WordNet
- used of flowers having more than the usual number of petals in crowded or overlapping arrangements; "double chrysanthemums have many rows of petals and are usually spherical or hemispherical"
- increase twofold; "The population doubled within 50 years" (同)duplicate
- a base hit on which the batter stops safely at second base; "he hit a double to deep centerfield" (同)two-base hit, two-bagger, two-baser
- someone who closely resembles a famous person (especially an actor); "he could be Gingrichs double"; "shes the very image of her mother" (同)image, look-alike
- a stand-in for movie stars to perform dangerous stunts; "his first job in Hollywood was as a double for Clark Gable" (同)stunt man, stunt woman
- a quantity that is twice as great as another; "36 is the double of 18"
- twice as great or many; "ate a double portion"; "the dose is doubled"; "a twofold increase" (同)doubled, twofold, two-fold
- consisting of or involving two parts or components usually in pairs; "an egg with a double yolk"; "a double (binary) star"; "double doors"; "dual controls for pilot and copilot"; "duple (or double) time consists of two (or a multiple of two) beats to a measure" (同)dual, duple
- having more than one decidedly dissimilar aspects or qualities; "a double (or dual) role for an actor"; "the office of a clergyman is twofold; public preaching and private influence"- R.W.Emerson; "every episode has its double and treble meaning"-Frederick Harrison (同)dual, twofold, two-fold, treble, threefold, three-fold
- having two meanings with intent to deceive; "a sly double meaning"; "spoke with forked tongue" (同)forked
- bridge: make a demand for (a card or suit)
- do double duty; serve two purposes or have two functions; "She doubles as his wife and secretary"
- downward and forward; "he was bent double with pain"
- hit a two-base hit
- large enough for two; "a double bed"; "a double room"
- two together; "some people sleep better double"
- drive (a vessel) ashore
- line consisting of a complex of fibers or filaments that are twisted together to form a thread or a rope or a cable
- a pattern forming a unity within a larger structural whole; "he tried to pick up the strands of his former life"; "I could hear several melodic strands simultaneously"
- a poetic term for a shore (as the area periodically covered and uncovered by the tides)
- relying on or requiring a person or thing for support, supply, or what is needed; "dependent children"; "dependent on moisture"
- addicted to a drug (同)dependant, drug-addicted, hooked, strung-out
- contingent on something else (同)dependant, qualified
- (of a clause) unable to stand alone syntactically as a complete sentence; "a subordinate (or dependent) clause functions as a noun or adjective or adverb within a sentence" (同)subordinate
- any of a large group of nitrogenous organic compounds that are essential constituents of living cells; consist of polymers of amino acids; essential in the diet of animals for growth and for repair of tissues; can be obtained from meat and eggs and milk and legumes; "a diet high in protein"
- the 18th letter of the Roman alphabet (同)r
PrepTutorEJDIC
- (数量・強さ・重さ・価値などが)『2倍の』,倍の / 『二重の』,二様の;複の,対の,2人用の / 表裏のある,二心ある / (意味が)二様にとれる,あいまいな / (花が)八重の,重弁の / 『2倍に』,2倍だけ(twice) / 二重に,二様に / 対をなして,二人いっしょに / 〈U〉『2倍』[の数量・価額など] / 〈C〉2倍のもの / 〈C〉よく似た人(物),生き写し / 〈C〉(映画の)代役 / 《複数形》《単数扱い》(テニスなどの)ダブルス / 〈C〉(獲物が追っ手を逃れるときなどの)逆走,急転回 / 〈C〉2塁打 / 〈C〉(ブリッジの点の)倍加 / 〈C〉(競馬・ドッグレースの)重勝式のかけ,複式 / …‘を'『2倍にする』 / …‘を'『二つ折りにする』 / …‘の'2倍の数(量)がある / 〈二役〉‘を'ひとりで演ずる / 〈船が〉〈岬〉‘を'回る / 『2倍になる』 / (…の役を)兼ねる《+『as』+『名』》 / (急に)取って返す,逆戻りする《+『back』》 / 二つ折りになる / (ブリッジで)相手のせり高を倍加する / 2塁打を打つ
- 〈船〉‘を'座礁させる / 《受動態で》〈人〉‘を'置き去りにする,困った状態におく / 〈船が〉座礁する / 〈人が〉途方に暮れる,立ち往生する / 岸,浜
- こ撚(よ)り(何本かより合わせて糸・なわなどにするその一本) / (より合わせた)糸,ひも;(頭髪の)房 / (真珠・ビーズなど)ひもに通したもの
- 『頼っている』,依存している,従属している / 扶養される人(家族)
- 蛋白(たんばく)質
- resistance / 17歳以下父兄同伴映画の表示 / rook
Wikipedia preview
出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2012/09/28 10:54:56」(JST)
[Wiki en表示]
| Eukaryotic translation initiation factor 2-alpha kinase 2 |
NMR structure of the double stranded RNA binding domain of EIF2AK2 based on PDB 1qu6. |
| Available structures |
| PDB |
Ortholog search: PDBe, RCSB |
| List of PDB id codes |
|
1QU6, 2A19, 2A1A
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| Identifiers |
| Symbols |
EIF2AK2; EIF2AK1; PKR; PRKR |
| External IDs |
OMIM: 176871 MGI: 1353449 HomoloGene: 48134 ChEMBL: 5785 GeneCards: EIF2AK2 Gene |
| EC number |
2.7.11.1 2.7.10.2, 2.7.11.1 |
| Gene Ontology |
| Molecular function |
• double-stranded RNA binding
• protein serine/threonine kinase activity
• eukaryotic translation initiation factor 2alpha kinase activity
• non-membrane spanning protein tyrosine kinase activity
• protein binding
• ATP binding
• protein phosphatase type 2A regulator activity
|
| Cellular component |
• cytosol
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| Biological process |
• translation
• protein phosphorylation
• virus-infected cell apoptotic process
• negative regulation of cell proliferation
• response to virus
• virus-host interaction
• modulation by virus of host cellular process
• viral infectious cycle
• evasion by virus of host immune response
• endoplasmic reticulum unfolded protein response
• negative regulation of osteoblast proliferation
• protein autophosphorylation
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| Sources: Amigo / QuickGO |
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| RNA expression pattern |
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| More reference expression data |
| Orthologs |
| Species |
Human |
Mouse |
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| Entrez |
5610 |
19106 |
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| Ensembl |
ENSG00000055332 |
ENSMUSG00000024079 |
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| UniProt |
P19525 |
Q03963 |
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| RefSeq (mRNA) |
NM_001135651.2 |
NM_011163.4 |
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| RefSeq (protein) |
NP_001129123.1 |
NP_035293.1 |
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| Location (UCSC) |
Chr 2:
37.33 – 37.38 Mb |
Chr 17:
78.85 – 78.88 Mb |
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| PubMed search |
[1] |
[2] |
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Protein kinase RNA-activated also known as protein kinase R (PKR), interferon-induced, double-stranded RNA-activated protein kinase, or eukaryotic translation initiation factor 2-alpha kinase 2 (EIF2AK2) is an enzyme that in humans is encoded by the EIF2AK2 gene.[1][2]
PKR protects against viral infections.
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Contents
- 1 Mechanism of action
- 2 Viral defense
- 3 Memory and learning
- 4 Fetal alcohol syndrome
- 5 Interactions
- 6 References
- 7 Further reading
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Mechanism of action
PKR is activated by double-stranded RNA (dsRNA), the synthesis of which is caused virally. PKR can also be activated by the protein PACT or by heparin. PKR contains an N-terminal dsRNA binding domain (dsRBD) and a C-terminal kinase domain, that gives it pro-apoptotic (cell-killing) functions. The dsRBD consists of two tandem copies of a conserved double stranded RNA binding motif, dsRBM1 and dsRBM2. PKR is induced by interferon in a latent state. Binding to dsRNA is believed to activate PKR by inducing dimerization and subsequent auto-phosphorylation reactions. In situations of viral infection, the dsRNA created by viral replication and gene expression binds to the N-terminal domain, activating the protein. Once active, PKR is able to phosphorylate the translation initiation factor EIF2A. This inhibits further cellular mRNA translation, thereby preventing viral protein synthesis. Active PKR is also able to mediate the activation of the transcription factor NFkB, by phosphorylating its inhibitory subunit, IkB. Activated NFkB upregulates the expression of Interferon cytokines, which work to spread the antiviral signal locally. Through complex mechanisms, active PKR is also able to induce cellular apoptosis, to prevent further viral spread.
Viral defense
Viruses have developed many mechanisms to outfox the PKR mechanism. It may be done by Decoy dsRNA, degradation, hiding of virus dsRNA, dimerization block, dephosphorylation of substrate or by a pseudosubstrate.
For instance, Epstein-Barr Virus (EBV) uses the gene EBER-1 to produce decoy dsRNA. This leads to cancers such as Burkitt's lymphoma, Hodgkin's Disease, nasopharyngeal carcinoma and various leukemias.
Viral defence mechanisms against PKR
| Defence type |
Virus |
Molecule |
| Decoy dsRNA |
Adenovirus |
VAI RNA |
| Epstein-Barr virus |
EBER |
| HIV |
TAR |
| PKR degradation |
Poliovirus |
2Apro |
| hide viral dsRNA |
Vaccinia virus |
E3L |
| Reovirus |
σ3 |
| Influenza virus |
NS1 |
| Dimerization block |
Influenza virus |
p58IPK |
| Hepatitis C virus |
NS5A |
| Pseudosubstrate |
Vaccinia virus |
K3L |
| HIV |
Tat |
| Dephosphorylation of substrate |
Herpes simplex virus |
ICP34.5 |
Memory and learning
PKR knockout mice or inhibition of PKR in mice enhances memory and learning.[3]
Fetal alcohol syndrome
PKR also mediates ethanol-induced protein synthesis inhibition and apoptosis which is linked to fetal alcohol syndrome.[4]
Interactions
Protein kinase R has been shown to interact with:
- ASK1,[5]
- DNAJC3,[6][6]
- ILF3,[7][8][9][10]
- METAP2,[11]
- P53,[12]
- PPP1CA,[13]
- PRKRA,[14][15]
- STAT1,[16][17] and
- TARBP2.[18][19]
References
- ^ "Entrez Gene: EIF2AK2 eukaryotic translation initiation factor 2-alpha kinase 2". http://www.ncbi.nlm.nih.gov/sites/entrez?db=gene&cmd=retrieve&dopt=default&list_uids=5610&rn=1.
- ^ Feng GS, Chong K, Kumar A, Williams BR (June 1992). "Identification of double-stranded RNA-binding domains in the interferon-induced double-stranded RNA-activated p68 kinase". Proc. Natl. Acad. Sci. U.S.A. 89 (12): 5447–51. doi:10.1073/pnas.89.12.5447. PMC 49309. PMID 1351683. //www.ncbi.nlm.nih.gov/pmc/articles/PMC49309/.
- ^ Zhu PJ, Huang W, Kalikulov D, Yoo JW, Placzek AN, Stoica L, Zhou H, Bell JC, Friedlander MJ, Krnjević K, Noebels JL, Costa-Mattioli M (December 2011). "Suppression of PKR Promotes Network Excitability and Enhanced Cognition by Interferon-γ-Mediated Disinhibition". Cell 147 (6): 1384–96. doi:10.1016/j.cell.2011.11.029. PMID 22153080. Lay summary – canada.com.
- ^ Chen G, Ma C, Bower KA, Ke Z, Luo J (June 2006). "Interaction between RAX and PKR modulates the effect of ethanol on protein synthesis and survival of neurons". J. Biol. Chem. 281 (23): 15909–15. doi:10.1074/jbc.M600612200. PMID 16574643.
- ^ Takizawa T, Tatematsu C, Nakanishi Y (December 2002). "Double-stranded RNA-activated protein kinase interacts with apoptosis signal-regulating kinase 1. Implications for apoptosis signaling pathways". Eur. J. Biochem. 269 (24): 6126–32. doi:10.1046/j.1432-1033.2002.03325.x. PMID 12473108.
- ^ a b Polyak, S J; Tang N, Wambach M, Barber G N, Katze M G (January 1996). "The P58 cellular inhibitor complexes with the interferon-induced, double-stranded RNA-dependent protein kinase, PKR, to regulate its autophosphorylation and activity". J. Biol. Chem. (UNITED STATES) 271 (3): 1702–7. doi:10.1074/jbc.271.3.1702. ISSN 0021-9258. PMID 8576172.
- ^ Saunders LR, Perkins DJ, Balachandran S, Michaels R, Ford R, Mayeda A, Barber GN (August 2001). "Characterization of two evolutionarily conserved, alternatively spliced nuclear phosphoproteins, NFAR-1 and -2, that function in mRNA processing and interact with the double-stranded RNA-dependent protein kinase, PKR". J. Biol. Chem. 276 (34): 32300–12. doi:10.1074/jbc.M104207200. PMID 11438536.
- ^ Langland JO, Kao PN, Jacobs BL (May 1999). "Nuclear factor-90 of activated T-cells: A double-stranded RNA-binding protein and substrate for the double-stranded RNA-dependent protein kinase, PKR". Biochemistry 38 (19): 6361–8. doi:10.1021/bi982410u. PMID 10320367.
- ^ Parker LM, Fierro-Monti I, Mathews MB (August 2001). "Nuclear factor 90 is a substrate and regulator of the eukaryotic initiation factor 2 kinase double-stranded RNA-activated protein kinase". J. Biol. Chem. 276 (35): 32522–30. doi:10.1074/jbc.M104408200. PMID 11438540.
- ^ Patel RC, Vestal DJ, Xu Z, Bandyopadhyay S, Guo W, Erme SM, Williams BR, Sen GC (July 1999). "DRBP76, a double-stranded RNA-binding nuclear protein, is phosphorylated by the interferon-induced protein kinase, PKR". J. Biol. Chem. 274 (29): 20432–7. doi:10.1074/jbc.274.29.20432. PMID 10400669.
- ^ Gil J, Esteban M, Roth D (December 2000). "In vivo regulation of the dsRNA-dependent protein kinase PKR by the cellular glycoprotein p67". Biochemistry 39 (51): 16016–25. doi:10.1021/bi001754t. PMID 11123929.
- ^ Cuddihy AR, Wong AH, Tam NW, Li S, Koromilas AE (April 1999). "The double-stranded RNA activated protein kinase PKR physically associates with the tumor suppressor p53 protein and phosphorylates human p53 on serine 392 in vitro". Oncogene 18 (17): 2690–702. doi:10.1038/sj.onc.1202620. PMID 10348343.
- ^ Tan SL, Tareen SU, Melville MW, Blakely CM, Katze MG (September 2002). "The direct binding of the catalytic subunit of protein phosphatase 1 to the PKR protein kinase is necessary but not sufficient for inactivation and disruption of enzyme dimer formation". J. Biol. Chem. 277 (39): 36109–17. doi:10.1074/jbc.M205109200. PMID 12138106.
- ^ Huang X, Hutchins B, Patel RC (August 2002). "The C-terminal, third conserved motif of the protein activator PACT plays an essential role in the activation of double-stranded-RNA-dependent protein kinase (PKR)". Biochem. J. 366 (Pt 1): 175–86. doi:10.1042/BJ20020204. PMC 1222748. PMID 11985496. //www.ncbi.nlm.nih.gov/pmc/articles/PMC1222748/.
- ^ Patel RC, Sen GC (August 1998). "PACT, a protein activator of the interferon-induced protein kinase, PKR". EMBO J. 17 (15): 4379–90. doi:10.1093/emboj/17.15.4379. PMC 1170771. PMID 9687506. //www.ncbi.nlm.nih.gov/pmc/articles/PMC1170771/.
- ^ Wong AH, Tam NW, Yang YL, Cuddihy AR, Li S, Kirchhoff S, Hauser H, Decker T, Koromilas AE (March 1997). "Physical association between STAT1 and the interferon-inducible protein kinase PKR and implications for interferon and double-stranded RNA signaling pathways". EMBO J. 16 (6): 1291–304. doi:10.1093/emboj/16.6.1291. PMC 1169727. PMID 9135145. //www.ncbi.nlm.nih.gov/pmc/articles/PMC1169727/.
- ^ Wong AH, Durbin JE, Li S, Dever TE, Decker T, Koromilas AE (April 2001). "Enhanced antiviral and antiproliferative properties of a STAT1 mutant unable to interact with the protein kinase PKR". J. Biol. Chem. 276 (17): 13727–37. doi:10.1074/jbc.M011240200. PMID 11278865.
- ^ Cosentino GP, Venkatesan S, Serluca FC, Green SR, Mathews MB, Sonenberg N (October 1995). "Double-stranded-RNA-dependent protein kinase and TAR RNA-binding protein form homo- and heterodimers in vivo". Proc. Natl. Acad. Sci. U.S.A. 92 (21): 9445–9. doi:10.1073/pnas.92.21.9445. PMC 40818. PMID 7568151. //www.ncbi.nlm.nih.gov/pmc/articles/PMC40818/.
- ^ Daher A, Longuet M, Dorin D, Bois F, Segeral E, Bannwarth S, Battisti PL, Purcell DF, Benarous R, Vaquero C, Meurs EF, Gatignol A (September 2001). "Two dimerization domains in the trans-activation response RNA-binding protein (TRBP) individually reverse the protein kinase R inhibition of HIV-1 long terminal repeat expression". J. Biol. Chem. 276 (36): 33899–905. doi:10.1074/jbc.M103584200. PMID 11438532.
Further reading
- Williams BR (1999). "PKR; a sentinel kinase for cellular stress.". Oncogene 18 (45): 6112–20. doi:10.1038/sj.onc.1203127. PMID 10557102.
- García MA, Meurs EF, Esteban M (2007). "The dsRNA protein kinase PKR: virus and cell control.". Biochimie 89 (6-7): 799–811. doi:10.1016/j.biochi.2007.03.001. PMID 17451862.
- Thomis DC, Doohan JP, Samuel CE (1992). "Mechanism of interferon action: cDNA structure, expression, and regulation of the interferon-induced, RNA-dependent P1/eIF-2 alpha protein kinase from human cells.". Virology 188 (1): 33–46. doi:10.1016/0042-6822(92)90732-5. PMID 1373553.
- McCormack SJ, Thomis DC, Samuel CE (1992). "Mechanism of interferon action: identification of a RNA binding domain within the N-terminal region of the human RNA-dependent P1/eIF-2 alpha protein kinase.". Virology 188 (1): 47–56. doi:10.1016/0042-6822(92)90733-6. PMID 1373554.
- Mellor H, Proud CG (1991). "A synthetic peptide substrate for initiation factor-2 kinases.". Biochem. Biophys. Res. Commun. 178 (2): 430–7. doi:10.1016/0006-291X(91)90125-Q. PMID 1677563.
- Meurs E, Chong K, Galabru J, et al. (1990). "Molecular cloning and characterization of the human double-stranded RNA-activated protein kinase induced by interferon.". Cell 62 (2): 379–90. doi:10.1016/0092-8674(90)90374-N. PMID 1695551.
- Silverman RH, Sengupta DN (1991). "Translational regulation by HIV leader RNA, TAT, and interferon-inducible enzymes.". J. Exp. Pathol. 5 (2): 69–77. PMID 1708818.
- Roy S, Katze MG, Parkin NT, et al. (1990). "Control of the interferon-induced 68-kilodalton protein kinase by the HIV-1 tat gene product.". Science 247 (4947): 1216–9. doi:10.1126/science.2180064. PMID 2180064.
- McMillan NA, Chun RF, Siderovski DP, et al. (1996). "HIV-1 Tat directly interacts with the interferon-induced, double-stranded RNA-dependent kinase, PKR.". Virology 213 (2): 413–24. doi:10.1006/viro.1995.0014. PMID 7491766.
- Cosentino GP, Venkatesan S, Serluca FC, et al. (1995). "Double-stranded-RNA-dependent protein kinase and TAR RNA-binding protein form homo- and heterodimers in vivo.". Proc. Natl. Acad. Sci. U.S.A. 92 (21): 9445–9. doi:10.1073/pnas.92.21.9445. PMC 40818. PMID 7568151. //www.ncbi.nlm.nih.gov/pmc/articles/PMC40818/.
- Barber GN, Edelhoff S, Katze MG, Disteche CM (1993). "Chromosomal assignment of the interferon-inducible double-stranded RNA-dependent protein kinase (PRKR) to human chromosome 2p21-p22 and mouse chromosome 17 E2.". Genomics 16 (3): 765–7. doi:10.1006/geno.1993.1262. PMID 7686883.
- Squire J, Meurs EF, Chong KL, et al. (1993). "Localization of the human interferon-induced, ds-RNA activated p68 kinase gene (PRKR) to chromosome 2p21-p22.". Genomics 16 (3): 768–70. doi:10.1006/geno.1993.1263. PMID 7686884.
- Prigmore E, Ahmed S, Best A, et al. (1995). "A 68-kDa kinase and NADPH oxidase component p67phox are targets for Cdc42Hs and Rac1 in neutrophils.". J. Biol. Chem. 270 (18): 10717–22. doi:10.1074/jbc.270.18.10717. PMID 7738010.
- Barber GN, Wambach M, Wong ML, et al. (1993). "Translational regulation by the interferon-induced double-stranded-RNA-activated 68-kDa protein kinase.". Proc. Natl. Acad. Sci. U.S.A. 90 (10): 4621–5. doi:10.1073/pnas.90.10.4621. PMC 46564. PMID 8099444. //www.ncbi.nlm.nih.gov/pmc/articles/PMC46564/.
- Polyak SJ, Tang N, Wambach M, et al. (1996). "The P58 cellular inhibitor complexes with the interferon-induced, double-stranded RNA-dependent protein kinase, PKR, to regulate its autophosphorylation and activity.". J. Biol. Chem. 271 (3): 1702–7. doi:10.1074/jbc.271.3.1702. PMID 8576172.
- Chen ZJ, Parent L, Maniatis T (1996). "Site-specific phosphorylation of IkappaBalpha by a novel ubiquitination-dependent protein kinase activity.". Cell 84 (6): 853–62. doi:10.1016/S0092-8674(00)81064-8. PMID 8601309.
- Kuhen KL, Shen X, Carlisle ER, et al. (1997). "Structural organization of the human gene (PKR) encoding an interferon-inducible RNA-dependent protein kinase (PKR) and differences from its mouse homolog.". Genomics 36 (1): 197–201. doi:10.1006/geno.1996.0446. PMID 8812437.
- Taylor DR, Lee SB, Romano PR, et al. (1996). "Autophosphorylation sites participate in the activation of the double-stranded-RNA-activated protein kinase PKR.". Mol. Cell. Biol. 16 (11): 6295–302. PMC 231632. PMID 8887659. //www.ncbi.nlm.nih.gov/pmc/articles/PMC231632/.
- Kuhen KL, Shen X, Samuel CE (1996). "Mechanism of interferon action sequence of the human interferon-inducible RNA-dependent protein kinase (PKR) deduced from genomic clones.". Gene 178 (1-2): 191–3. doi:10.1016/0378-1119(96)00314-9. PMID 8921913.
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PDB gallery
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1qu6: STRUCTURE OF THE DOUBLE-STRANDED RNA-BINDING DOMAIN OF THE PROTEIN KINASE PKR REVEALS THE MOLECULAR BASIS OF ITS DSRNA-MEDIATED ACTIVATION
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2a19: PKR kinase domain- eIF2alpha- AMP-PNP complex.
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2a1a: PKR kinase domain-eIF2alpha Complex
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Proteins: enzymes
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| Topics |
- Active site
- Allosteric regulation
- Binding site
- Catalytically perfect enzyme
- Coenzyme
- Cofactor
- Cooperativity
- EC number
- Enzyme catalysis
- Enzyme inhibitor
- Enzyme kinetics
- Lineweaver–Burk plot
- Michaelis–Menten kinetics
- List of enzymes
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| Types |
- EC1 Oxidoreductases/list
- EC2 Transferases/list
- EC3 Hydrolases/list
- EC4 Lyases/list
- EC5 Isomerases/list
- EC6 Ligases/list
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- B
- enzm
- 1.1
- 2
- 3
- 4
- 5
- 6
- 7
- 8
- 10
- 11
- 13
- 14
- 15-18
- 2.1
- 2.7.10
- 2.7.11-12
- 3.1
- 4.1
- 5.1
- 6.1-3
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Transferases: phosphorus-containing groups (EC 2.7)
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2.7.1-2.7.4:
phosphotransferase/kinase
(PO4) |
| 2.7.1: OH acceptor |
- Hexo-
- Gluco-
- Fructo-
- Galacto-
- Phosphofructo-
- 1
- Liver
- Muscle
- Platelet
- 2
- Riboflavin
- Shikimate
- Thymidine
- NAD+
- Glycerol
- Pantothenate
- Mevalonate
- Pyruvate
- Deoxycytidine
- PFP
- Diacylglycerol
- Phosphoinositide 3
- Class I PI 3
- Class II PI 3
- Sphingosine
- Glucose-1,6-bisphosphate synthase
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| 2.7.2: COOH acceptor |
- Phosphoglycerate
- Aspartate
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| 2.7.3: N acceptor |
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| 2.7.4: PO4 acceptor |
- Phosphomevalonate
- Adenylate
- Nucleoside-diphosphate
- Uridylate
- Guanylate
- Thiamine-diphosphate
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2.7.6: diphosphotransferase
(P2O7) |
- Ribose-phosphate diphosphokinase
- Thiamine diphosphokinase
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2.7.7: nucleotidyltransferase
(PO4-nucleoside) |
| Polymerase |
| DNA polymerase |
- DNA-directed DNA polymerase
- DNA polymerase I
- DNA polymerase II
- DNA polymerase III holoenzyme
- RNA-directed DNA polymerase
- Reverse transcriptase
- Telomerase
- DNA nucleotidylexotransferase/Terminal deoxynucleotidyl transferase
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| RNA nucleotidyltransferase |
- RNA polymerase/DNA-directed RNA polymerase
- RNA polymerase I
- RNA polymerase II
- RNA polymerase III
- RNA polymerase IV
- Primase
- RNA-dependent RNA polymerase
- PNPase
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Phosphorolytic
3' to 5' exoribonuclease |
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| Uridylyltransferase |
- Glucose-1-phosphate uridylyltransferase
- Galactose-1-phosphate uridylyltransferase
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| Guanylyltransferase |
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| Other |
- Recombinase (Integrase)
- Transposase
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| 2.7.8: miscellaneous |
| Phosphatidyltransferases |
- CDP-diacylglycerol—glycerol-3-phosphate 3-phosphatidyltransferase
- CDP-diacylglycerol—serine O-phosphatidyltransferase
- CDP-diacylglycerol—inositol 3-phosphatidyltransferase
- CDP-diacylglycerol—choline O-phosphatidyltransferase
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| Glycosyl-1-phosphotransferase |
- N-acetylglucosamine-1-phosphate transferase
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2.7.10-2.7.13: protein kinase
(PO4; protein acceptor) |
| 2.7.10: protein-tyrosine |
|
|
| 2.7.11: protein-serine/threonine |
- see serine/threonine-specific protein kinases
|
|
| 2.7.12: protein-dual-specificity |
- see serine/threonine-specific protein kinases
|
|
| 2.7.13: protein-histidine |
- Protein-histidine pros-kinase
- Protein-histidine tele-kinase
- Histidine kinase
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|
|
- B
- enzm
- 1.1
- 2
- 3
- 4
- 5
- 6
- 7
- 8
- 10
- 11
- 13
- 14
- 15-18
- 2.1
- 2.7.10
- 2.7.11-12
- 3.1
- 4.1
- 5.1
- 6.1-3
|
|
|
|
|
Kinases: Serine/threonine-specific protein kinases (EC 2.7.11-12)
|
|
|
Serine/threonine-specific protein kinases (EC 2.7.11.1-EC 2.7.11.20)
|
|
|
|
|
|
|
Serine/threonine-specific protein kinases (EC 2.7.11.21-EC 2.7.11.30)
|
|
| Polo kinase (EC 2.7.11.21) |
|
|
| Cyclin-dependent kinase (EC 2.7.11.22) |
- CDK1
- CDK2
- CDKL2
- CDK3
- CDK4
- CDK5
- CDKL5
- CDK6
- CDK7
- CDK8
- CDK9
- CDK10
- CDC2L5
- CRKRS
- PCTK1
- PCTK2
- PCTK3
- PFTK1
- CDC2L1
|
|
| (RNA-polymerase)-subunit kinase (EC 2.7.11.23) |
- RPS6KA5
- RPS6KA4
- P70S6 kinase
- P70-S6 Kinase 1
- RPS6KB2
- RPS6KA2
- RPS6KA3
- RPS6KA1
- RPS6KC1
|
|
| Mitogen-activated protein kinase (EC 2.7.11.24) |
- Extracellular signal-regulated
- MAPK1
- MAPK3
- MAPK4
- MAPK6
- MAPK7
- MAPK12
- MAPK15
- C-Jun N-terminal
- P38 mitogen-activated protein
|
|
| MAP3K (EC 2.7.11.25) |
- MAP kinase kinase kinases
- MAP3K1
- MAP3K2
- MAP3K3
- MAP3K4
- MAP3K5
- MAP3K6
- MAP3K7
- MAP3K8
- RAFs
- MLKs
- MAP3K12
- MAP3K13
- MAP3K9
- MAP3K10
- MAP3K11
- MAP3K7
- ZAK
- CDC7
- MAP3K14
|
|
| Tau-protein kinase (EC 2.7.11.26) |
|
|
| (acetyl-CoA carboxylase) kinase (EC 2.7.11.27) |
-
|
|
| Tropomyosin kinase (EC 2.7.11.28) |
-
|
|
| Low-density-lipoprotein receptor kinase (EC 2.7.11.29) |
-
|
|
| Receptor protein serine/threonine kinase (EC 2.7.11.30) |
- Bone morphogenetic protein receptors
- BMPR1
- BMPR1A
- BMPR1B
- BMPR2
- ACVR1
- ACVR1B
- ACVR1C
- ACVR2A
- ACVR2B
- ACVRL1
- Anti-Müllerian hormone receptor
|
|
|
|
|
Dual-specificity kinases (EC 2.7.12)
|
|
| MAP2K |
- MAP2K1
- MAP2K2
- MAP2K3
- MAP2K4
- MAP2K5
- MAP2K6
- MAP2K7
|
|
|
|
- B
- enzm
- 1.1
- 2
- 3
- 4
- 5
- 6
- 7
- 8
- 10
- 11
- 13
- 14
- 15-18
- 2.1
- 2.7.10
- 2.7.11-12
- 3.1
- 4.1
- 5.1
- 6.1-3
|
|
|
|
UpToDate Contents
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Japanese Journal
- DNAメチル化阻害剤ゼブラリンによるヒト肝細胞癌に対する細胞毒性
- Double-stranded RNA-dependent protein kinase regulates insulin-stimulated chondrogenesis in mouse clonal chondrogenic cells, ATDC-5
Related Links
- 1. Cell. 2010 Feb 5;140(3):338-48. doi: 10.1016/j.cell.2010.01.001. Double-stranded RNA-dependent protein kinase links pathogen sensing with stress and metabolic homeostasis. Nakamura T, Furuhashi M, Li P, Cao H, Tuncman G ...
- Abstract Double-stranded RNA-dependent protein kinase (PKR) has been implicated in interferon (IFN) induction, antiviral response and tumor suppression. We have generated mice devoid of functional PKR (Pkr%). Although the mice ...
★リンクテーブル★
[★]
- 英
- double-stranded RNA-dependent protein kinase
[★]
- 英
- double-stranded RNA-dependent protein kinase
[★]
- 座礁させる、(岸に)打ち上げられる、(浜に)取り残される
- a 26-year-old woman is stranded for more than a week when her hiking trip is interrupted by an avalanche.
[★]
[★]
- 関
- depend、dependence、dependency、dependently
[★]
- 同
- リボ核酸 ribonucleic acid RNA
- 関
- DNA
[★]
- 同
- outlet right ventricle