The gene spans 3,233 bases.

6 alternatively spliced mRNA variants have been reported; 1 unspliced form. The best characterized mRNA variant is 1355bp long arising from 5 exons: 32bp 5 UTR, 636bp coding sequence, 687 bp 3 UTR.

Primary protein product is a 211 amino acid hydrophilic, basic protein (pI 9.6) with a calculated molecular weight of 24.4 kD (Siderovski et al., 1994).
Possibly three additional functional proteins arising from alternative translation initiation of AUG codons corresponding to amino acid residues 5, 16, and 33 of full-length protein (Gu et al., 2008).
RGS2 can be phosphorylated by PKC and PKGIalpha (Cunningham et al., 2001; Tang et al., 2003).

RGS2 is ubiquitously expressed and its mRNA is found at medium to high levels in brain, heart, lung, kidney, intestine, lymphocytes, placenta, and testis (Larminie et al., 2004).
RGS2 expression (mRNA and protein) can be upregulated in response to Gs- and Gq-mediated signals (Song et al., 1999; Miles et al., 2000; Roy et al., 2006b; Zou et al., 2006), as well as a variety of stressful stimuli including heat shock (Zmijewski et al., 2001), oxidative stress (Zmijewski et al., 2001), DNA damage (Song and Jope, 2006), and infection (McCaffrey et al., 2004).

RGS2 is localized to the nucleus and the plasma membrane (Roy et al., 2003; Gu et al., 2007).

Canonical functions: RGS proteins bind to heterotrimeric G proteins by way of their RGS domain and act as GAPs (GTPase accelerating protein) to turn off G protein coupled receptor (GPCR) signals (Ross and Wilkie, 2000). RGS2 is unique in its selective GAP activity toward Galphaq and its low affinity for Galphai/o subunits (Heximer et al., 1997; Heximer et al., 1999; Cladman and Chidiac, 2002). RGS2 has also been shown to regulate Galphas-mediated signals in a GAP-independent manner, which likely reflects its ability to interact with other components of the G protein signaling machinery to interfere with G protein-effector interactions. These include adenylyl cyclase (Salim et al., 2003; Roy et al., 2006a), select GPCRs (Bernstein et al., 2004; Hague et al., 2005; Roy et al., 2006a), and the GPCR-scaffolding protein, spinophilin (Wang et al., 2005). RGS2 has been implicated in the control of vascular and neurological functions (Ingi et al., 1998; Kammermeier and Ikeda, 1999; Oliveira-Dos-Santos et al., 2000; Heximer et al., 2003; Tang et al., 2003).
Noncanonical functions: RGS2 has been shown to bind and regulate the activity of proteins outside the realm of GPCR signaling networks including tubulin (Heo et al., 2006), the TRPV6 calcium channel (Schoeber et al., 2006), and the eukaryotic initation factor, eIF2B (Nguyen et al., 2009).

All RGS proteins share a homologous (45-80%) 120 amino acid RGS domain that confers their binding to heterotrimeric G protein alpha subunits. RGS2 shares highest homology to other members of the B/R4 subfamily (Ross and Wilkie, 2000; Sierra et al., 2002).