STAM2

Signal transducing adaptor molecule (SH3 domain and ITAM motif) 2

PDB rendering based on 1x2q.
Identifiers
Symbols STAM2; DKFZp564C047; Hbp; STAM2A; STAM2B
External IDs OMIM606244 MGI1929100 HomoloGene68490 GeneCards: STAM2 Gene
RNA expression pattern
More reference expression data
Orthologs
Species Human Mouse
Entrez 10254 56324
Ensembl ENSG00000115145 ENSMUSG00000055371
UniProt O75886 Q3TGH8
RefSeq (mRNA) NM_005843 NM_019667.2
RefSeq (protein) NP_005834 NP_062641.1
Location (UCSC) Chr 2:
152.97 – 153.03 Mb
Chr 2:
52.55 – 52.6 Mb
PubMed search [1] [2]

Signal transducing adapter molecule 2 is a protein that in humans is encoded by the STAM2 gene.[1][2][3]

The protein encoded by this gene is closely related to STAM, an adaptor protein involved in the downstream signaling of cytokine receptors, both of which contain a SH3 domain and the immunoreceptor tyrosine-based activation motif (ITAM). Similar to STAM, this protein acts downstream of JAK kinases, and is phosphorylated in response to cytokine stimulation. This protein and STAM thus are thought to exhibit compensatory effects on the signaling pathway downstream of JAK kinases upon cytokine stimulation.[3]

Interactions

STAM2 has been shown to interact with HGS,[4][5] Janus kinase 1[2][1] and USP8.[6][7]

References

  1. ^ a b Endo K, Takeshita T, Kasai H, Sasaki Y, Tanaka N, Asao H, Kikuchi K, Yamada M, Chenb M, O'Shea JJ, Sugamura K (Aug 2000). "STAM2, a new member of the STAM family, binding to the Janus kinases". FEBS Lett 477 (1–2): 55–61. doi:10.1016/S0014-5793(00)01760-9. PMID 10899310. 
  2. ^ a b Pandey A, Fernandez MM, Steen H, Blagoev B, Nielsen MM, Roche S, Mann M, Lodish HF (Jan 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. 
  3. ^ a b "Entrez Gene: STAM2 signal transducing adaptor molecule (SH3 domain and ITAM motif) 2". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10254. 
  4. ^ Rual, Jean-François; Venkatesan Kavitha, Hao Tong, Hirozane-Kishikawa Tomoko, Dricot Amélie, Li Ning, Berriz Gabriel F, Gibbons Francis D, Dreze Matija, Ayivi-Guedehoussou Nono, Klitgord Niels, Simon Christophe, Boxem Mike, Milstein Stuart, Rosenberg Jennifer, Goldberg Debra S, Zhang Lan V, Wong Sharyl L, Franklin Giovanni, Li Siming, Albala Joanna S, Lim Janghoo, Fraughton Carlene, Llamosas Estelle, Cevik Sebiha, Bex Camille, Lamesch Philippe, Sikorski Robert S, Vandenhaute Jean, Zoghbi Huda Y, Smolyar Alex, Bosak Stephanie, Sequerra Reynaldo, Doucette-Stamm Lynn, Cusick Michael E, Hill David E, Roth Frederick P, Vidal Marc (Oct. 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature (England) 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514. 
  5. ^ Bache, Kristi G; Raiborg Camilla, Mehlum Anja, Stenmark Harald (Apr. 2003). "STAM and Hrs are subunits of a multivalent ubiquitin-binding complex on early endosomes". J. Biol. Chem. (United States) 278 (14): 12513–21. doi:10.1074/jbc.M210843200. ISSN 0021-9258. PMID 12551915. 
  6. ^ Kaneko, Tomonori; Kumasaka Takashi, Ganbe Tadashi, Sato Takao, Miyazawa Keiji, Kitamura Naomi, Tanaka Nobuo (Nov. 2003). "Structural insight into modest binding of a non-PXXP ligand to the signal transducing adaptor molecule-2 Src homology 3 domain". J. Biol. Chem. (United States) 278 (48): 48162–8. doi:10.1074/jbc.M306677200. ISSN 0021-9258. PMID 13129930. 
  7. ^ Kato, M; Miyazawa K, Kitamura N (Dec. 2000). "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. (UNITED STATES) 275 (48): 37481–7. doi:10.1074/jbc.M007251200. ISSN 0021-9258. PMID 10982817. 

Further reading