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O14983 (AT2A1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 150. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Sarcoplasmic/endoplasmic reticulum calcium ATPase 1

Short name=SERCA1
Short name=SR Ca(2+)-ATPase 1
EC=3.6.3.8
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 names
Name:ATP2A1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1001 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 activity

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

Enzyme regulation

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.

Subunit structure

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

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein. Sarcoplasmic reticulum membrane; Multi-pass membrane protein.

Tissue specificity

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

Developmental stage

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

Induction

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

Involvement in disease

Brody myopathy (BRM) [MIM:601003]: A disorder of muscle function that is characterized by painless muscle cramping and exercise-induced impairment of muscle relaxation.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.5

Sequence similarities

Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IIA subfamily. [View classification]

Ontologies

Keywords
   Biological processCalcium transport
Ion transport
Transport
   Cellular componentEndoplasmic reticulum
Membrane
Sarcoplasmic reticulum
   Coding sequence diversityAlternative splicing
   DiseaseDisease mutation
   DomainTransmembrane
Transmembrane helix
   LigandATP-binding
Calcium
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionHydrolase
   PTMDisulfide bond
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processATP catabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

apoptotic mitochondrial changes

Inferred from mutant phenotype PubMed 19061639. Source: BHF-UCL

blood coagulation

Traceable author statement. Source: Reactome

calcium ion import

Inferred from mutant phenotype PubMed 8040329. Source: BHF-UCL

calcium ion transmembrane transport

Inferred from direct assay PubMed 1329967. Source: GOC

calcium ion transport

Inferred from direct assay PubMed 11402072. Source: UniProtKB

intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress

Inferred from mutant phenotype PubMed 19061639. Source: BHF-UCL

ion transmembrane transport

Traceable author statement. Source: Reactome

maintenance of mitochondrion location

Inferred from mutant phenotype PubMed 19061639. Source: BHF-UCL

negative regulation of endoplasmic reticulum calcium ion concentration

Inferred from mutant phenotype PubMed 11402072PubMed 19061639. Source: BHF-UCL

negative regulation of striated muscle contraction

Inferred from mutant phenotype Ref.5. Source: UniProtKB

positive regulation of endoplasmic reticulum calcium ion concentration

Inferred from mutant phenotype PubMed 11402072. Source: BHF-UCL

positive regulation of fast-twitch skeletal muscle fiber contraction

Inferred from direct assay PubMed 12479237. Source: UniProtKB

positive regulation of mitochondrial calcium ion concentration

Inferred from mutant phenotype PubMed 19061639. Source: BHF-UCL

regulation of striated muscle contraction

Inferred from mutant phenotype PubMed 9405806. Source: UniProtKB

relaxation of skeletal muscle

Inferred from direct assay PubMed 8841193. Source: BHF-UCL

response to endoplasmic reticulum stress

Inferred from mutant phenotype PubMed 19061639. Source: BHF-UCL

transmembrane transport

Traceable author statement. Source: Reactome

   Cellular_componentH zone

Inferred from direct assay PubMed 1329967. Source: UniProtKB

I band

Inferred from direct assay PubMed 1329967. Source: UniProtKB

calcium channel complex

Inferred by curator PubMed 11402072. Source: BHF-UCL

endoplasmic reticulum membrane

Inferred from direct assay PubMed 11402072. Source: UniProtKB

endoplasmic reticulum-Golgi intermediate compartment

Inferred from sequence or structural similarity. Source: UniProtKB

integral component of membrane

Non-traceable author statement PubMed 9405806. Source: UniProtKB

membrane

Inferred from sequence or structural similarity. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

platelet dense tubular network membrane

Traceable author statement. Source: Reactome

sarcoplasmic reticulum

Inferred from sequence or structural similarity. Source: UniProtKB

sarcoplasmic reticulum membrane

Traceable author statement PubMed 11402072. Source: BHF-UCL

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

calcium ion binding

Inferred from mutant phenotype PubMed 9405806. Source: UniProtKB

calcium-transporting ATPase activity

Inferred from direct assay PubMed 8729696PubMed 1329967. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 9295312. Source: UniProtKB

protein homodimerization activity

Inferred from physical interaction PubMed 11402072. Source: BHF-UCL

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform SERCA1B (identifier: O14983-1)

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.
Isoform SERCA1A (identifier: O14983-2)

Also known as: ATP2A1A; Adult;

The sequence of this isoform differs from the canonical sequence as follows:
     994-1001: DPEDERRK → G
Isoform 3 (identifier: O14983-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-125: Missing.
     994-1001: DPEDERRK → G
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10011001Sarcoplasmic/endoplasmic reticulum calcium ATPase 1
PRO_0000046187

Regions

Topological domain1 – 4848Cytoplasmic By similarity
Transmembrane49 – 6921Helical; Name=1; By similarity
Topological domain70 – 8920Lumenal By similarity
Transmembrane90 – 11021Helical; Name=2; By similarity
Topological domain111 – 253143Cytoplasmic By similarity
Transmembrane254 – 27320Helical; Name=3; By similarity
Topological domain274 – 29522Lumenal By similarity
Transmembrane296 – 31318Helical; Name=4; By similarity
Topological domain314 – 757444Cytoplasmic By similarity
Transmembrane758 – 77720Helical; Name=5; By similarity
Topological domain778 – 78710Lumenal By similarity
Transmembrane788 – 80821Helical; Name=6; By similarity
Topological domain809 – 82820Cytoplasmic By similarity
Transmembrane829 – 85123Helical; Name=7; By similarity
Topological domain852 – 89746Lumenal By similarity
Transmembrane898 – 91720Helical; Name=8; By similarity
Topological domain918 – 93013Cytoplasmic By similarity
Transmembrane931 – 94919Helical; Name=9; By similarity
Topological domain950 – 96415Lumenal By similarity
Transmembrane965 – 98521Helical; Name=10; By similarity
Topological domain986 – 100116Cytoplasmic By similarity
Region370 – 40031Interacts with phospholamban 1 By similarity
Region788 – 80821Interacts with phospholamban 2 By similarity

Sites

Active site35114-aspartylphosphate intermediate By similarity
Metal binding3041Calcium 2; via carbonyl oxygen By similarity
Metal binding3051Calcium 2; via carbonyl oxygen By similarity
Metal binding3071Calcium 2; via carbonyl oxygen By similarity
Metal binding3091Calcium 2 By similarity
Metal binding7031Magnesium By similarity
Metal binding7071Magnesium By similarity
Metal binding7681Calcium 1 By similarity
Metal binding7711Calcium 1 By similarity
Metal binding7961Calcium 2 By similarity
Metal binding7991Calcium 1 By similarity
Metal binding8001Calcium 1 By similarity
Metal binding8001Calcium 2 By similarity
Metal binding9081Calcium 1 By similarity

Amino acid modifications

Disulfide bond876 ↔ 888 Ref.4

Natural variations

Alternative sequence1 – 125125Missing in isoform 3.
VSP_054770
Alternative sequence994 – 10018DPEDERRK → G in isoform SERCA1A and isoform 3.
VSP_000355
Natural variant7891P → L in BRM; almost complete loss of Ca(2+) transport activity because of reduced Ca(2+) affinity. Ref.5
VAR_015588

Sequences

Sequence LengthMass (Da)Tools
Isoform SERCA1B (ATP2A1B) (Neonatal) [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: C8F33809B56FDDEE

FASTA1,001110,252
        10         20         30         40         50         60 
MEAAHAKTTE ECLAYFGVSE TTGLTPDQVK RNLEKYGLNE LPAEEGKTLW ELVIEQFEDL 

        70         80         90        100        110        120 
LVRILLLAAC ISFVLAWFEE GEETITAFVE PFVILLILIA NAIVGVWQER NAENAIEALK 

       130        140        150        160        170        180 
EYEPEMGKVY RADRKSVQRI KARDIVPGDI VEVAVGDKVP ADIRILAIKS TTLRVDQSIL 

       190        200        210        220        230        240 
TGESVSVIKH TEPVPDPRAV NQDKKNMLFS GTNIAAGKAL GIVATTGVGT EIGKIRDQMA 

       250        260        270        280        290        300 
ATEQDKTPLQ QKLDEFGEQL SKVISLICVA VWLINIGHFN DPVHGGSWFR GAIYYFKIAV 

       310        320        330        340        350        360 
ALAVAAIPEG LPAVITTCLA LGTRRMAKKN AIVRSLPSVE TLGCTSVICS DKTGTLTTNQ 

       370        380        390        400        410        420 
MSVCKMFIID KVDGDICLLN EFSITGSTYA PEGEVLKNDK PVRPGQYDGL VELATICALC 

       430        440        450        460        470        480 
NDSSLDFNEA KGVYEKVGEA TETALTTLVE KMNVFNTDVR SLSKVERANA CNSVIRQLMK 

       490        500        510        520        530        540 
KEFTLEFSRD RKSMSVYCSP AKSSRAAVGN KMFVKGAPEG VIDRCNYVRV GTTRVPLTGP 

       550        560        570        580        590        600 
VKEKIMAVIK EWGTGRDTLR CLALATRDTP PKREEMVLDD SARFLEYETD LTFVGVVGML 

       610        620        630        640        650        660 
DPPRKEVTGS IQLCRDAGIR VIMITGDNKG TAIAICRRIG IFGENEEVAD RAYTGREFDD 

       670        680        690        700        710        720 
LPLAEQREAC RRACCFARVE PSHKSKIVEY LQSYDEITAM TGDGVNDAPA LKKAEIGIAM 

       730        740        750        760        770        780 
GSGTAVAKTA SEMVLADDNF STIVAAVEEG RAIYNNMKQF IRYLISSNVG EVVCIFLTAA 

       790        800        810        820        830        840 
LGLPEALIPV QLLWVNLVTD GLPATALGFN PPDLDIMDRP PRSPKEPLIS GWLFFRYMAI 

       850        860        870        880        890        900 
GGYVGAATVG AAAWWFLYAE DGPHVNYSQL THFMQCTEDN THFEGIDCEV FEAPEPMTMA 

       910        920        930        940        950        960 
LSVLVTIEMC NALNSLSENQ SLLRMPPWVN IWLLGSICLS MSLHFLILYV DPLPMIFKLR 

       970        980        990       1000 
ALDLTQWLMV LKISLPVIGL DEILKFVARN YLEDPEDERR K 

« Hide

Isoform SERCA1A (ATP2A1A) (Adult) [UniParc].

Checksum: 3C07972DB585C083
Show »

FASTA994109,283
Isoform 3 [UniParc].

Checksum: A1D5541B75BA3014
Show »

FASTA86995,199

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U96781 expand/collapse EMBL AC list , U96773, U96774, U96775, U96776, U96777, U96778, U96779, U96780 Genomic DNA. Translation: AAB53113.1.
U96781 expand/collapse EMBL AC list , 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.
CCDSCCDS10643.1. [O14983-1]
CCDS42139.1. [O14983-2]
RefSeqNP_001273004.1. NM_001286075.1. [O14983-3]
NP_004311.1. NM_004320.4. [O14983-2]
NP_775293.1. NM_173201.3. [O14983-1]
UniGeneHs.657344.

3D structure databases

ProteinModelPortalO14983.
SMRO14983. Positions 1-993.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106977. 8 interactions.
IntActO14983. 3 interactions.
MINTMINT-1158140.
STRING9606.ENSP00000349595.

Chemistry

BindingDBO14983.
ChEMBLCHEMBL3136.

PTM databases

PhosphoSiteO14983.

Proteomic databases

MaxQBO14983.
PaxDbO14983.
PRIDEO14983.

Protocols and materials databases

DNASU487.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000357084; ENSP00000349595; ENSG00000196296. [O14983-1]
ENST00000395503; ENSP00000378879; ENSG00000196296. [O14983-2]
ENST00000536376; ENSP00000443101; ENSG00000196296.
GeneID487.
KEGGhsa:487.
UCSCuc002drn.1. human. [O14983-2]
uc002dro.1. human. [O14983-1]

Organism-specific databases

CTD487.
GeneCardsGC16P028889.
HGNCHGNC:811. ATP2A1.
HPACAB002310.
CAB032706.
MIM108730. gene.
601003. phenotype.
neXtProtNX_O14983.
Orphanet53347. Brody myopathy.
PharmGKBPA25105.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0474.
HOGENOMHOG000265621.
HOVERGENHBG105648.
KOK05853.
OMANEDVADR.
OrthoDBEOG73Z2SF.
PhylomeDBO14983.
TreeFamTF300651.

Enzyme and pathway databases

ReactomeREACT_15518. Transmembrane transport of small molecules.
REACT_604. Hemostasis.

Gene expression databases

ArrayExpressO14983.
BgeeO14983.
CleanExHS_ATP2A1.
GenevestigatorO14983.

Family and domain databases

Gene3D1.20.1110.10. 2 hits.
2.70.150.10. 2 hits.
3.40.1110.10. 1 hit.
InterProIPR005782. 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]
PfamPF00689. Cation_ATPase_C. 1 hit.
PF00690. Cation_ATPase_N. 1 hit.
PF00122. E1-E2_ATPase. 1 hit.
PF00702. Hydrolase. 1 hit.
[Graphical view]
PRINTSPR00119. CATATPASE.
PR00120. HATPASE.
SMARTSM00831. Cation_ATPase_N. 1 hit.
[Graphical view]
SUPFAMSSF56784. SSF56784. 1 hit.
SSF81660. SSF81660. 1 hit.
TIGRFAMsTIGR01116. ATPase-IIA1_Ca. 1 hit.
TIGR01494. ATPase_P-type. 2 hits.
PROSITEPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiATP2A1.
GenomeRNAi487.
NextBio2023.
PROO14983.
SOURCESearch...

Entry information

Entry nameAT2A1_HUMAN
AccessionPrimary (citable) accession number: O14983
Secondary accession number(s): A8K5J9, B3KY17, O14984
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: January 1, 1998
Last modified: July 9, 2014
This is version 150 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM