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Protein

Sarcoplasmic/endoplasmic reticulum calcium ATPase 1

Gene

ATP2A1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Key regulator of striated muscle performance by acting as the major Ca2+ ATPase responsible for the reuptake of cytosolic Ca2+ into the sarcoplasmic reticulum. 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

Inhibited by sarcolipin (SLN), phospholamban (PLN) and myoregulin (MLN). 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

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

  • ATP binding Source: UniProtKB
  • calcium ion binding Source: UniProtKB
  • calcium-transporting ATPase activity Source: UniProtKB
  • protein homodimerization activity Source: BHF-UCL

GO - Biological processi

  • apoptotic mitochondrial changes Source: BHF-UCL
  • blood coagulation Source: Reactome
  • calcium ion import Source: BHF-UCL
  • calcium ion transmembrane transport Source: GOC
  • calcium ion transport Source: UniProtKB
  • intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress Source: BHF-UCL
  • ion transmembrane transport Source: Reactome
  • maintenance of mitochondrion location Source: BHF-UCL
  • negative regulation of endoplasmic reticulum calcium ion concentration Source: BHF-UCL
  • negative regulation of striated muscle contraction Source: UniProtKB
  • positive regulation of endoplasmic reticulum calcium ion concentration Source: BHF-UCL
  • positive regulation of fast-twitch skeletal muscle fiber contraction Source: UniProtKB
  • positive regulation of mitochondrial calcium ion concentration Source: BHF-UCL
  • regulation of striated muscle contraction Source: UniProtKB
  • relaxation of skeletal muscle Source: BHF-UCL
  • response to endoplasmic reticulum stress Source: BHF-UCL
  • transmembrane transport Source: Reactome
Complete GO annotation...

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 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:811. ATP2A1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 4848CytoplasmicBy similarityAdd
BLAST
Transmembranei49 – 6921Helical; Name=1By similarityAdd
BLAST
Topological domaini70 – 8920LumenalBy similarityAdd
BLAST
Transmembranei90 – 11021Helical; Name=2By similarityAdd
BLAST
Topological domaini111 – 253143CytoplasmicBy similarityAdd
BLAST
Transmembranei254 – 27320Helical; Name=3By similarityAdd
BLAST
Topological domaini274 – 29522LumenalBy similarityAdd
BLAST
Transmembranei296 – 31318Helical; Name=4By similarityAdd
BLAST
Topological domaini314 – 757444CytoplasmicBy similarityAdd
BLAST
Transmembranei758 – 77720Helical; Name=5By similarityAdd
BLAST
Topological domaini778 – 78710LumenalBy similarity
Transmembranei788 – 80821Helical; Name=6By similarityAdd
BLAST
Topological domaini809 – 82820CytoplasmicBy similarityAdd
BLAST
Transmembranei829 – 85123Helical; Name=7By similarityAdd
BLAST
Topological domaini852 – 89746LumenalBy similarityAdd
BLAST
Transmembranei898 – 91720Helical; Name=8By similarityAdd
BLAST
Topological domaini918 – 93013CytoplasmicBy similarityAdd
BLAST
Transmembranei931 – 94919Helical; Name=9By similarityAdd
BLAST
Topological domaini950 – 96415LumenalBy similarityAdd
BLAST
Transmembranei965 – 98521Helical; Name=10By similarityAdd
BLAST
Topological domaini986 – 100116CytoplasmicBy similarityAdd
BLAST

GO - Cellular componenti

  • calcium channel complex Source: BHF-UCL
  • endoplasmic reticulum-Golgi intermediate compartment Source: UniProtKB
  • endoplasmic reticulum membrane Source: UniProtKB
  • H zone Source: UniProtKB
  • I band Source: UniProtKB
  • integral component of membrane Source: UniProtKB
  • membrane Source: UniProtKB
  • mitochondrion Source: GOC
  • perinuclear region of cytoplasm Source: UniProtKB
  • platelet dense tubular network membrane Source: Reactome
  • sarcoplasmic reticulum Source: UniProtKB
  • sarcoplasmic reticulum membrane Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Sarcoplasmic reticulum

Pathology & Biotechi

Involvement in diseasei

Brody myopathy (BRM)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA disorder of muscle function that is characterized by painless muscle cramping and exercise-induced impairment of muscle relaxation.

See also OMIM:601003
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.

Polymorphism and mutation databases

BioMutaiATP2A1.

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

BgeeiO14983.
CleanExiHS_ATP2A1.
ExpressionAtlasiO14983. baseline and differential.
GenevisibleiO14983. HS.

Organism-specific databases

HPAiCAB002310.
CAB032706.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi106977. 13 interactions.
IntActiO14983. 3 interactions.
MINTiMINT-1158140.
STRINGi9606.ENSP00000349595.

Structurei

3D structure databases

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

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.
GeneTreeiENSGT00800000124056.
HOGENOMiHOG000265621.
HOVERGENiHBG105648.
InParanoidiO14983.
KOiK05853.
OMAiARFMEYE.
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.
InterProiIPR006068. ATPase_P-typ_cation-transptr_C.
IPR004014. ATPase_P-typ_cation-transptr_N.
IPR023299. ATPase_P-typ_cyto_domN.
IPR018303. ATPase_P-typ_P_site.
IPR023298. ATPase_P-typ_TM_dom.
IPR008250. ATPase_P-typ_transduc_dom_A.
IPR023214. HAD-like_dom.
IPR005782. P-type_ATPase_IIA.
IPR001757. P_typ_ATPase.
IPR030332. SERCA1.
[Graphical view]
PANTHERiPTHR24093:SF215. PTHR24093:SF215. 1 hit.
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. AlignAdd to basket

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

        10         20         30         40         50
MEAAHAKTTE ECLAYFGVSE TTGLTPDQVK RNLEKYGLNE LPAEEGKTLW
60 70 80 90 100
ELVIEQFEDL LVRILLLAAC ISFVLAWFEE GEETITAFVE PFVILLILIA
110 120 130 140 150
NAIVGVWQER NAENAIEALK EYEPEMGKVY RADRKSVQRI KARDIVPGDI
160 170 180 190 200
VEVAVGDKVP ADIRILAIKS TTLRVDQSIL TGESVSVIKH TEPVPDPRAV
210 220 230 240 250
NQDKKNMLFS GTNIAAGKAL GIVATTGVGT EIGKIRDQMA ATEQDKTPLQ
260 270 280 290 300
QKLDEFGEQL SKVISLICVA VWLINIGHFN DPVHGGSWFR GAIYYFKIAV
310 320 330 340 350
ALAVAAIPEG LPAVITTCLA LGTRRMAKKN AIVRSLPSVE TLGCTSVICS
360 370 380 390 400
DKTGTLTTNQ MSVCKMFIID KVDGDICLLN EFSITGSTYA PEGEVLKNDK
410 420 430 440 450
PVRPGQYDGL VELATICALC NDSSLDFNEA KGVYEKVGEA TETALTTLVE
460 470 480 490 500
KMNVFNTDVR SLSKVERANA CNSVIRQLMK KEFTLEFSRD RKSMSVYCSP
510 520 530 540 550
AKSSRAAVGN KMFVKGAPEG VIDRCNYVRV GTTRVPLTGP VKEKIMAVIK
560 570 580 590 600
EWGTGRDTLR CLALATRDTP PKREEMVLDD SARFLEYETD LTFVGVVGML
610 620 630 640 650
DPPRKEVTGS IQLCRDAGIR VIMITGDNKG TAIAICRRIG IFGENEEVAD
660 670 680 690 700
RAYTGREFDD LPLAEQREAC RRACCFARVE PSHKSKIVEY LQSYDEITAM
710 720 730 740 750
TGDGVNDAPA LKKAEIGIAM GSGTAVAKTA SEMVLADDNF STIVAAVEEG
760 770 780 790 800
RAIYNNMKQF IRYLISSNVG EVVCIFLTAA LGLPEALIPV QLLWVNLVTD
810 820 830 840 850
GLPATALGFN PPDLDIMDRP PRSPKEPLIS GWLFFRYMAI GGYVGAATVG
860 870 880 890 900
AAAWWFLYAE DGPHVNYSQL THFMQCTEDN THFEGIDCEV FEAPEPMTMA
910 920 930 940 950
LSVLVTIEMC NALNSLSENQ SLLRMPPWVN IWLLGSICLS MSLHFLILYV
960 970 980 990 1000
DPLPMIFKLR ALDLTQWLMV LKISLPVIGL DEILKFVARN YLEDPEDERR

K
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:
EMBLi
GenBanki
DDBJi
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.
ENST00000395503; ENSP00000378879; ENSG00000196296. [O14983-2]
ENST00000536376; ENSP00000443101; ENSG00000196296. [O14983-3]
GeneIDi487.
KEGGihsa:487.
UCSCiuc002drn.1. human. [O14983-2]
uc002dro.1. human. [O14983-1]
uc002drp.1. human.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

BioGridi106977. 13 interactions.
IntActiO14983. 3 interactions.
MINTiMINT-1158140.
STRINGi9606.ENSP00000349595.

Chemistry

BindingDBiO14983.
ChEMBLiCHEMBL3136.

PTM databases

PhosphoSiteiO14983.

Polymorphism and mutation databases

BioMutaiATP2A1.

Proteomic databases

MaxQBiO14983.
PaxDbiO14983.
PRIDEiO14983.

Protocols and materials databases

DNASUi487.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000357084; ENSP00000349595; ENSG00000196296.
ENST00000395503; ENSP00000378879; ENSG00000196296. [O14983-2]
ENST00000536376; ENSP00000443101; ENSG00000196296. [O14983-3]
GeneIDi487.
KEGGihsa:487.
UCSCiuc002drn.1. human. [O14983-2]
uc002dro.1. human. [O14983-1]
uc002drp.1. human.

Organism-specific databases

CTDi487.
GeneCardsiGC16P028889.
HGNCiHGNC:811. ATP2A1.
HPAiCAB002310.
CAB032706.
MIMi108730. gene.
601003. phenotype.
neXtProtiNX_O14983.
Orphaneti53347. Brody myopathy.
PharmGKBiPA25105.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0474.
GeneTreeiENSGT00800000124056.
HOGENOMiHOG000265621.
HOVERGENiHBG105648.
InParanoidiO14983.
KOiK05853.
OMAiARFMEYE.
OrthoDBiEOG73Z2SF.
PhylomeDBiO14983.
TreeFamiTF300651.

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.

Miscellaneous databases

GeneWikiiATP2A1.
GenomeRNAii487.
NextBioi2023.
PROiO14983.
SOURCEiSearch...

Gene expression databases

BgeeiO14983.
CleanExiHS_ATP2A1.
ExpressionAtlasiO14983. baseline and differential.
GenevisibleiO14983. HS.

Family and domain databases

Gene3Di1.20.1110.10. 2 hits.
2.70.150.10. 2 hits.
3.40.1110.10. 1 hit.
InterProiIPR006068. ATPase_P-typ_cation-transptr_C.
IPR004014. ATPase_P-typ_cation-transptr_N.
IPR023299. ATPase_P-typ_cyto_domN.
IPR018303. ATPase_P-typ_P_site.
IPR023298. ATPase_P-typ_TM_dom.
IPR008250. ATPase_P-typ_transduc_dom_A.
IPR023214. HAD-like_dom.
IPR005782. P-type_ATPase_IIA.
IPR001757. P_typ_ATPase.
IPR030332. SERCA1.
[Graphical view]
PANTHERiPTHR24093:SF215. PTHR24093:SF215. 1 hit.
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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: July 22, 2015
This is version 158 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

Similar proteinsi

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