MPP2

From Wikipedia, the free encyclopedia

Membrane protein, palmitoylated 2 (MAGUK p55 subfamily member 2)

Identifiers

MPP2; DLG2; DKFZp686A06252; DKFZp686J2189; DKFZp761D0712

External IDs

OMIM: 600723 MGI: 1858257 HomoloGene: 3920

Gene ontology
Molecular Function:	• guanylate kinase activity • protein binding
Cellular Component:	• membrane fraction • integral to plasma membrane • cell surface • membrane
Biological Process:	• protein complex assembly • signal transduction

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_005374 (mRNA)
NP_005365 (protein)

NM_016695 (mRNA)
NP_057904 (protein)

Location

Chr 17: 39.31 - 39.34 Mb

Chr 11: 101.87 - 101.9 Mb

Pubmed search

[1]

[2]

Membrane protein, palmitoylated 2 (MAGUK p55 subfamily member 2), also known as MPP2, is a human gene.^[1]

Palmitoylated membrane protein 2 is a member 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 2 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.^[1]

[edit] References

^ ^a ^b Entrez Gene: MPP2 membrane protein, palmitoylated 2 (MAGUK p55 subfamily member 2).

[edit] Further reading

Mazoyer S, Gayther SA, Nagai MA, et al. (1995). "A gene (DLG2) located at 17q12-q21 encodes a new homologue of the Drosophila tumor suppressor dIg-A.". Genomics 28 (1): 25-31. PMID 7590743.
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. PMID 8125298.
Smith SA, Holik P, Stevens J, et al. (1997). "Isolation of a gene (DLG3) encoding a second member of the discs-large family on chromosome 17q12-q21.". Genomics 31 (2): 145-50. doi:10.1006/geno.1996.0025. PMID 8824795.
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. PMID 9373149.
Wiemann S, Weil B, Wellenreuther R, et al. (2001). "Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs.". Genome Res. 11 (3): 422-35. doi:10.1101/gr.154701. PMID 11230166.
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. PMID 12477932.
Shin BK, Wang H, Yim AM, et al. (2003). "Global profiling of the cell surface proteome of cancer cells uncovers an abundance of proteins with chaperone function.". J. Biol. Chem. 278 (9): 7607-16. doi:10.1074/jbc.M210455200. PMID 12493773.
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. PMID 15489334.
Wierstra I, Alves J (2006). "Despite its strong transactivation domain, transcription factor FOXM1c is kept almost inactive by two different inhibitory domains.". Biol. Chem. 387 (7): 963-76. doi:10.1515/BC.2006.120. PMID 16913846.