Ruder C., Reimer T., Delgado-Martinez I., Hermosilla R., Engelsberg A., Nehring R., Dorken B., Rehm A.

Mol. Biol. Cell 16:1245-1257(2005) GeneRIF 23557 · Mapped (8)
EBAG9 and Snapin have roles in controlling exocytosis processes GeneRIF 23557

Talbot K., Cho D.S., Ong W.Y., Benson M.A., Han L.Y., Kazi H.A., Kamins J., Hahn C.G., Blake D.J., Arnold S.E.

Hum. Mol. Genet. 15:3041-3054(2006) GeneRIF 23557 · UniProtKB (2) · Mapped (5)
results demonstrate that snapin is a binding partner of dysbindin-1 in vitro and in the brain; both dysbindin-1 and snapin are concentrated in tissue enriched in synaptic vesicle membranes and less commonly in postsynaptic densities GeneRIF 23557

Suzuki F., Morishima S., Tanaka T., Muramatsu I.

J. Biol. Chem. 282:29563-29573(2007) GeneRIF 23557 · Mapped (5)
Snapin links the alpha(1A)-AR to TRPC6 augmenting Ca(2+) influx via ROC channels GeneRIF 23557

Mistry A.C., Mallick R., Klein J.D., Weimbs T., Sands J.M., Frohlich O.

Am. J. Physiol. Renal Physiol. 297:F292-300(2009) GeneRIF 23557 · Mapped (1)
Snapin plays an important role as a linker between the water channel and the t-SNARE complex leading to the fusion event and the pairing with specific t-SNAREs is essential for the specificity of membrane recognition and fusion. GeneRIF 23557

Davila S., Froeling F.E., Tan A., Bonnard C., Boland G.J., Snippe H., Hibberd M.L., Seielstad M.

Genes Immun. 11:232-238(2010) GeneRIF 23557 · Mapped (4,258)
Observational study of gene-disease association. (HuGE Navigator) GeneRIF 23557

Song W.J., Seshadri M., Ashraf U., Mdluli T., Mondal P., Keil M., Azevedo M., Kirschner L.S., Stratakis C.A., Hussain M.A.

Cell Metab. 13:308-319(2011) GeneRIF 23557 · Mapped (10)
PKA-dependent phosphorylation of snapin increases interaction among insulin secretory vesicle-associated proteins thereby potentiating glucose-stimulated insulin secretion. GeneRIF 23557

Shi B., Huang Q., Tak P.P., Vervoordeldonk M.J., Huang C.C., Dorfleutner A., Stehlik C., Pope R.M.

Ann. Rheum. Dis. 71:1411-1417(2012) GeneRIF 23557 · Mapped (3)
These observations identify Snapin as a novel endogenous TLR2 ligand in rheumatoid arthritis and thus support a role for persistent TLR2 signalling in pathogenesis. GeneRIF 23557

Ungewickell E., Ungewickell H., Holstein S.E., Lindner R., Prasad K., Barouch W., Martin B., Greene L.E., Eisenberg E.

Nature 378:632-635(1995) Reactome REACT_11123 · Mapped (45)

Acton S.L., Wong D.H., Parham P., Brodsky F.M., Jackson A.P.

Mol. Biol. Cell 4:647-660(1993) Reactome REACT_11123 · Mapped (45)

Lee D.W., Zhao X., Zhang F., Eisenberg E., Greene L.E.

J. Cell. Sci. 118:4311-4321(2005) Reactome REACT_11123 · Mapped (45)

Bryant N.J., Govers R., James D.E.

Nat. Rev. Mol. Cell Biol. 3:267-277(2002) Reactome REACT_11123 · Mapped (55)

Borner G.H., Harbour M., Hester S., Lilley K.S., Robinson M.S.

J. Cell Biol. 175:571-578(2006) Reactome REACT_11123 · Mapped (56)

Hirst J., Lindsay M.R., Robinson M.S.

Mol. Biol. Cell 12:3573-3588(2001) Reactome REACT_11123 · Mapped (43)

Maier O., Knoblich M., Westermann P.

Biochem. Biophys. Res. Commun. 223:229-233(1996) Reactome REACT_11123 · Mapped (45)

Farsad K., Ringstad N., Takei K., Floyd S.R., Rose K., De Camilli P.

J. Cell Biol. 155:193-200(2001) Reactome REACT_11123 · UniProtKB (3) · Mapped (47)

Musacchio A., Smith C.J., Roseman A.M., Harrison S.C., Kirchhausen T., Pearse B.M.

Mol. Cell 3:761-770(1999) Reactome REACT_11123 · Mapped (46)

Colland F., Jacq X., Trouplin V., Mougin C., Groizeleau C., Hamburger A., Meil A., Wojcik J., Legrain P., Gauthier J.M.

Genome Res. 14:1324-1332(2004) MINT MINT-5002303 · Mapped (539)
MINT-61600. SMAD2 (uniprotkb:Q15796) physically interacts (MI:0915) with SNAPIN (uniprotkb:O95295) by two hybrid (MI:0018). From mint MINT MINT-5002303

Stelzl U., Worm U., Lalowski M., Haenig C., Brembeck F.H., Goehler H., Stroedicke M., Zenkner M., Schoenherr A., Koeppen S. et al.

Cell 122:957-968(2005) MINT MINT-5002303 MINT MINT-5002303 MINT MINT-5002303 MINT MINT-5002303 MINT MINT-5002303 MINT MINT-5002303 MINT MINT-5002303 MINT MINT-5002303 MINT MINT-5002303 MINT MINT-5002303 MINT MINT-5002303 · UniProtKB (1) · Mapped (1,466)
MINT-63275. SNAPIN (uniprotkb:O95295) physically interacts (MI:0915) with MYST2 (uniprotkb:O95251) by two hybrid (MI:0018). From mint MINT MINT-5002303 MINT-63276. SNAPIN (uniprotkb:O95295) physically interacts (MI:0915) with LAMC1 (uniprotkb:P11047) by two hybrid (MI:0018). From mint MINT MINT-5002303 MINT-63277. SNAPIN (uniprotkb:O95295) physically interacts (MI:0915) with EEF1G (uniprotkb:P26641) by two hybrid (MI:0018). From mint MINT MINT-5002303 MINT-63278. SNAPIN (uniprotkb:O95295) physically interacts (MI:0915) with HAP1 (uniprotkb:P54257) by two hybrid (MI:0018). From mint MINT MINT-5002303 MINT-63279. SNAPIN (uniprotkb:O95295) physically interacts (MI:0915) with IMMT (uniprotkb:Q16891) by two hybrid (MI:0018). From mint MINT MINT-5002303 MINT-63280. SNAPIN (uniprotkb:O95295) physically interacts (MI:0915) with q59gb8_human (uniprotkb:Q59GB8) by two hybrid (MI:0018). From mint MINT MINT-5002303 MINT-63281. SNAPIN (uniprotkb:O95295) physically interacts (MI:0915) with IKBKAP (uniprotkb:Q5JTR5) by two hybrid (MI:0018). From mint MINT MINT-5002303 MINT-63282. SNAPIN (uniprotkb:O95295) physically interacts (MI:0915) with GPRASP1 (uniprotkb:Q5JY77) by two hybrid (MI:0018). From mint MINT MINT-5002303 MINT-63283. SNAPIN (uniprotkb:O95295) physically interacts (MI:0915) with KAT5 (uniprotkb:Q92993) by two hybrid (MI:0018). From mint MINT MINT-5002303 MINT-63284. SNAPIN (uniprotkb:O95295) physically interacts (MI:0915) with SPAG5 (uniprotkb:Q96R06) by two hybrid (MI:0018). From mint MINT MINT-5002303 MINT-64069. DDR1 (uniprotkb:Q08345) physically interacts (MI:0915) with SNAPIN (uniprotkb:O95295) by two hybrid (MI:0018). From mint MINT MINT-5002303