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MAP2K1IP1

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From Wikipedia, the free encyclopedia

Protein-coding gene in the species Homo sapiens

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)^[1]

Band	4q23	Start	99,878,336bp^[1]
Band	4q23	End	99,894,428bp^[1]

Gene location (Mouse)

Chr.	Chromosome 3 (mouse)^[2]

Band	3\|3 G3	Start	137,624,267bp^[2]
Band	3\|3 G3	End	137,634,661bp^[2]

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

^[3]

^[4]

Wikidata

View/Edit Human

View/Edit Mouse

Mitogen-activated protein kinase scaffold protein 1 is a scaffold protein that in humans is encoded by theMAPKSP1gene.^[5]^[6]^[7]

Function

[edit]

The protein encoded by this gene was identified as an interacting protein that binds specifically toMAP kinase kinase MAP2K1/MEK1 and toMAP kinase MAPK2/ERK1. This protein enhances the activation ofMAPK2, and thus is thought to function as an adaptor to enhance the efficiency of theMAP kinase cascade.^[7]

Interactions

[edit]

MAP2K1IP1 has been shown tointeract withMAP2K1.^[5]^[8]

References

[edit]

^^a ^b ^cGRCh38: Ensembl release 89: ENSG00000109270 –Ensembl, May 2017
^^a ^b ^cGRCm38: Ensembl release 89: ENSMUSG00000091512 –Ensembl, May 2017
^"Human PubMed Reference:".National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:".National Center for Biotechnology Information, U.S. National Library of Medicine.
^^a ^bSchaeffer 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.
^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.
^^a ^b"Entrez Gene: MAP2K1IP1 mitogen-activated protein kinase kinase 1 interacting protein 1".
^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.

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.

v t e PDB gallery
1sko: MP1-p14 Complex 1vet: Crystal Structure of p14/MP1 at 1.9 A resolution 1veu: Crystal structure of the p14/MP1 complex at 2.15 A resolution