MAP2K1IP1

Mitogen-activated protein kinase scaffold protein 1 is a scaffold protein that in humans is encoded by the MAPKSP1 gene.[5][6][7]

LAMTOR3
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1SKO, 2ZL1, 3CPT
Identifiers
Aliases	LAMTOR3, MAP2K1IP1, MAPBP, MAPKSP1, MP1, PRO0633, Ragulator3, late endosomal/lysosomal adaptor, MAPK and MTOR activator 3
External IDs	OMIM: 603296 MGI: 1929467 HomoloGene: 10539 GeneCards: LAMTOR3
Gene location (Human) Chr. Chromosome 4 (human)[1] Band 4q23 Start 99,878,336 bp[1] End 99,894,428 bp[1]
Gene location (Mouse) Chr. Chromosome 3 (mouse)[2] Band 3|3 G3 Start 137,918,506 bp[2] End 137,928,900 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • guanyl-nucleotide exchange factor activity • GO:0001948 protein binding • GO:0032947 molecular adaptor activity • kinase activator activity Cellular component • endosome • membrane • late endosome membrane • focal adhesion • Ragulator complex • lysosomal membrane • endosome membrane • extracellular exosome • late endosome • cell membrane • specific granule membrane • tertiary granule membrane Biological process • regulation of TOR signaling • MAPK cascade • cellular protein localization • cell cycle arrest • cellular response to amino acid stimulus • positive regulation of TOR signaling • activation of MAPKK activity • neutrophil degranulation • regulation of macroautophagy Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	8649	56692
Ensembl	ENSG00000109270	ENSMUSG00000091512
UniProt	Q9UHA4	O88653
RefSeq (mRNA)	NM_001243736 NM_021970	NM_019920
RefSeq (protein)	NP_001230665 NP_068805	NP_064304
Location (UCSC)	Chr 4: 99.88 – 99.89 Mb	Chr 3: 137.92 – 137.93 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Function

The protein encoded by this gene was identified as an interacting protein that binds specifically to MAP kinase kinase MAP2K1/MEK1 and to MAP kinase MAPK2/ERK1. This protein enhances the activation of MAPK2, and thus is thought to function as an adaptor to enhance the efficiency of the MAP kinase cascade.[7]

Interactions

MAP2K1IP1 has been shown to interact with MAP2K1.[5][8]

References

1. GRCh38: Ensembl release 89: ENSG00000109270 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000091512 - 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. Schaeffer HJ, Catling AD, Eblen ST, Collier LS, Krauss A, Weber MJ (Oct 1998). "MP1: a MEK binding partner that enhances enzymatic activation of the MAP kinase cascade". Science. 281 (5383): 1668–71. doi:10.1126/science.281.5383.1668. PMID 9733512.
6. Lunin VV, Munger C, Wagner J, Ye Z, Cygler M, Sacher M (May 2004). "The structure of the MAPK scaffold, MP1, bound to its partner, p14. A complex with a critical role in endosomal map kinase signaling". J. Biol. Chem. 279 (22): 23422–30. doi:10.1074/jbc.M401648200. PMID 15016825.
7. "Entrez Gene: MAP2K1IP1 mitogen-activated protein kinase kinase 1 interacting protein 1".
8. Wunderlich W, Fialka I, Teis D, Alpi A, Pfeifer A, Parton RG, Lottspeich F, Huber LA (Feb 2001). "A novel 14-kilodalton protein interacts with the mitogen-activated protein kinase scaffold mp1 on a late endosomal/lysosomal compartment". J. Cell Biol. 152 (4): 765–76. doi:10.1083/jcb.152.4.765. PMC 2195784. PMID 11266467.

Further reading

• Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
• Okabe S, Tauchi T, Morita H, Ohashi H, Yoshimura A, Ohyashiki K (1999). "Thrombopoietin induces an SH2-containing protein, CIS1, which binds to Mpl: involvement of the ubiquitin proteosome pathway". Exp. Hematol. 27 (10): 1542–7. doi:10.1016/S0301-472X(99)00094-6. PMID 10517496.
• Wunderlich W, Fialka I, Teis D, Alpi A, Pfeifer A, Parton RG, Lottspeich F, Huber LA (2001). "A novel 14-kilodalton protein interacts with the mitogen-activated protein kinase scaffold mp1 on a late endosomal/lysosomal compartment". J. Cell Biol. 152 (4): 765–76. doi:10.1083/jcb.152.4.765. PMC 2195784. PMID 11266467.
• Teis D, Wunderlich W, Huber LA (2002). "Localization of the MP1-MAPK scaffold complex to endosomes is mediated by p14 and required for signal transduction". Dev. Cell. 3 (6): 803–14. doi:10.1016/S1534-5807(02)00364-7. PMID 12479806.
• Channavajhala PL, Wu L, Cuozzo JW, Hall JP, Liu W, Lin LL, Zhang Y (2003). "Identification of a novel human kinase supporter of Ras (hKSR-2) that functions as a negative regulator of Cot (Tpl2) signaling". J. Biol. Chem. 278 (47): 47089–97. doi:10.1074/jbc.M306002200. PMID 12975377.
• Paces-Fessy M, Boucher D, Petit E, Paute-Briand S, Blanchet-Tournier MF (2004). "The negative regulator of Gli, Suppressor of fused (Sufu), interacts with SAP18, Galectin3 and other nuclear proteins". Biochem. J. 378 (Pt 2): 353–62. doi:10.1042/BJ20030786. PMC 1223961. PMID 14611647.
• Vomastek T, Schaeffer HJ, Tarcsafalvi A, Smolkin ME, Bissonette EA, Weber MJ (2004). "Modular construction of a signaling scaffold: MORG1 interacts with components of the ERK cascade and links ERK signaling to specific agonists". Proc. Natl. Acad. Sci. U.S.A. 101 (18): 6981–6. doi:10.1073/pnas.0305894101. PMC 406452. PMID 15118098.
• Kurzbauer R, Teis D, de Araujo ME, Maurer-Stroh S, Eisenhaber F, Bourenkov GP, Bartunik HD, Hekman M, Rapp UR, Huber LA, Clausen T (2004). "Crystal structure of the p14/MP1 scaffolding complex: how a twin couple attaches mitogen-activated protein kinase signaling to late endosomes". Proc. Natl. Acad. Sci. U.S.A. 101 (30): 10984–9. doi:10.1073/pnas.0403435101. PMC 503730. PMID 15263099.
• Sharma C, Vomastek T, Tarcsafalvi A, Catling AD, Schaeffer HJ, Eblen ST, Weber MJ (2005). "MEK partner 1 (MP1): regulation of oligomerization in MAP kinase signaling". J. Cell. Biochem. 94 (4): 708–19. doi:10.1002/jcb.20344. PMID 15547943.
• Pullikuth A, McKinnon E, Schaeffer HJ, Catling AD (2005). "The MEK1 scaffolding protein MP1 regulates cell spreading by integrating PAK1 and Rho signals". Mol. Cell. Biol. 25 (12): 5119–33. doi:10.1128/MCB.25.12.5119-5133.2005. PMC 1140582. PMID 15923628.
• Villegas SN, Njaine B, Linden R, Carri NG (2006). "Glial-derived neurotrophic factor (GDNF) prevents ethanol (EtOH) induced B92 glial cell death by both PI3K/AKT and MEK/ERK signaling pathways". Brain Res. Bull. 71 (1–3): 116–26. doi:10.1016/j.brainresbull.2006.08.014. PMID 17113937.
• Teis D, Taub N, Kurzbauer R, Hilber D, de Araujo ME, Erlacher M, Offterdinger M, Villunger A, Geley S, Bohn G, Klein C, Hess MW, Huber LA (2006). "p14-MP1-MEK1 signaling regulates endosomal traffic and cellular proliferation during tissue homeostasis". J. Cell Biol. 175 (6): 861–8. doi:10.1083/jcb.200607025. PMC 2064696. PMID 17178906.
• Brahma A, Dalby KN (2007). "Regulation of protein phosphorylation within the MKK1-ERK2 complex by MP1 and the MP1*P14 heterodimer". Arch. Biochem. Biophys. 460 (1): 85–91. doi:10.1016/j.abb.2006.11.031. PMC 2853909. PMID 17254543.
• Vomastek T, Iwanicki MP, Schaeffer HJ, Tarcsafalvi A, Parsons JT, Weber MJ (2007). "RACK1 targets the extracellular signal-regulated kinase/mitogen-activated protein kinase pathway to link integrin engagement with focal adhesion disassembly and cell motility". Mol. Cell. Biol. 27 (23): 8296–305. doi:10.1128/MCB.00598-07. PMC 2169169. PMID 17908799.