P16615 · AT2A2_HUMAN
- ProteinSarcoplasmic/endoplasmic reticulum calcium ATPase 2
- GeneATP2A2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1042 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Involved in autophagy in response to starvation. Upon interaction with VMP1 and activation, controls ER-isolation membrane contacts for autophagosome formation (PubMed:28890335).
Also modulates ER contacts with lipid droplets, mitochondria and endosomes (PubMed:28890335).
In coordination with FLVCR2 mediates heme-stimulated switching from mitochondrial ATP synthesis to thermogenesis (By similarity).
Isoform 2
Catalytic activity
- ATP + Ca2+(in) + H2O = ADP + Ca2+(out) + H+ + phosphateThis reaction proceeds in the forward direction.
CHEBI:30616 + Ca2+ (in)CHEBI:29108+ CHEBI:15377 = CHEBI:456216 + Ca2+ (out)CHEBI:29108+ CHEBI:15378 + CHEBI:43474
Cofactor
Activity regulation
Enhanced by DWORF; DWORF increases activity by displacing sarcolipin (SLN), phospholamban (PLN) and myoregulin (MRLN) (By similarity).
Stabilizes SERCA2 in its E2 state (PubMed:28890335).
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 304 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Binding site | 305 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 307 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: I | ||||||
Binding site | 309 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Active site | 351 | 4-aspartylphosphate intermediate | ||||
Sequence: D | ||||||
Binding site | 351 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 353 | ATP (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 353 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 442 | ATP (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 489 | ATP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 514 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 559 | ATP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 624 | ATP (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 625 | ATP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 626 | ATP (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 677 | ATP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 683 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 702 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 705 | ATP (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 767 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 770 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 795 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 798 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 799 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 799 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 907 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: E |
GO annotations
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameSarcoplasmic/endoplasmic reticulum calcium ATPase 2
- EC number
- Short namesSERCA2; SR Ca(2+)-ATPase 2
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP16615
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-48 | Cytoplasmic | ||||
Sequence: MENAHTKTVEEVLGHFGVNESTGLSLEQVKKLKERWGSNELPAEEGKT | ||||||
Transmembrane | 49-69 | Helical; Name=1 | ||||
Sequence: LLELVIEQFEDLLVRILLLAA | ||||||
Topological domain | 70-89 | Lumenal | ||||
Sequence: CISFVLAWFEEGEETITAFV | ||||||
Transmembrane | 90-110 | Helical; Name=2 | ||||
Sequence: EPFVILLILVANAIVGVWQER | ||||||
Topological domain | 111-253 | Cytoplasmic | ||||
Sequence: NAENAIEALKEYEPEMGKVYRQDRKSVQRIKAKDIVPGDIVEIAVGDKVPADIRLTSIKSTTLRVDQSILTGESVSVIKHTDPVPDPRAVNQDKKNMLFSGTNIAAGKAMGVVVATGVNTEIGKIRDEMVATEQERTPLQQKL | ||||||
Transmembrane | 254-273 | Helical; Name=3 | ||||
Sequence: DEFGEQLSKVISLICIAVWI | ||||||
Topological domain | 274-295 | Lumenal | ||||
Sequence: INIGHFNDPVHGGSWIRGAIYY | ||||||
Transmembrane | 296-313 | Helical; Name=4 | ||||
Sequence: FKIAVALAVAAIPEGLPA | ||||||
Topological domain | 314-756 | Cytoplasmic | ||||
Sequence: VITTCLALGTRRMAKKNAIVRSLPSVETLGCTSVICSDKTGTLTTNQMSVCRMFILDRVEGDTCSLNEFTITGSTYAPIGEVHKDDKPVNCHQYDGLVELATICALCNDSALDYNEAKGVYEKVGEATETALTCLVEKMNVFDTELKGLSKIERANACNSVIKQLMKKEFTLEFSRDRKSMSVYCTPNKPSRTSMSKMFVKGAPEGVIDRCTHIRVGSTKVPMTSGVKQKIMSVIREWGSGSDTLRCLALATHDNPLRREEMHLEDSANFIKYETNLTFVGCVGMLDPPRIEVASSVKLCRQAGIRVIMITGDNKGTAVAICRRIGIFGQDEDVTSKAFTGREFDELNPSAQRDACLNARCFARVEPSHKSKIVEFLQSFDEITAMTGDGVNDAPALKKAEIGIAMGSGTAVAKTASEMVLADDNFSTIVAAVEEGRAIYNNM | ||||||
Transmembrane | 757-776 | Helical; Name=5 | ||||
Sequence: KQFIRYLISSNVGEVVCIFL | ||||||
Topological domain | 777-786 | Lumenal | ||||
Sequence: TAALGFPEAL | ||||||
Transmembrane | 787-807 | Helical; Name=6 | ||||
Sequence: IPVQLLWVNLVTDGLPATALG | ||||||
Topological domain | 808-827 | Cytoplasmic | ||||
Sequence: FNPPDLDIMNKPPRNPKEPL | ||||||
Transmembrane | 828-850 | Helical; Name=7 | ||||
Sequence: ISGWLFFRYLAIGCYVGAATVGA | ||||||
Topological domain | 851-896 | Lumenal | ||||
Sequence: AAWWFIAADGGPRVSFYQLSHFLQCKEDNPDFEGVDCAIFESPYPM | ||||||
Transmembrane | 897-916 | Helical; Name=8 | ||||
Sequence: TMALSVLVTIEMCNALNSLS | ||||||
Topological domain | 917-929 | Cytoplasmic | ||||
Sequence: ENQSLLRMPPWEN | ||||||
Transmembrane | 930-948 | Helical; Name=9 | ||||
Sequence: IWLVGSICLSMSLHFLILY | ||||||
Topological domain | 949-963 | Lumenal | ||||
Sequence: VEPLPLIFQITPLNV | ||||||
Transmembrane | 964-984 | Helical; Name=10 | ||||
Sequence: TQWLMVLKISLPVILMDETLK | ||||||
Topological domain | 985-1042 | Cytoplasmic | ||||
Sequence: FVARNYLEPGKECVQPATKSCSFSACTDGISWPFVLLIMPLVIWVYSTDTNFSDMFWS |
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Acrokeratosis verruciformis (AKV)
- Note
- 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.
- See alsoMIM:101900
Natural variants in AKV
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_017532 | 602 | P>L | in AKV; no effect on protein abundance; loss of calcium ion transmembrane transport; dbSNP:rs121912737 |
Darier disease (DD)
- Note
- 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 intellectual disability, 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.
- See alsoMIM:124200
Natural variants in DD
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_008608 | 23 | G>E | in DD; dbSNP:rs28929478 | |
VAR_008609 | 39 | N>T | in DD | |
VAR_063398 | 41 | missing | in DD; comedonal type | |
VAR_008610 | 47 | K>KMFLTGK | in DD | |
VAR_008611 | 65 | L>S | in DD; severe form | |
VAR_079685 | 74-108 | missing | in DD | |
VAR_079686 | 101 | N>S | in DD; dbSNP:rs1873379168 | |
VAR_008612 | 131 | R>Q | in DD; dbSNP:rs121912738 | |
VAR_008613 | 160 | P>L | in DD | |
VAR_008614 | 186 | S>P | in DD | |
VAR_079687 | 194-197 | missing | in DD | |
VAR_008615 | 211 | G>D | in DD; severe form | |
VAR_008616 | 223 | V>M | in DD | |
VAR_008617 | 268 | C>F | in DD; haemorrhagic lesions; dbSNP:rs121912733 | |
VAR_008618 | 310 | G>V | in DD | |
VAR_008619 | 318 | C>R | in DD; severe form | |
VAR_008620 | 348 | I>T | in DD | |
VAR_009508 | 357 | T>K | in DD | |
VAR_008621 | 412 | E>G | in DD | |
VAR_008622 | 495 | S>F | in DD | |
VAR_008623 | 560 | C>R | in DD; neuropsychiatric phenotype; dbSNP:rs121912734 | |
VAR_079688 | 590 | L>P | in DD | |
VAR_079689 | 625 | G>A | in DD | |
VAR_079690 | 626 | D>E | in DD | |
VAR_079691 | 666-1042 | missing | in DD | |
VAR_079692 | 672 | A>P | in DD | |
VAR_008624 | 675 | F>S | in DD; multiple neuropsychiatric features | |
VAR_008625 | 683 | K>E | in DD; depression | |
VAR_079693 | 691 | Q>P | in DD | |
VAR_008626 | 702 | D>N | in DD; moderate form | |
VAR_008627 | 745 | A>D | in DD; moderate form | |
VAR_009509 | 749 | G>R | in DD | |
VAR_079694 | 750 | R>W | in DD | |
VAR_008628 | 754 | missing | in DD | |
VAR_008629 | 765 | S>L | in DD | |
VAR_079695 | 765 | S>W | in DD | |
VAR_008630 | 767 | N>S | in DD; haemorrhagic lesions and neuropsychiatric phenotype; dbSNP:rs121912732 | |
VAR_008631 | 769 | G>R | in DD; dbSNP:rs121912736 | |
VAR_008632 | 803 | A>T | in DD; mild/moderate form | |
VAR_008633 | 838 | A>P | in DD; severe form; petit mal epilepsy | |
VAR_008634 | 843 | V>F | in DD; depression | |
VAR_079696 | 849 | G>GG | in DD | |
VAR_008635 | 875 | C>G | in DD; retinitis pigmentosa | |
VAR_079697 | 900 | L>P | in DD | |
VAR_008636 | 920 | S>Y | in DD; mild/moderate/severe form; one patient with epilepsy | |
VAR_008637 | 943 | H>R | in DD; learning difficulties | |
VAR_008638 | 975 | P>R | in DD |
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_008608 | 23 | in DD; dbSNP:rs28929478 | |||
Sequence: G → E | ||||||
Natural variant | VAR_008609 | 39 | in DD | |||
Sequence: N → T | ||||||
Natural variant | VAR_063398 | 41 | in DD; comedonal type | |||
Sequence: Missing | ||||||
Natural variant | VAR_008610 | 47 | in DD | |||
Sequence: K → KMFLTGK | ||||||
Natural variant | VAR_008611 | 65 | in DD; severe form | |||
Sequence: L → S | ||||||
Natural variant | VAR_079685 | 74-108 | in DD | |||
Sequence: Missing | ||||||
Natural variant | VAR_079686 | 101 | in DD; dbSNP:rs1873379168 | |||
Sequence: N → S | ||||||
Natural variant | VAR_008612 | 131 | in DD; dbSNP:rs121912738 | |||
Sequence: R → Q | ||||||
Natural variant | VAR_008613 | 160 | in DD | |||
Sequence: P → L | ||||||
Natural variant | VAR_008614 | 186 | in DD | |||
Sequence: S → P | ||||||
Natural variant | VAR_079687 | 194-197 | in DD | |||
Sequence: Missing | ||||||
Natural variant | VAR_008615 | 211 | in DD; severe form | |||
Sequence: G → D | ||||||
Natural variant | VAR_008616 | 223 | in DD | |||
Sequence: V → M | ||||||
Mutagenesis | 256 | No effect on interaction with VMP1. | ||||
Sequence: F → V | ||||||
Natural variant | VAR_008617 | 268 | in DD; haemorrhagic lesions; dbSNP:rs121912733 | |||
Sequence: C → F | ||||||
Natural variant | VAR_008618 | 310 | in DD | |||
Sequence: G → V | ||||||
Natural variant | VAR_008619 | 318 | in DD; severe form | |||
Sequence: C → R | ||||||
Natural variant | VAR_008620 | 348 | in DD | |||
Sequence: I → T | ||||||
Natural variant | VAR_009508 | 357 | in DD | |||
Sequence: T → K | ||||||
Natural variant | VAR_008621 | 412 | in DD | |||
Sequence: E → G | ||||||
Natural variant | VAR_008622 | 495 | in DD | |||
Sequence: S → F | ||||||
Natural variant | VAR_008623 | 560 | in DD; neuropsychiatric phenotype; dbSNP:rs121912734 | |||
Sequence: C → R | ||||||
Natural variant | VAR_079688 | 590 | in DD | |||
Sequence: L → P | ||||||
Natural variant | VAR_017532 | 602 | in AKV; no effect on protein abundance; loss of calcium ion transmembrane transport; dbSNP:rs121912737 | |||
Sequence: P → L | ||||||
Natural variant | VAR_079689 | 625 | in DD | |||
Sequence: G → A | ||||||
Natural variant | VAR_079690 | 626 | in DD | |||
Sequence: D → E | ||||||
Natural variant | VAR_079691 | 666-1042 | in DD | |||
Sequence: Missing | ||||||
Natural variant | VAR_079692 | 672 | in DD | |||
Sequence: A → P | ||||||
Natural variant | VAR_008624 | 675 | in DD; multiple neuropsychiatric features | |||
Sequence: F → S | ||||||
Natural variant | VAR_008625 | 683 | in DD; depression | |||
Sequence: K → E | ||||||
Natural variant | VAR_079693 | 691 | in DD | |||
Sequence: Q → P | ||||||
Natural variant | VAR_008626 | 702 | in DD; moderate form | |||
Sequence: D → N | ||||||
Natural variant | VAR_008627 | 745 | in DD; moderate form | |||
Sequence: A → D | ||||||
Natural variant | VAR_009509 | 749 | in DD | |||
Sequence: G → R | ||||||
Natural variant | VAR_079694 | 750 | in DD | |||
Sequence: R → W | ||||||
Natural variant | VAR_008628 | 754 | in DD | |||
Sequence: Missing | ||||||
Natural variant | VAR_008629 | 765 | in DD | |||
Sequence: S → L | ||||||
Natural variant | VAR_079695 | 765 | in DD | |||
Sequence: S → W | ||||||
Natural variant | VAR_008630 | 767 | in DD; haemorrhagic lesions and neuropsychiatric phenotype; dbSNP:rs121912732 | |||
Sequence: N → S | ||||||
Natural variant | VAR_008631 | 769 | in DD; dbSNP:rs121912736 | |||
Sequence: G → R | ||||||
Natural variant | VAR_008632 | 803 | in DD; mild/moderate form | |||
Sequence: A → T | ||||||
Natural variant | VAR_008633 | 838 | in DD; severe form; petit mal epilepsy | |||
Sequence: A → P | ||||||
Natural variant | VAR_008634 | 843 | in DD; depression | |||
Sequence: V → F | ||||||
Natural variant | VAR_079696 | 849 | in DD | |||
Sequence: G → GG | ||||||
Natural variant | VAR_008635 | 875 | in DD; retinitis pigmentosa | |||
Sequence: C → G | ||||||
Natural variant | VAR_079697 | 900 | in DD | |||
Sequence: L → P | ||||||
Natural variant | VAR_008636 | 920 | in DD; mild/moderate/severe form; one patient with epilepsy | |||
Sequence: S → Y | ||||||
Natural variant | VAR_008637 | 943 | in DD; learning difficulties | |||
Sequence: H → R | ||||||
Natural variant | VAR_008638 | 975 | in DD | |||
Sequence: P → R |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 736 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue, modified residue (large scale data), disulfide bond.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000046196 | 1-1042 | UniProt | Sarcoplasmic/endoplasmic reticulum calcium ATPase 2 | |||
Sequence: MENAHTKTVEEVLGHFGVNESTGLSLEQVKKLKERWGSNELPAEEGKTLLELVIEQFEDLLVRILLLAACISFVLAWFEEGEETITAFVEPFVILLILVANAIVGVWQERNAENAIEALKEYEPEMGKVYRQDRKSVQRIKAKDIVPGDIVEIAVGDKVPADIRLTSIKSTTLRVDQSILTGESVSVIKHTDPVPDPRAVNQDKKNMLFSGTNIAAGKAMGVVVATGVNTEIGKIRDEMVATEQERTPLQQKLDEFGEQLSKVISLICIAVWIINIGHFNDPVHGGSWIRGAIYYFKIAVALAVAAIPEGLPAVITTCLALGTRRMAKKNAIVRSLPSVETLGCTSVICSDKTGTLTTNQMSVCRMFILDRVEGDTCSLNEFTITGSTYAPIGEVHKDDKPVNCHQYDGLVELATICALCNDSALDYNEAKGVYEKVGEATETALTCLVEKMNVFDTELKGLSKIERANACNSVIKQLMKKEFTLEFSRDRKSMSVYCTPNKPSRTSMSKMFVKGAPEGVIDRCTHIRVGSTKVPMTSGVKQKIMSVIREWGSGSDTLRCLALATHDNPLRREEMHLEDSANFIKYETNLTFVGCVGMLDPPRIEVASSVKLCRQAGIRVIMITGDNKGTAVAICRRIGIFGQDEDVTSKAFTGREFDELNPSAQRDACLNARCFARVEPSHKSKIVEFLQSFDEITAMTGDGVNDAPALKKAEIGIAMGSGTAVAKTASEMVLADDNFSTIVAAVEEGRAIYNNMKQFIRYLISSNVGEVVCIFLTAALGFPEALIPVQLLWVNLVTDGLPATALGFNPPDLDIMNKPPRNPKEPLISGWLFFRYLAIGCYVGAATVGAAAWWFIAADGGPRVSFYQLSHFLQCKEDNPDFEGVDCAIFESPYPMTMALSVLVTIEMCNALNSLSENQSLLRMPPWENIWLVGSICLSMSLHFLILYVEPLPLIFQITPLNVTQWLMVLKISLPVILMDETLKFVARNYLEPGKECVQPATKSCSFSACTDGISWPFVLLIMPLVIWVYSTDTNFSDMFWS | |||||||
Modified residue | 38 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 38 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 170 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 186 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 294 | UniProt | 3'-nitrotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 295 | UniProt | 3'-nitrotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 338 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 346 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 357 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 358 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 362 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 378 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 441 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 441 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 443 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 473 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 488 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 497 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 499 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 504 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 525 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 531 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 532 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 553 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 555 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 580 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 580 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 608 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 653 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 663 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 663 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Disulfide bond | 875↔887 | UniProt | |||||
Sequence: CKEDNPDFEGVDC |
Post-translational modification
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Gene expression databases
Organism-specific databases
Interaction
Subunit
Interacts with phospholamban (PLN); the interaction inhibits ATP2A2 Ca2+ affinity (PubMed:28890335).
Interacts with myoregulin (MRLN) (By similarity).
Interacts with DWORF (By similarity).
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).
Interacts with TMX1 (PubMed:27502484).
Interacts with TMX2 (PubMed:31735293).
Interacts with VMP1; VMP1 competes with PLN and SLN to prevent them from forming an inhibitory complex with ATP2A2 (PubMed:28890335).
Interacts with ULK1 (PubMed:28890335).
Interacts with S100A1 in a Ca2+-dependent manner (PubMed:12804600).
Interacts with TUNAR (By similarity).
Interacts with FLVCR2; this interaction occurs in the absence of heme and promotes ATP2A2 proteasomal degradation; this complex is dissociated upon heme binding (By similarity).
Interacts with FNIP1 (By similarity).
Isoform 1
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P16615 | F2RL1 P55085 | 2 | EBI-358933, EBI-4303189 | |
BINARY | P16615 | OPRD1 P41143 | 3 | EBI-358933, EBI-2624456 | |
BINARY | P16615 | WFS1 O76024 | 3 | EBI-358933, EBI-720609 | |
BINARY | P16615-1 | CFTR P13569 | 6 | EBI-11613988, EBI-349854 | |
XENO | P16615-1 | Piezo1 E2JF22 | 2 | EBI-11613988, EBI-9837938 |
Protein-protein interaction databases
Chemistry
Miscellaneous
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 575-594 | Interaction with HAX1 | ||||
Sequence: MHLEDSANFIKYETNLTFVG | ||||||
Region | 787-807 | Interaction with PLN | ||||
Sequence: IPVQLLWVNLVTDGLPATALG | ||||||
Region | 788-1042 | Interaction with TMEM64 and PDIA3 | ||||
Sequence: PVQLLWVNLVTDGLPATALGFNPPDLDIMNKPPRNPKEPLISGWLFFRYLAIGCYVGAATVGAAAWWFIAADGGPRVSFYQLSHFLQCKEDNPDFEGVDCAIFESPYPMTMALSVLVTIEMCNALNSLSENQSLLRMPPWENIWLVGSICLSMSLHFLILYVEPLPLIFQITPLNVTQWLMVLKISLPVILMDETLKFVARNYLEPGKECVQPATKSCSFSACTDGISWPFVLLIMPLVIWVYSTDTNFSDMFWS | ||||||
Region | 931-942 | Interaction with PLN | ||||
Sequence: WLVGSICLSMSL |
Domain
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 5 isoforms produced by Alternative splicing. SERCA2 transcripts differ only in their 3'-UTR region and are expressed in a tissue-specific manner.
P16615-1
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.
- Name1
- SynonymsATP2A2B, Class 2-4, HK1, SERCA2b
- NoteUbiquitous housekeeping isoform.
- Length1,042
- Mass (Da)114,757
- Last updated1990-08-01 v1
- Checksum5462FF2DA7FB630A
P16615-2
- Name2
- SynonymsATP2A2A, Class 1, HK2, SERCA2a
- NoteCardiac/slow twitch, muscle specific isoform. Has a lower affinity for calcium and a higher catalytic turnover rate.
- Differences from canonical
- 994-1042: GKECVQPATKSCSFSACTDGISWPFVLLIMPLVIWVYSTDTNFSDMFWS → AILE
P16615-3
- Name3
- SynonymsSERCA2C
- Differences from canonical
- 994-1042: GKECVQPATKSCSFSACTDGISWPFVLLIMPLVIWVYSTDTNFSDMFWS → VLSSEL
P16615-4
- Name4
- Differences from canonical
- 155-181: Missing
P16615-5
- Name5
- Differences from canonical
- 994-1042: GKECVQPATKSCSFSACTDGISWPFVLLIMPLVIWVYSTDTNFSDMFWS → DIIK
Computationally mapped potential isoform sequences
There are 4 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
F8W1Z7 | F8W1Z7_HUMAN | ATP2A2 | 21 | ||
A0A0C4DH86 | A0A0C4DH86_HUMAN | ATP2A2 | 46 | ||
H7C5W9 | H7C5W9_HUMAN | ATP2A2 | 933 | ||
J3QSY6 | J3QSY6_HUMAN | ATP2A2 | 50 |
Sequence caution
Features
Showing features for alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_039392 | 155-181 | in isoform 4 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_000358 | 994-1042 | in isoform 2 | |||
Sequence: GKECVQPATKSCSFSACTDGISWPFVLLIMPLVIWVYSTDTNFSDMFWS → AILE | ||||||
Alternative sequence | VSP_039393 | 994-1042 | in isoform 3 | |||
Sequence: GKECVQPATKSCSFSACTDGISWPFVLLIMPLVIWVYSTDTNFSDMFWS → VLSSEL | ||||||
Alternative sequence | VSP_039394 | 994-1042 | in isoform 5 | |||
Sequence: GKECVQPATKSCSFSACTDGISWPFVLLIMPLVIWVYSTDTNFSDMFWS → DIIK |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M23114 EMBL· GenBank· DDBJ | AAA53193.1 EMBL· GenBank· DDBJ | mRNA | ||
M23116 EMBL· GenBank· DDBJ | AAA52757.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M23115 EMBL· GenBank· DDBJ | AAA53194.1 EMBL· GenBank· DDBJ | mRNA | ||
M23278 EMBL· GenBank· DDBJ | AAA52758.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M23116 EMBL· GenBank· DDBJ | AAA52758.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AC006088 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC035588 EMBL· GenBank· DDBJ | AAH35588.1 EMBL· GenBank· DDBJ | mRNA | ||
AK293877 EMBL· GenBank· DDBJ | BAG57266.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AY186578 EMBL· GenBank· DDBJ | AAO47398.1 EMBL· GenBank· DDBJ | mRNA |