Q6R327 · RICTR_HUMAN
- ProteinRapamycin-insensitive companion of mTOR
- GeneRICTOR
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1708 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Subunit of mTORC2, which regulates cell growth and survival in response to hormonal signals. mTORC2 is activated by growth factors, but, in contrast to mTORC1, seems to be nutrient-insensitive. mTORC2 seems to function upstream of Rho GTPases to regulate the actin cytoskeleton, probably by activating one or more Rho-type guanine nucleotide exchange factors. mTORC2 promotes the serum-induced formation of stress-fibers or F-actin. mTORC2 plays a critical role in AKT1 'Ser-473' phosphorylation, which may facilitate the phosphorylation of the activation loop of AKT1 on 'Thr-308' by PDK1 which is a prerequisite for full activation. mTORC2 regulates the phosphorylation of SGK1 at 'Ser-422'. mTORC2 also modulates the phosphorylation of PRKCA on 'Ser-657'. Plays an essential role in embryonic growth and development.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameRapamycin-insensitive companion of mTOR
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ6R327
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Disease & Variants
Features
Showing features for mutagenesis, natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 274 | Abolishes deubiquitination by USP9X and increases interaction with MTOR. No effect on interaction with SIN1. | ||||
Sequence: K → G | ||||||
Natural variant | VAR_051320 | 837 | in dbSNP:rs2043112 | |||
Sequence: S → F | ||||||
Mutagenesis | 1695 | Reduced GSK3-mediated phosphorylation, reduced interaction with FBXW7, reduced FBXW7-mediated ubiquitination and increased stability. | ||||
Sequence: T → G |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 2,794 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue, modified residue (large scale data), cross-link.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000308179 | 1-1708 | UniProt | Rapamycin-insensitive companion of mTOR | |||
Sequence: MAAIGRGRSLKNLRVRGRNDSGEENVPLDLTREPSDNLREILQNVARLQGVSNMRKLGHLNNFTKLLCDIGHSEEKLGFHYEDIIICLRLALLNEAKEVRAAGLRALRYLIQDSSILQKVLKLKVDYLIARCIDIQQSNEVERTQALRLVRKMITVNASLFPSSVTNSLIAVGNDGLQERDRMVRACIAIICELALQNPEVVALRGGLNTILKNVIDCQLSRINEALITTILHLLNHPKTRQYVRADVELERILAPYTDFHYRHSPDTAEGQLKEDREARFLASKMGIIATFRSWAGIINLCKPGNSGIQSLIGVLCIPNMEIRRGLLEVLYDIFRLPLPVVTEEFIEALLSVDPGRFQDSWRLSDGFVAAEAKTILPHRARSRPDLMDNYLALILSAFIRNGLLEGLVEVITNSDDHISVRATILLGELLHMANTILPHSHSHHLHCLPTLMNMAASFDIPKEKRLRASAALNCLKRFHEMKKRGPKPYSLHLDHIIQKAIATHQKRDQYLRVQKDIFILKDTEEALLINLRDSQVLQHKENLEWNWNLIGTILKWPNVNLRNYKDEQLHRFVRRLLYFYKPSSKLYANLDLDFAKAKQLTVVGCQFTEFLLESEEDGQGYLEDLVKDIVQWLNASSGMKPERSLQNNGLLTTLSQHYFLFIGTLSCHPHGVKMLEKCSVFQCLLNLCSLKNQDHLLKLTVSSLDYSRDGLARVILSKILTAATDACRLYATKHLRVLLRANVEFFNNWGIELLVTQLHDKNKTISSEALDILDEACEDKANLHALIQMKPALSHLGDKGLLLLLRFLSIPKGFSYLNERGYVAKQLEKWHREYNSKYVDLIEEQLNEALTTYRKPVDGDNYVRRSNQRLQRPHVYLPIHLYGQLVHHKTGCHLLEVQNIITELCRNVRTPDLDKWEEIKKLKASLWALGNIGSSNWGLNLLQEENVIPDILKLAKQCEVLSIRGTCVYVLGLIAKTKQGCDILKCHNWDAVRHSRKHLWPVVPDDVEQLCNELSSIPSTLSLNSESTSSRHNSESESVPSSMFILEDDRFGSSSTSTFFLDINEDTEPTFYDRSGPIKDKNSFPFFASSKLVKNRILNSLTLPNKKHRSSSDPKGGKLSSESKTSNRRIRTLTEPSVDFNHSDDFTPISTVQKTLQLETSFMGNKHIEDTGSTPSIGENDLKFTKNFGTENHRENTSRERLVVESSTSSHMKIRSQSFNTDTTTSGISSMSSSPSRETVGVDATTMDTDCGSMSTVVSTKTIKTSHYLTPQSNHLSLSKSNSVSLVPPGSSHTLPRRAQSLKAPSIATIKSLADCNFSYTSSRDAFGYATLKRLQQQRMHPSLSHSEALASPAKDVLFTDTITMKANSFESRLTPSRFMKALSYASLDKEDLLSPINQNTLQRSSSVRSMVSSATYGGSDDYIGLALPVDINDIFQVKDIPYFQTKNIPPHDDRGARAFAHDAGGLPSGTGGLVKNSFHLLRQQMSLTEIMNSIHSDASLFLESTEDTGLQEHTDDNCLYCVCIEILGFQPSNQLSAICSHSDFQDIPYSDWCEQTIHNPLEVVPSKFSGISGCSDGVSQEGSASSTKSTELLLGVKTIPDDTPMCRILLRKEVLRLVINLSSSVSTKCHETGLLTIKEKYPQTFDDICLYSEVSHLLSHCTFRLPCRRFIQELFQDVQFLQMHEEAEAVLATPPKQPIVDTSAES | |||||||
Modified residue | 21 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 21 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 265 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 274 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 863 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 1035 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1101 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1103 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1103 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 1135 | UniProt | Phosphothreonine; by RPS6KB1 | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1135 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1138 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1144 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1148 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 1162 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1162 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1172 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1174 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1175 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1177 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1199 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1211 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1219 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1224 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1231 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1233 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1235 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1235 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1269 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 1271 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 1278 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1278 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1280 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1282 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1282 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1284 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1284 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1286 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1292 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1295 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1295 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 1302 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1302 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1313 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1313 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1320 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1330 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 1332 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1332 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 1346 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1346 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1353 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1353 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1370 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1373 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1376 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 1385 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1385 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1386 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 1388 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1388 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1396 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1396 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1402 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 1411 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1411 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1470 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1574 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1577 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1581 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1585 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1587 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1588 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1591 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1591 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1592 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 1695 | UniProt | Phosphothreonine; by GSK3-alpha and GSK3-beta | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1708 | PRIDE | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Phosphorylated by MTOR; when part of mTORC2 (PubMed:15467718).
Phosphorylated at Thr-1135 by RPS6KB1; phosphorylation of RICTOR inhibits mTORC2 and AKT1 signaling (PubMed:19995915).
Phosphorylated at Thr-1695 by GSK3A and GSK3B which facilitates RICTOR ubiquitination and subsequent degradation (PubMed:25897075).
Phosphorylated at Thr-1135 by RPS6KB1; phosphorylation of RICTOR inhibits mTORC2 and AKT1 signaling (PubMed:19995915).
Phosphorylated at Thr-1695 by GSK3A and GSK3B which facilitates RICTOR ubiquitination and subsequent degradation (PubMed:25897075).
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).
Deubiquitinated by USP9X; deubiquitination stabilizes RICTOR and enhances its binding to MTOR, thus promoting mTORC2 complex assembly (PubMed:33378666).
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Part of the mechanistic target of rapamycin complex 2 (mTORC2) which contains MTOR, MLST8, PRR5, RICTOR, MAPKAP1 and DEPTOR (PubMed:15268862, PubMed:15467718, PubMed:17461779, PubMed:17599906, PubMed:34519268).
Contrary to mTORC1, mTORC2 does not bind to and is not sensitive to FKBP12-rapamycin. Binds directly to MTOR and PRR5 within the TORC2 complex; interaction with MTOR is enhanced by deubiquitination of RICTOR by USP9X (PubMed:15268862, PubMed:17461779, PubMed:17599906, PubMed:33378666).
Interaction with MAPKAP1 is not enhanced by RICTOR deubiquitination by USP9X (PubMed:33378666).
Interacts with CCDC28B (PubMed:23727834).
Interacts with NBN (PubMed:23762398).
Interacts with PRR5L (PubMed:17461779, PubMed:21964062).
Interacts with SIK3 (PubMed:30232230).
Interacts with NCKAP1L (PubMed:32647003).
Interacts with kinases GSK3A and GSK3B; the interactions lead to phosphorylation of RICTOR at 'Thr-1695' which facilitates its FBXW7-mediated ubiquitination and subsequent degradation (PubMed:25897075).
Interacts with FBXW7; the interaction is enhanced by GSK3-mediated phosphorylation of 'Thr-1695' and results in RICTOR ubiquitination and degradation (PubMed:25897075).
Interacts with USP9X; the interaction results in deubiquitination of RICTOR and protection from proteasomal degradation, thus promoting mTORC2 complex assembly (PubMed:33378666).
Interacts with ARMH4 (via cytoplasmic tail); this interaction bridges ARMH4 to the mTORC2 complex and inhibits the mTORC2 kinase activity (By similarity).
Interacts with UBXN2A (PubMed:37037900).
Interacts with TSPAN8 (PubMed:25761241, PubMed:35904232).
Contrary to mTORC1, mTORC2 does not bind to and is not sensitive to FKBP12-rapamycin. Binds directly to MTOR and PRR5 within the TORC2 complex; interaction with MTOR is enhanced by deubiquitination of RICTOR by USP9X (PubMed:15268862, PubMed:17461779, PubMed:17599906, PubMed:33378666).
Interaction with MAPKAP1 is not enhanced by RICTOR deubiquitination by USP9X (PubMed:33378666).
Interacts with CCDC28B (PubMed:23727834).
Interacts with NBN (PubMed:23762398).
Interacts with PRR5L (PubMed:17461779, PubMed:21964062).
Interacts with SIK3 (PubMed:30232230).
Interacts with NCKAP1L (PubMed:32647003).
Interacts with kinases GSK3A and GSK3B; the interactions lead to phosphorylation of RICTOR at 'Thr-1695' which facilitates its FBXW7-mediated ubiquitination and subsequent degradation (PubMed:25897075).
Interacts with FBXW7; the interaction is enhanced by GSK3-mediated phosphorylation of 'Thr-1695' and results in RICTOR ubiquitination and degradation (PubMed:25897075).
Interacts with USP9X; the interaction results in deubiquitination of RICTOR and protection from proteasomal degradation, thus promoting mTORC2 complex assembly (PubMed:33378666).
Interacts with ARMH4 (via cytoplasmic tail); this interaction bridges ARMH4 to the mTORC2 complex and inhibits the mTORC2 kinase activity (By similarity).
Interacts with UBXN2A (PubMed:37037900).
Interacts with TSPAN8 (PubMed:25761241, PubMed:35904232).
(Microbial infection) Interacts with vaccinia virus protein F17; this interaction dysregulates MTOR.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q6R327 | ILK Q13418 | 8 | EBI-1387196, EBI-747644 | |
BINARY | Q6R327 | MTOR P42345 | 37 | EBI-1387196, EBI-359260 | |
BINARY | Q6R327 | PREX1 Q8TCU6 | 3 | EBI-1387196, EBI-1046542 | |
BINARY | Q6R327 | SFN P31947 | 4 | EBI-1387196, EBI-476295 | |
BINARY | Q6R327 | YWHAE P62258 | 5 | EBI-1387196, EBI-356498 | |
BINARY | Q6R327 | YWHAZ P63104 | 5 | EBI-1387196, EBI-347088 |
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-789 | Interaction with NBN | ||||
Sequence: MAAIGRGRSLKNLRVRGRNDSGEENVPLDLTREPSDNLREILQNVARLQGVSNMRKLGHLNNFTKLLCDIGHSEEKLGFHYEDIIICLRLALLNEAKEVRAAGLRALRYLIQDSSILQKVLKLKVDYLIARCIDIQQSNEVERTQALRLVRKMITVNASLFPSSVTNSLIAVGNDGLQERDRMVRACIAIICELALQNPEVVALRGGLNTILKNVIDCQLSRINEALITTILHLLNHPKTRQYVRADVELERILAPYTDFHYRHSPDTAEGQLKEDREARFLASKMGIIATFRSWAGIINLCKPGNSGIQSLIGVLCIPNMEIRRGLLEVLYDIFRLPLPVVTEEFIEALLSVDPGRFQDSWRLSDGFVAAEAKTILPHRARSRPDLMDNYLALILSAFIRNGLLEGLVEVITNSDDHISVRATILLGELLHMANTILPHSHSHHLHCLPTLMNMAASFDIPKEKRLRASAALNCLKRFHEMKKRGPKPYSLHLDHIIQKAIATHQKRDQYLRVQKDIFILKDTEEALLINLRDSQVLQHKENLEWNWNLIGTILKWPNVNLRNYKDEQLHRFVRRLLYFYKPSSKLYANLDLDFAKAKQLTVVGCQFTEFLLESEEDGQGYLEDLVKDIVQWLNASSGMKPERSLQNNGLLTTLSQHYFLFIGTLSCHPHGVKMLEKCSVFQCLLNLCSLKNQDHLLKLTVSSLDYSRDGLARVILSKILTAATDACRLYATKHLRVLLRANVEFFNNWGIELLVTQLHDKNKTISSEALDILDEACEDKANLHALIQ | ||||||
Region | 1022-1041 | Disordered | ||||
Sequence: LSLNSESTSSRHNSESESVP | ||||||
Region | 1103-1134 | Disordered | ||||
Sequence: TLPNKKHRSSSDPKGGKLSSESKTSNRRIRTL | ||||||
Region | 1204-1252 | Disordered | ||||
Sequence: VVESSTSSHMKIRSQSFNTDTTTSGISSMSSSPSRETVGVDATTMDTDC | ||||||
Region | 1275-1298 | Disordered | ||||
Sequence: NHLSLSKSNSVSLVPPGSSHTLPR |
Sequence similarities
Belongs to the RICTOR family.
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
Q6R327-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length1,708
- Mass (Da)192,218
- Last updated2004-07-05 v1
- ChecksumDB7B1E4A45DAE2AB
Q6R327-4
- Name2
- NoteMay be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
Q6R327-3
- Name3
- Differences from canonical
- 1379-1379: R → RIDFKKKHVGGIRSLRPTITNNLFR
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
D6R9S6 | D6R9S6_HUMAN | RICTOR | 1692 | ||
A0AA34QVL6 | A0AA34QVL6_HUMAN | RICTOR | 246 | ||
A0AA34QVX7 | A0AA34QVX7_HUMAN | RICTOR | 1694 |
Sequence caution
Features
Showing features for alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_038362 | 252-257 | in isoform 2 | |||
Sequence: RILAPY → NFSTLY | ||||||
Alternative sequence | VSP_038363 | 258-1708 | in isoform 2 | |||
Sequence: Missing | ||||||
Sequence conflict | 545 | in Ref. 2; CAH18135 | ||||
Sequence: E → G | ||||||
Sequence conflict | 815 | in Ref. 2; CAH18135 | ||||
Sequence: F → L | ||||||
Sequence conflict | 1283 | in Ref. 2; CAH18135 | ||||
Sequence: N → S | ||||||
Alternative sequence | VSP_052581 | 1379 | in isoform 3 | |||
Sequence: R → RIDFKKKHVGGIRSLRPTITNNLFR | ||||||
Sequence conflict | 1699 | in Ref. 5; AAH51729 | ||||
Sequence: Q → R |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AY515854 EMBL· GenBank· DDBJ | AAS79796.1 EMBL· GenBank· DDBJ | mRNA | ||
AL834497 EMBL· GenBank· DDBJ | CAD39155.1 EMBL· GenBank· DDBJ | mRNA | ||
CR749280 EMBL· GenBank· DDBJ | CAH18135.1 EMBL· GenBank· DDBJ | mRNA | Sequence problems. | |
AC008964 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC109467 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471119 EMBL· GenBank· DDBJ | EAW55980.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC051729 EMBL· GenBank· DDBJ | AAH51729.1 EMBL· GenBank· DDBJ | mRNA | ||
BC137163 EMBL· GenBank· DDBJ | AAI37164.1 EMBL· GenBank· DDBJ | mRNA | ||
BC137164 EMBL· GenBank· DDBJ | AAI37165.1 EMBL· GenBank· DDBJ | mRNA | ||
BC144509 EMBL· GenBank· DDBJ | AAI44510.1 EMBL· GenBank· DDBJ | mRNA | ||
AB082530 EMBL· GenBank· DDBJ | BAC02708.1 EMBL· GenBank· DDBJ | mRNA |