MAPK8IP1

Protein-coding gene in the species Homo sapiens

MAPK8IP1
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

2G01, 2GMX, 2H96, 3OXI, 3PTG, 3VUD, 3VUG, 3VUH, 3VUI, 3VUK, 3VUL, 3VUM, 4E73, 4G1W, 4H39, 4HYS, 4HYU, 4IZY

Identifiers
AliasesMAPK8IP1, IB1, JIP-1, JIP1, PRKM8IP, mitogen-activated protein kinase 8 interacting protein 1
External IDsOMIM: 604641; MGI: 1309464; HomoloGene: 31314; GeneCards: MAPK8IP1; OMA:MAPK8IP1 - orthologs
Gene location (Human)
Chromosome 11 (human)
Chr.Chromosome 11 (human)[1]
Chromosome 11 (human)
Genomic location for MAPK8IP1
Genomic location for MAPK8IP1
Band11p11.2Start45,885,651 bp[1]
End45,906,465 bp[1]
Gene location (Mouse)
Chromosome 2 (mouse)
Chr.Chromosome 2 (mouse)[2]
Chromosome 2 (mouse)
Genomic location for MAPK8IP1
Genomic location for MAPK8IP1
Band2|2 E1Start92,214,021 bp[2]
End92,231,608 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • C1 segment

  • right frontal lobe

  • anterior pituitary

  • right hemisphere of cerebellum

  • tibial nerve

  • anterior cingulate cortex

  • prefrontal cortex

  • ventricular zone

  • Brodmann area 9

  • Brodmann area 10
Top expressed in
  • superior frontal gyrus

  • primary visual cortex

  • entorhinal cortex

  • perirhinal cortex

  • cerebellar cortex

  • dentate gyrus of hippocampal formation granule cell

  • superior surface of tongue

  • gallbladder

  • dorsomedial hypothalamic nucleus

  • central gray substance of midbrain
More reference expression data
BioGPS


More reference expression data
Gene ontology
Molecular function
  • MAP-kinase scaffold activity
  • protein kinase inhibitor activity
  • protein binding
  • kinesin binding
  • protein kinase binding
  • JUN kinase binding
  • mitogen-activated protein kinase kinase binding
  • mitogen-activated protein kinase kinase kinase binding
Cellular component
  • cytoplasm
  • cell body
  • cytosol
  • dendritic growth cone
  • endoplasmic reticulum membrane
  • mitochondrial membranes
  • membrane
  • dentate gyrus mossy fiber
  • axonal growth cone
  • synapse
  • axon
  • dendrite
  • endoplasmic reticulum
  • mitochondrion
  • perinuclear region of cytoplasm
  • neuron projection
  • nucleus
  • plasma membrane
Biological process
  • regulation of transcription, DNA-templated
  • negative regulation of intrinsic apoptotic signaling pathway
  • negative regulation of apoptotic process
  • negative regulation of JNK cascade
  • regulation of JNK cascade
  • JUN phosphorylation
  • negative regulation of JUN kinase activity
  • vesicle-mediated transport
  • signal transduction
  • positive regulation of MAPK cascade
  • positive regulation of JNK cascade
  • regulation of CD8-positive, alpha-beta T cell proliferation
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

9479

19099

Ensembl

ENSG00000121653

ENSMUSG00000027223

UniProt

Q9UQF2

Q9WVI9

RefSeq (mRNA)

NM_005456

NM_001202445
NM_001202446
NM_011162

RefSeq (protein)

NP_005447

NP_001189374
NP_001189375
NP_035292

Location (UCSC)Chr 11: 45.89 – 45.91 MbChr 2: 92.21 – 92.23 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

C-jun-amino-terminal kinase-interacting protein 1 is an enzyme that in humans is encoded by the MAPK8IP1 gene.[5][6]

The protein encoded by this gene is a regulator of the pancreatic beta-cell function. It is highly similar to JIP-1, a mouse protein known to be a regulator of c-Jun amino-terminal kinase (Mapk8). This protein has been shown to prevent MAPK8 mediated activation of transcription factors, and decrease IL-1 beta and MAP kinase kinase 1 (MEKK1) induced apoptosis in pancreatic beta cells. This protein also functions as a DNA-binding transactivator of the glucose transporter GLUT2. RE1-silencing transcription factor (REST) is reported to repress the expression of this gene in insulin-secreting beta cells. This gene is found to be mutated in a type 2 diabetes family, and thus is thought to be a susceptibility gene for type 2 diabetes.[7]

Interactions

MAPK8IP1 has been shown to interact with MAP3K10,[8] DUSP16,[9] Mitogen-activated protein kinase 9,[8][10] MAPK8,[10][11] LRP2,[12][13] LRP1,[12] MAP3K12,[8] MAP2K7,[8] MAPK8IP2[8] and MAP3K11.[8]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000121653 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000027223 – 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. ^ Dickens M, Rogers JS, Cavanagh J, Raitano A, Xia Z, Halpern JR, Greenberg ME, Sawyers CL, Davis RJ (August 1997). "A cytoplasmic inhibitor of the JNK signal transduction pathway". Science. 277 (5326): 693–6. doi:10.1126/science.277.5326.693. PMID 9235893.
  6. ^ Bonny C, Nicod P, Waeber G (March 1998). "IB1, a JIP-1-related nuclear protein present in insulin-secreting cells". J Biol Chem. 273 (4): 1843–6. doi:10.1074/jbc.273.4.1843. PMID 9442013.
  7. ^ "Entrez Gene: MAPK8IP1 mitogen-activated protein kinase 8 interacting protein 1".
  8. ^ a b c d e f Yasuda J, Whitmarsh A J, Cavanagh J, Sharma M, Davis R J (October 1999). "The JIP Group of Mitogen-Activated Protein Kinase Scaffold Proteins". Mol. Cell. Biol. 19 (10): 7245–54. doi:10.1128/mcb.19.10.7245. ISSN 0270-7306. PMC 84717. PMID 10490659.
  9. ^ Willoughby EA, Perkins Gordon R, Collins Mary K, Whitmarsh Alan J (March 2003). "The JNK-interacting protein-1 scaffold protein targets MAPK phosphatase-7 to dephosphorylate JNK". J. Biol. Chem. 278 (12): 10731–6. doi:10.1074/jbc.M207324200. ISSN 0021-9258. PMID 12524447.
  10. ^ a b Whitmarsh AJ, Cavanagh J, Tournier C, Yasuda J, Davis R J (September 1998). "A mammalian scaffold complex that selectively mediates MAP kinase activation". Science. 281 (5383): 1671–4. Bibcode:1998Sci...281.1671W. doi:10.1126/science.281.5383.1671. ISSN 0036-8075. PMID 9733513.
  11. ^ Cai Y, Lechner Mark S, Nihalani Deepak, Prindle Marc J, Holzman Lawrence B, Dressler Gregory R (January 2002). "Phosphorylation of Pax2 by the c-Jun N-terminal kinase and enhanced Pax2-dependent transcription activation". J. Biol. Chem. 277 (2): 1217–22. doi:10.1074/jbc.M109663200. ISSN 0021-9258. PMID 11700324.
  12. ^ a b Gotthardt M, Trommsdorff M, Nevitt M F, Shelton J, Richardson J A, Stockinger W, Nimpf J, Herz J (August 2000). "Interactions of the low density lipoprotein receptor gene family with cytosolic adaptor and scaffold proteins suggest diverse biological functions in cellular communication and signal transduction". J. Biol. Chem. 275 (33): 25616–24. doi:10.1074/jbc.M000955200. ISSN 0021-9258. PMID 10827173.
  13. ^ Petersen HH, Hilpert Jan, Militz Daniel, Zandler Valerie, Jacobsen Christian, Roebroek Anton J M, Willnow Thomas E (February 2003). "Functional interaction of megalin with the megalinbinding protein (MegBP), a novel tetratrico peptide repeat-containing adaptor molecule". J. Cell Sci. 116 (Pt 3): 453–61. doi:10.1242/jcs.00243. ISSN 0021-9533. PMID 12508107.

Further reading

  • Andersson B, Wentland MA, Ricafrente JY, Liu W, Gibbs RA (1996). "A "double adaptor" method for improved shotgun library construction". Anal. Biochem. 236 (1): 107–13. doi:10.1006/abio.1996.0138. PMID 8619474.
  • Yu W, Andersson B, Worley KC, Muzny DM, Ding Y, Liu W, Ricafrente JY, Wentland MA, Lennon G (1997). "Large-Scale Concatenation cDNA Sequencing". Genome Res. 7 (4): 353–8. doi:10.1101/gr.7.4.353. PMC 139146. PMID 9110174.
  • Whitmarsh AJ, Cavanagh J, Tournier C, Yasuda J, Davis RJ (1998). "A mammalian scaffold complex that selectively mediates MAP kinase activation". Science. 281 (5383): 1671–4. Bibcode:1998Sci...281.1671W. doi:10.1126/science.281.5383.1671. PMID 9733513.
  • Mooser V, Maillard A, Bonny C, Steinmann M, Shaw P, Yarnall DP, Burns DK, Schorderet DF, Nicod P (1999). "Genomic organization, fine-mapping, and expression of the human islet-brain 1 (IB1)/c-Jun –amino-terminal kinase interacting protein-1 (JIP-1) gene". Genomics. 55 (2): 202–8. doi:10.1006/geno.1998.5641. PMID 9933567.
  • Yasuda J, Whitmarsh AJ, Cavanagh J, Sharma M, Davis RJ (2000). "The JIP Group of Mitogen-Activated Protein Kinase Scaffold Proteins". Mol. Cell. Biol. 19 (10): 7245–54. doi:10.1128/mcb.19.10.7245. PMC 84717. PMID 10490659.
  • Meyer D, Liu A, Margolis B (2000). "Interaction of c-Jun amino-terminal kinase interacting protein-1 with p190 rhoGEF and its localization in differentiated neurons". J. Biol. Chem. 274 (49): 35113–8. doi:10.1074/jbc.274.49.35113. PMID 10574993.
  • Kelkar N, Gupta S, Dickens M, Davis RJ (2000). "Interaction of a Mitogen-Activated Protein Kinase Signaling Module with the Neuronal Protein JIP3". Mol. Cell. Biol. 20 (3): 1030–43. doi:10.1128/MCB.20.3.1030-1043.2000. PMC 85220. PMID 10629060.
  • Waeber G, Delplanque J, Bonny C, Mooser V, Steinmann M, Widmann C, Maillard A, Miklossy J, Dina C (2000). "The gene MAPK8IP1, encoding islet-brain-1, is a candidate for type 2 diabetes". Nat. Genet. 24 (3): 291–5. doi:10.1038/73523. PMID 10700186. S2CID 5964917.
  • Bonny C, Oberson A, Steinmann M, Schorderet DF, Nicod P, Waeber G (2000). "IB1 reduces cytokine-induced apoptosis of insulin-secreting cells". J. Biol. Chem. 275 (22): 16466–72. doi:10.1074/jbc.M908297199. PMID 10748095.
  • Gotthardt M, Trommsdorff M, Nevitt MF, Shelton J, Richardson JA, Stockinger W, Nimpf J, Herz J (2000). "Interactions of the low density lipoprotein receptor gene family with cytosolic adaptor and scaffold proteins suggest diverse biological functions in cellular communication and signal transduction". J. Biol. Chem. 275 (33): 25616–24. doi:10.1074/jbc.M000955200. PMID 10827173.
  • Bonny C, Oberson A, Negri S, Sauser C, Schorderet DF (2001). "Cell-permeable peptide inhibitors of JNK: novel blockers of beta-cell death". Diabetes. 50 (1): 77–82. doi:10.2337/diabetes.50.1.77. PMID 11147798.
  • Verhey KJ, Meyer D, Deehan R, Blenis J, Schnapp BJ, Rapoport TA, Margolis B (2001). "Cargo of Kinesin Identified as Jip Scaffolding Proteins and Associated Signaling Molecules". J. Cell Biol. 152 (5): 959–70. doi:10.1083/jcb.152.5.959. PMC 2198804. PMID 11238452.
  • Matsuda S, Yasukawa T, Homma Y, Ito Y, Niikura T, Hiraki T, Hirai S, Ohno S, Kita Y (2001). "c-Jun N-terminal kinase (JNK)-interacting protein-1b/islet-brain-1 scaffolds Alzheimer's amyloid precursor protein with JNK". J. Neurosci. 21 (17): 6597–607. doi:10.1523/JNEUROSCI.21-17-06597.2001. PMC 6763068. PMID 11517249.
  • Abderrahmani A, Steinmann M, Plaisance V, Niederhauser G, Haefliger JA, Mooser V, Bonny C, Nicod P, Waeber G (2001). "The Transcriptional Repressor REST Determines the Cell-Specific Expression of the Human MAPK8IP1 Gene Encoding IB1 (JIP-1)". Mol. Cell. Biol. 21 (21): 7256–67. doi:10.1128/MCB.21.21.7256-7267.2001. PMC 99900. PMID 11585908.
  • Cai Y, Lechner MS, Nihalani D, Prindle MJ, Holzman LB, Dressler GR (2002). "Phosphorylation of Pax2 by the c-Jun N-terminal kinase and enhanced Pax2-dependent transcription activation". J. Biol. Chem. 277 (2): 1217–22. doi:10.1074/jbc.M109663200. PMID 11700324.
  • Scheinfeld MH, Roncarati R, Vito P, Lopez PA, Abdallah M, d'Adamio L (2002). "Jun NH2-terminal kinase (JNK) interacting protein 1 (JIP1) binds the cytoplasmic domain of the Alzheimer's beta-amyloid precursor protein (APP)". J. Biol. Chem. 277 (5): 3767–75. doi:10.1074/jbc.M108357200. PMID 11724784.
  • Ikeda A, Hasegawa K, Masaki M, Moriguchi T, Nishida E, Kozutsumi Y, Oka S, Kawasaki T (2002). "Mixed lineage kinase LZK forms a functional signaling complex with JIP-1, a scaffold protein of the c-Jun NH(2)-terminal kinase pathway". J. Biochem. 130 (6): 773–81. doi:10.1093/oxfordjournals.jbchem.a003048. PMID 11726277.
  • Hashimoto M, Hsu LJ, Rockenstein E, Takenouchi T, Mallory M, Masliah E (2002). "alpha-Synuclein protects against oxidative stress via inactivation of the c-Jun N-terminal kinase stress-signaling pathway in neuronal cells". J. Biol. Chem. 277 (13): 11465–72. doi:10.1074/jbc.M111428200. PMID 11790792.
  • v
  • t
  • e
  • 2fpd: Sad structure determination: crystal structure of the intrinsic dimerization sh3 domain of the ib1 scaffold protein
    2fpd: Sad structure determination: crystal structure of the intrinsic dimerization sh3 domain of the ib1 scaffold protein
  • 2fpe: Conserved dimerization of the ib1 src-homology 3 domain
    2fpe: Conserved dimerization of the ib1 src-homology 3 domain
  • 2fpf: Crystal structure of the ib1 sh3 dimer at low resolution
    2fpf: Crystal structure of the ib1 sh3 dimer at low resolution