MPP1

Membrane protein, palmitoylated 1, 55kDa
PDB rendering based on 2ev8.
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 2EJY​, 2EV8​, 3NEY​
Identifiers
Symbols	MPP1 ; AAG12; DXS552E; EMP55; MRG1; PEMP
External IDs	OMIM: 305360 MGI: 105941 HomoloGene: 1826 GeneCards: MPP1 Gene
Gene ontology Molecular function • guanylate kinase activity • protein binding Cellular component • intracellular • integral component of plasma membrane • membrane • cortical cytoskeleton • stereocilium Biological process • signal transduction • nucleotide phosphorylation • regulation of neutrophil chemotaxis Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	4354	17524
Ensembl	ENSG00000130830	ENSMUSG00000031402
UniProt	Q00013	P70290
RefSeq (mRNA)	NM_001166460	NM_008621
RefSeq (protein)	NP_001159932	NP_032647
Location (UCSC)	Chr X: 154.78 – 154.82 Mb	Chr X: 75.11 – 75.13 Mb
PubMed search

55 kDa erythrocyte membrane protein is a protein that in humans is encoded by the MPP1 gene.^[1][2]

Palmitoylated membrane protein 1 is the prototype of a family of membrane-associated proteins termed MAGUKs (membrane-associated guanylate kinase homologs). MAGUKs interact with the cytoskeleton and regulate cell proliferation, signaling pathways, and intracellular junctions. Palmitoylated membrane protein 1 contains a conserved sequence, called the SH3 (src homology 3) motif, found in several other proteins that associate with the cytoskeleton and are suspected to play important roles in signal transduction.^[2]

References

1. Ruff P, Speicher DW, Husain-Chishti A (Sep 1991). "Molecular identification of a major palmitoylated erythrocyte membrane protein containing the src homology 3 motif". Proc Natl Acad Sci U S A 88 (15): 6595–9. doi:10.1073/pnas.88.15.6595. PMC 52133. PMID 1713685.
2. "Entrez Gene: MPP1 membrane protein, palmitoylated 1, 55kDa".

Further reading

• Metzenberg AB, Gitschier J (1993). "The gene encoding the palmitoylated erythrocyte membrane protein, p55, originates at the CpG island 3' to the factor VIII gene". Hum. Mol. Genet. 1 (2): 97–101. doi:10.1093/hmg/1.2.97. PMID 1301163.
• Bryant PJ, Woods DF (1992). "A major palmitoylated membrane protein of human erythrocytes shows homology to yeast guanylate kinase and to the product of a Drosophila tumor suppressor gene". Cell 68 (4): 621–2. doi:10.1016/0092-8674(92)90136-Z. PMID 1310897.
• Marfatia SM, Leu RA, Branton D, Chishti AH (1995). "Identification of the protein 4.1 binding interface on glycophorin C and p55, a homologue of the Drosophila discs-large tumor suppressor protein". J. Biol. Chem. 270 (2): 715–9. doi:10.1074/jbc.270.2.715. PMID 7822301.
• 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.
• Kim AC, Metzenberg AB, Sahr KE, et al. (1997). "Complete genomic organization of the human erythroid p55 gene (MPP1), a membrane-associated guanylate kinase homologue". Genomics 31 (2): 223–9. doi:10.1006/geno.1996.0035. PMID 8824805.
• Marfatia SM, Morais-Cabral JH, Kim AC, et al. (1997). "The PDZ domain of human erythrocyte p55 mediates its binding to the cytoplasmic carboxyl terminus of glycophorin C. Analysis of the binding interface by in vitro mutagenesis". J. Biol. Chem. 272 (39): 24191–7. doi:10.1074/jbc.272.39.24191. PMID 9305870.
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (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.
• Simpson JC, Wellenreuther R, Poustka A, et al. (2001). "Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing". EMBO Rep. 1 (3): 287–92. doi:10.1093/embo-reports/kvd058. PMC 1083732. PMID 11256614.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
• Stelzl U, Worm U, Lalowski M, et al. (2005). "A human protein-protein interaction network: a resource for annotating the proteome". Cell 122 (6): 957–68. doi:10.1016/j.cell.2005.08.029. PMID 16169070.
• Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
• Kusunoki H, Kohno T (2006). "Solution structure of human erythroid p55 PDZ domain". Proteins 64 (3): 804–7. doi:10.1002/prot.21028. PMID 16741958.
• Gosens I, van Wijk E, Kersten FF, et al. (2007). "MPP1 links the Usher protein network and the Crumbs protein complex in the retina". Hum. Mol. Genet. 16 (16): 1993–2003. doi:10.1093/hmg/ddm147. PMID 17584769.