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Nature - Human host factors required for influenza virus replication near-final version

A

Alan

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http://www.nature.com/nature/journal/vnfv/ncurrent/abs/nature08699.html



Nature advance online publication 21 December 2009 | doi:10.1038/nature08699; Received 24 September 2009; Accepted 24 November 2009; Published online 21 December 2009

Human host factors required for influenza virus replicationnear-final version

Renate K?nig1,9, Silke Stertz4,9, Yingyao Zhou7, Atsushi Inoue1, H. -Heinrich Hoffmann4, Suchita Bhattacharyya2, Judith G. Alamares4, Donna M. Tscherne4, Mila B. Ortigoza4, Yuhong Liang4, Qinshan Gao4, Shane E. Andrews3, Sourav Bandyopadhyay8, Paul De Jesus1, Buu P. Tu7, Lars Pache1, Crystal Shih1, Anthony Orth7, Ghislain Bonamy7, Loren Miraglia7, Trey Ideker8, Adolfo Garc?a-Sastre4,5,6, John A. T. Young2, Peter Palese4,5, Megan L. Shaw4,9 & Sumit K. Chanda1,9

1. Infectious and Inflammatory Disease Center, Burnham Institute for Medical Research, 10901 North Torrey Pines Road,
2. Nomis Center for Immunobiology and Microbial Pathogenesis, The Salk Institute for Biological Studies, 10010 North Torrey Pines Road,
3. Gene Expression Laboratory, The Salk Institute for Biological Studies, 10010 North Torrey Pines Road, La Jolla, California 92037, USA
4. Department of Microbiology,
5. Department of Medicine, Division of Infectious Diseases,
6. Global Health and Emerging Pathogens Institute, Mount Sinai School of Medicine, One Gustave L. Levy Place, New York, New York 10029, USA
7. Genomics Institute of the Novartis Research Foundation, 10675 John J Hopkins Drive, San Diego, California 92121, USA
8. Departments of Medicine and Bioengineering, University of California, San Diego, Pharmaceutical Sciences Building, 9500 Gilman Drive, La Jolla, California 92093, USA
9. These authors contributed equally to this work.

Correspondence to: Megan L. Shaw4,9Sumit K. Chanda1,9 Correspondence and requests for materials should be addressed to S.K.C. (Email: schanda@burnham.org) or M.L.S. (Email: megan.shaw@mssm.edu).

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Influenza A virus is an RNA virus that encodes up to 11 proteins and this small coding capacity demands that the virus use the host cellular machinery for many aspects of its life cycle1. Knowledge of these host cell requirements not only informs us of the molecular pathways exploited by the virus but also provides further targets that could be pursued for antiviral drug development. Here we use an integrative systems approach, based on genome-wide RNA interference screening, to identify 295 cellular cofactors required for early-stage influenza virus replication. Within this group, those involved in kinase-regulated signalling, ubiquitination and phosphatase activity are the most highly enriched, and 181 factors assemble into a highly significant host?pathogen interaction network. Moreover, 219 of the 295 factors were confirmed to be required for efficient wild-type influenza virus growth, and further analysis of a subset of genes showed 23 factors necessary for viral entry, including members of the vacuolar ATPase (vATPase) and COPI-protein families, fibroblast growth factor receptor (FGFR) proteins, and glycogen synthase kinase 3 (GSK3)-β. Furthermore, 10 proteins were confirmed to be involved in post-entry steps of influenza virus replication. These include nuclear import components, proteases, and the calcium/calmodulin-dependent protein kinase (CaM kinase) IIβ (CAMK2B). Notably, growth of swine-origin H1N1 influenza virus is also dependent on the identified host factors, and we show that small molecule inhibitors of several factors, including vATPase and CAMK2B, antagonize influenza virus replication.
 
Re: Nature - Human host factors required for influenza virus replicationnear-final version

Re: Nature - Human host factors required for influenza virus replicationnear-final version

CAMK2B

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<!-- start content --> <table style="background: rgb(255, 255, 255) none repeat scroll 0% 0%; -moz-background-clip: border; -moz-background-origin: padding; -moz-background-inline-policy: continuous; width: 280px;" align="right" border="0"> <tbody><tr> <td align="right">edit</td> </tr> </tbody></table> <table class="infobox" style="width: 22em; font-size: 88%; line-height: 1.5em;"> <tbody><tr> <th colspan="3" style="font-size: 125%; text-align: center;">Calcium/calmodulin-dependent protein kinase (CaM kinase) II beta</th> </tr> <tr> <td colspan="3" style="text-align: center;"></td> </tr> <tr> <td colspan="3" style="text-align: center;">PDB rendering based on 2ux0.</td> </tr> <tr> <th colspan="3" style="text-align: center; background-color: rgb(221, 221, 221);">Available structures</th> </tr> <tr> <td colspan="3" style="text-align: center;">2ux0</td> </tr> <tr> <th colspan="3" style="text-align: center; background-color: rgb(221, 221, 221);">Identifiers</th> </tr> <tr> <th style="background-color: rgb(195, 253, 184); text-align: left;">Symbols</th> <td colspan="2" style="background-color: rgb(238, 238, 238); text-align: center;">CAMK2B; CAM2; CAMK2; CAMKB; MGC29528</td> </tr> <tr> <th style="background-color: rgb(195, 253, 184); text-align: left;">External IDs</th> <td colspan="2" style="background-color: rgb(238, 238, 238); text-align: center;">OMIM: 607707 MGI: 88257 HomoloGene: 69002</td> </tr> <tr> <td colspan="3" style="margin: 0pt; padding: 0pt; text-align: center;"> <table id="collapsibleTable0" class="collapsible collapsed" style="border: medium none ; width: 100%;"> <tbody><tr> <th colspan="3" style="background-color: rgb(221, 221, 221);">[show]Gene ontology</th> </tr> <tr style="display: none;"> <th style="background-color: rgb(195, 253, 184); text-align: left;">Molecular function</th> <td colspan="2" style="background-color: rgb(238, 238, 238); text-align: left;"><big>?</big> nucleotide binding
<big>?</big> protein serine/threonine kinase activity
<big>?</big> calmodulin-dependent protein kinase activity
<big>?</big> calmodulin binding
<big>?</big> ATP binding
<big>?</big> transferase activity
</td> </tr> <tr style="display: none;"> <th style="background-color: rgb(195, 253, 184); text-align: left;">Biological process</th> <td colspan="2" style="background-color: rgb(238, 238, 238); text-align: left;"><big>?</big> G1/S transition of mitotic cell cycle
<big>?</big> calcium ion transport
<big>?</big> signal transduction
<big>?</big> protein amino acid autophosphorylation
</td> </tr> </tbody></table> </td> </tr> <tr> <th colspan="3" style="text-align: center; background-color: rgb(221, 221, 221);">RNA expression pattern</th> </tr> <tr> <td colspan="3" style="text-align: center;"></td> </tr> <tr> <td colspan="3" style="text-align: center;"></td> </tr> <tr> <td colspan="3" style="text-align: center;"></td> </tr> <tr> <td colspan="3" style="text-align: center;">More reference expression data</td> </tr> <tr> <th colspan="3" style="text-align: center; background-color: rgb(221, 221, 221);">Orthologs</th> </tr> <tr> <th style="background-color: rgb(195, 253, 184); text-align: left;">Species</th> <th style="background-color: rgb(238, 238, 238); text-align: left;">Human</th> <th style="background-color: rgb(238, 238, 238); text-align: left;">Mouse</th> </tr> <tr> <th style="background-color: rgb(195, 253, 184); text-align: left;">Entrez</th> <td style="background-color: rgb(238, 238, 238);">816</td> <td style="background-color: rgb(238, 238, 238);">12323</td> </tr> <tr> <th style="background-color: rgb(195, 253, 184); text-align: left;">Ensembl</th> <td style="background-color: rgb(238, 238, 238);">ENSG00000058404</td> <td style="background-color: rgb(238, 238, 238);">ENSMUSG00000057897</td> </tr> <tr> <th style="background-color: rgb(195, 253, 184); text-align: left;">UniProt</th> <td style="background-color: rgb(238, 238, 238);">Q13554</td> <td style="background-color: rgb(238, 238, 238);">Q8BL41</td> </tr> <tr> <th rowspan="2" style="background-color: rgb(195, 253, 184); text-align: left;">RefSeq</th> <td style="background-color: rgb(238, 238, 238);">XM_001125861 (mRNA)</td> <td style="background-color: rgb(238, 238, 238);">NM_007595 (mRNA)</td> </tr> <tr> <td style="background-color: rgb(238, 238, 238);">XP_001125861 (protein)</td> <td style="background-color: rgb(238, 238, 238);">NP_031621 (protein)</td> </tr> <tr> <th style="background-color: rgb(195, 253, 184); text-align: left;">Location</th> <td style="background-color: rgb(238, 238, 238);">Chr 7:
44.23 - 44.33 Mb</td> <td style="background-color: rgb(238, 238, 238);">Chr 11:
5.87 - 5.97 Mb</td> </tr> <tr> <th style="background-color: rgb(195, 253, 184); text-align: left;">PubMed search</th> <td style="background-color: rgb(238, 238, 238);">[1]</td> <td style="background-color: rgb(238, 238, 238);">[2]</td> </tr> </tbody></table> Calcium/calmodulin-dependent protein kinase type II beta chain is an enzyme that in humans is encoded by the CAMK2B gene.
The product of this gene belongs to the serine/threonine protein kinase family and to the Ca(2+)/calmodulin-dependent protein kinase subfamily. Calcium signaling is crucial for several aspects of plasticity at glutamatergic synapses. In mammalian cells, the enzyme is composed of four different chains: alpha, beta, gamma, and delta. The product of this gene is a beta chain. It is possible that distinct isoforms of this chain have different cellular localizations and interact differently with calmodulin. Eight transcript variants encoding eight distinct isoforms have been identified for this gene.<sup id="cite_ref-entrez_0-0" class="reference">[1]</sup>
[edit] Interactions

CAMK2B has been shown to interact with Actinin alpha 4.<sup id="cite_ref-pmid11160423_1-0" class="reference">[2]</sup>
[edit] References


  1. ^ "Entrez Gene: CAMK2B calcium/calmodulin-dependent protein kinase (CaM kinase) II beta". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=816.
  2. ^ Walikonis, R S; Oguni A, Khorosheva E M, Jeng C J, Asuncion F J, Kennedy M B (Jan. 2001). "Densin-180 forms a ternary complex with the (alpha)-subunit of Ca2+/calmodulin-dependent protein kinase II and (alpha)-actinin". J. Neurosci. (United States) 21 (2): 423?33. PMID 11160423.

[edit] Further reading


  • Yamamoto H (2002). "[Molecular mechanisms of the intracellular localizations of Ca2+/calmodulin-dependent protein kinase II isoforms, and their physiological functions]". Tanpakushitsu Kakusan Koso 47 (3): 241?7. PMID 11889801.
  • Thiel G, Czernik AJ, Gorelick F, et al. (1988). "Ca2+/calmodulin-dependent protein kinase II: identification of threonine-286 as the autophosphorylation site in the alpha subunit associated with the generation of Ca2+-independent activity.". Proc. Natl. Acad. Sci. U.S.A. 85 (17): 6337?41. doi:10.1073/pnas.85.17.6337. PMID 2842767.
  • Schworer CM, Colbran RJ, Keefer JR, Soderling TR (1988). "Ca2+/calmodulin-dependent protein kinase II. Identification of a regulatory autophosphorylation site adjacent to the inhibitory and calmodulin-binding domains.". J. Biol. Chem. 263 (27): 13486?9. PMID 3417668.
  • Penad?s JR, Bernal D, Revert F, et al. (1995). "Characterization and expression of multiple alternatively spliced transcripts of the Goodpasture antigen gene region. Goodpasture antibodies recognize recombinant proteins representing the autoantigen and one of its alternative forms.". Eur. J. Biochem. 229 (3): 754?60. doi:10.1111/j.1432-1033.1995.tb20524.x. PMID 7758473.
  • Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene 138 (1-2): 171?4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
  • Omkumar RV, Kiely MJ, Rosenstein AJ, et al. (1997). "Identification of a phosphorylation site for calcium/calmodulindependent protein kinase II in the NR2B subunit of the N-methyl-D-aspartate receptor.". J. Biol. Chem. 271 (49): 31670?8. doi:10.1074/jbc.271.49.31670. PMID 8940188.
  • Tombes RM, Krystal GW (1997). "Identification of novel human tumor cell-specific CaMK-II variants.". Biochim. Biophys. Acta 1355 (3): 281?92. doi:10.1016/S0167-4889(96)00141-3. PMID 9060999.
  • Moyers JS, Bilan PJ, Zhu J, Kahn CR (1997). "Rad and Rad-related GTPases interact with calmodulin and calmodulin-dependent protein kinase II.". J. Biol. Chem. 272 (18): 11832?9. doi:10.1074/jbc.272.18.11832. PMID 9115241.
  • Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library.". Gene 200 (1-2): 149?56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
  • Chang BH, Mukherji S, Soderling TR (1998). "Characterization of a calmodulin kinase II inhibitor protein in brain.". Proc. Natl. Acad. Sci. U.S.A. 95 (18): 10890?5. doi:10.1073/pnas.95.18.10890. PMID 9724800.
  • Rochlitz H, Voigt A, Lankat-Buttgereit B, et al. (2000). "Cloning and quantitative determination of the human Ca2+/calmodulin-dependent protein kinase II (CaMK II) isoforms in human beta cells.". Diabetologia 43 (4): 465?73. doi:10.1007/s001250051330. PMID 10819240.
  • Wang P, Wu YL, Zhou TH, et al. (2000). "Identification of alternative splicing variants of the beta subunit of human Ca(2+)/calmodulin-dependent protein kinase II with different activities.". FEBS Lett. 475 (2): 107?10. doi:10.1016/S0014-5793(00)01634-3. PMID 10858498.
  • Novak G, Seeman P, Tallerico T (2001). "Schizophrenia: elevated mRNA for calcium-calmodulin-dependent protein kinase IIbeta in frontal cortex.". Brain Res. Mol. Brain Res. 82 (1-2): 95?100. doi:10.1016/S0169-328X(00)00188-1. PMID 11042361.
  • Hartley JL, Temple GF, Brasch MA (2001). "DNA cloning using in vitro site-specific recombination.". Genome Res. 10 (11): 1788?95. doi:10.1101/gr.143000. PMID 11076863.
  • Walikonis RS, Oguni A, Khorosheva EM, et al. (2001). "Densin-180 forms a ternary complex with the (alpha)-subunit of Ca2+/calmodulin-dependent protein kinase II and (alpha)-actinin.". J. Neurosci. 21 (2): 423?33. PMID 11160423.
  • Liao GY, Wagner DA, Hsu MH, Leonard JP (2001). "Evidence for direct protein kinase-C mediated modulation of N-methyl-D-aspartate receptor current.". Mol. Pharmacol. 59 (5): 960?4. PMID 11306676.
  • Yue C, Sanborn BM (2001). "KN-93 inhibition of G protein signaling is independent of the ability of Ca2+/calmodulin-dependent protein kinase II to phosphorylate phospholipase Cbeta3 on 537-Ser.". Mol. Cell. Endocrinol. 175 (1-2): 149?56. doi:10.1016/S0303-7207(01)00383-5. PMID 11325525.
  • Schell MJ, Erneux C, Irvine RF (2001). "Inositol 1,4,5-trisphosphate 3-kinase A associates with F-actin and dendritic spines via its N terminus.". J. Biol. Chem. 276 (40): 37537?46. doi:10.1074/jbc.M104101200. PMID 11468283.
  • Li G, Laabich A, Liu LO, et al. (2002). "Molecular cloning and sequence analyses of calcium/calmodulin-dependent protein kinase II from fetal and adult human brain. Sequence analyses of human brain calciuum/calmodulin-dependent protein kinase II.". Mol. Biol. Rep. 28 (1): 35?41. doi:10.1023/A:1011951814898. PMID 11710563.
  • Poggi A, Carosio R, Spaggiari GM, et al. (2002). "NK cell activation by dendritic cells is dependent on LFA-1-mediated induction of calcium-calmodulin kinase II: inhibition by HIV-1 Tat C-terminal domain.". J. Immunol. 168 (1): 95?101. PMID 11751951.
 
Re: Nature - Human host factors required for influenza virus replicationnear-final version

Re: Nature - Human host factors required for influenza virus replicationnear-final version

ATPase

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<!-- start content -->
Adenosine triphosphate



Adenosine diphosphate


ATPases are a class of enzymes that catalyze the decomposition of adenosine triphosphate (ATP) into adenosine diphosphate (ADP) and a free phosphate ion. This dephosphorylation reaction releases energy, which the enzyme (in most cases) harnesses to drive other chemical reactions that would not otherwise occur. This process is widely used in all known forms of life.
Some such enzymes are integral membrane proteins (anchored within biological membranes), and move solutes across the membrane, typically against their concentration gradient. These are called transmembrane ATPases.
<table id="toc" class="toc"> <tbody><tr> <td> Contents

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</td> </tr> </tbody></table> <script type="text/javascript"> //<![CDATA[ if (window.showTocToggle) { var tocShowText = "show"; var tocHideText = "hide"; showTocToggle(); } //]]> </script> [edit] Functions


Na<sup>+</sup>/K<sup>+</sup>ATPase


Transmembrane ATPases import many of the metabolites necessary for cell metabolism and export toxins, wastes, and solutes that can hinder cellular processes. An important example is the sodium-potassium exchanger (or Na<sup>+</sup>/K<sup>+</sup>ATPase), which establishes the ionic concentration balance that maintains the cell potential. Another example is the hydrogen potassium ATPase (H<sup>+</sup>/K<sup>+</sup>ATPase or gastric proton pump) that acidifies the contents of the stomach.
Besides exchangers, other categories of transmembrane ATPase include co-transporters and pumps (however, some exchangers are also pumps). Some of these, like the Na<sup>+</sup>/K<sup>+</sup>ATPase, cause a net flow of charge, but others do not. These are called "electrogenic" and "nonelectrogenic" transporters, respectively.
[edit] Mechanism

The coupling between ATP hydrolysis and transport is more or less a strict chemical reaction, in which a fixed number of solute molecules are transported for each ATP molecule that is hydrolyzed; for example, 3 Na<sup>+</sup> ions out of the cell and 2 K<sup>+</sup> ions inward per ATP hydrolyzed, for the Na<sup>+</sup>/K<sup>+</sup> exchanger.
Transmembrane ATPases harness the chemical potential energy of ATP, because they perform mechanical work: they transport solutes in a direction opposite to their thermodynamically preferred direction of movement?that is, from the side of the membrane where they are in low concentration to the side where they are in high concentration. This process is considered active transport.
For example, the blocking of the vesicular H+-ATPAses would increase the pH inside vesicles and decrease the pH of the cytoplasm.
[edit] Transmembrane ATP synthases

Main article: ATP synthase
The ATP synthase of mitochondria and chloroplasts is an anabolic enzyme that harnesses the energy of a transmembrane proton gradient as an energy source for adding an inorganic phosphate group to a molecule of adenosine diphosphate (ADP) to form a molecule of adenosine triphosphate (ATP).
This enzyme works when a proton moves down the concentration gradient, giving the enzyme a spinning motion. This unique spinning motion bonds ADP and P together to create ATP.
ATP synthase can also function in reverse, that is, use energy released by ATP hydrolysis to pump protons against their thermodynamic gradient.
[edit] Classification

There are different types of ATPases, which can differ in function (ATP synthesis and/or hydrolysis), structure (F-, V- and A-ATPases contain rotary motors) and in the type of ions they transport.

  • F-ATPases (F1FO-ATPases) in mitochondria, chloroplasts and bacterial plasma membranes are the prime producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts).
  • V-ATPases (V1VO-ATPases) are primarily found in eukaryotic vacuoles, catalysing ATP hydrolysis to transport solutes and lower pH in organelles.
  • A-ATPases (A1AO-ATPases) are found in Archaea and function like F-ATPases.
  • P-ATPases (E1E2-ATPases) are found in bacteria, fungi and in eukaryotic plasma membranes and organelles, and function to transport a variety of different ions across membranes.
  • E-ATPases are cell-surface enzymes that hydrolyse a range of NTPs, including extracellular ATP.
[edit] P-ATPase

Main article: P-ATPase
P-ATPases (sometime known as E1-E2 ATPases) are found in bacteria and in a number of eukaryotic plasma membranes and organelles. P-ATPases function to transport a variety of different compounds, including ions and phospholipids, across a membrane using ATP hydrolysis for energy. There are many different classes of P-ATPases, each of which transports a specific type of ion: H+, Na+, K+, Mg2+, Ca2+, Ag+ and Ag2+, Zn2+, Co2+, Pb2+, Ni2+, Cd2+, Cu+ and Cu2+. P-ATPases can be composed of one or two polypeptides, and can usually assume two main conformations called E1 and E2.
[edit] Human genes

(See Human ATPase)

[edit] See also


[edit] Additional images

<table class="gallery" cellpadding="0" cellspacing="0"> <tbody><tr> <td>

AAA+ ATPases (three examples)


</td> </tr> </tbody></table> [edit] External links


<table class="navbox" style="" cellspacing="0"> <tbody><tr> <td style="padding: 2px;"> <table id="collapsibleTable0" class="nowraplinks collapsible autocollapse" style="background: transparent none repeat scroll 0% 0%; width: 100%; -moz-background-clip: border; -moz-background-origin: padding; -moz-background-inline-policy: continuous; color: inherit;" cellspacing="0"> <tbody><tr> <th style="background: rgb(231, 220, 195) none repeat scroll 0% 0%; -moz-background-clip: border; -moz-background-origin: padding; -moz-background-inline-policy: continuous;" colspan="2" class="navbox-title">[show]
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Membrane transport protein: ion pumps</th> </tr> <tr style="height: 2px; display: none;"> <td></td> </tr> <tr style="display: none;"> <td class="navbox-group" style="background-color: AntiqueWhite;">Symporter, Cotransporter</td> <td style="padding: 0px; text-align: left; border-left-width: 2px; border-left-style: solid; width: 100%;" class="navbox-list navbox-odd"> Na+/K+/2Cl- - Na/Pi3 - Na+/Cl- - Na/glucose - Na+/I- - Cl-/K+ (4, 5)
</td> </tr> <tr style="height: 2px; display: none;"> <td></td> </tr> <tr style="display: none;"> <td class="navbox-group" style="background-color: AntiqueWhite;">Antiporter (exchanger)</td> <td style="padding: 0px; text-align: left; border-left-width: 2px; border-left-style: solid; width: 100%;" class="navbox-list navbox-even"> Na+/H+ - Na+/Ca2+ (Na+/(Ca2+-K+)) - Cl-/HCO3- (Band 3) - Cl-formate exchanger - Cl-oxalate exchanger
</td> </tr> <tr style="height: 2px; display: none;"> <td></td> </tr> <tr style="display: none;"> <td class="navbox-group" style="background-color: AntiqueWhite;">P-type ATPase</td> <td style="padding: 0px; text-align: left; border-left-width: 2px; border-left-style: solid; width: 100%;" class="navbox-list navbox-odd"> Cu++ - Ca+ (SERCA, PMCA, SPCA) - Na+/K+ - H+/K+ - H+
</td> </tr> <tr style="height: 2px; display: none;"> <td></td> </tr> <tr style="display: none;"> <td class="navbox-group" style="background-color: AntiqueWhite;">F- and V-type ATPase</td> <td style="padding: 0px; text-align: left; border-left-width: 2px; border-left-style: solid; width: 100%;" class="navbox-list navbox-even"> ATP synthase - H+ (F-type) - H+ (V-type)
</td> </tr> <tr style="height: 2px; display: none;"> <td></td> </tr> <tr style="display: none;"> <td class="navbox-group" style="background-color: AntiqueWhite;">Other</td> <td style="padding: 0px; text-align: left; border-left-width: 2px; border-left-style: solid; width: 100%;" class="navbox-list navbox-odd"> Halorhodopsin (Cl-) - bacteriorhodopsin (H+)
</td> </tr> </tbody></table> </td> </tr> </tbody></table> <table class="navbox" style="" cellspacing="0"> <tbody><tr> <td style="padding: 2px;"> <table id="collapsibleTable1" class="nowraplinks collapsible autocollapse" style="background: transparent none repeat scroll 0% 0%; width: 100%; -moz-background-clip: border; -moz-background-origin: padding; -moz-background-inline-policy: continuous; color: inherit;" cellspacing="0"> <tbody><tr> <th style="background: rgb(231, 220, 195) none repeat scroll 0% 0%; -moz-background-clip: border; -moz-background-origin: padding; -moz-background-inline-policy: continuous;" colspan="2" class="navbox-title">[show]
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Hydrolases: acid anhydride hydrolases (EC 3.6)</th> </tr> <tr style="height: 2px; display: none;"> <td></td> </tr> <tr style="display: none;"> <td class="navbox-group" style="background-color: AntiqueWhite;">3.6.1</td> <td style="padding: 0px; text-align: left; border-left-width: 2px; border-left-style: solid; width: 100%;" class="navbox-list navbox-odd"> Pyrophosphatase (Inorganic, Thiamine) ? Apyrase ? Thiamine triphosphatase
</td> </tr> <tr style="height: 2px; display: none;"> <td></td> </tr> <tr style="display: none;"> <td class="navbox-group" style="background-color: AntiqueWhite;">3.6.2</td> <td style="padding: 0px; text-align: left; border-left-width: 2px; border-left-style: solid; width: 100%;" class="navbox-list navbox-even"> Adenylylsulfatase ? Phosphoadenylylsulfatase
</td> </tr> <tr style="height: 2px; display: none;"> <td></td> </tr> <tr style="display: none;"> <td class="navbox-group" style="background-color: AntiqueWhite;">3.6.3-4: ATPase</td> <td style="padding: 0px; text-align: left; border-left-width: 2px; border-left-style: solid; width: 100%;" class="navbox-list navbox-odd"> <table class="nowraplinks navbox-subgroup" style="width: 100%;" cellspacing="0"> <tbody><tr> <td class="navbox-group" style="padding-left: 0em; padding-right: 0em; background-color: AntiqueWhite;"> 3.6.3
</td> <td style="padding: 0px; text-align: left; border-left-width: 2px; border-left-style: solid; width: 100%;" class="navbox-list navbox-odd"> <table class="nowraplinks navbox-subgroup" style="width: 100%;" cellspacing="0"> <tbody><tr> <td class="navbox-group" style="padding-left: 0em; padding-right: 0em; background-color: AntiqueWhite;"> Cu++ (3.6.3.4)
</td> <td style="padding: 0px; text-align: left; border-left-width: 2px; border-left-style: solid; width: 100%;" class="navbox-list navbox-odd"> Menkes/ATP7A ? Wilson/ATP7B
</td> </tr> <tr style="height: 2px;"> <td></td> </tr> <tr> <td class="navbox-group" style="padding-left: 0em; padding-right: 0em; background-color: AntiqueWhite;"> Ca+ (3.6.3.8)
</td> <td style="padding: 0px; text-align: left; border-left-width: 2px; border-left-style: solid; width: 100%;" class="navbox-list navbox-even"> SERCA (ATP2A1, ATP2A2, ATP2A3) ? Plasma membrane (ATP2B1, ATP2B2, ATP2B3, ATP2B4) ? SPCA (ATP2C1, ATP2C2)
</td> </tr> <tr style="height: 2px;"> <td></td> </tr> <tr> <td class="navbox-group" style="padding-left: 0em; padding-right: 0em; background-color: AntiqueWhite;"> Na+/K+ (3.6.3.9)
</td> <td style="padding: 0px; text-align: left; border-left-width: 2px; border-left-style: solid; width: 100%;" class="navbox-list navbox-odd"> ATP1A1 ? ATP1A2 ? ATP1A3 ? ATP1A4 ? ATP1B1 ? ATP1B2 ? ATP1B3 ? ATP1B4
</td> </tr> <tr style="height: 2px;"> <td></td> </tr> <tr> <td class="navbox-group" style="padding-left: 0em; padding-right: 0em; background-color: AntiqueWhite;"> H+/K+ (3.6.3.10)
</td> <td style="padding: 0px; text-align: left; border-left-width: 2px; border-left-style: solid; width: 100%;" class="navbox-list navbox-even"> ATP4A
</td> </tr> <tr style="height: 2px;"> <td></td> </tr> <tr> <td class="navbox-group" style="padding-left: 0em; padding-right: 0em; background-color: AntiqueWhite;"> Other P-type ATPase
</td> <td style="padding: 0px; text-align: left; border-left-width: 2px; border-left-style: solid; width: 100%;" class="navbox-list navbox-odd"> ATP8B1 ? ATP10A ? ATP11B ? ATP12A ? ATP13A2 ? ATP13A3 ?
</td> </tr> </tbody></table> </td> </tr> <tr style="height: 2px;"> <td></td> </tr> <tr> <td class="navbox-group" style="padding-left: 0em; padding-right: 0em; background-color: AntiqueWhite;"> 3.6.4
</td> <td style="padding: 0px; text-align: left; border-left-width: 2px; border-left-style: solid; width: 100%;" class="navbox-list navbox-even"> Dynein ? Kinesin ? Myosin
</td> </tr> </tbody></table> </td> </tr> <tr style="height: 2px; display: none;"> <td></td> </tr> <tr style="display: none;"> <td class="navbox-group" style="background-color: AntiqueWhite;">3.6.5: GTPase</td> <td style="padding: 0px; text-align: left; border-left-width: 2px; border-left-style: solid; width: 100%;" class="navbox-list navbox-even"> <table class="nowraplinks navbox-subgroup" style="width: 100%;" cellspacing="0"> <tbody><tr> <td class="navbox-group" style="padding-left: 0em; padding-right: 0em; background-color: AntiqueWhite;"> 3.6.5.1: Heterotrimeric G protein
</td> <td style="padding: 0px; text-align: left; border-left-width: 2px; border-left-style: solid; width: 100%;" class="navbox-list navbox-odd"> G<sub>αs</sub> ? G<sub>αi</sub> (GNAI1, GNAI2, GNAI3) ? G<sub>αq/11</sub> (GNAQ, GNA11) ? G<sub>α12/13</sub> (GNA12, GNA13) ? Transducin (GNAT1, GNAT2)
</td> </tr> <tr style="height: 2px;"> <td></td> </tr> <tr> <td class="navbox-group" style="padding-left: 0em; padding-right: 0em; background-color: AntiqueWhite;"> 3.6.5.2: Small GTPase > Ras superfamily
</td> <td style="padding: 0px; text-align: left; border-left-width: 2px; border-left-style: solid; width: 100%;" class="navbox-list navbox-even"> Ras ? Rab (Rab27) ? Arf (Arf6) ? Ran ? Rheb ? Rho family (RhoA, RhoB, CDC42, Rac1) ? Rap
</td> </tr> <tr style="height: 2px;"> <td></td> </tr> <tr> <td class="navbox-group" style="padding-left: 0em; padding-right: 0em; background-color: AntiqueWhite;"> 3.6.5.3: Elongation factor
</td> <td style="padding: 0px; text-align: left; border-left-width: 2px; border-left-style: solid; width: 100%;" class="navbox-list navbox-odd"> Prokaryotic (EF-Tu, EF-Ts, EF-G) ? Eukaryotic
</td> </tr> <tr style="height: 2px;"> <td></td> </tr> <tr> <td class="navbox-group" style="padding-left: 0em; padding-right: 0em; background-color: AntiqueWhite;"> 3.6.5.5-6: Other
</td> <td style="padding: 0px; text-align: left; border-left-width: 2px; border-left-style: solid; width: 100%;" class="navbox-list navbox-even"> Dynamin (is a GTPase, is not a G protein) ? Tubulin
</td> </tr> </tbody></table> </td> </tr> </tbody></table> </td> </tr> </tbody></table> [show]
v ? d ? e
​
Hydrolases: acid anhydride hydrolases (EC 3.6)
 
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