ATP2A1

Category: Politics
Comments: 0
View: 12

www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=487.

^ a b Asahi, Michio; Kurzydlowski Kazimierz, Tada Michihiko, MacLennan David H (Jul. 2002). “Sarcolipin inhibits polymerization of phospholamban to induce superinhibition of sarco(endo)plasmic reticulum Ca2+-ATPases (SERCAs)”. J. Biol. Chem. (United States) 277 (30): 267258. doi:10.1074/jbc.C200269200. ISSN 0021-9258. PMID 12032137.

^ Asahi, M; Kimura Y, Kurzydlowski K, Tada M, MacLennan D H (Nov. 1999). “Transmembrane helix M6 in sarco(endo)plasmic reticulum Ca(2+)-ATPase forms a functional interaction site with phospholamban. Evidence for physical interactions at other sites”. J. Biol. Chem. (UNITED STATES) 274 (46): 3285562. ISSN 0021-9258. PMID 10551848.

^ Asahi, M; Green N M, Kurzydlowski K, Tada M, MacLennan D H (Aug. 2001). “Phospholamban domain IB forms an interaction site with the loop between transmembrane helices M6 and M7 of sarco(endo)plasmic reticulum Ca2+ ATPases”. Proc. Natl. Acad. Sci. U.S.A. (United States) 98 (18): 100616. doi:10.1073/pnas.181348298. ISSN 0027-8424. PMID 11526231.

^ Asahi, Michio; Sugita Yuji, Kurzydlowski Kazimierz, De Leon Stella, Tada Michihiko, Toyoshima Chikashi, MacLennan David H (Apr. 2003). “Sarcolipin regulates sarco(endo)plasmic reticulum Ca2+-ATPase (SERCA) by binding to transmembrane helices alone or in association with phospholamban”. Proc. Natl. Acad. Sci. U.S.A. (United States) 100 (9): 50405. doi:10.1073/pnas.0330962100. ISSN 0027-8424. PMID 12692302.

Further reading

Baba-Aissa F, Raeymaekers L, Wuytack F, et al. (1998). “Distribution and isoform diversity of the organellar Ca2+ pumps in the brain.”. Mol. Chem. Neuropathol. 33 (3): 199208. doi:10.1007/BF02815182. PMID 9642673.

Callen DF, Baker E, Lane S, et al. (1992). “Regional mapping of the Batten disease locus (CLN3) to human chromosome 16p12.”. Am. J. Hum. Genet. 49 (6): 13727. PMID 1746562.

MacLennan DH, Brandl CJ, Champaneria S, et al. (1988). “Fast-twitch and slow-twitch/cardiac Ca2+ ATPase genes map to human chromosomes 16 and 12.”. Somat. Cell Mol. Genet. 13 (4): 3416. doi:10.1007/BF01534928. PMID 2842876.

Brandl CJ, Green NM, Korczak B, MacLennan DH (1986). “Two Ca2+ ATPase genes: homologies and mechanistic implications of deduced amino acid sequences.”. Cell 44 (4): 597607. doi:10.1016/0092-8674(86)90269-2. PMID 2936465.

Benders AA, Wevers RA, Veerkamp JH (1996). “Ion transport in human skeletal muscle cells: disturbances in myotonic dystrophy and Brody’s disease.”. Acta Physiol. Scand. 156 (3): 35567. doi:10.1046/j.1365-201X.1996.202000.x. PMID 8729696.

Zhang Y, Fujii J, Phillips MS, et al. (1997). “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.”. Genomics 30 (3): 41524. doi:10.1006/geno.1995.1259. PMID 8825625.

Odermatt A, Taschner PE, Khanna VK, et al. (1996). “Mutations in the gene-encoding SERCA1, the fast-twitch skeletal muscle sarcoplasmic reticulum Ca2+ ATPase, are associated with Brody disease.”. Nat. Genet. 14 (2): 1914. doi:10.1038/ng1096-191. PMID 8841193.

Bonaldo MF, Lennon G, Soares MB (1997). “Normalization and subtraction: two approaches to facilitate gene discovery.”. Genome Res. 6 (9): 791806. doi:10.1101/gr.6.9.791. PMID 8889548.

Algenstaedt P, Antonetti DA, Yaffe MB, Kahn CR (1997). “Insulin receptor substrate proteins create a link between the tyrosine phosphorylation cascade and the Ca2+-ATPases in muscle and heart.”. J. Biol. Chem. 272 (38): 23696702. doi:10.1074/jbc.272.38.23696. PMID 9295312.

Odermatt A, Taschner PE, Scherer SW, et al. (1998). “Characterization of the gene encoding human sarcolipin (SLN), a proteolipid associated with SERCA1: absence of structural mutations in five patients with Brody disease.”. Genomics 45 (3): 54153. doi:10.1006/geno.1997.4967. PMID 9367679.

MacLennan DH, Rice WJ, Odermatt A (1998). “Structure/function analysis of the Ca2+ binding and translocation domain of SERCA1 and the role in Brody disease of the ATP2A1 gene encoding SERCA1.”. Ann. N. Y. Acad. Sci. 834: 17585. doi:10.1111/j.1749-6632.1997.tb52249.x. PMID 9405806.

Odermatt A, Becker S, Khanna VK, et al. (1998). “Sarcolipin regulates the activity of SERCA1, the fast-twitch skeletal muscle sarcoplasmic reticulum Ca2+-ATPase.”. J. Biol. Chem. 273 (20): 123609. doi:10.1074/jbc.273.20.12360. PMID 9575189.

Asahi M, Kimura Y, Kurzydlowski K, et al. (2000). “Transmembrane helix M6 in sarco(endo)plasmic reticulum Ca(2+)-ATPase forms a functional interaction site with phospholamban. Evidence for physical interactions at other sites.”. J. Biol. Chem. 274 (46): 3285562. doi:10.1074/jbc.274.46.32855. PMID 10551848.

Odermatt A, Barton K, Khanna VK, et al. (2000). “The mutation of Pro789 to Leu reduces the activity of the fast-twitch skeletal muscle sarco(endo)plasmic reticulum Ca2+ ATPase (SERCA1) and is associated with Brody disease.”. Hum. Genet. 106 (5): 48291. doi:10.1007/s004390000297. PMID 10914677.

Daiho T, Yamasaki K, Saino T, et al. (2001). “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.”. J. Biol. Chem. 276 (35): 327718. doi:10.1074/jbc.M101229200. PMID 11438520.

Asahi M, Green NM, Kurzydlowski K, et al. (2001). “Phospholamban domain IB forms an interaction site with the loop between transmembrane helices M6 and M7 of sarco(endo)plasmic reticulum Ca2+ ATPases.”. Proc. Natl. Acad. Sci. U.S.A. 98 (18): 100616. doi:10.1073/pnas.181348298. PMID 11526231.

Strausberg RL, Feingold EA, Grouse LH, et al. (2003). “Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.”. Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899903. doi:10.1073/pnas.242603899. PMID 12477932.

Pieske B, Maier LS, Schmidt-Schweda S (2002). “Sarcoplasmic reticulum Ca2+ load in human heart failure.”. Basic Res. Cardiol. 97 Suppl 1: I6371. PMID 12479237.

Toyoshima C, Asahi M, Sugita Y, et al. (2003). “Modeling of the inhibitory interaction of phospholamban with the Ca2+ ATPase.”. Proc. Natl. Acad. Sci. U.S.A. 100 (2): 46772. doi:10.1073/pnas.0237326100. PMID 12525698.

v  d  e

PDB Gallery

1iwo: Crystal structure of the SR Ca2+-ATPase in the absence of Ca2+

1kju: Ca2+-ATPase in the E2 State

1su4: Crystal structure of calcium ATPase with two bound calcium ions

1t5s: Structure of the (SR)Ca2+-ATPase Ca2-E1-AMPPCP form

1t5t: Structure of the (SR)Ca2+-ATPase Ca2-E1-ADP:AlF4- form

1vfp: Crystal structure of the SR CA2+-ATPase with bound AMPPCP

1wpe:

1wpg: Crystal structure of the SR CA2+-ATPase with MGF4

1xp5: Structure Of The (Sr)Ca2+-ATPase E2-AlF4- Form

2agv: Crystal structure of the SR CA2+-ATPASE with BHQ and TG

2by4: SR CA(2+)-ATPASE IN THE HNE2 STATE COMPLEXED WITH THE THAPSIGARGIN DERIVATIVE BOC-12ADT.

2c88: CRYSTAL STRUCTURE OF (SR) CALCIUM-ATPASE E2(TG):AMPPCP FORM

2c8k: CRYSTAL STRUCTURE OF (SR) CALCIUM-ATPASE E2(TG) WITH PARTIALLY OCCUPIED AMPPCP SITE

2c8l: CRYSTAL STRUCTURE OF (SR) CALCIUM-ATPASE E2(TG) FORM

2c9m: STRUCTURE OF (SR) CALCIUM-ATPASE IN THE CA2E1 STATE SOLVED IN A P1 CRYSTAL FORM.

2dqs: Crystal structure of the calcium pump with amppcp in the absence of calcium

2ear: P21 crystal of the SR CA2+-ATPase with bound TG

2eas: Crystal structure of the SR CA2+-ATPASE with bound CPA

2eat: Crystal structure of the SR CA2+-ATPASE with bound CPA and TG

2eau: Crystal structure of the SR CA2+-ATPASE with bound CPA in the presence of curcumin

2o9j: Crystal structure of calcium atpase with bound magnesium fluoride and cyclopiazonic acid

2oa0: Crystal structure of Calcium ATPase with bound ADP and cyclopiazonic acid

v  d  e

v  d  e

Hydrolases: acid anhydride hydrolases (EC 3.6)

3.6.1

Pyrophosphatase (Inorganic, Thiamine) Apyrase Thiamine triphosphatase

3.6.2

Adenylylsulfatase Phosphoadenylylsulfatase

3.6.3-4: ATPase

3.6.3

Cu++ (3.6.3.4)

Menkes/ATP7A Wilson/ATP7B

Ca+ (3.6.3.8)

SERCA (ATP2A1, ATP2A2, ATP2A3) Plasma membrane (ATP2B1, ATP2B2, ATP2B3, ATP2B4) SPCA (ATP2C1, ATP2C2)

Na+/K+ (3.6.3.9)

ATP1A1 ATP1A2 ATP1A3 ATP1A4 ATP1B1 ATP1B2 ATP1B3 ATP1B4

H+/K+ (3.6.3.10)

ATP4A

Other P-type ATPase

ATP8B1 ATP10A ATP11B ATP12A ATP13A2 ATP13A3

3.6.4

Dynein Kinesin Myosin

3.6.5: GTPase

3.6.5.1: Heterotrimeric G protein

Gs Gi (GNAI1, GNAI2, GNAI3) Gq/11 (GNAQ, GNA11) G12/13 (GNA12, GNA13) Transducin (GNAT1, GNAT2)

3.6.5.2: Small GTPase > Ras superfamily

Ras Rab (Rab27) Arf (Arf6) Ran Rheb Rho family (RhoA, RhoB, CDC42, Rac1) Rap

3.6.5.3: Elongation factor

Prokaryotic (EF-Tu, EF-G) Eukaryotic

3.6.5.5-6: Other

Dynamin (is a GTPase, is not a G protein) Tubulin

Categories: Human proteins | Chromosome 16 gene stubs