STAM

From Wikipedia, the free encyclopedia

Signal transducing adaptor molecule (SH3 domain and ITAM motif) 1

Identifiers

STAM; DKFZp686J2352; STAM1

External IDs

OMIM: 601899 MGI: 1329014 HomoloGene: 37788

Gene ontology
Molecular Function:	• SH3/SH2 adaptor activity • protein binding
Biological Process:	• intracellular protein transport • signal transduction

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_003473 (mRNA)
NP_003464 (protein)

NM_011484 (mRNA)
NP_035614 (protein)

Location

Chr 10: 17.73 - 17.8 Mb

Chr 2: 13.99 - 14.07 Mb

Pubmed search

[1]

[2]

Signal transducing adaptor molecule (SH3 domain and ITAM motif) 1, also known as STAM, is a human gene.^[1]

This gene was identified by the rapid tyrosine-phosphorylation of its product in response to cytokine stimulation. The encoded protein contains an SH3 domain and the immunoreceptor tyrosine-based activation motif (ITAM). This protein associates with JAK3 and JAK2 kinases via its ITAM region, and is phosphorylated by the JAK kinases upon cytokine stimulation, which suggests the function of this protein is as an adaptor molecule involved in the downstream signaling of cytokine receptors. HGS/HRS (hepatocyte growth factor-regulated tyrosine kinase substrate) has been found to bind and counteract the function of this protein.^[1]

[edit] References

^ ^a ^b Entrez Gene: STAM signal transducing adaptor molecule (SH3 domain and ITAM motif) 1.

[edit] Further reading

Takeshita T, Arita T, Asao H, et al. (1996). "Cloning of a novel signal-transducing adaptor molecule containing an SH3 domain and ITAM.". Biochem. Biophys. Res. Commun. 225 (3): 1035-9. doi:10.1006/bbrc.1996.1290. PMID 8780729.
Takeshita T, Arita T, Higuchi M, et al. (1997). "STAM, signal transducing adaptor molecule, is associated with Janus kinases and involved in signaling for cell growth and c-myc induction.". Immunity 6 (4): 449-57. PMID 9133424.
Asao H, Sasaki Y, Arita T, et al. (1998). "Hrs is associated with STAM, a signal-transducing adaptor molecule. Its suppressive effect on cytokine-induced cell growth.". J. Biol. Chem. 272 (52): 32785-91. PMID 9407053.
Tanaka N, Kaneko K, Asao H, et al. (1999). "Possible involvement of a novel STAM-associated molecule "AMSH" in intracellular signal transduction mediated by cytokines.". J. Biol. Chem. 274 (27): 19129-35. PMID 10383417.
Endo K, Takeshita T, Kasai H, et al. (2000). "STAM2, a new member of the STAM family, binding to the Janus kinases.". FEBS Lett. 477 (1-2): 55-61. PMID 10899310.
Kato M, Miyazawa K, Kitamura N (2001). "A deubiquitinating enzyme UBPY interacts with the Src homology 3 domain of Hrs-binding protein via a novel binding motif PX(V/I)(D/N)RXXKP.". J. Biol. Chem. 275 (48): 37481-7. doi:10.1074/jbc. M007251200. PMID 10982817.
Pandey A, Fernandez MM, Steen H, et al. (2001). "Identification of a novel immunoreceptor tyrosine-based activation motif-containing molecule, STAM2, by mass spectrometry and its involvement in growth factor and cytokine receptor signaling pathways.". J. Biol. Chem. 275 (49): 38633-9. doi:10.1074/jbc. M007849200. PMID 10993906.
Steen H, Kuster B, Fernandez M, et al. (2002). "Tyrosine phosphorylation mapping of the epidermal growth factor receptor signaling pathway.". J. Biol. Chem. 277 (2): 1031-9. doi:10.1074/jbc. M109992200. PMID 11687594.
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.
Bache KG, Raiborg C, Mehlum A, Stenmark H (2003). "STAM and Hrs are subunits of a multivalent ubiquitin-binding complex on early endosomes.". J. Biol. Chem. 278 (14): 12513-21. doi:10.1074/jbc. M210843200. PMID 12551915.
Blackstone C, Roberts RG, Seeburg DP, Sheng M (2003). "Interaction of the deafness-dystonia protein DDP/TIMM8a with the signal transduction adaptor molecule STAM1.". Biochem. Biophys. Res. Commun. 305 (2): 345-52. PMID 12745081.
Mizuno E, Kawahata K, Kato M, et al. (2004). "STAM proteins bind ubiquitinated proteins on the early endosome via the VHS domain and ubiquitin-interacting motif.". Mol. Biol. Cell 14 (9): 3675-89. doi:10.1091/mbc. E02-12-0823. PMID 12972556.
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.
Mizuno E, Kawahata K, Okamoto A, et al. (2005). "Association with Hrs is required for the early endosomal localization, stability, and function of STAM.". J. Biochem. 135 (3): 385-96. PMID 15113837.
Colland F, Jacq X, Trouplin V, et al. (2004). "Functional proteomics mapping of a human signaling pathway.". Genome Res. 14 (7): 1324-32. doi:10.1101/gr.2334104. PMID 15231748.
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.
Kobayashi H, Tanaka N, Asao H, et al. (2005). "Hrs, a mammalian master molecule in vesicular transport and protein sorting, suppresses the degradation of ESCRT proteins signal transducing adaptor molecule 1 and 2.". J. Biol. Chem. 280 (11): 10468-77. doi:10.1074/jbc. M409969200. PMID 15640163.
Row PE, Clague MJ, Urbé S (2005). "Growth factors induce differential phosphorylation profiles of the Hrs-STAM complex: a common node in signalling networks with signal-specific properties.". Biochem. J. 389 (Pt 3): 629-36. doi:10.1042/BJ20050067. PMID 15828871.
Zhang Y, Wolf-Yadlin A, Ross PL, et al. (2005). "Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules.". Mol. Cell Proteomics 4 (9): 1240-50. doi:10.1074/mcp. M500089-MCP200. PMID 15951569.
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.