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Protein

Rapamycin-insensitive companion of mTOR

Gene

Rictor

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.4 Publications

GO - Molecular functioni

  • protein kinase binding Source: MGI
  • ribosome binding Source: UniProtKB

GO - Biological processi

  • actin cytoskeleton reorganization Source: UniProtKB
  • embryo development Source: UniProtKB
  • peptidyl-serine phosphorylation Source: MGI
  • positive regulation of actin filament polymerization Source: MGI
  • positive regulation of endothelial cell proliferation Source: Ensembl
  • positive regulation of peptidyl-tyrosine phosphorylation Source: MGI
  • positive regulation of protein kinase B signaling Source: Ensembl
  • positive regulation of TOR signaling Source: MGI
  • regulation of actin cytoskeleton organization Source: MGI
  • regulation of establishment of cell polarity Source: MGI
  • regulation of gene expression Source: MGI
  • regulation of GTPase activity Source: MGI
  • regulation of inflammatory response Source: MGI
  • regulation of peptidyl-serine phosphorylation Source: MGI
  • regulation of protein kinase B signaling Source: UniProtKB
  • regulation of protein phosphorylation Source: CACAO
  • TOR signaling Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Enzyme and pathway databases

ReactomeiR-MMU-1257604. PIP3 activates AKT signaling.
R-MMU-389357. CD28 dependent PI3K/Akt signaling.
R-MMU-5218920. VEGFR2 mediated vascular permeability.

Names & Taxonomyi

Protein namesi
Recommended name:
Rapamycin-insensitive companion of mTOR
Alternative name(s):
AVO3 homolog
Short name:
mAVO3
Protein pianissimo
Gene namesi
Name:RictorBy similarity
Synonyms:Kiaa1999Imported
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 15

Organism-specific databases

MGIiMGI:1926007. Rictor.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Disruption phenotypei

Mice develop normally until E9.5, and then display growth arrest and embryonic lethality by E11.5.2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 17081708Rapamycin-insensitive companion of mTORPRO_0000308180Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei21 – 211PhosphoserineCombined sources
Modified residuei1135 – 11351Phosphothreonine; by RPS6KB1By similarity
Modified residuei1234 – 12341PhosphoserineCombined sources
Modified residuei1281 – 12811PhosphoserineBy similarity
Modified residuei1283 – 12831PhosphoserineBy similarity
Modified residuei1312 – 13121PhosphoserineCombined sources
Modified residuei1384 – 13841PhosphoserineCombined sources
Modified residuei1387 – 13871PhosphoserineCombined sources
Modified residuei1395 – 13951PhosphoserineBy similarity
Modified residuei1410 – 14101PhosphoserineBy similarity
Modified residuei1591 – 15911PhosphoserineBy similarity

Post-translational modificationi

Phosphorylated by MTOR; when part of mTORC2. Phosphorylated at Thr-1135 by RPS6KB1; phosphorylation of RICTOR inhibits mTORC2 and AKT1 signaling (By similarity).By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ6QI06.
MaxQBiQ6QI06.
PaxDbiQ6QI06.
PRIDEiQ6QI06.

PTM databases

iPTMnetiQ6QI06.
PhosphoSiteiQ6QI06.

Expressioni

Gene expression databases

BgeeiQ6QI06.
CleanExiMM_4921505C17RIK.
GenevisibleiQ6QI06. MM.

Interactioni

Subunit structurei

Part of the mammalian target of rapamycin complex 2 (mTORC2) which contains MTOR, MLST8, PRR5, RICTOR, MAPKAP1 and DEPTOR. 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. Interacts with CCDC28B and NBN. May interact with PRR5L.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
MtorQ9JLN98EBI-4286572,EBI-1571628

GO - Molecular functioni

Protein-protein interaction databases

BioGridi219616. 2 interactions.
DIPiDIP-46323N.
IntActiQ6QI06. 7 interactions.
STRINGi10090.ENSMUSP00000051809.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 789789Interaction with NBNBy similarityAdd
BLAST

Sequence similaritiesi

Belongs to the RICTOR family.Curated

Phylogenomic databases

eggNOGiKOG3694. Eukaryota.
ENOG410XQ5Z. LUCA.
GeneTreeiENSGT00390000002096.
HOVERGENiHBG060827.
InParanoidiQ6QI06.
KOiK08267.
OMAiCSDDAEC.
OrthoDBiEOG7SBNMS.
TreeFamiTF343656.

Family and domain databases

InterProiIPR016024. ARM-type_fold.
IPR028268. Pianissimo_fam.
IPR028267. Pianissimo_N.
IPR029453. Rictor_IV.
IPR029451. RICTOR_M.
IPR029259. RICTOR_phospho.
IPR029452. RICTOR_V.
[Graphical view]
PANTHERiPTHR13298. PTHR13298. 3 hits.
PfamiPF14663. RasGEF_N_2. 1 hit.
PF14666. RICTOR_M. 1 hit.
PF14664. RICTOR_N. 1 hit.
PF14665. RICTOR_phospho. 1 hit.
PF14668. RICTOR_V. 1 hit.
[Graphical view]
SMARTiSM01307. RICTOR_M. 1 hit.
SM01308. RICTOR_N. 1 hit.
SM01309. RICTOR_phospho. 1 hit.
SM01310. RICTOR_V. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 6 hits.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 12 Publications (identifier: Q6QI06-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MAAIGRGRSL KNLRIRGRND SGEENVPLDL TREPSDNLRE ILQNVAKLQG
60 70 80 90 100
VSNMRKLGHL NNFTKLLCDI GHSEEKLGFN YEDIIICLRL ALLNEAKEVR
110 120 130 140 150
AAGLRALRYL IQDSSILQKV LKLKVDYLIA RCIDIQQSNE VERTQALRLV
160 170 180 190 200
RKMITVNASL FPSSVANSLI AVGNDGLQER DRMVRACIAI ICELALQNPE
210 220 230 240 250
VVALRGGLNT ILKNVIDCQL SRINEALITT ILHLLNHPKT RQYVRADVEL
260 270 280 290 300
ERILAPYTDF HYRHSPDTAE GQLKEDREAR FLASKMGIIA TFRSWAGIIN
310 320 330 340 350
LCKPGNSGIQ SLIGVLCIPN MEIRRGLLEV LYDIFRLPLP VVTDEFIEAL
360 370 380 390 400
LSVDPGRFQD SWRLSDGFVA AEAKTILPHR ARSRPDLMDN YLALILSAFI
410 420 430 440 450
RNGLLEGLVE VITNSDDHIS VRATILLGEL LHMANTILPH SHSHHLHCLP
460 470 480 490 500
TLMNMAASFD IPKEKRLRAS AALNCLNRFH EMKKRGPKPY SLHLDHIIQK
510 520 530 540 550
AIATHHKRDQ YLRVQKDIFV LKDTEEALLI NLRDSQVLQH KENLDWDWNL
560 570 580 590 600
IGTILKWPNV NLRNYKDEQL HRFVRRLLYF YKPSSKLYAS LDLDLAKSKQ
610 620 630 640 650
LTVVGCQFTE FLLESEEDGQ GYLEDLVKDI VQWLNASSGV KPERSLQNNG
660 670 680 690 700
LLTTLSQHYF LFIGTLSCHP HGVKMLEKCS VFQCLLNLCS LKNQDHLIKL
710 720 730 740 750
TVSSLDYSRD GLARVILSKI LTAATDACRL YATKHLRVLL RANVEFFNNW
760 770 780 790 800
GIELLVTQLH DKNKTISSEA LDILDEACED KANLHALIQM KPALSHLGDK
810 820 830 840 850
GLLLLLRFLS IPKGFSYLNE RGYVAKQLEK WHKEYNSKYV DLIEEQLNEA
860 870 880 890 900
LTTYRKPIDG DNYVRRSNQR LQRPHVYLPV HLYGQLVHHK TGCHLLEVQS
910 920 930 940 950
IITELCHNVR TPDLDKWEDI KKLKASLWAL GNIGSSNWGL NLLQEENVIP
960 970 980 990 1000
DILKLAKQCE VLSIRGTCVY VLGLIAKTKQ GCDILKCHSW DSVRHSRKHL
1010 1020 1030 1040 1050
WPVVPDDVEQ LCNELSSVPS TLSLNSESTS SRHNSESESA PSSMFMLEDD
1060 1070 1080 1090 1100
RFGSTSTSTF FLDINEDAEP AFYDRPGPIK DKNSFPFFGS SKLVKNRILN
1110 1120 1130 1140 1150
SLTLPTKKHR SSSDPKGGKL SSENKTSNRR IRTLTEPSVD LNHSEDFTSS
1160 1170 1180 1190 1200
SAQKSLQLEP SFVGNKHLED AGSTPSIGEN DLKFPKSFGT ETHRENTSRE
1210 1220 1230 1240 1250
RLVVEGSASS HIKIRSQSFN TDTTTSGISS MSSSPSRETV AVDPTAMDTD
1260 1270 1280 1290 1300
CGSLSTVVST KTVKTSHYLT PQSNHLSLSK SNSVSLVPPG SSHTLPRRAQ
1310 1320 1330 1340 1350
SLKAPSIATI KSLADCNFSY TSSRDAFGYA TLKRLQQQRM HPSLSHSEAL
1360 1370 1380 1390 1400
ASPAKDVLFT DTITMKANSF ESRLTPSRFM KALSYASLDK EDLLSPINHN
1410 1420 1430 1440 1450
TLQRSSSVRS MVSSATYGGS DDYIGLALPV DINDIFQIKD VPYFQSKHVP
1460 1470 1480 1490 1500
PPDDRGARMF SHDGAGLSSG AGGLVKNSFH LLRQQMSLTE IMNSVHSDAS
1510 1520 1530 1540 1550
LFLESTEDTG LQEHTDDNCL YCVCIELLGF QPSNQLSSIC SHSDLQDIPY
1560 1570 1580 1590 1600
SDWCEQTIHN PLEVVPSKFS GISGCSDGAS QEEGSASSTK STELLLGVKT
1610 1620 1630 1640 1650
IPDDTPMCRI LLRKEVLRLV VNLSSSVSTK CHETGLLTIK EKYPQTFDDI
1660 1670 1680 1690 1700
CLYSEVSHLL SHCTFRLQCR RFIQELFQDV QFLQMHEEAE AVLAIPPIQP

IVDESAES
Length:1,708
Mass (Da):191,570
Last modified:July 27, 2011 - v2
Checksum:i309CEE9B1404316D
GO
Isoform 21 Publication (identifier: Q6QI06-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-152: Missing.

Note: No experimental confirmation available.Curated
Show »
Length:1,556
Mass (Da):174,268
Checksum:i80A368FADB2B90EC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti15 – 151I → V in AAR89074 (PubMed:15467718).Curated
Sequence conflicti185 – 1851R → Q in AAR89074 (PubMed:15467718).Curated
Sequence conflicti405 – 4051L → I in AAR89074 (PubMed:15467718).Curated
Sequence conflicti698 – 6981I → L in AAS46920 (PubMed:16962829).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 152152Missing in isoform 2. 1 PublicationVSP_052583Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY497009 mRNA. Translation: AAR89074.1.
AY540053 mRNA. Translation: AAS46920.1.
AC102825 Genomic DNA. No translation available.
AC158901 Genomic DNA. No translation available.
BC058643 mRNA. Translation: AAH58643.1.
BC120903 mRNA. Translation: AAI20904.1.
AK036149 mRNA. Translation: BAC29321.2.
AK075662 mRNA. Translation: BAC35882.1.
AK173326 mRNA. Translation: BAD32604.1.
CCDSiCCDS37032.1. [Q6QI06-1]
RefSeqiNP_084444.3. NM_030168.3. [Q6QI06-1]
UniGeneiMm.275811.

Genome annotation databases

EnsembliENSMUST00000061656; ENSMUSP00000051809; ENSMUSG00000050310. [Q6QI06-1]
GeneIDi78757.
KEGGimmu:78757.
UCSCiuc007vdr.2. mouse. [Q6QI06-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY497009 mRNA. Translation: AAR89074.1.
AY540053 mRNA. Translation: AAS46920.1.
AC102825 Genomic DNA. No translation available.
AC158901 Genomic DNA. No translation available.
BC058643 mRNA. Translation: AAH58643.1.
BC120903 mRNA. Translation: AAI20904.1.
AK036149 mRNA. Translation: BAC29321.2.
AK075662 mRNA. Translation: BAC35882.1.
AK173326 mRNA. Translation: BAD32604.1.
CCDSiCCDS37032.1. [Q6QI06-1]
RefSeqiNP_084444.3. NM_030168.3. [Q6QI06-1]
UniGeneiMm.275811.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi219616. 2 interactions.
DIPiDIP-46323N.
IntActiQ6QI06. 7 interactions.
STRINGi10090.ENSMUSP00000051809.

PTM databases

iPTMnetiQ6QI06.
PhosphoSiteiQ6QI06.

Proteomic databases

EPDiQ6QI06.
MaxQBiQ6QI06.
PaxDbiQ6QI06.
PRIDEiQ6QI06.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000061656; ENSMUSP00000051809; ENSMUSG00000050310. [Q6QI06-1]
GeneIDi78757.
KEGGimmu:78757.
UCSCiuc007vdr.2. mouse. [Q6QI06-1]

Organism-specific databases

CTDi253260.
MGIiMGI:1926007. Rictor.
RougeiSearch...

Phylogenomic databases

eggNOGiKOG3694. Eukaryota.
ENOG410XQ5Z. LUCA.
GeneTreeiENSGT00390000002096.
HOVERGENiHBG060827.
InParanoidiQ6QI06.
KOiK08267.
OMAiCSDDAEC.
OrthoDBiEOG7SBNMS.
TreeFamiTF343656.

Enzyme and pathway databases

ReactomeiR-MMU-1257604. PIP3 activates AKT signaling.
R-MMU-389357. CD28 dependent PI3K/Akt signaling.
R-MMU-5218920. VEGFR2 mediated vascular permeability.

Miscellaneous databases

NextBioi349448.
PROiQ6QI06.
SOURCEiSearch...

Gene expression databases

BgeeiQ6QI06.
CleanExiMM_4921505C17RIK.
GenevisibleiQ6QI06. MM.

Family and domain databases

InterProiIPR016024. ARM-type_fold.
IPR028268. Pianissimo_fam.
IPR028267. Pianissimo_N.
IPR029453. Rictor_IV.
IPR029451. RICTOR_M.
IPR029259. RICTOR_phospho.
IPR029452. RICTOR_V.
[Graphical view]
PANTHERiPTHR13298. PTHR13298. 3 hits.
PfamiPF14663. RasGEF_N_2. 1 hit.
PF14666. RICTOR_M. 1 hit.
PF14664. RICTOR_N. 1 hit.
PF14665. RICTOR_phospho. 1 hit.
PF14668. RICTOR_V. 1 hit.
[Graphical view]
SMARTiSM01307. RICTOR_M. 1 hit.
SM01308. RICTOR_N. 1 hit.
SM01309. RICTOR_phospho. 1 hit.
SM01310. RICTOR_V. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 6 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Mammalian TOR complex 2 controls the actin cytoskeleton and is rapamycin insensitive."
    Jacinto E., Loewith R., Schmidt A., Lin S., Ruegg M.A., Hall A., Hall M.N.
    Nat. Cell Biol. 6:1122-1128(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), IDENTIFICATION IN TORC2 COMPLEX.
    Strain: C3H/HeJImported.
  2. "Multiallelic disruption of the rictor gene in mice reveals that mTOR complex 2 is essential for fetal growth and viability."
    Shiota C., Woo J.-T., Lindner J., Shelton K.D., Magnuson M.A.
    Dev. Cell 11:583-589(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, IDENTIFICATION IN TORC2 COMPLEX, DISRUPTION PHENOTYPE.
    Strain: LAF1Imported.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Strain: C57BL/6JImported.
    Tissue: BrainImported.
  5. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-825 (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1347-1708 (ISOFORM 1/2).
    Strain: C57BL/6JImported.
    Tissue: CerebellumImported and EmbryoImported.
  6. "Prediction of the coding sequences of mouse homologues of KIAA gene: IV. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H., Nagase T., Ohara O., Koga H.
    DNA Res. 11:205-218(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 826-1708 (ISOFORM 1/2).
    Tissue: ThymusImported.
  7. "mTOR.RICTOR is the Ser473 kinase for Akt/protein kinase B in 3T3-L1 adipocytes."
    Hresko R.C., Mueckler M.
    J. Biol. Chem. 280:40406-40416(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "SIN1/MIP1 maintains rictor-mTOR complex integrity and regulates Akt phosphorylation and substrate specificity."
    Jacinto E., Facchinetti V., Liu D., Soto N., Wei S., Jung S.Y., Huang Q., Qin J., Su B.
    Cell 127:125-137(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN TORC2 COMPLEX.
  9. "Ablation in mice of the mTORC components raptor, rictor, or mLST8 reveals that mTORC2 is required for signaling to Akt-FOXO and PKCalpha, but not S6K1."
    Guertin D.A., Stevens D.M., Thoreen C.C., Burds A.A., Kalaany N.Y., Moffat J., Brown M., Fitzgerald K.J., Sabatini D.M.
    Dev. Cell 11:859-871(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-1234; SER-1312; SER-1384 AND SER-1387, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Kidney, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiRICTR_MOUSE
AccessioniPrimary (citable) accession number: Q6QI06
Secondary accession number(s): E9QPE0
, Q0VAV4, Q69Z40, Q6PDL2, Q6RI74, Q8BPH9, Q8CBF2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 23, 2007
Last sequence update: July 27, 2011
Last modified: May 11, 2016
This is version 98 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.