Enzyme and pathway databases

ReactomeiR-HSA-1912420 Pre-NOTCH Processing in Golgi
R-HSA-418359 Reduction of cytosolic Ca++ levels
R-HSA-5578775 Ion homeostasis
R-HSA-936837 Ion transport by P-type ATPases
SignaLinkiP16615
SIGNORiP16615

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
ATP2A2 human

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
488

Pharos

More...
Pharosi
P16615

Protein Ontology

More...
PROi
PR:P16615

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000174437 Expressed in 244 organ(s), highest expression level in heart
ExpressionAtlasiP16615 baseline and differential
GenevisibleiP16615 HS

Family and domain databases

Gene3Di3.40.1110.10, 1 hit
3.40.50.1000, 1 hit
InterProiView protein in InterPro
IPR006068 ATPase_P-typ_cation-transptr_C
IPR004014 ATPase_P-typ_cation-transptr_N
IPR023299 ATPase_P-typ_cyto_dom_N
IPR018303 ATPase_P-typ_P_site
IPR023298 ATPase_P-typ_TM_dom_sf
IPR008250 ATPase_P-typ_transduc_dom_A_sf
IPR036412 HAD-like_sf
IPR023214 HAD_sf
IPR005782 P-type_ATPase_IIA
IPR001757 P_typ_ATPase
IPR030332 SERCA1/2
PANTHERiPTHR42861:SF18 PTHR42861:SF18, 1 hit
PfamiView protein in Pfam
PF00689 Cation_ATPase_C, 1 hit
PF00690 Cation_ATPase_N, 1 hit
PRINTSiPR00120 HATPASE
SMARTiView protein in SMART
SM00831 Cation_ATPase_N, 1 hit
SUPFAMiSSF56784 SSF56784, 1 hit
SSF81653 SSF81653, 1 hit
SSF81660 SSF81660, 1 hit
SSF81665 SSF81665, 1 hit
TIGRFAMsiTIGR01116 ATPase-IIA1_Ca, 1 hit
TIGR01494 ATPase_P-type, 2 hits
PROSITEiView protein in PROSITE
PS00154 ATPASE_E1_E2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiAT2A2_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P16615
Secondary accession number(s): A6NDN7
, B4DF05, P16614, Q86VJ2
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: September 18, 2019
This is version 228 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
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