MAP3K14
Mitogenom-aktivirana protein kinaza kinaza kinaza 14 | |||||||||
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Identifikatori | |||||||||
Simboli | MAP3K14; FTDCR1B; HS; HSNIK; NIK | ||||||||
Vanjski ID | OMIM: 604655 MGI: 1858204 HomoloGene: 2940 GeneCards: MAP3K14 Gene | ||||||||
EC broj | 2.7.11.25 | ||||||||
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Pregled RNK izražavanja | |||||||||
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podaci | |||||||||
Ortolozi | |||||||||
Vrsta | Čovek | Miš | |||||||
Entrez | 9020 | 53859 | |||||||
Ensembl | ENSG00000006062 | ENSMUSG00000020941 | |||||||
UniProt | Q99558 | Q544K4 | |||||||
RefSeq (mRNA) | NM_003954 | NM_016896 | |||||||
RefSeq (protein) | NP_003945 | NP_058592 | |||||||
Lokacija (UCSC) | Chr 17: 40.7 - 40.75 Mb | Chr 11: 103.04 - 103.08 Mb | |||||||
PubMed pretraga | [1] | [2] |
MAP3K14 (Mitogenom-aktivirana protein kinaza kinaza kinaza 14, NF-kapa-B-indukujuća kinaza, NIK), je enzim koji je kod čoveka kodiran MAP3K14 genom.[1][2]
Funkcija
Ovaj gen kodira mitogenom-activiranu kinaza kinaza kinazu 14, koja je serin/treonin-specifična proteinska kinaza. Ova kinaza se vezuje za TRAF2 i stimuliše NF-κB aktivnost. Ona je kritična kinaza alternativnog NF-κB aktivacionog puta. Njena sekvenca je slična sa nekoliko drugih MAPKK kinaza. Ona učestvuje u NF-κB-indukovanoj signalnoj kaskadi koja je zajednička za receptore TNF/NGF) familije i za interleukinski-1 tip-I receptor.[2]
Interakcije
Za MAP3K14 je pokazano da interaguje sa TRAF2,[3][4] IKK2[3][5] i CHUK.[3][6][7][8]
Reference
- ^ Malinin NL, Boldin MP, Kovalenko AV, Wallach D (1997). „MAP3K-related kinase involved in NF-kappaB induction by TNF, CD95 and IL-1”. Nature. 385 (6616): 540—4. PMID 9020361. doi:10.1038/385540a0.
- ^ а б „Entrez Gene: MAP3K14 mitogen-activated protein kinase kinase kinase 14”.
- ^ а б в Luftig, M A; Cahir-McFarland E; et al. (2001). „Effects of the NIK aly mutation on NF-kappaB activation by the Epstein-Barr virus latent infection membrane protein, lymphotoxin beta receptor, and CD40”. J. Biol. Chem. United States. 276 (18): 14602—6. ISSN 0021-9258. PMID 11278268. doi:10.1074/jbc.C100103200.
- ^ Malinin, N L; Boldin M P; et al. (1997). „MAP3K-related kinase involved in NF-kappaB induction by TNF, CD95 and IL-1”. Nature. ENGLAND. 385 (6616): 540—4. ISSN 0028-0836. PMID 9020361. doi:10.1038/385540a0.
- ^ Woronicz, J D; Gao X; et al. (1997). „IkappaB kinase-beta: NF-kappaB activation and complex formation with IkappaB kinase-alpha and NIK”. Science. UNITED STATES. 278 (5339): 866—9. ISSN 0036-8075. PMID 9346485. doi:10.1126/science.278.5339.866.
- ^ Régnier, C H; Song H Y; et al. (1997). „Identification and characterization of an IkappaB kinase”. Cell. UNITED STATES. 90 (2): 373—83. ISSN 0092-8674. PMID 9244310. doi:10.1016/S0092-8674(00)80344-X.
- ^ Xiao, G; Sun S C (2000). „Negative regulation of the nuclear factor kappa B-inducing kinase by a cis-acting domain”. J. Biol. Chem. UNITED STATES. 275 (28): 21081—5. ISSN 0021-9258. PMID 10887201. doi:10.1074/jbc.M002552200.
- ^ Ninomiya-Tsuji, J; Kishimoto K; et al. (1999). „The kinase TAK1 can activate the NIK-I kappaB as well as the MAP kinase cascade in the IL-1 signalling pathway”. Nature. ENGLAND. 398 (6724): 252—6. ISSN 0028-0836. PMID 10094049. doi:10.1038/18465.
Literatura
- Régnier CH; Song HY; Gao X; et al. (1997). „Identification and characterization of an IkappaB kinase.”. Cell. 90 (2): 373—83. PMID 9244310. doi:10.1016/S0092-8674(00)80344-X.
- Song HY; Régnier CH; Kirschning CJ; et al. (1997). „Tumor necrosis factor (TNF)-mediated kinase cascades: bifurcation of nuclear factor-kappaB and c-jun N-terminal kinase (JNK/SAPK) pathways at TNF receptor-associated factor 2.”. Proc. Natl. Acad. Sci. U.S.A. 94 (18): 9792—6. PMC 23270
. PMID 9275204. doi:10.1073/pnas.94.18.9792.
- Woronicz JD; Gao X; Cao Z; et al. (1997). „IkappaB kinase-beta: NF-kappaB activation and complex formation with IkappaB kinase-alpha and NIK.”. Science. 278 (5339): 866—9. PMID 9346485. doi:10.1126/science.278.5339.866.
- Ling L, Cao Z, Goeddel DV (1998). „NF-kappaB-inducing kinase activates IKK-alpha by phosphorylation of Ser-176.”. Proc. Natl. Acad. Sci. U.S.A. 95 (7): 3792—7. PMC 19916
. PMID 9520446. doi:10.1073/pnas.95.7.3792.
- Lee FS, Peters RT, Dang LC, Maniatis T (1998). „MEKK1 activates both IkappaB kinase alpha and IkappaB kinase beta.”. Proc. Natl. Acad. Sci. U.S.A. 95 (16): 9319—24. PMC 21336
. PMID 9689078. doi:10.1073/pnas.95.16.9319.
- Lin X; Mu Y; Cunningham ET; et al. (1998). „Molecular determinants of NF-kappaB-inducing kinase action.”. Mol. Cell. Biol. 18 (10): 5899—907. PMC 109176
. PMID 9742107.
- Cohen L, Henzel WJ, Baeuerle PA (1998). „IKAP is a scaffold protein of the IkappaB kinase complex.”. Nature. 395 (6699): 292—6. PMID 9751059. doi:10.1038/26254.
- Aronsson FC; Magnusson P; Andersson B; et al. (1998). „The NIK protein kinase and C17orf1 genes: chromosomal mapping, gene structures and mutational screening in frontotemporal dementia and parkinsonism linked to chromosome 17.”. Hum. Genet. 103 (3): 340—5. PMID 9799091. doi:10.1007/s004390050827.
- Nemoto S, DiDonato JA, Lin A (1998). „Coordinate regulation of IkappaB kinases by mitogen-activated protein kinase kinase kinase 1 and NF-kappaB-inducing kinase.”. Mol. Cell. Biol. 18 (12): 7336—43. PMC 109315
. PMID 9819420.
- Li Y; Kang J; Friedman J; et al. (1999). „Identification of a cell protein (FIP-3) as a modulator of NF-kappaB activity and as a target of an adenovirus inhibitor of tumor necrosis factor alpha-induced apoptosis.”. Proc. Natl. Acad. Sci. U.S.A. 96 (3): 1042—7. PMC 15347
. PMID 9927690. doi:10.1073/pnas.96.3.1042.
- Lallena MJ; Diaz-Meco MT; Bren G; et al. (1999). „Activation of IkappaB kinase beta by protein kinase C isoforms.”. Mol. Cell. Biol. 19 (3): 2180—8. PMC 84010
. PMID 10022904.
- Lin X; Cunningham ET; Mu Y; et al. (1999). „The proto-oncogene Cot kinase participates in CD3/CD28 induction of NF-kappaB acting through the NF-kappaB-inducing kinase and IkappaB kinases.”. Immunity. 10 (2): 271—80. PMID 10072079. doi:10.1016/S1074-7613(00)80027-8.
- Ninomiya-Tsuji J; Kishimoto K; Hiyama A; et al. (1999). „The kinase TAK1 can activate the NIK-I kappaB as well as the MAP kinase cascade in the IL-1 signalling pathway.”. Nature. 398 (6724): 252—6. PMID 10094049. doi:10.1038/18465.
- Delhase M, Hayakawa M, Chen Y, Karin M (1999). „Positive and negative regulation of IkappaB kinase activity through IKKbeta subunit phosphorylation.”. Science. 284 (5412): 309—13. PMID 10195894. doi:10.1126/science.284.5412.309.
- Hu WH, Johnson H, Shu HB (1999). „Tumor necrosis factor-related apoptosis-inducing ligand receptors signal NF-kappaB and JNK activation and apoptosis through distinct pathways.”. J. Biol. Chem. 274 (43): 30603—10. PMID 10521444. doi:10.1074/jbc.274.43.30603.
- Yamamoto Y, Yin MJ, Gaynor RB (2000). „IkappaB kinase alpha (IKKalpha) regulation of IKKbeta kinase activity.”. Mol. Cell. Biol. 20 (10): 3655—66. PMC 85658
. PMID 10779355. doi:10.1128/MCB.20.10.3655-3666.2000.
- Xiao G, Sun SC (2000). „Negative regulation of the nuclear factor kappa B-inducing kinase by a cis-acting domain.”. J. Biol. Chem. 275 (28): 21081—5. PMID 10887201. doi:10.1074/jbc.M002552200.
- Chaudhary PM; Eby MT; Jasmin A; et al. (2000). „Activation of the NF-kappaB pathway by caspase 8 and its homologs.”. Oncogene. 19 (39): 4451—60. PMID 11002417. doi:10.1038/sj.onc.1203812.
- Kumar A; Eby MT; Sinha S; et al. (2001). „The ectodermal dysplasia receptor activates the nuclear factor-kappaB, JNK, and cell death pathways and binds to ectodysplasin A.”. J. Biol. Chem. 276 (4): 2668—77. PMID 11035039. doi:10.1074/jbc.M008356200.
- 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
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(1) Serin/treonin-specifične proteinske kinaze (EC 2.7.11.1-EC 2.7.11.20) | |||||||||||||||||||||||||||||||||||||||||||
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(2) Serin/treonin-specifične proteinske kinaze (EC 2.7.11.21-EC 2.7.11.30) | |||||||||||||||||||||
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(3) Kinaze dualne-specifičnosti (EC 2.7.12) | |||
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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