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O14983

- AT2A1_HUMAN

UniProt

O14983 - AT2A1_HUMAN

Protein

Sarcoplasmic/endoplasmic reticulum calcium ATPase 1

Gene

ATP2A1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 152 (01 Oct 2014)
      Sequence version 1 (01 Jan 1998)
      Previous versions | rss
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    Functioni

    This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol to the sarcoplasmic reticulum lumen. Contributes to calcium sequestration involved in muscular excitation/contraction.

    Catalytic activityi

    ATP + H2O + Ca2+(Side 1) = ADP + phosphate + Ca2+(Side 2).

    Enzyme regulationi

    Reversibly inhibited by phospholamban (PLN) at low calcium concentrations. Dephosphorylated PLN decreases the apparent affinity of the ATPase for calcium. This inhibition is regulated by the phosphorylation of PLN By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi304 – 3041Calcium 2; via carbonyl oxygenBy similarity
    Metal bindingi305 – 3051Calcium 2; via carbonyl oxygenBy similarity
    Metal bindingi307 – 3071Calcium 2; via carbonyl oxygenBy similarity
    Metal bindingi309 – 3091Calcium 2By similarity
    Active sitei351 – 35114-aspartylphosphate intermediateBy similarity
    Metal bindingi703 – 7031MagnesiumBy similarity
    Metal bindingi707 – 7071MagnesiumBy similarity
    Metal bindingi768 – 7681Calcium 1By similarity
    Metal bindingi771 – 7711Calcium 1By similarity
    Metal bindingi796 – 7961Calcium 2By similarity
    Metal bindingi799 – 7991Calcium 1By similarity
    Metal bindingi800 – 8001Calcium 1By similarity
    Metal bindingi800 – 8001Calcium 2By similarity
    Metal bindingi908 – 9081Calcium 1By similarity

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. calcium ion binding Source: UniProtKB
    3. calcium-transporting ATPase activity Source: UniProtKB
    4. protein binding Source: UniProtKB
    5. protein homodimerization activity Source: BHF-UCL

    GO - Biological processi

    1. apoptotic mitochondrial changes Source: BHF-UCL
    2. ATP catabolic process Source: UniProtKB
    3. blood coagulation Source: Reactome
    4. calcium ion import Source: BHF-UCL
    5. calcium ion transmembrane transport Source: GOC
    6. calcium ion transport Source: UniProtKB
    7. intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress Source: BHF-UCL
    8. ion transmembrane transport Source: Reactome
    9. maintenance of mitochondrion location Source: BHF-UCL
    10. negative regulation of endoplasmic reticulum calcium ion concentration Source: BHF-UCL
    11. negative regulation of striated muscle contraction Source: UniProtKB
    12. positive regulation of endoplasmic reticulum calcium ion concentration Source: BHF-UCL
    13. positive regulation of fast-twitch skeletal muscle fiber contraction Source: UniProtKB
    14. positive regulation of mitochondrial calcium ion concentration Source: BHF-UCL
    15. regulation of striated muscle contraction Source: UniProtKB
    16. relaxation of skeletal muscle Source: BHF-UCL
    17. response to endoplasmic reticulum stress Source: BHF-UCL
    18. transmembrane transport Source: Reactome

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Calcium transport, Ion transport, Transport

    Keywords - Ligandi

    ATP-binding, Calcium, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_118798. Pre-NOTCH Processing in Golgi.
    REACT_23765. Reduction of cytosolic Ca++ levels.
    REACT_25149. Ion transport by P-type ATPases.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Sarcoplasmic/endoplasmic reticulum calcium ATPase 1 (EC:3.6.3.8)
    Short name:
    SERCA1
    Short name:
    SR Ca(2+)-ATPase 1
    Alternative name(s):
    Calcium pump 1
    Calcium-transporting ATPase sarcoplasmic reticulum type, fast twitch skeletal muscle isoform
    Endoplasmic reticulum class 1/2 Ca(2+) ATPase
    Gene namesi
    Name:ATP2A1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:811. ATP2A1.

    Subcellular locationi

    GO - Cellular componenti

    1. calcium channel complex Source: BHF-UCL
    2. endoplasmic reticulum-Golgi intermediate compartment Source: UniProtKB
    3. endoplasmic reticulum membrane Source: UniProtKB
    4. H zone Source: UniProtKB
    5. I band Source: UniProtKB
    6. integral component of membrane Source: UniProtKB
    7. membrane Source: UniProtKB
    8. perinuclear region of cytoplasm Source: UniProtKB
    9. platelet dense tubular network membrane Source: Reactome
    10. sarcoplasmic reticulum Source: UniProtKB
    11. sarcoplasmic reticulum membrane Source: BHF-UCL

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane, Sarcoplasmic reticulum

    Pathology & Biotechi

    Involvement in diseasei

    Brody myopathy (BRM) [MIM:601003]: A disorder of muscle function that is characterized by painless muscle cramping and exercise-induced impairment of muscle relaxation.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti789 – 7891P → L in BRM; almost complete loss of Ca(2+) transport activity because of reduced Ca(2+) affinity. 1 Publication
    VAR_015588

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi601003. phenotype.
    Orphaneti53347. Brody myopathy.
    PharmGKBiPA25105.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10011001Sarcoplasmic/endoplasmic reticulum calcium ATPase 1PRO_0000046187Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi876 ↔ 8881 Publication

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    MaxQBiO14983.
    PaxDbiO14983.
    PRIDEiO14983.

    PTM databases

    PhosphoSiteiO14983.

    Expressioni

    Tissue specificityi

    Skeletal muscle, fast twitch muscle (type II) fibers.

    Developmental stagei

    Isoform SERCA1A accounts for more than 99% of SERCA1 isoforms expressed in adult skeletal muscle, while isoform SERCA1B predominates in neo-natal skeletal muscle.

    Inductioni

    Increased contractile activity leads to a decrease in SERCA1 expression, while decreased contractile activity leads to an increase in SERCA1 expression.

    Gene expression databases

    ArrayExpressiO14983.
    BgeeiO14983.
    CleanExiHS_ATP2A1.
    GenevestigatoriO14983.

    Organism-specific databases

    HPAiCAB002310.
    CAB032706.

    Interactioni

    Subunit structurei

    Associated with sarcolipin (SLN) and phospholamban (PLN).By similarity

    Protein-protein interaction databases

    BioGridi106977. 9 interactions.
    IntActiO14983. 3 interactions.
    MINTiMINT-1158140.
    STRINGi9606.ENSP00000349595.

    Structurei

    3D structure databases

    ProteinModelPortaliO14983.
    SMRiO14983. Positions 1-993.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 4848CytoplasmicBy similarityAdd
    BLAST
    Topological domaini70 – 8920LumenalBy similarityAdd
    BLAST
    Topological domaini111 – 253143CytoplasmicBy similarityAdd
    BLAST
    Topological domaini274 – 29522LumenalBy similarityAdd
    BLAST
    Topological domaini314 – 757444CytoplasmicBy similarityAdd
    BLAST
    Topological domaini778 – 78710LumenalBy similarity
    Topological domaini809 – 82820CytoplasmicBy similarityAdd
    BLAST
    Topological domaini852 – 89746LumenalBy similarityAdd
    BLAST
    Topological domaini918 – 93013CytoplasmicBy similarityAdd
    BLAST
    Topological domaini950 – 96415LumenalBy similarityAdd
    BLAST
    Topological domaini986 – 100116CytoplasmicBy similarityAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei49 – 6921Helical; Name=1By similarityAdd
    BLAST
    Transmembranei90 – 11021Helical; Name=2By similarityAdd
    BLAST
    Transmembranei254 – 27320Helical; Name=3By similarityAdd
    BLAST
    Transmembranei296 – 31318Helical; Name=4By similarityAdd
    BLAST
    Transmembranei758 – 77720Helical; Name=5By similarityAdd
    BLAST
    Transmembranei788 – 80821Helical; Name=6By similarityAdd
    BLAST
    Transmembranei829 – 85123Helical; Name=7By similarityAdd
    BLAST
    Transmembranei898 – 91720Helical; Name=8By similarityAdd
    BLAST
    Transmembranei931 – 94919Helical; Name=9By similarityAdd
    BLAST
    Transmembranei965 – 98521Helical; Name=10By similarityAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni370 – 40031Interacts with phospholamban 1By similarityAdd
    BLAST
    Regioni788 – 80821Interacts with phospholamban 2By similarityAdd
    BLAST

    Sequence similaritiesi

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0474.
    HOGENOMiHOG000265621.
    HOVERGENiHBG105648.
    KOiK05853.
    OMAiNEDVADR.
    OrthoDBiEOG73Z2SF.
    PhylomeDBiO14983.
    TreeFamiTF300651.

    Family and domain databases

    Gene3Di1.20.1110.10. 2 hits.
    2.70.150.10. 2 hits.
    3.40.1110.10. 1 hit.
    InterProiIPR005782. ATPase_P-typ_Ca-transp_IIA.
    IPR006068. ATPase_P-typ_cation-transptr_C.
    IPR004014. ATPase_P-typ_cation-transptr_N.
    IPR023299. ATPase_P-typ_cyto_domN.
    IPR018303. ATPase_P-typ_P_site.
    IPR023298. ATPase_P-typ_TM_dom.
    IPR008250. ATPase_P-typ_transduc_dom_A.
    IPR001757. Cation_transp_P_typ_ATPase.
    IPR023214. HAD-like_dom.
    [Graphical view]
    PfamiPF00689. 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.
    PR00120. HATPASE.
    SMARTiSM00831. Cation_ATPase_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF56784. SSF56784. 1 hit.
    SSF81660. SSF81660. 1 hit.
    TIGRFAMsiTIGR01116. ATPase-IIA1_Ca. 1 hit.
    TIGR01494. ATPase_P-type. 2 hits.
    PROSITEiPS00154. ATPASE_E1_E2. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform SERCA1B (identifier: O14983-1) [UniParc]FASTAAdd to Basket

    Also known as: ATP2A1B, Neonatal

    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

    MEAAHAKTTE ECLAYFGVSE TTGLTPDQVK RNLEKYGLNE LPAEEGKTLW     50
    ELVIEQFEDL LVRILLLAAC ISFVLAWFEE GEETITAFVE PFVILLILIA 100
    NAIVGVWQER NAENAIEALK EYEPEMGKVY RADRKSVQRI KARDIVPGDI 150
    VEVAVGDKVP ADIRILAIKS TTLRVDQSIL TGESVSVIKH TEPVPDPRAV 200
    NQDKKNMLFS GTNIAAGKAL GIVATTGVGT EIGKIRDQMA ATEQDKTPLQ 250
    QKLDEFGEQL SKVISLICVA VWLINIGHFN DPVHGGSWFR GAIYYFKIAV 300
    ALAVAAIPEG LPAVITTCLA LGTRRMAKKN AIVRSLPSVE TLGCTSVICS 350
    DKTGTLTTNQ MSVCKMFIID KVDGDICLLN EFSITGSTYA PEGEVLKNDK 400
    PVRPGQYDGL VELATICALC NDSSLDFNEA KGVYEKVGEA TETALTTLVE 450
    KMNVFNTDVR SLSKVERANA CNSVIRQLMK KEFTLEFSRD RKSMSVYCSP 500
    AKSSRAAVGN KMFVKGAPEG VIDRCNYVRV GTTRVPLTGP VKEKIMAVIK 550
    EWGTGRDTLR CLALATRDTP PKREEMVLDD SARFLEYETD LTFVGVVGML 600
    DPPRKEVTGS IQLCRDAGIR VIMITGDNKG TAIAICRRIG IFGENEEVAD 650
    RAYTGREFDD LPLAEQREAC RRACCFARVE PSHKSKIVEY LQSYDEITAM 700
    TGDGVNDAPA LKKAEIGIAM GSGTAVAKTA SEMVLADDNF STIVAAVEEG 750
    RAIYNNMKQF IRYLISSNVG EVVCIFLTAA LGLPEALIPV QLLWVNLVTD 800
    GLPATALGFN PPDLDIMDRP PRSPKEPLIS GWLFFRYMAI GGYVGAATVG 850
    AAAWWFLYAE DGPHVNYSQL THFMQCTEDN THFEGIDCEV FEAPEPMTMA 900
    LSVLVTIEMC NALNSLSENQ SLLRMPPWVN IWLLGSICLS MSLHFLILYV 950
    DPLPMIFKLR ALDLTQWLMV LKISLPVIGL DEILKFVARN YLEDPEDERR 1000
    K 1001
    Length:1,001
    Mass (Da):110,252
    Last modified:January 1, 1998 - v1
    Checksum:iC8F33809B56FDDEE
    GO
    Isoform SERCA1A (identifier: O14983-2) [UniParc]FASTAAdd to Basket

    Also known as: ATP2A1A, Adult

    The sequence of this isoform differs from the canonical sequence as follows:
         994-1001: DPEDERRK → G

    Show »
    Length:994
    Mass (Da):109,283
    Checksum:i3C07972DB585C083
    GO
    Isoform 3 (identifier: O14983-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-125: Missing.
         994-1001: DPEDERRK → G

    Note: No experimental confirmation available.

    Show »
    Length:869
    Mass (Da):95,199
    Checksum:iA1D5541B75BA3014
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti789 – 7891P → L in BRM; almost complete loss of Ca(2+) transport activity because of reduced Ca(2+) affinity. 1 Publication
    VAR_015588

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 125125Missing in isoform 3. 1 PublicationVSP_054770Add
    BLAST
    Alternative sequencei994 – 10018DPEDERRK → G in isoform SERCA1A and isoform 3. 2 PublicationsVSP_000355

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U96781
    , U96773, U96774, U96775, U96776, U96777, U96778, U96779, U96780 Genomic DNA. Translation: AAB53113.1.
    U96781
    , U96773, U96774, U96775, U96776, U96777, U96778, U96779, U96780 Genomic DNA. Translation: AAB53112.1.
    AK128456 mRNA. Translation: BAG54679.1.
    AK291314 mRNA. Translation: BAF84003.1.
    AC109460 Genomic DNA. No translation available.
    AC133550 Genomic DNA. No translation available.
    CCDSiCCDS10643.1. [O14983-1]
    CCDS42139.1. [O14983-2]
    CCDS66997.1. [O14983-3]
    RefSeqiNP_001273004.1. NM_001286075.1. [O14983-3]
    NP_004311.1. NM_004320.4. [O14983-2]
    NP_775293.1. NM_173201.3. [O14983-1]
    UniGeneiHs.657344.

    Genome annotation databases

    EnsembliENST00000357084; ENSP00000349595; ENSG00000196296. [O14983-1]
    ENST00000395503; ENSP00000378879; ENSG00000196296. [O14983-2]
    ENST00000536376; ENSP00000443101; ENSG00000196296. [O14983-3]
    GeneIDi487.
    KEGGihsa:487.
    UCSCiuc002drn.1. human. [O14983-2]
    uc002dro.1. human. [O14983-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U96781
    , U96773 , U96774 , U96775 , U96776 , U96777 , U96778 , U96779 , U96780 Genomic DNA. Translation: AAB53113.1 .
    U96781
    , U96773 , U96774 , U96775 , U96776 , U96777 , U96778 , U96779 , U96780 Genomic DNA. Translation: AAB53112.1 .
    AK128456 mRNA. Translation: BAG54679.1 .
    AK291314 mRNA. Translation: BAF84003.1 .
    AC109460 Genomic DNA. No translation available.
    AC133550 Genomic DNA. No translation available.
    CCDSi CCDS10643.1. [O14983-1 ]
    CCDS42139.1. [O14983-2 ]
    CCDS66997.1. [O14983-3 ]
    RefSeqi NP_001273004.1. NM_001286075.1. [O14983-3 ]
    NP_004311.1. NM_004320.4. [O14983-2 ]
    NP_775293.1. NM_173201.3. [O14983-1 ]
    UniGenei Hs.657344.

    3D structure databases

    ProteinModelPortali O14983.
    SMRi O14983. Positions 1-993.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106977. 9 interactions.
    IntActi O14983. 3 interactions.
    MINTi MINT-1158140.
    STRINGi 9606.ENSP00000349595.

    Chemistry

    BindingDBi O14983.
    ChEMBLi CHEMBL3136.

    PTM databases

    PhosphoSitei O14983.

    Proteomic databases

    MaxQBi O14983.
    PaxDbi O14983.
    PRIDEi O14983.

    Protocols and materials databases

    DNASUi 487.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000357084 ; ENSP00000349595 ; ENSG00000196296 . [O14983-1 ]
    ENST00000395503 ; ENSP00000378879 ; ENSG00000196296 . [O14983-2 ]
    ENST00000536376 ; ENSP00000443101 ; ENSG00000196296 . [O14983-3 ]
    GeneIDi 487.
    KEGGi hsa:487.
    UCSCi uc002drn.1. human. [O14983-2 ]
    uc002dro.1. human. [O14983-1 ]

    Organism-specific databases

    CTDi 487.
    GeneCardsi GC16P028889.
    HGNCi HGNC:811. ATP2A1.
    HPAi CAB002310.
    CAB032706.
    MIMi 108730. gene.
    601003. phenotype.
    neXtProti NX_O14983.
    Orphaneti 53347. Brody myopathy.
    PharmGKBi PA25105.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0474.
    HOGENOMi HOG000265621.
    HOVERGENi HBG105648.
    KOi K05853.
    OMAi NEDVADR.
    OrthoDBi EOG73Z2SF.
    PhylomeDBi O14983.
    TreeFami TF300651.

    Enzyme and pathway databases

    Reactomei REACT_118798. Pre-NOTCH Processing in Golgi.
    REACT_23765. Reduction of cytosolic Ca++ levels.
    REACT_25149. Ion transport by P-type ATPases.

    Miscellaneous databases

    GeneWikii ATP2A1.
    GenomeRNAii 487.
    NextBioi 2023.
    PROi O14983.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O14983.
    Bgeei O14983.
    CleanExi HS_ATP2A1.
    Genevestigatori O14983.

    Family and domain databases

    Gene3Di 1.20.1110.10. 2 hits.
    2.70.150.10. 2 hits.
    3.40.1110.10. 1 hit.
    InterProi IPR005782. ATPase_P-typ_Ca-transp_IIA.
    IPR006068. ATPase_P-typ_cation-transptr_C.
    IPR004014. ATPase_P-typ_cation-transptr_N.
    IPR023299. ATPase_P-typ_cyto_domN.
    IPR018303. ATPase_P-typ_P_site.
    IPR023298. ATPase_P-typ_TM_dom.
    IPR008250. ATPase_P-typ_transduc_dom_A.
    IPR001757. Cation_transp_P_typ_ATPase.
    IPR023214. HAD-like_dom.
    [Graphical view ]
    Pfami PF00689. Cation_ATPase_C. 1 hit.
    PF00690. Cation_ATPase_N. 1 hit.
    PF00122. E1-E2_ATPase. 1 hit.
    PF00702. Hydrolase. 1 hit.
    [Graphical view ]
    PRINTSi PR00119. CATATPASE.
    PR00120. HATPASE.
    SMARTi SM00831. Cation_ATPase_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56784. SSF56784. 1 hit.
    SSF81660. SSF81660. 1 hit.
    TIGRFAMsi TIGR01116. ATPase-IIA1_Ca. 1 hit.
    TIGR01494. ATPase_P-type. 2 hits.
    PROSITEi PS00154. ATPASE_E1_E2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Characterization of cDNA and genomic DNA encoding SERCA1, the Ca(2+)-ATPase of human fast-twitch skeletal muscle sarcoplasmic reticulum, and its elimination as a candidate gene for Brody disease."
      Zhang Y., Fujii J., Phillips M.S., Chen H.-S., Karpati G., Yee W.-C., Schrank B., Cornblath D.R., Boylan K.B., Maclennan D.H.
      Genomics 30:415-424(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS SERCA1A AND SERCA1B).
      Tissue: Skeletal muscle.
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS SERCA1A AND 3).
      Tissue: Tongue.
    3. "The sequence and analysis of duplication-rich human chromosome 16."
      Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
      , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
      Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Tissue: Thymus.
    4. "Mutations of either or both Cys876 and Cys888 residues of sarcoplasmic reticulum Ca2+-ATPase result in a complete loss of Ca2+ transport activity without a loss of Ca2+-dependent ATPase activity. Role of the Cys876-Cys888 disulfide bond."
      Daiho T., Yamasaki K., Saino T., Kamidochi M., Satoh K., Iizuka H., Suzuki H.
      J. Biol. Chem. 276:32771-32778(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISULFIDE BOND.
    5. "The mutation of Pro(789) to Leu reduces the activity of the fast-twitch skeletal muscle sarco(endo)plasmic reticulum Ca(2+) ATPase (SERCA1) and is associated with Brody disease."
      Odermatt A., Barton K., Khanna V.K., Mathieu J., Escolar D., Kuntzer T., Karpati G., MacLennan D.H.
      Hum. Genet. 106:482-491(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT BRM LEU-789.

    Entry informationi

    Entry nameiAT2A1_HUMAN
    AccessioniPrimary (citable) accession number: O14983
    Secondary accession number(s): A8K5J9, B3KY17, O14984
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: January 1, 1998
    Last modified: October 1, 2014
    This is version 152 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 16
      Human chromosome 16: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3