MAP3K14

Protein-coding gene in the species Homo sapiens
MAP3K14
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

4DN5, 4G3D, 4IDT, 4IDV

Identifiers
AliasesMAP3K14, FTDCR1B, HS, HSNIK, NIK, mitogen-activated protein kinase kinase kinase 14
External IDsOMIM: 604655; MGI: 1858204; HomoloGene: 2940; GeneCards: MAP3K14; OMA:MAP3K14 - orthologs
Gene location (Human)
Chromosome 17 (human)
Chr.Chromosome 17 (human)[1]
Chromosome 17 (human)
Genomic location for MAP3K14
Genomic location for MAP3K14
Band17q21.31Start45,263,119 bp[1]
End45,317,029 bp[1]
Gene location (Mouse)
Chromosome 11 (mouse)
Chr.Chromosome 11 (mouse)[2]
Chromosome 11 (mouse)
Genomic location for MAP3K14
Genomic location for MAP3K14
Band11 E1|11 66.8 cMStart103,110,588 bp[2]
End103,158,298 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • granulocyte

  • gastrocnemius muscle

  • muscle layer of sigmoid colon

  • apex of heart

  • gastric mucosa

  • lymph node

  • tibialis anterior muscle

  • spleen

  • right auricle

  • anterior pituitary
Top expressed in
  • granulocyte

  • lumbar spinal ganglion

  • gastrula

  • submandibular gland

  • blood

  • mesenteric lymph nodes

  • muscle of thigh

  • thymus

  • spleen

  • lip
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
  • transferase activity
  • protein kinase activity
  • nucleotide binding
  • NF-kappaB-inducing kinase activity
  • protein binding
  • MAP kinase kinase kinase activity
  • ATP binding
  • kinase activity
  • protein serine/threonine kinase activity
Cellular component
  • cytoplasm
  • fibrillar center
  • nucleus
  • cytosol
  • intracellular membrane-bounded organelle
Biological process
  • phosphorylation
  • tumor necrosis factor-mediated signaling pathway
  • MAPK cascade
  • protein phosphorylation
  • cellular response to mechanical stimulus
  • immune response
  • positive regulation of I-kappaB kinase/NF-kappaB signaling
  • I-kappaB kinase/NF-kappaB signaling
  • NIK/NF-kappaB signaling
  • regulation of mitotic cell cycle
  • signal transduction
  • stress-activated protein kinase signaling cascade
  • activation of protein kinase activity
  • regulation of apoptotic process
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

9020

53859

Ensembl

ENSG00000006062
ENSG00000282637

ENSMUSG00000020941

UniProt

Q99558

Q9WUL6

RefSeq (mRNA)

NM_003954

NM_016896

RefSeq (protein)

NP_003945

NP_058592

Location (UCSC)Chr 17: 45.26 – 45.32 MbChr 11: 103.11 – 103.16 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Mitogen-activated protein kinase kinase kinase 14 also known as NF-kappa-B-inducing kinase (NIK) is an enzyme that in humans is encoded by the MAP3K14 gene.[5][6]

Function

This gene encodes mitogen-activated protein kinase kinase kinase 14, NIK, which is a serine/threonine protein-kinase. This kinase binds to TRAF2 and stimulates NF-κB activity. It is a critical kinase of the alternative NF-κB activation pathway. It shares sequence similarity with several other MAPKK kinases. It participates in an NF-κB-inducing signalling cascade common to receptors of the tumour-necrosis/nerve-growth factor (TNF/NGF) family and to the interleukin-1 type-I receptor.[6]

Interactions

MAP3K14 has been shown to interact with:

References

  1. ^ a b c ENSG00000282637 GRCh38: Ensembl release 89: ENSG00000006062, ENSG00000282637 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000020941 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ a b Malinin NL, Boldin MP, Kovalenko AV, Wallach D (March 1997). "MAP3K-related kinase involved in NF-kappaB induction by TNF, CD95 and IL-1". Nature. 385 (6616): 540–4. doi:10.1038/385540a0. PMID 9020361. S2CID 4366355.
  6. ^ a b "Entrez Gene: MAP3K14 mitogen-activated protein ki kinase kinase 14".
  7. ^ a b c Luftig MA, Cahir-McFarland E, Mosialos G, Kieff E (May 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. 276 (18): 14602–6. doi:10.1074/jbc.C100103200. PMID 11278268.
  8. ^ Régnier CH, Song HY, Gao X, Goeddel DV, Cao Z, Rothe M (July 1997). "Identification and characterization of an IkappaB kinase". Cell. 90 (2): 373–83. doi:10.1016/S0092-8674(00)80344-X. PMID 9244310. S2CID 16217708.
  9. ^ Xiao G, Sun SC (July 2000). "Negative regulation of the nuclear factor kappa B-inducing kinase by a cis-acting domain". J. Biol. Chem. 275 (28): 21081–5. doi:10.1074/jbc.M002552200. PMID 10887201.
  10. ^ Ninomiya-Tsuji J, Kishimoto K, Hiyama A, Inoue J, Cao Z, Matsumoto K (March 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. Bibcode:1999Natur.398..252N. doi:10.1038/18465. PMID 10094049. S2CID 4421236.
  11. ^ Woronicz JD, Gao X, Cao Z, Rothe M, Goeddel DV (October 1997). "IkappaB kinase-beta: NF-kappaB activation and complex formation with IkappaB kinase-alpha and NIK". Science. 278 (5339): 866–9. Bibcode:1997Sci...278..866W. doi:10.1126/science.278.5339.866. PMID 9346485.

Further reading

  • Régnier CH, Song HY, Gao X, Goeddel DV, Cao Z, Rothe M (1997). "Identification and characterization of an IkappaB kinase". Cell. 90 (2): 373–83. doi:10.1016/S0092-8674(00)80344-X. PMID 9244310. S2CID 16217708.
  • Song HY, Régnier CH, Kirschning CJ, Goeddel DV, Rothe M (1997). "Tumor necrosis factor (TNF)-mediated kinase cascades: Bifurcation of Nuclear Factor-κB 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. Bibcode:1997PNAS...94.9792S. doi:10.1073/pnas.94.18.9792. PMC 23270. PMID 9275204.
  • Woronicz JD, Gao X, Cao Z, Rothe M, Goeddel DV (1997). "IkappaB kinase-beta: NF-kappaB activation and complex formation with IkappaB kinase-alpha and NIK". Science. 278 (5339): 866–9. Bibcode:1997Sci...278..866W. doi:10.1126/science.278.5339.866. PMID 9346485.
  • Ling L, Cao Z, Goeddel DV (1998). "NF-κB-inducing kinase activates IKK-α by phosphorylation of Ser-176". Proc. Natl. Acad. Sci. U.S.A. 95 (7): 3792–7. Bibcode:1998PNAS...95.3792L. doi:10.1073/pnas.95.7.3792. PMC 19916. PMID 9520446.
  • Lee FS, Peters RT, Dang LC, Maniatis T (1998). "MEKK1 activates both IκB kinase α and IκB kinase β". Proc. Natl. Acad. Sci. U.S.A. 95 (16): 9319–24. Bibcode:1998PNAS...95.9319L. doi:10.1073/pnas.95.16.9319. PMC 21336. PMID 9689078.
  • Lin X, Mu Y, Cunningham ET, Marcu KB, Geleziunas R, Greene WC (1998). "Molecular Determinants of NF-κB-Inducing Kinase Action". Mol. Cell. Biol. 18 (10): 5899–907. doi:10.1128/mcb.18.10.5899. 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. Bibcode:1998Natur.395..292C. doi:10.1038/26254. PMID 9751059. S2CID 4327300.
  • Aronsson FC, Magnusson P, Andersson B, Karsten SL, Shibasaki Y, Lendon CL, Goate AM, Brookes AJ (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. doi:10.1007/s004390050827. PMID 9799091. S2CID 11305597.
  • Nemoto S, DiDonato JA, Lin A (1998). "Coordinate Regulation of IκB Kinases by Mitogen-Activated Protein Kinase Kinase Kinase 1 and NF-κB-Inducing Kinase". Mol. Cell. Biol. 18 (12): 7336–43. doi:10.1128/mcb.18.12.7336. PMC 109315. PMID 9819420.
  • Li Y, Kang J, Friedman J, Tarassishin L, Ye J, Kovalenko A, Wallach D, Horwitz MS (1999). "Identification of a cell protein (FIP-3) as a modulator of NF-κB activity and as a target of an adenovirus inhibitor of tumor necrosis factor α-induced apoptosis". Proc. Natl. Acad. Sci. U.S.A. 96 (3): 1042–7. Bibcode:1999PNAS...96.1042L. doi:10.1073/pnas.96.3.1042. PMC 15347. PMID 9927690.
  • Lallena MJ, Diaz-Meco MT, Bren G, Payá CV, Moscat J (1999). "Activation of IκB Kinase β by Protein Kinase C Isoforms". Mol. Cell. Biol. 19 (3): 2180–8. doi:10.1128/MCB.19.3.2180. PMC 84010. PMID 10022904.
  • Lin X, Cunningham ET, Mu Y, Geleziunas R, Greene WC (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. doi:10.1016/S1074-7613(00)80027-8. PMID 10072079.
  • Ninomiya-Tsuji J, Kishimoto K, Hiyama A, Inoue J, Cao Z, Matsumoto K (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. Bibcode:1999Natur.398..252N. doi:10.1038/18465. PMID 10094049. S2CID 4421236.
  • 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. doi:10.1126/science.284.5412.309. PMID 10195894.
  • 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. doi:10.1074/jbc.274.43.30603. PMID 10521444.
  • Yamamoto Y, Yin MJ, Gaynor RB (2000). "IκB Kinase α (IKKα) Regulation of IKKβ Kinase Activity". Mol. Cell. Biol. 20 (10): 3655–66. doi:10.1128/MCB.20.10.3655-3666.2000. PMC 85658. PMID 10779355.
  • 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. doi:10.1074/jbc.M002552200. PMID 10887201.
  • Chaudhary PM, Eby MT, Jasmin A, Kumar A, Liu L, Hood L (2000). "Activation of the NF-kappaB pathway by caspase 8 and its homologs". Oncogene. 19 (39): 4451–60. doi:10.1038/sj.onc.1203812. PMID 11002417.
  • Kumar A, Eby MT, Sinha S, Jasmin A, Chaudhary PM (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. doi:10.1074/jbc.M008356200. PMID 11035039.
  • v
  • t
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Non-specific serine/threonine protein kinases (EC 2.7.11.1)
Pyruvate dehydrogenase kinase (EC 2.7.11.2)
Dephospho-(reductase kinase) kinase (EC 2.7.11.3)
3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring) kinase (EC 2.7.11.4)
(isocitrate dehydrogenase (NADP+)) kinase (EC 2.7.11.5)
(tyrosine 3-monooxygenase) kinase (EC 2.7.11.6)
Myosin-heavy-chain kinase (EC 2.7.11.7)
Fas-activated serine/threonine kinase (EC 2.7.11.8)
Goodpasture-antigen-binding protein kinase (EC 2.7.11.9)
  • -
IκB kinase (EC 2.7.11.10)
cAMP-dependent protein kinase (EC 2.7.11.11)
cGMP-dependent protein kinase (EC 2.7.11.12)
Protein kinase C (EC 2.7.11.13)
Rhodopsin kinase (EC 2.7.11.14)
Beta adrenergic receptor kinase (EC 2.7.11.15)
G-protein coupled receptor kinases (EC 2.7.11.16)
Ca2+/calmodulin-dependent (EC 2.7.11.17)
Myosin light-chain kinase (EC 2.7.11.18)
Phosphorylase kinase (EC 2.7.11.19)
Elongation factor 2 kinase (EC 2.7.11.20)
Polo kinase (EC 2.7.11.21)
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)
(RNA-polymerase)-subunit kinase (EC 2.7.11.23)
Mitogen-activated protein kinase (EC 2.7.11.24)
MAP3K (EC 2.7.11.25)
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)
MAP2K
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