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Sep. 10, 2014:
A total of 174 experimentally verified S-nitrosylation sites on 94 S-nitrosylated proteins from individualized human colorectal cancer tissues using a label-free quantitation strategy.

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Protein Name: Rapamycin-insensitive companion of mTOR

UniprotKB/SwissProt ID: Q6R327 (Q6R327)

Gene Name: RICTOR

Organism: Homo sapiens (Human)

Function: Component of the mechanistic target of rapamycin complex 2 (mTORC2), which transduces signals from growth factors to pathways involved in proliferation, cytoskeletal organization, lipogenesis and anabolic output (PubMed:15268862, PubMed:15718470, PubMed:19720745, PubMed:19995915, PubMed:21343617, PubMed:33158864, PubMed:35904232, PubMed:35926713). In response to growth factors, mTORC2 phosphorylates and activates AGC protein kinase family members, including AKT (AKT1, AKT2 and AKT3), PKC (PRKCA, PRKCB and PRKCE) and SGK1 (PubMed:19720745, PubMed:19935711, PubMed:19995915). In contrast to mTORC1, mTORC2 is nutrient-insensitive (PubMed:15467718, PubMed:21343617). Within the mTORC2 complex, RICTOR probably acts as a molecular adapter (PubMed:21343617, PubMed:33158864, PubMed:35926713). RICTOR is responsible for the FKBP12-rapamycin-insensitivity of mTORC2 (PubMed:33158864). mTORC2 plays a critical role in AKT1 activation by mediating phosphorylation of different sites depending on the context, such as 'Thr-450', 'Ser-473', 'Ser-477' or 'Thr-479', facilitating the phosphorylation of the activation loop of AKT1 on 'Thr-308' by PDPK1/PDK1 which is a prerequisite for full activation (PubMed:15718470, PubMed:19720745, PubMed:19935711, PubMed:35926713). mTORC2 catalyzes the phosphorylation of SGK1 at 'Ser-422' and of PRKCA on 'Ser-657' (By similarity). The mTORC2 complex also phosphorylates various proteins involved in insulin signaling, such as FBXW8 and IGF2BP1 (By similarity). mTORC2 acts upstream of Rho GTPases to regulate the actin cytoskeleton, probably by activating one or more Rho-type guanine nucleotide exchange factors (PubMed:15467718). mTORC2 promotes the serum-induced formation of stress-fibers or F-actin (PubMed:15467718)

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Cell membrane. Endoplasmic reticulum membrane. Lysosome membrane

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR016024 ARM-type_fold
IPR028268 Pianissimo_fam
IPR028267 Pianissimo_N
IPR029453 Rictor_IV
IPR029451 RICTOR_M
IPR029259 RICTOR_phospho
IPR029452 RICTOR_V

The S-nitrosylation sites of Q6R327

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 1252 GVDATTMDTD C GSMSTVVSTK   
2 1576 VPSKFSGISG C SDGVSQEGSA   
3 1608 VKTIPDDTPM C RILLRKEVLR   
4 778 SEALDILDEA C EDKANLHALI   
5 906 LEVQNIITEL C RNVRTPDLDK