Mitogenom-aktivirana proteinska kinaza 1

Mitogenom-aktivirana proteinska kinaza 1
PDB prikaz baziran na PDB: 1erk​.
Dostupne strukture
1erk​, 1gol​, 1pme​, 1tvo​, 1wzy​, 2erk​, 2fys​, 2gph​, 2ojg​, 2oji​, 2ojj​, 3erk​, 4erk
Identifikatori
Simboli MAPK1; p38; ERK; p40; ERK2; ERT1; MAPK2; P42MAPK; PRKM1; PRKM2; p41; p41mapk
Vanjski ID OMIM: 176948 MGI: 1346858 HomoloGene: 37670 GeneCards: MAPK1 Gene
Ontologija gena
Molekularna funkcija vezivanje nukleotida
vezivanje fosfotirozina
aktivnost proteinske serin/treoninske kinaze
aktivnost MAP kinaze
vezivanje proteina
ATP vezivanje
aktivnost transferaze
Celularna komponenta jedro
citoplazma
Biološki proces MAPKKK kaskada
fosforilacija proteinskih aminokiselina
uvod u apoptozu
hemotaksa
respons na stimulus DNK oštećenja
ćelijski ciklus
transdukcija signala
sinaptička transmisija
morfogeneza organa
citozinski metabolički proces
Pregled RNK izražavanja
podaci
Ortolozi
Vrsta Čovek Miš
Entrez 5594 26413
Ensembl ENSG00000100030 ENSMUSG00000063358
UniProt P28482 Q3UF82
RefSeq (mRNA) NM_002745 NM_001038663
RefSeq (protein) NP_002736 NP_001033752
Lokacija (UCSC) Chr 22:
20.45 - 20.55 Mb
Chr 16:
16.9 - 16.96 Mb
PubMed pretraga [1] [2]

Mitogenom-aktivirana proteinska kinaza 1, takođe poznata kao MAPK1, p42MAPK, i ERK2, je enzim koji je kod ljudi kodiran MAPK1 genom.[1]

Funkcije

Protein kodiran ovim genom je član familije MAP kinaza. Mitogenom-aktivirane proteinske kinaze, su takođe poznate kao ekstracelularnim signalom regulisane kinaze (ERK). One deluju kao tačka integracije višestrukih biohemijskih signala, i učestvuju u širokom varijetetu ćelijskih procesa kao što su proliferacija, diferencijacija, i regulacija transkripcije i razvoja. Prirekvizit aktivacije ove kinaze je njena fosforilisana uzvodnim kinazama. Nakon aktivacije, ova kinaza se translocira u jedro stimulisanih ćelija, gde ona fosforiliše proteine jedra. Dve alternativno splajsovane transkriptne varijante, koje se razlikuju u netranskribovanim regionima, kodiraju isti protein.[2]

Interakcije

Za MAPK1 je bilo pokazano da interaguje sa TSC2,[3] PEA15,[4] DUSP1,[5][6] NEK2,[7] DUSP3,[8] STAT5A,[9][10] MAPK14,[11][12] FHL2,[13] TNIP1,[14] RPS6KA3,[15][16] RPS6KA2,[15][17] MAP2K1,[11][18][19][20][21][22] RPS6KA1,[16][17][23] PTPN7,[24][25] MKNK1,[26] CIITA,[27] TOB1,[28] Fosfatidiletanolamin vezujući protein 1,[19] DUSP22,[29] Myc,[30][31][32] ADAM17,[33] SORBS3,[34] ELK1,[23][35] VAV1,[36][37] HDAC4,[38] MKNK2,[26][39] MAP3K1[40] i UBR5.[23]

Vidi još

Reference

  1. ^ Owaki H, Makar R, Boulton TG, Cobb MH, Geppert TD (1992). „Extracellular signal-regulated kinases in T cells: characterization of human ERK1 and ERK2 cDNAs”. Biochem. Biophys. Res. Commun. 182 (3): 1416—22. PMID 1540184. doi:10.1016/0006-291X(92)91891-S. 
  2. ^ „Entrez Gene: MAPK1 mitogen-activated protein kinase 1”. 
  3. ^ Ma, Li; Chen Zhenbang; et al. (2005). „Phosphorylation and functional inactivation of TSC2 by Erk implications for tuberous sclerosis and cancer pathogenesis”. Cell. United States. 121 (2): 179—93. ISSN 0092-8674. PMID 15851026. doi:10.1016/j.cell.2005.02.031. 
  4. ^ Formstecher, E; Ramos J W; et al. (2001). „PEA-15 mediates cytoplasmic sequestration of ERK MAP kinase”. Dev. Cell. United States. 1 (2): 239—50. ISSN 1534-5807. PMID 11702783. doi:10.1016/S1534-5807(01)00035-1. 
  5. ^ Slack, D N; Seternes O M; et al. (2001). „Distinct binding determinants for ERK2/p38alpha and JNK map kinases mediate catalytic activation and substrate selectivity of map kinase phosphatase-1”. J. Biol. Chem. United States. 276 (19): 16491—500. ISSN 0021-9258. PMID 11278799. doi:10.1074/jbc.M010966200. 
  6. ^ Calvisi, Diego F; Pinna Federico; et al. (2008). „Dual-specificity phosphatase 1 ubiquitination in extracellular signal-regulated kinase-mediated control of growth in human hepatocellular carcinoma”. Cancer Res. United States. 68 (11): 4192—200. PMID 18519678. doi:10.1158/0008-5472.CAN-07-6157. 
  7. ^ Lou, Yang; Xie Wei; et al. (2004). „Nek2A specifies the centrosomal localization of Erk2”. Biochem. Biophys. Res. Commun. United States. 321 (2): 495—501. ISSN 0006-291X. PMID 15358203. doi:10.1016/j.bbrc.2004.06.171. 
  8. ^ Todd, J L; Tanner K G; Denu J M (1999). „Extracellular regulated kinases (ERK) 1 and ERK2 are authentic substrates for the dual-specificity protein-tyrosine phosphatase VHR. A novel role in down-regulating the ERK pathway”. J. Biol. Chem. UNITED STATES. 274 (19): 13271—80. ISSN 0021-9258. PMID 10224087. doi:10.1074/jbc.274.19.13271. 
  9. ^ Pircher, T J; Petersen H; et al. (1999). „Extracellular signal-regulated kinase (ERK) interacts with signal transducer and activator of transcription (STAT) 5a”. Mol. Endocrinol. UNITED STATES. 13 (4): 555—65. ISSN 0888-8809. PMID 10194762. doi:10.1210/me.13.4.555. 
  10. ^ Dinerstein-Cali, H; Ferrag F; et al. (2000). „Growth hormone (GH) induces the formation of protein complexes involving Stat5, Erk2, Shc and serine phosphorylated proteins”. Mol. Cell. Endocrinol. IRELAND. 166 (2): 89—99. ISSN 0303-7207. PMID 10996427. doi:10.1016/S0303-7207(00)00277-X. 
  11. ^ а б Sanz-Moreno, Victoria; Casar Berta; Crespo Piero (2003). „p38alpha isoform Mxi2 binds to extracellular signal-regulated kinase 1 and 2 mitogen-activated protein kinase and regulates its nuclear activity by sustaining its phosphorylation levels”. Mol. Cell. Biol. United States. 23 (9): 3079—90. ISSN 0270-7306. PMC 153192 Слободан приступ. PMID 12697810. doi:10.1128/MCB.23.9.3079-3090.2003. 
  12. ^ Tanoue, T; Maeda R; et al. (2001). „Identification of a docking groove on ERK and p38 MAP kinases that regulates the specificity of docking interactions”. EMBO J. England. 20 (3): 466—79. ISSN 0261-4189. PMC 133461 Слободан приступ. PMID 11157753. doi:10.1093/emboj/20.3.466. 
  13. ^ Purcell, Nicole H; Darwis Dina; et al. (2004). „Extracellular signal-regulated kinase 2 interacts with and is negatively regulated by the LIM-only protein FHL2 in cardiomyocytes”. Mol. Cell. Biol. United States. 24 (3): 1081—95. ISSN 0270-7306. PMC 321437 Слободан приступ. PMID 14729955. doi:10.1128/MCB.24.3.1081-1095.2004. 
  14. ^ Zhang, Shengliang; Fukushi Masaya; et al. (2002). „A new ERK2 binding protein, Naf1, attenuates the EGF/ERK2 nuclear signaling”. Biochem. Biophys. Res. Commun. United States. 297 (1): 17—23. ISSN 0006-291X. PMID 12220502. doi:10.1016/S0006-291X(02)02086-7. 
  15. ^ а б Zhao, Y; Bjorbaek C; Moller D E (1996). „Regulation and interaction of pp90(rsk) isoforms with mitogen-activated protein kinases”. J. Biol. Chem. UNITED STATES. 271 (47): 29773—9. ISSN 0021-9258. PMID 8939914. doi:10.1074/jbc.271.47.29773. 
  16. ^ а б Smith, J A; Poteet-Smith C E; et al. (1999). „Identification of an extracellular signal-regulated kinase (ERK) docking site in ribosomal S6 kinase, a sequence critical for activation by ERK in vivo”. J. Biol. Chem. UNITED STATES. 274 (5): 2893—8. ISSN 0021-9258. PMID 9915826. doi:10.1074/jbc.274.5.2893. 
  17. ^ а б Roux, Philippe P; Richards Stephanie A; Blenis John (2003). „Phosphorylation of p90 ribosomal S6 kinase (RSK) regulates extracellular signal-regulated kinase docking and RSK activity”. Mol. Cell. Biol. United States. 23 (14): 4796—804. ISSN 0270-7306. PMC 162206 Слободан приступ. PMID 12832467. doi:10.1128/MCB.23.14.4796-4804.2003. 
  18. ^ Robinson, Fred L; Whitehurst Angelique W; et al. (2002). „Identification of novel point mutations in ERK2 that selectively disrupt binding to MEK1”. J. Biol. Chem. United States. 277 (17): 14844—52. ISSN 0021-9258. PMID 11823456. doi:10.1074/jbc.M107776200. 
  19. ^ а б Yeung, K; Janosch P; et al. (2000). „Mechanism of suppression of the Raf/MEK/extracellular signal-regulated kinase pathway by the raf kinase inhibitor protein”. Mol. Cell. Biol. UNITED STATES. 20 (9): 3079—85. ISSN 0270-7306. PMC 85596 Слободан приступ. PMID 10757792. doi:10.1128/MCB.20.9.3079-3085.2000. 
  20. ^ Wunderlich, W; Fialka I; et al. (2001). „A novel 14-kilodalton protein interacts with the mitogen-activated protein kinase scaffold mp1 on a late endosomal/lysosomal compartment”. J. Cell Biol. United States. 152 (4): 765—76. ISSN 0021-9525. PMC 2195784 Слободан приступ. PMID 11266467. doi:10.1083/jcb.152.4.765. 
  21. ^ Xu Be, Be; Stippec S; et al. (2001). „Hydrophobic as well as charged residues in both MEK1 and ERK2 are important for their proper docking”. J. Biol. Chem. United States. 276 (28): 26509—15. ISSN 0021-9258. PMID 11352917. doi:10.1074/jbc.M102769200. 
  22. ^ Chen, Z; Cobb M H (2001). „Regulation of stress-responsive mitogen-activated protein (MAP) kinase pathways by TAO2”. J. Biol. Chem. United States. 276 (19): 16070—5. ISSN 0021-9258. PMID 11279118. doi:10.1074/jbc.M100681200. 
  23. ^ а б в Eblen, Scott T; Kumar N Vinay; et al. (2003). „Identification of novel ERK2 substrates through use of an engineered kinase and ATP analogs”. J. Biol. Chem. United States. 278 (17): 14926—35. ISSN 0021-9258. PMID 12594221. doi:10.1074/jbc.M300485200. 
  24. ^ Pettiford, S M; Herbst R (2000). „The MAP-kinase ERK2 is a specific substrate of the protein tyrosine phosphatase HePTP”. Oncogene. ENGLAND. 19 (7): 858—69. ISSN 0950-9232. PMID 10702794. doi:10.1038/sj.onc.1203408. 
  25. ^ Saxena, M; Williams S; et al. (1999). „Inhibition of T cell signaling by mitogen-activated protein kinase-targeted hematopoietic tyrosine phosphatase (HePTP)”. J. Biol. Chem. UNITED STATES. 274 (17): 11693—700. ISSN 0021-9258. PMID 10206983. doi:10.1074/jbc.274.17.11693. 
  26. ^ а б Waskiewicz, A J; Flynn A; et al. (1997). „Mitogen-activated protein kinases activate the serine/threonine kinases Mnk1 and Mnk2”. EMBO J. ENGLAND. 16 (8): 1909—20. ISSN 0261-4189. PMC 1169794 Слободан приступ. PMID 9155017. doi:10.1093/emboj/16.8.1909. 
  27. ^ Voong, Lilien N; Slater Allison R; et al. (2008). „Mitogen-activated protein kinase ERK1/2 regulates the class II transactivator”. J. Biol. Chem. United States. 283 (14): 9031—9. ISSN 0021-9258. PMC 2431044 Слободан приступ. PMID 18245089. doi:10.1074/jbc.M706487200. 
  28. ^ Maekawa, Momoko; Nishida Eisuke; Tanoue Takuji (2002). „Identification of the Anti-proliferative protein Tob as a MAPK substrate”. J. Biol. Chem. United States. 277 (40): 37783—7. ISSN 0021-9258. PMID 12151396. doi:10.1074/jbc.M204506200. 
  29. ^ Aoyama, K; Nagata M; et al. (2001). „Molecular cloning and characterization of a novel dual specificity phosphatase, LMW-DSP2, that lacks the cdc25 homology domain”. J. Biol. Chem. United States. 276 (29): 27575—83. ISSN 0021-9258. PMID 11346645. doi:10.1074/jbc.M100408200. 
  30. ^ Jin, Zhaohui; Gao Fengqin; et al. (2004). „Tobacco-specific nitrosamine 4-(methylnitrosamino)-1-(3-pyridyl)-1-butanone promotes functional cooperation of Bcl2 and c-Myc through phosphorylation in regulating cell survival and proliferation”. J. Biol. Chem. United States. 279 (38): 40209—19. ISSN 0021-9258. PMID 15210690. doi:10.1074/jbc.M404056200. 
  31. ^ Gupta, S; Davis R J (1994). „MAP kinase binds to the NH2-terminal activation domain of c-Myc”. FEBS Lett. NETHERLANDS. 353 (3): 281—5. ISSN 0014-5793. PMID 7957875. doi:10.1016/0014-5793(94)01052-8. 
  32. ^ Tournier, C; Whitmarsh A J; et al. (1997). „Mitogen-activated protein kinase kinase 7 is an activator of the c-Jun NH2-terminal kinase”. Proc. Natl. Acad. Sci. U.S.A. UNITED STATES. 94 (14): 7337—42. ISSN 0027-8424. PMC 23822 Слободан приступ. PMID 9207092. doi:10.1073/pnas.94.14.7337. 
  33. ^ Díaz-Rodríguez, Elena; Montero Juan Carlos; et al. (2002). „Extracellular signal-regulated kinase phosphorylates tumor necrosis factor alpha-converting enzyme at threonine 735: a potential role in regulated shedding”. Mol. Biol. Cell. United States. 13 (6): 2031—44. ISSN 1059-1524. PMC 117622 Слободан приступ. PMID 12058067. doi:10.1091/mbc.01-11-0561. 
  34. ^ Mitsushima, Masaru; Suwa Akira; et al. (2004). „Extracellular signal-regulated kinase activated by epidermal growth factor and cell adhesion interacts with and phosphorylates vinexin”. J. Biol. Chem. United States. 279 (33): 34570—7. ISSN 0021-9258. PMID 15184391. doi:10.1074/jbc.M402304200. 
  35. ^ Cano, E; Hazzalin C A; et al. (1995). „Neither ERK nor JNK/SAPK MAP kinase subtypes are essential for histone H3/HMG-14 phosphorylation or c-fos and c-jun induction”. J. Cell. Sci. ENGLAND. 108 ( Pt 11): 3599—609. ISSN 0021-9533. PMID 8586671. 
  36. ^ Song, J S; Gomez J; et al. (1996). „Association of a p95 Vav-containing signaling complex with the FcepsilonRI gamma chain in the RBL-2H3 mast cell line. Evidence for a constitutive in vivo association of Vav with Grb2, Raf-1, and ERK2 in an active complex”. J. Biol. Chem. UNITED STATES. 271 (43): 26962—70. ISSN 0021-9258. PMID 8900182. doi:10.1074/jbc.271.43.26962. 
  37. ^ Lee, I S; Liu Y; et al. (1997). „Vav is associated with signal transducing molecules gp130, Grb2 and Erk2, and is tyrosine phosphorylated in response to interleukin-6”. FEBS Lett. NETHERLANDS. 401 (2-3): 133—7. ISSN 0014-5793. PMID 9013873. doi:10.1016/S0014-5793(96)01456-1. 
  38. ^ Zhou, X; Richon V M; et al. (2000). „Histone deacetylase 4 associates with extracellular signal-regulated kinases 1 and 2, and its cellular localization is regulated by oncogenic Ras”. Proc. Natl. Acad. Sci. U.S.A. UNITED STATES. 97 (26): 14329—33. ISSN 0027-8424. PMC 18918 Слободан приступ. PMID 11114188. doi:10.1073/pnas.250494697. 
  39. ^ Scheper, Gert C; Parra Josep L; et al. (2003). „The N and C termini of the splice variants of the human mitogen-activated protein kinase-interacting kinase Mnk2 determine activity and localization”. Mol. Cell. Biol. United States. 23 (16): 5692—705. ISSN 0270-7306. PMC 166352 Слободан приступ. PMID 12897141. doi:10.1128/MCB.23.16.5692-5705.2003. 
  40. ^ Karandikar, M; Xu S; Cobb M H (2000). „MEKK1 binds raf-1 and the ERK2 cascade components”. J. Biol. Chem. UNITED STATES. 275 (51): 40120—7. ISSN 0021-9258. PMID 10969079. doi:10.1074/jbc.M005926200. 

Literatura

  • Morishima-Kawashima M; Hasegawa M; Takio K; et al. (1995). „Hyperphosphorylation of tau in PHF.”. Neurobiol. Aging. 16 (3): 365—71; discussion 371—80. PMID 7566346. doi:10.1016/0197-4580(95)00027-C. 
  • Davis RJ (1996). „Transcriptional regulation by MAP kinases.”. Mol. Reprod. Dev. 42 (4): 459—67. PMID 8607977. doi:10.1002/mrd.1080420414. 
  • Peruzzi F, Gordon J, Darbinian N, Amini S (2003). „Tat-induced deregulation of neuronal differentiation and survival by nerve growth factor pathway.”. J. Neurovirol. 8 Suppl 2: 91—6. PMID 12491158. doi:10.1080/13550280290167885. 
  • Greenway AL; Holloway G; McPhee DA; et al. (2004). „HIV-1 Nef control of cell signalling molecules: multiple strategies to promote virus replication.”. J. Biosci. 28 (3): 323—35. PMID 12734410. doi:10.1007/BF02970151. 
  • Meloche S, Pouysségur J (2007). „The ERK1/2 mitogen-activated protein kinase pathway as a master regulator of the G1- to S-phase transition.”. Oncogene. 26 (22): 3227—39. PMID 17496918. doi:10.1038/sj.onc.1210414. 
  • Nicholas C. Price; Lewis Stevens (1999). Fundamentals of Enzymology: The Cell and Molecular Biology of Catalytic Proteins (Third изд.). USA: Oxford University Press. ISBN 019850229X. 
  • Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 изд.). Wiley-Interscience. ISBN 0471205036. 
  • Branden C; Tooze J. Introduction to Protein Structure. New York, NY: Garland Publishing. ISBN 0-8153-2305-0. 
  • Irwin H. Segel. Enzyme Kinetics: Behavior and Analysis of Rapid Equilibrium and Steady-State Enzyme Systems (Book 44 изд.). Wiley Classics Library. ISBN 0471303097. 

Spoljašnje veze

  • п
  • р
  • у
PDB Galerija
  • 1erk​: Struktura signalom regulisane kinaze
    1erk: Struktura signalom regulisane kinaze
  • 1gol​: MAP kinaza (ERK2) pacova sa arginin mutacijom u poziciji 52
    1gol: MAP kinaza (ERK2) pacova sa arginin mutacijom u poziciji 52
  • 1pme​: Struktura penta mutanta ljudske ERK2 MAP kinaze u kompleksu sa specifičnim inhibitorom ljudske p38 MAP kinaze
    1pme: Struktura penta mutanta ljudske ERK2 MAP kinaze u kompleksu sa specifičnim inhibitorom ljudske p38 MAP kinaze
  • 1tvo​: ERK2 struktura u kompleksu sa inhibitorom
    1tvo: ERK2 struktura u kompleksu sa inhibitorom
  • 1wzy​: Kristalna struktura ljudske ERK2 kinaze u kompleksu sa pirazolopiridazin derivatom
    1wzy: Kristalna struktura ljudske ERK2 kinaze u kompleksu sa pirazolopiridazin derivatom
  • 2erk​: Fosforilisana MAP kinaza ERK2
    2erk: Fosforilisana MAP kinaza ERK2
  • 2fys​: Kristalna struktura of Erk2 u kompleksu sa KIM peptidom izvedenim iz MKP3
    2fys: Kristalna struktura of Erk2 u kompleksu sa KIM peptidom izvedenim iz MKP3
  • 2gph​: Doking motiv interakcija MAP kinaze ERK2
    2gph: Doking motiv interakcija MAP kinaze ERK2
  • 2ojg​: Kristalna struktura ERK2 u kompleksu sa N,N-dimetil-4-(4-fenil-1H-pirazol-3-il)-1H-pirol-2-karboksamidom
    2ojg: Kristalna struktura ERK2 u kompleksu sa N,N-dimetil-4-(4-fenil-1H-pirazol-3-il)-1H-pirol-2-karboksamidom
  • 2oji​: Kristalna struktura ERK2 u kompleksu sa N-benzil-4-(4-(3-hlorofenil)-1H-pirazol-3-il)-1H-pirol-2-carboksamid
    2oji: Kristalna struktura ERK2 u kompleksu sa N-benzil-4-(4-(3-hlorofenil)-1H-pirazol-3-il)-1H-pirol-2-carboksamid
  • 2ojj​: Kristalna struktura ERK2 u kompleksu sa (S)-N-(1-(3-hloro-4-fluorofenil)-2-hidroksietil)-4-(4-(3-hlorofenil)-1H-pirazol-3-il)-1H-pirol-2-larboksamid
    2ojj: Kristalna struktura ERK2 u kompleksu sa (S)-N-(1-(3-hloro-4-fluorofenil)-2-hidroksietil)-4-(4-(3-hlorofenil)-1H-pirazol-3-il)-1H-pirol-2-larboksamid
  • 3erk​: Kompleks strukture MAP kinaze ERK2/SB220025
    3erk: Kompleks strukture MAP kinaze ERK2/SB220025
  • 4erk​: Kompleks strukture MAP kinaze ERK2/OLOMOUCINE
    4erk: Kompleks strukture MAP kinaze ERK2/OLOMOUCINE
  • п
  • р
  • у
(1) Serin/treonin-specifične proteinske kinaze (EC 2.7.11.1-EC 2.7.11.20)
Nespecifična serin/treonin proteinske kinaze (EC 2.7.11.1)
LATS1, LATS2, MAST1, MAST2, STK38, STK38L, CIT, ROCK1, SGK, SGK2, SGK3, Proteinska kinaza B (AKT1, AKT2, AKT3), Ataksija telangiektazija mutirani, Sisarski cilj rapamicina, EIF-2 kinaze (PKR, HRI), Wee1 (WEE1)
Piruvat dehidrogenazna kinaza (EC 2.7.11.2)
Defosfo-(reduktaza kinaza) kinaza (EC 2.7.11.3)
AMP-activated protein kinase,
(3-metil-2-oksobutanoat dehidrogenaza (prenos acetila)) (EC 2.7.11.4)
BCKDK, BCKDHA, BCKDHB
(izocitrat dehidrogenaza (NADP+)) kinaza (EC 2.7.11.5)
IDH2, IDH3A, IDH3B, IDH3G
tirozin 3-monooksigenazna kinaza (EC 2.7.11.6)
Miozin-teški-lanac kinaza (EC 2.7.11.7)
Aurora kinaza (Aurora A kinaza, Aurora B kinaza)
Fas-aktivirana serin/treoninska kinaza (EC 2.7.11.8)
Goodpasture-antigen-vezujuća proteinska kinaza (EC 2.7.11.9)
-
IκB kinaza (EC 2.7.11.10)
CHUK, IKK2, TBK1, IKBKE, IKBKG, IKBKAP
cAMP-zavisna proteinska kinaza (EC 2.7.11.11)
Proteinska kinaza A, PRKACG, PRKACB, PRKACA, PRKY
cGMP-zavisna proteinska kinaza (EC 2.7.11.12)
Protein kinaza C (EC 2.7.11.13)
Protein kinaza C, Protein kinaza Cζ, PKC alfa, PRKCB1, PRKCD, PRKCE, PRKCH, PRKCG, PRKCI, PRKCQ, Proteinska zavisna proteinska N1, PKN2, PKN3,
Rodopsinska kinaza (EC 2.7.11.14)
Beta adrenergički receptor kinaza (EC 2.7.11.15)
Beta adrenergički receptor kinaza, Beta adrenergički receptor kinaza-2
G protein spregnuti receptor kinaza (EC 2.7.11.16)
GRK4, GRK5, GRK6
Ca2+/kalmodulin-zavisna (EC 2.7.11.17)
BRSK2, CAMK1, CAMK2A, CAMK2B, CAMK2D, CAMK2G, CAMK4, MLCK, CASK, CHEK1, CHEK2, DAPK1, DAPK2, DAPK3, STK11, MAPKAPK2, MAPKAPK3, MAPKAPK5, MARK1, MARK2, MARK3, MARK4, MELK, MKNK1, MKNK2, NUAK1, NUAK2, OBSCN, PASK, PHKG1, PHKG2, PIM1, PIM2, PKD1, PRKD2, PRKD3, PSKH1, SNF1LK2, KIAA0999, STK40, SNF1LK, SNRK, SPEG, TSSK2, Kalirin, TRIB1, TRIB2, TRIB3, TRIO, Titin, DCLK1
Miozin laki-lanac kinaza (EC 2.7.11.18)
MYLK, MYLK2, MYLK3, MYLK4
Fosforilazna kinaza (EC 2.7.11.19)
PHKA1, PHKA2, PHKB, PHKG1, PHKG2
Faktor elongacije 2 kinaza (EC 2.7.11.20)
Polo kinaza (EC 2.7.11.21)
PLK1, PLK2, PLK3, PLK4
(2) Serin/treonin-specifične proteinske kinaze (EC 2.7.11.21-EC 2.7.11.30)
Polo kinaza (EC 2.7.11.21)
PLK1, PLK2, PLK3, PLK4
Ciklin-zavisna kinaza (EC 2.7.11.22)
CDK1, CDK2, CDKL2, CDK3, CDK4, CDK5, CDKL5, CDK6, CDK7, CDK8, CDK9, CDK10, CDC2L5, CRKRS, PCTK1, PCTK2, PCTK3, PFTK1, CDC2L1
(RNK-polimerazna)-podjedinica kinaza (EC 2.7.11.23)
RPS6KA5, RPS6KA4, P70S6 kinaza, P70-S6 kinaza 1, RPS6KB2, RPS6KA2, RPS6KA3, RPS6KA1, RPS6KC1
Mitogenom-aktivirana proteinska kinaza (EC 2.7.11.24)
Ekstracelularnim signalom regulisane (MAPK1, MAPK3, MAPK4, MAPK6, MAPK7, MAPK12, MAPK15), C-Jun N-terminal (MAPK8, MAPK9, MAPK10), P38 mitogenom-aktivirani protein (MAPK11, MAPK13, MAPK14)
MAP3K (EC 2.7.11.25)
MAP kinaza kinaza kinaze (MAP3K1, MAP3K2, MAP3K3, MAP3K4, MAP3K5, MAP3K6, MAP3K7, MAP3K8) RAFs (ARAF, BRAF, KSR1, KSR2), MLK (MAP3K12, MAP3K13, MAP3K9, MAP3K10, MAP3K11, MAP3K7, ZAK), CDC7, MAP3K14
Tau-proteinska kinaza (EC 2.7.11.26)
TPK1, TTK, GSK-3
acetil-CoA karboksilazna kinaza] (EC 2.7.11.27)
-
Tropomiozinska kinaza (EC 2.7.11.28)
-
Receptor lipoproteina-niske-gustine kinaza (EC 2.7.11.29)
-
Receptor protein serin/treonin kinaza (EC 2.7.11.30)
Koštani morfogenetski proteinski receptori (BMPR1, BMPR1A, BMPR1B, BMPR2), ACVR1, ACVR1B, ACVR1C, ACVR2A, ACVR2B, ACVRL1, Anti-Mulerianski hormonski receptor
(3) Kinaze dualne-specifičnosti (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, 2.1/2/3/4/5/6/7/8, 2.7.10, 2.7.11-12, 3.1/2/3/4/5/6/7, 3.1.3.48, 3.4.21/22/23/24, 4.1/2/3/4/5/6, 5.1/2/3/4/99, 6.1-3/4/5-6
  • п
  • р
  • у
(1) Serin/treonin-specifične proteinske kinaze (EC 2.7.11.1-EC 2.7.11.20)
Nespecifična serin/treonin proteinske kinaze (EC 2.7.11.1)
LATS1, LATS2, MAST1, MAST2, STK38, STK38L, CIT, ROCK1, SGK, SGK2, SGK3, Proteinska kinaza B (AKT1, AKT2, AKT3), Ataksija telangiektazija mutirani, Sisarski cilj rapamicina, EIF-2 kinaze (PKR, HRI), Wee1 (WEE1)
Piruvat dehidrogenazna kinaza (EC 2.7.11.2)
Defosfo-(reduktaza kinaza) kinaza (EC 2.7.11.3)
AMP-activated protein kinase,
(3-metil-2-oksobutanoat dehidrogenaza (prenos acetila)) (EC 2.7.11.4)
BCKDK, BCKDHA, BCKDHB
(izocitrat dehidrogenaza (NADP+)) kinaza (EC 2.7.11.5)
IDH2, IDH3A, IDH3B, IDH3G
tirozin 3-monooksigenazna kinaza (EC 2.7.11.6)
Miozin-teški-lanac kinaza (EC 2.7.11.7)
Aurora kinaza (Aurora A kinaza, Aurora B kinaza)
Fas-aktivirana serin/treoninska kinaza (EC 2.7.11.8)
Goodpasture-antigen-vezujuća proteinska kinaza (EC 2.7.11.9)
-
IκB kinaza (EC 2.7.11.10)
CHUK, IKK2, TBK1, IKBKE, IKBKG, IKBKAP
cAMP-zavisna proteinska kinaza (EC 2.7.11.11)
Proteinska kinaza A, PRKACG, PRKACB, PRKACA, PRKY
cGMP-zavisna proteinska kinaza (EC 2.7.11.12)
Protein kinaza C (EC 2.7.11.13)
Protein kinaza C, Protein kinaza Cζ, PKC alfa, PRKCB1, PRKCD, PRKCE, PRKCH, PRKCG, PRKCI, PRKCQ, Proteinska zavisna proteinska N1, PKN2, PKN3,
Rodopsinska kinaza (EC 2.7.11.14)
Beta adrenergički receptor kinaza (EC 2.7.11.15)
Beta adrenergički receptor kinaza, Beta adrenergički receptor kinaza-2
G protein spregnuti receptor kinaza (EC 2.7.11.16)
GRK4, GRK5, GRK6
Ca2+/kalmodulin-zavisna (EC 2.7.11.17)
BRSK2, CAMK1, CAMK2A, CAMK2B, CAMK2D, CAMK2G, CAMK4, MLCK, CASK, CHEK1, CHEK2, DAPK1, DAPK2, DAPK3, STK11, MAPKAPK2, MAPKAPK3, MAPKAPK5, MARK1, MARK2, MARK3, MARK4, MELK, MKNK1, MKNK2, NUAK1, NUAK2, OBSCN, PASK, PHKG1, PHKG2, PIM1, PIM2, PKD1, PRKD2, PRKD3, PSKH1, SNF1LK2, KIAA0999, STK40, SNF1LK, SNRK, SPEG, TSSK2, Kalirin, TRIB1, TRIB2, TRIB3, TRIO, Titin, DCLK1
Miozin laki-lanac kinaza (EC 2.7.11.18)
MYLK, MYLK2, MYLK3, MYLK4
Fosforilazna kinaza (EC 2.7.11.19)
PHKA1, PHKA2, PHKB, PHKG1, PHKG2
Faktor elongacije 2 kinaza (EC 2.7.11.20)
Polo kinaza (EC 2.7.11.21)
PLK1, PLK2, PLK3, PLK4
(2) Serin/treonin-specifične proteinske kinaze (EC 2.7.11.21-EC 2.7.11.30)
Polo kinaza (EC 2.7.11.21)
PLK1, PLK2, PLK3, PLK4
Ciklin-zavisna kinaza (EC 2.7.11.22)
CDK1, CDK2, CDKL2, CDK3, CDK4, CDK5, CDKL5, CDK6, CDK7, CDK8, CDK9, CDK10, CDC2L5, CRKRS, PCTK1, PCTK2, PCTK3, PFTK1, CDC2L1
(RNK-polimerazna)-podjedinica kinaza (EC 2.7.11.23)
RPS6KA5, RPS6KA4, P70S6 kinaza, P70-S6 kinaza 1, RPS6KB2, RPS6KA2, RPS6KA3, RPS6KA1, RPS6KC1
Mitogenom-aktivirana proteinska kinaza (EC 2.7.11.24)
Ekstracelularnim signalom regulisane (MAPK1, MAPK3, MAPK4, MAPK6, MAPK7, MAPK12, MAPK15), C-Jun N-terminal (MAPK8, MAPK9, MAPK10), P38 mitogenom-aktivirani protein (MAPK11, MAPK13, MAPK14)
MAP3K (EC 2.7.11.25)
MAP kinaza kinaza kinaze (MAP3K1, MAP3K2, MAP3K3, MAP3K4, MAP3K5, MAP3K6, MAP3K7, MAP3K8) RAFs (ARAF, BRAF, KSR1, KSR2), MLK (MAP3K12, MAP3K13, MAP3K9, MAP3K10, MAP3K11, MAP3K7, ZAK), CDC7, MAP3K14
Tau-proteinska kinaza (EC 2.7.11.26)
TPK1, TTK, GSK-3
acetil-CoA karboksilazna kinaza] (EC 2.7.11.27)
-
Tropomiozinska kinaza (EC 2.7.11.28)
-
Receptor lipoproteina-niske-gustine kinaza (EC 2.7.11.29)
-
Receptor protein serin/treonin kinaza (EC 2.7.11.30)
Koštani morfogenetski proteinski receptori (BMPR1, BMPR1A, BMPR1B, BMPR2), ACVR1, ACVR1B, ACVR1C, ACVR2A, ACVR2B, ACVRL1, Anti-Mulerianski hormonski receptor
(3) Kinaze dualne-specifičnosti (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, 2.1/2/3/4/5/6/7/8, 2.7.10, 2.7.11-12, 3.1/2/3/4/5/6/7, 3.1.3.48, 3.4.21/22/23/24, 4.1/2/3/4/5/6, 5.1/2/3/4/99, 6.1-3/4/5-6
  • п
  • р
  • у
Teme
Tipovi
  • B enzm: 1.1/2/3/4/5/6/7/8/10/11/13/14/15-18, 2.1/2/3/4/5/6/7/8, 2.7.10, 2.7.11-12, 3.1/2/3/4/5/6/7, 3.1.3.48, 3.4.21/22/23/24, 4.1/2/3/4/5/6, 5.1/2/3/4/99, 6.1-3/4/5-6
Portali:
  •  Molekularna i ćelijska biologija
  •  Hemija