PAG1

PAG1
Identifiers
Aliases	PAG1, CBP, PAG, phosphoprotein membrane anchor with glycosphingolipid microdomains 1
External IDs	OMIM: 605767 MGI: 2443160 HomoloGene: 10198 GeneCards: PAG1
Gene location (Human)
Chr.	Chromosome 8 (human)
End	81,112,068 bp
Gene location (Mouse)
Chr.	Chromosome 3 (mouse)
End	9,898,739 bp
RNA expression pattern
	Top expressed in
	secondary oocyte; ; visceral pleura; ; endothelial cell; ; lower lobe of lung; ; jejunal mucosa; ; spinal ganglia; ; tibia; ; blood; ; Brodmann area 23; ; pylorus;
	Top expressed in
	pineal gland; ; superior cervical ganglion; ; ciliary body; ; left lung lobe; ; substantia nigra; ; blood; ; trigeminal ganglion; ; iris; ; hair follicle; ; lateral geniculate nucleus;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	SH2 domain binding; protein binding; transmembrane receptor protein tyrosine kinase adaptor activity;
Cellular component	integral component of membrane; membrane raft; plasma membrane; membrane; integral component of plasma membrane; intracellular anatomical structure;
Biological process	intracellular signal transduction; T cell receptor signaling pathway; adaptive immune response; regulation of T cell activation; signal transduction; immune system process; positive regulation of signal transduction; transmembrane receptor protein tyrosine kinase signaling pathway; negative regulation of T cell activation;
	Sources:Amigo / QuickGO
Orthologs
	55824
	94212
	ENSG00000076641
	ENSMUSG00000027508
	Q9NWQ8
	Q3U1F9
	NM_018440; NM_001007549
	NM_001195031; NM_053182
	NP_060910
	NP_001181960; NP_444412
	Wikidata
View/Edit Human	View/Edit Mouse

Phosphoprotein associated with glycosphingolipid-enriched microdomains 1 is a protein that in humans is encoded by the PAG1 gene.^[5]^[6]

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.^[6]

Interactions

PAG1 has been shown to interact with FYN,^[5] C-src tyrosine kinase,^[5] Sodium-hydrogen antiporter 3 regulator 1^[7] and Abl gene.^[8]

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000076641 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000027508 - 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.
1 2 3 Brdicka T, Pavlistová D, Leo A, Bruyns E, Korínek V, Angelisová P, Scherer J, Shevchenko A, Hilgert I, Cerný J, Drbal K, Kuramitsu Y, Kornacker B, Horejsí 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". The Journal of Experimental Medicine. 191 (9): 1591–604. doi:10.1084/jem.191.9.1591. PMC 2213442. PMID 10790433.
1 2 "Entrez Gene: PAG1 phosphoprotein associated with glycosphingolipid microdomains 1".
↑ Brdicková N, Brdicka T, Andera L, Spicka J, Angelisová P, Milgram SL, Horejsí V (October 2001). "Interaction between two adapter proteins, PAG and EBP50: a possible link between membrane rafts and actin cytoskeleton". FEBS Letters. 507 (2): 133–6. doi:10.1016/S0014-5793(01)02955-6. PMID 11684085. S2CID 12676563.
↑ Wen ST, Van Etten RA (October 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 & Development. 11 (19): 2456–67. doi:10.1101/gad.11.19.2456. PMC 316562. PMID 9334312.

Wen ST, Van Etten RA (October 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 & Development. 11 (19): 2456–67. doi:10.1101/gad.11.19.2456. PMC 316562. PMID 9334312.
Brdicková N, Brdicka T, Andera L, Spicka J, Angelisová P, Milgram SL, Horejsí V (October 2001). "Interaction between two adapter proteins, PAG and EBP50: a possible link between membrane rafts and actin cytoskeleton". FEBS Letters. 507 (2): 133–6. doi:10.1016/S0014-5793(01)02955-6. PMID 11684085. S2CID 12676563.
Tedoldi S, Paterson JC, Hansmann ML, Natkunam Y, Rüdiger T, Angelisova P, Du MQ, Roberton H, Roncador G, Sanchez L, Pozzobon M, Masir N, Barry R, Pileri S, Mason DY, Marafioti T, Horejsí V (January 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. S2CID 340034.
Jiang LQ, Feng X, Zhou W, Knyazev PG, Ullrich A, Chen Z (September 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 (June 2006). "Expression and purification of human PAG, a transmembrane adapter protein using an insect cell expression system and its structure basis". The Protein Journal. 25 (4): 295–9. doi:10.1007/s10930-006-9015-6. PMID 16947079. S2CID 11529404.
Roberts AE, Araki T, Swanson KD, Montgomery KT, Schiripo TA, Joshi VA, Li L, Yassin Y, Tamburino AM, Neel BG, Kucherlapati RS (January 2007). "Germline gain-of-function mutations in SOS1 cause Noonan syndrome". Nature Genetics. 39 (1): 70–4. doi:10.1038/ng1926. PMID 17143285. S2CID 10222262.
Smida M, Posevitz-Fejfar A, Horejsi V, Schraven B, Lindquist JA (July 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.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000076641 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000027508 - Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid10790433-5] 1 2 3 Brdicka T, Pavlistová D, Leo A, Bruyns E, Korínek V, Angelisová P, Scherer J, Shevchenko A, Hilgert I, Cerný J, Drbal K, Kuramitsu Y, Kornacker B, Horejsí 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". The Journal of Experimental Medicine. 191 (9): 1591–604. doi:10.1084/jem.191.9.1591. PMC 2213442. PMID 10790433.

[entrez-6] 1 2 "Entrez Gene: PAG1 phosphoprotein associated with glycosphingolipid microdomains 1".

[pmid11684085-7] Brdicková N, Brdicka T, Andera L, Spicka J, Angelisová P, Milgram SL, Horejsí V (October 2001). "Interaction between two adapter proteins, PAG and EBP50: a possible link between membrane rafts and actin cytoskeleton". FEBS Letters. 507 (2): 133–6. doi:10.1016/S0014-5793(01)02955-6. PMID 11684085. S2CID 12676563.

[pmid9334312-8] Wen ST, Van Etten RA (October 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 & Development. 11 (19): 2456–67. doi:10.1101/gad.11.19.2456. PMC 316562. PMID 9334312.

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Interactions

References

Further reading