PAG1

Phosphoprotein associated with glycosphingolipid microdomains 1
Identifiers
Symbols	PAG1; CBP; FLJ37858; MGC138364; PAG
External IDs	OMIM: 605767 MGI: 2443160 HomoloGene: 10198 GeneCards: PAG1 Gene
Gene Ontology Molecular function • SH3/SH2 adaptor activity • protein binding • SH2 domain binding Cellular component • intracellular • plasma membrane • plasma membrane • plasma membrane • integral to membrane • membrane raft Biological process • signal transduction • epidermal growth factor receptor signaling pathway • intracellular signal transduction • T cell receptor signaling pathway • regulation of T cell activation • negative regulation of T cell activation Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	55824	94212
Ensembl	ENSG00000076641	ENSMUSG00000027508
UniProt	Q9NWQ8	Q3U1F9
RefSeq (mRNA)	NM_018440	XM_976665
RefSeq (protein)	NP_060910	XP_981759
Location (UCSC)	Chr 8: 81.88 – 82.02 Mb	Chr 3: 9.69 – 9.83 Mb
PubMed search	[1]	[2]

Phosphoprotein associated with glycosphingolipid-enriched microdomains 1 is a protein that in humans is encoded by the PAG1 gene.^[1][2]

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.^[2]

Interactions

PAG1 has been shown to interact with FYN,^[1] C-src tyrosine kinase,^[1] Sodium-hydrogen antiporter 3 regulator 1^[3] and Abl gene.^[4]

References

1. ^ ^{a b c} Brdicka T, Pavlistova D, Leo A, Bruyns E, Korinek V, Angelisova P, Scherer J, Shevchenko A, Hilgert I, Cerny J, Drbal K, Kuramitsu Y, Kornacker B, Horejsi V, Schraven B (May 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. doi:10.1084/jem.191.9.1591. PMC 2213442. PMID 10790433. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2213442. 
2. ^ ^{a b} "Entrez Gene: PAG1 phosphoprotein associated with glycosphingolipid microdomains 1". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=55824. 
3. ^ Brdicková, N; Brdicka T, Andera L, Spicka J, Angelisová P, Milgram S L, Horejsí V (Oct. 2001). "Interaction between two adapter proteins, PAG and EBP50: a possible link between membrane rafts and actin cytoskeleton". FEBS Lett. (Netherlands) 507 (2): 133–6. doi:10.1016/S0014-5793(01)02955-6. ISSN 0014-5793. PMID 11684085. 
4. ^ Wen, S T; Van Etten R A (Oct. 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. (UNITED STATES) 11 (19): 2456–67. doi:10.1101/gad.11.19.2456. ISSN 0890-9369. PMC 316562. PMID 9334312. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=316562. 

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. doi:10.1101/gad.11.19.2456. PMC 316562. PMID 9334312. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=316562. 
• 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. doi:10.1016/S0014-5793(01)02955-6. 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. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241. 
• 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=528928. 
• 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.