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Protein STAM2 PDB 1x2q.png
Available structures
PDB Ortholog search: PDBe RCSB
Aliases STAM2, Hbp, STAM2A, STAM2B, signal transducing adaptor molecule 2
External IDs MGI: 1929100 HomoloGene: 68490 GeneCards: STAM2
RNA expression pattern
PBB GE STAM2 215044 s at fs.png

PBB GE STAM2 209649 at fs.png

PBB GE STAM2 208194 s at fs.png
More reference expression data
Species Human Mouse
RefSeq (mRNA)



RefSeq (protein)



Location (UCSC) Chr 2: 152.12 – 152.18 Mb Chr 2: 52.69 – 52.74 Mb
PubMed search [1] [2]
View/Edit Human View/Edit Mouse

Signal transducing adapter molecule 2 is a protein that in humans is encoded by the STAM2 gene.[3][4][5]


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.[5]


STAM2 has been shown to interact with HGS,[6][7] Janus kinase 1[3]{[4] and USP8.[8][9]


  1. ^ "Human PubMed Reference:". 
  2. ^ "Mouse PubMed Reference:". 
  3. ^ 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 (Jul 2000). "STAM2, a new member of the STAM family, binding to the Janus kinases". FEBS Letters. 477 (1-2): 55–61. doi:10.1016/S0014-5793(00)01760-9. PMID 10899310. 
  4. ^ a b Pandey A, Fernandez MM, Steen H, Blagoev B, Nielsen MM, Roche S, Mann M, Lodish HF (Dec 2000). "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". The Journal of Biological Chemistry. 275 (49): 38633–9. doi:10.1074/jbc.M007849200. PMID 10993906. 
  5. ^ a b "Entrez Gene: STAM2 signal transducing adaptor molecule (SH3 domain and ITAM motif) 2". 
  6. ^ Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (Oct 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514. 
  7. ^ Bache KG, Raiborg C, Mehlum A, Stenmark H (Apr 2003). "STAM and Hrs are subunits of a multivalent ubiquitin-binding complex on early endosomes". The Journal of Biological Chemistry. 278 (14): 12513–21. doi:10.1074/jbc.M210843200. PMID 12551915. 
  8. ^ Kaneko T, Kumasaka T, Ganbe T, Sato T, Miyazawa K, Kitamura N, Tanaka N (Nov 2003). "Structural insight into modest binding of a non-PXXP ligand to the signal transducing adaptor molecule-2 Src homology 3 domain". The Journal of Biological Chemistry. 278 (48): 48162–8. doi:10.1074/jbc.M306677200. PMID 13129930. 
  9. ^ 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". The Journal of Biological Chemistry. 275 (48): 37481–7. doi:10.1074/jbc.M007251200. PMID 10982817. 

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