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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; OMA:LAMTOR3 - orthologs
Gene location (Human) Chr. Chromosome 4 (human) Band 4q23 Start 99,878,336 bp End 99,894,428 bp
Gene location (Mouse) Chr. Chromosome 3 (mouse) Band 3|3 G3 Start 137,624,267 bp End 137,634,661 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in mucosa of sigmoid colon oocyte retinal pigment epithelium ventricular zone islet of Langerhans Achilles tendon secondary oocyte palpebral conjunctiva rectum ganglionic eminence Top expressed in fossa facial motor nucleus secondary oocyte condyle renal corpuscle medullary collecting duct trigeminal ganglion atrioventricular junction vestibular membrane of cochlear duct Paneth cell More reference expression data BioGPS More reference expression data
Gene ontology Molecular function guanyl-nucleotide exchange factor activity protein binding 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 plasma membrane specific granule membrane tertiary granule membrane Biological process regulation of TOR signaling MAPK cascade cellular response to amino acid stimulus positive regulation of TOR signaling 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: 137.62 – 137.63 Mb PubMed search
Wikidata
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Mitogen-activated protein kinase scaffold protein 1 is a scaffold protein that in humans is encoded by the MAPKSP1 gene.

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.

Interactions

MAP2K1IP1 has been shown to interact with MAP2K1.

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. Bibcode:1998Sci...281.1668S. 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. Bibcode:2004PNAS..101.6981V. 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. Bibcode:2004PNAS..10110984K. 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. S2CID 19060718.
• 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. S2CID 27498866.
• 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.

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