PAG1

From Wikipedia, the free encyclopedia

Phosphoprotein associated with glycosphingolipid microdomains 1

Identifiers

PAG1; CBP; PAG; FLJ37858; MGC138364

External IDs

OMIM: 605767 MGI: 2443160 HomoloGene: 10198

Gene ontology
Molecular Function:	• SH3/SH2 adaptor activity • protein binding • SH2 domain binding
Cellular Component:	• plasma membrane • integral to membrane • lipid raft
Biological Process:	• immune response • intracellular signaling cascade • antimicrobial humoral response • regulation of T cell activation

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_018440 (mRNA)
NP_060910 (protein)

XM_976665 (mRNA)
XP_981759 (protein)

Location

Chr 8: 82.04 - 82.19 Mb

Chr 3: 9.67 - 9.82 Mb

Pubmed search

[1]

[2]

Phosphoprotein associated with glycosphingolipid microdomains 1, also known as PAG1, is a human gene.^[1]

The protein encoded by this gene is a type III transmembrane adaptor protein that binds to the tyrosine kinase csk protein. It is thought to be involved in the regulation of T cell activation.^[1]

[edit] References

^ ^a ^b Entrez Gene: PAG1 phosphoprotein associated with glycosphingolipid microdomains 1.

[edit] Further reading

Wen ST, Van Etten RA (1997). "The PAG gene product, a stress-induced protein with antioxidant properties, is an Abl SH3-binding protein and a physiological inhibitor of c-Abl tyrosine kinase activity.". Genes Dev. 11 (19): 2456–67. PMID 9334312.
Brdicka T, Pavlistová D, Leo A, et al. (2000). "Phosphoprotein associated with glycosphingolipid-enriched microdomains (PAG), a novel ubiquitously expressed transmembrane adaptor protein, binds the protein tyrosine kinase csk and is involved in regulation of T cell activation.". J. Exp. Med. 191 (9): 1591–604. PMID 10790433.
Brdicková N, Brdicka T, Andera L, et al. (2001). "Interaction between two adapter proteins, PAG and EBP50: a possible link between membrane rafts and actin cytoskeleton.". FEBS Lett. 507 (2): 133–6. PMID 11684085.
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.
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. PMID 15489334.
Tedoldi S, Paterson JC, Hansmann ML, et al. (2006). "Transmembrane adaptor molecules: a new category of lymphoid-cell markers.". Blood 107 (1): 213–21. doi:10.1182/blood-2005-06-2273. PMID 16160011.
Jiang LQ, Feng X, Zhou W, et al. (2006). "Csk-binding protein (Cbp) negatively regulates epidermal growth factor-induced cell transformation by controlling Src activation.". Oncogene 25 (40): 5495–506. doi:10.1038/sj.onc.1209554. PMID 16636672.
Takeuchi S (2007). "Expression and purification of human PAG, a transmembrane adapter protein using an insect cell expression system and its structure basis.". Protein J. 25 (4): 295–9. doi:10.1007/s10930-006-9015-6. PMID 16947079.
Roberts AE, Araki T, Swanson KD, et al. (2007). "Germline gain-of-function mutations in SOS1 cause Noonan syndrome.". Nat. Genet. 39 (1): 70–4. doi:10.1038/ng1926. PMID 17143285.
Smida M, Posevitz-Fejfar A, Horejsi V, et al. (2007). "A novel negative regulatory function of the phosphoprotein associated with glycosphingolipid-enriched microdomains: blocking Ras activation.". Blood 110 (2): 596–615. doi:10.1182/blood-2006-07-038752. PMID 17389760.