RICTOR
entrez
253260
canonical
uniprot
Q6R327
canonical
ensembl
ENSG00000164327
resolver
ensp
ENSP00000296782
resolver
ensp
ENSP00000349959
resolver
ensp
ENSP00000423162
resolver
ensp
ENSP00000518562
resolver
ensp
ENSP00000527184
resolver
enst
ENST00000514735
resolver
enst
ENST00000711063
resolver
genesymbol
RICTOR
resolver
genesymbol_syn
KIAA1999
resolver
hgnc
HGNC:28611
resolver
uniprot
A0AA34QVX7
resolver
uniprot
B2RNX0
resolver
uniprot
B7ZMF7
resolver
uniprot
D6R9S6
resolver
uniprot
Q68DT5
resolver
uniprot
Q86UB7
resolver
uniprot
Q8N3A0
resolver
uniprot
Q8NCM6
resolver
uniprot_entry
A0AA34QVX7_HUMAN
resolver
uniprot_entry
D6R9S6_HUMAN
resolver
uniprot_entry
RICTR_HUMAN
resolver
uniprot_sec
B2RNX0
resolver
uniprot_sec
B7ZMF7
resolver
uniprot_sec
Q68DT5
resolver
uniprot_sec
Q86UB7
resolver
uniprot_sec
Q8N3A0
resolver
uniprot_sec
Q8NCM6
resolver
amino_acid_sequence
MAAIGRGRSLKNLRVRGRNDSGEENVPLDLTREPSDNLREILQNVARLQGVSNMRKLGHLNNFTKLLCDIGHSEEKLGFHYEDIIICLRLALLNEAKEVRAAGLRALRYLIQDSSILQKVLKLKVDYLIARCIDIQQSNEVERTQALRLVRKMITVNASLFPSSVTNSLIAVGNDGLQERDRMVRACIAIICELALQNPEVVALRGGLNTILKNVIDCQLSRINEALITTILHLLNHPKTRQYVRADVELERILAPYTDFHYRHSPDTAEGQLKEDREARFLASKMGIIATFRSWAGIINLCKPGNSGIQSLIGVLCIPNMEIRRGLLEVLYDIFRLPLPVVTEEFIEALLSVDPGRFQDSWRLSDGFVAAEAKTILPHRARSRPDLMDNYLALILSAFIRNGLLEGLVEVITNSDDHISVRATILLGELLHMANTILPHSHSHHLHCLPTLMNMAASFDIPKEKRLRASAALNCLKRFHEMKKRGPKPYSLHLDHIIQKAIATHQKRDQYLRVQKDIFILKDTEEALLINLRDSQVLQHKENLEWNWNLIGTILKWPNVNLRNYKDEQLHRFVRRLLYFYKPSSKLYANLDLDFAKAKQLTVVGCQFTEFLLESEEDGQGYLEDLVKDIVQWLNASSGMKPERSLQNNGLLTTLSQHYFLFIGTLSCHPHGVKMLEKCSVFQCLLNLCSLKNQDHLLKLTVSSLDYSRDGLARVILSKILTAATDACRLYATKHLRVLLRANVEFFNNWGIELLVTQLHDKNKTISSEALDILDEACEDKANLHALIQMKPALSHLGDKGLLLLLRFLSIPKGFSYLNERGYVAKQLEKWHREYNSKYVDLIEEQLNEALTTYRKPVDGDNYVRRSNQRLQRPHVYLPIHLYGQLVHHKTGCHLLEVQNIITELCRNVRTPDLDKWEEIKKLKASLWALGNIGSSNWGLNLLQEENVIPDILKLAKQCEVLSIRGTCVYVLGLIAKTKQGCDILKCHNWDAVRHSRKHLWPVVPDDVEQLCNELSSIPSTLSLNSESTSSRHNSESESVPSSMFILEDDRFGSSSTSTFFLDINEDTEPTFYDRSGPIKDKNSFPFFASSKLVKNRILNSLTLPNKKHRSSSDPKGGKLSSESKTSNRRIRTLTEPSVDFNHSDDFTPISTVQKTLQLETSFMGNKHIEDTGSTPSIGENDLKFTKNFGTENHRENTSRERLVVESSTSSHMKIRSQSFNTDTTTSGISSMSSSPSRETVGVDATTMDTDCGSMSTVVSTKTIKTSHYLTPQSNHLSLSKSNSVSLVPPGSSHTLPRRAQSLKAPSIATIKSLADCNFSYTSSRDAFGYATLKRLQQQRMHPSLSHSEALASPAKDVLFTDTITMKANSFESRLTPSRFMKALSYASLDKEDLLSPINQNTLQRSSSVRSMVSSATYGGSDDYIGLALPVDINDIFQVKDIPYFQTKNIPPHDDRGARAFAHDAGGLPSGTGGLVKNSFHLLRQQMSLTEIMNSIHSDASLFLESTEDTGLQEHTDDNCLYCVCIEILGFQPSNQLSAICSHSDFQDIPYSDWCEQTIHNPLEVVPSKFSGISGCSDGVSQEGSASSTKSTELLLGVKTIPDDTPMCRILLRKEVLRLVINLSSSVSTKCHETGLLTIKEKYPQTFDDICLYSEVSHLLSHCTFRLPCRRFIQELFQDVQFLQMHEEAEAVLATPPKQPIVDTSAES
uniprot
proteins
function
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). {ECO:0000250|UniProtKB:Q6QI06, ECO:0000269|PubMed:15268862, ECO:0000269|PubMed:15467718, ECO:0000269|PubMed:15718470, ECO:0000269|PubMed:19720745, ECO:0000269|PubMed:19935711, ECO:0000269|PubMed:19995915, ECO:0000269|PubMed:21343617, ECO:0000269|PubMed:33158864, ECO:0000269|PubMed:35904232, ECO:0000269|PubMed:35926713}.
uniprot
proteins
mass_dalton
192218
uniprot
proteins
mutagenesis
MUTAGEN 274; /note="K->G: Abolishes deubiquitination by USP9X and increases interaction with MTOR. No effect on interaction with SIN1."; /evidence="ECO:0000269|PubMed:33378666"; MUTAGEN 1080..1082; /note="KDK->RDR: In M1; does not affect acetylation."; /evidence="ECO:0000269|PubMed:22084251"; MUTAGEN 1092..1095; /note="KLVK->RLVR: In M2; decreased acetylation and activity of the mTORC2 complex."; /evidence="ECO:0000269|PubMed:22084251"; MUTAGEN 1107..1108; /note="KK->RR: In M3; does not affect acetylation."; /evidence="ECO:0000269|PubMed:22084251"; MUTAGEN 1116..1125; /note="KGGKLSSESK->RGGRLSSESR: In M4; decreased acetylation and activity of the mTORC2 complex."; /evidence="ECO:0000269|PubMed:22084251, ECO:0000269|PubMed:26170313"; MUTAGEN 1135; /note="T->A: Impaired phosphorylation by RPS6KB1, leading to increased activity of the mTORC2 complex."; /evidence="ECO:0000269|PubMed:19720745, ECO:0000269|PubMed:19935711"; MUTAGEN 1235; /note="S->A: Impaired phosphorylation by GSK3B in response to stress, leading to increased mTORC2 activity."; /evidence="ECO:0000269|PubMed:21343617"; MUTAGEN 1235; /note="S->D: Mimics phosphorylation; decreased activity of mTORC2."; /evidence="ECO:0000269|PubMed:21343617"; MUTAGEN 1695; /note="T->G: Reduced GSK3-mediated phosphorylation, reduced interaction with FBXW7, reduced FBXW7-mediated ubiquitination and increased stability."; /evidence="ECO:0000269|PubMed:25897075
uniprot
proteins
post_translational_modification
PTM: Phosphorylated by MTOR; when part of mTORC2 (PubMed:15467718). Phosphorylated at Thr-1135 by RPS6KB1 downstream of the mTORC1 complex: phosphorylation of RICTOR inhibits mTORC2 signaling by creating a binding site for 14-3-3 proteins (PubMed:19720745, PubMed:19935711, PubMed:19995915). Phosphorylated at Thr-1695 by GSK3A and GSK3B which facilitates RICTOR ubiquitination and subsequent degradation (PubMed:25897075). Phosphorylated at Ser-1235 by GSK3B in response to endoplasmic stress, inhibiting mTORC2 signaling (PubMed:21343617). {ECO:0000269|PubMed:15467718, ECO:0000269|PubMed:19720745, ECO:0000269|PubMed:19935711, ECO:0000269|PubMed:19995915, ECO:0000269|PubMed:21343617, ECO:0000269|PubMed:25897075}.; PTM: Ubiquitinated by the SCF(FBXW7) complex, leading to its degradation by the proteasome (PubMed:25897075). Deubiquitinated by USP9X; deubiquitination stabilizes RICTOR and enhances its binding to MTOR, thus promoting mTORC2 complex assembly (PubMed:33378666). {ECO:0000269|PubMed:25897075, ECO:0000269|PubMed:33378666}.; PTM: Acetylated by EP300/p300 in response to glucose, leading to activate the mTORC2 complex (PubMed:22084251, PubMed:26170313). Acetylation by BLOC1S1/GCN5L1 in response to hypotoxic stress protects RICTOR against ubiquitination and subsequent degradation by the proteasome (PubMed:38281616). {ECO:0000269|PubMed:22084251, ECO:0000269|PubMed:26170313, ECO:0000269|PubMed:38281616}.
uniprot
proteins
protein_family
RICTOR family
uniprot
proteins
pubmed
12056414
uniprot
proteins
pubmed
15268862
uniprot
proteins
pubmed
15372022
uniprot
proteins
pubmed
15467718
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15718470
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
17461779
uniprot
proteins
pubmed
17599906
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
18220336
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18691976
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
19720745
uniprot
proteins
pubmed
19935711
uniprot
proteins
pubmed
19995915
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21343617
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
21867682
uniprot
proteins
pubmed
21964062
uniprot
proteins
pubmed
22084251
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23727834
uniprot
proteins
pubmed
23762398
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25761241
uniprot
proteins
pubmed
25897075
uniprot
proteins
pubmed
26170313
uniprot
proteins
pubmed
26176550
uniprot
proteins
pubmed
27239959
uniprot
proteins
pubmed
29424687
uniprot
proteins
pubmed
29567957
uniprot
proteins
pubmed
30078703
uniprot
proteins
pubmed
30232230
uniprot
proteins
pubmed
31130364
uniprot
proteins
pubmed
32647003
uniprot
proteins
pubmed
33158864
uniprot
proteins
pubmed
33378666
uniprot
proteins
pubmed
34519268
uniprot
proteins
pubmed
35904232
uniprot
proteins
pubmed
35926713
uniprot
proteins
pubmed
37037900
uniprot
proteins
pubmed
38281616
uniprot
proteins
sequence_length
1708
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21867682}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:21867682}. Lysosome membrane {ECO:0000269|PubMed:31130364}. Note=The mTORC2 complex localizes to membranes: mTORC2 is active at the plasma membrane, endoplasmic reticulum membrane and lysosomes (PubMed:21867682). In lysosomal membrane, mTORC2 is sensitive to lysosomal positioning in the cell (PubMed:31130364). {ECO:0000269|PubMed:21867682, ECO:0000269|PubMed:31130364}.
uniprot
proteins