Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q6R327

- RICTR_HUMAN

UniProt

Q6R327 - RICTR_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Rapamycin-insensitive companion of mTOR

Gene

RICTOR

Organism
Homo sapiens (Human)
Status
Reviewed - 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.3 Publications

GO - Molecular functioni

  1. protein kinase binding Source: ParkinsonsUK-UCL
  2. ribosome binding Source: Ensembl

GO - Biological processi

  1. actin cytoskeleton reorganization Source: UniProtKB
  2. embryo development Source: UniProtKB
  3. epidermal growth factor receptor signaling pathway Source: Reactome
  4. Fc-epsilon receptor signaling pathway Source: Reactome
  5. fibroblast growth factor receptor signaling pathway Source: Reactome
  6. innate immune response Source: Reactome
  7. neurotrophin TRK receptor signaling pathway Source: Reactome
  8. peptidyl-serine phosphorylation Source: ParkinsonsUK-UCL
  9. phosphatidylinositol-mediated signaling Source: Reactome
  10. positive regulation of actin filament polymerization Source: Ensembl
  11. positive regulation of endothelial cell proliferation Source: Ensembl
  12. positive regulation of peptidyl-tyrosine phosphorylation Source: Ensembl
  13. positive regulation of protein kinase B signaling Source: Ensembl
  14. positive regulation of TOR signaling Source: UniProtKB
  15. regulation of actin cytoskeleton organization Source: UniProtKB
  16. regulation of protein kinase B signaling Source: UniProtKB
  17. regulation of Rac GTPase activity Source: Ensembl
  18. T cell costimulation Source: Reactome
  19. TOR signaling Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Enzyme and pathway databases

ReactomeiREACT_147727. Constitutive PI3K/AKT Signaling in Cancer.
REACT_19358. CD28 dependent PI3K/Akt signaling.
REACT_75829. PIP3 activates AKT signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
Rapamycin-insensitive companion of mTOR
Alternative name(s):
AVO3 homolog
Short name:
hAVO3
Gene namesi
Name:RICTORImported
Synonyms:KIAA1999Imported
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 5

Organism-specific databases

HGNCiHGNC:28611. RICTOR.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. TORC2 complex Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA165660455.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 17081708Rapamycin-insensitive companion of mTORPRO_0000308179Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei21 – 211Phosphoserine7 Publications
Modified residuei1135 – 11351Phosphothreonine; by RPS6KB11 Publication
Modified residuei1282 – 12821Phosphoserine1 Publication
Modified residuei1284 – 12841Phosphoserine1 Publication
Modified residuei1388 – 13881Phosphoserine2 Publications
Modified residuei1396 – 13961Phosphoserine2 Publications
Modified residuei1411 – 14111Phosphoserine1 Publication
Modified residuei1591 – 15911Phosphoserine1 Publication

Post-translational modificationi

Phosphorylated by MTOR; when part of mTORC2. Phosphorylated at Thr-1135 by RPS6KB1; phosphorylation of RICTOR inhibits mTORC2 and AKT1 signaling.9 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ6R327.
PaxDbiQ6R327.
PRIDEiQ6R327.

PTM databases

PhosphoSiteiQ6R327.

Expressioni

Gene expression databases

BgeeiQ6R327.
ExpressionAtlasiQ6R327. baseline and differential.
GenevestigatoriQ6R327.

Organism-specific databases

HPAiHPA037802.

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.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ILKQ134188EBI-1387196,EBI-747644
MTORP4234527EBI-1387196,EBI-359260
PREX1Q8TCU63EBI-1387196,EBI-1046542

Protein-protein interaction databases

BioGridi128962. 55 interactions.
DIPiDIP-39479N.
IntActiQ6R327. 27 interactions.
MINTiMINT-3976651.
STRINGi9606.ENSP00000349959.

Structurei

3D structure databases

ProteinModelPortaliQ6R327.
SMRiQ6R327. Positions 308-335, 399-428, 752-777, 890-975.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

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

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1016 – 105843Ser-richSequence AnalysisAdd
BLAST

Sequence similaritiesi

Belongs to the pianissimo family.Curated

Phylogenomic databases

eggNOGiNOG305760.
GeneTreeiENSGT00390000002096.
HOGENOMiHOG000154126.
HOVERGENiHBG060827.
InParanoidiQ6R327.
KOiK08267.
OMAiRFHEMKK.
OrthoDBiEOG7SBNMS.
PhylomeDBiQ6R327.
TreeFamiTF343656.

Family and domain databases

Gene3Di1.25.10.10. 4 hits.
InterProiIPR011989. ARM-like.
IPR016024. 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. 1 hit.
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]
SUPFAMiSSF48371. SSF48371. 5 hits.

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 11 Publication (identifier: Q6R327-1) [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 KNLRVRGRND SGEENVPLDL TREPSDNLRE ILQNVARLQG
60 70 80 90 100
VSNMRKLGHL NNFTKLLCDI GHSEEKLGFH YEDIIICLRL ALLNEAKEVR
110 120 130 140 150
AAGLRALRYL IQDSSILQKV LKLKVDYLIA RCIDIQQSNE VERTQALRLV
160 170 180 190 200
RKMITVNASL FPSSVTNSLI 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 VVTEEFIEAL
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 AALNCLKRFH EMKKRGPKPY SLHLDHIIQK
510 520 530 540 550
AIATHQKRDQ YLRVQKDIFI LKDTEEALLI NLRDSQVLQH KENLEWNWNL
560 570 580 590 600
IGTILKWPNV NLRNYKDEQL HRFVRRLLYF YKPSSKLYAN LDLDFAKAKQ
610 620 630 640 650
LTVVGCQFTE FLLESEEDGQ GYLEDLVKDI VQWLNASSGM KPERSLQNNG
660 670 680 690 700
LLTTLSQHYF LFIGTLSCHP HGVKMLEKCS VFQCLLNLCS LKNQDHLLKL
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 WHREYNSKYV DLIEEQLNEA
860 870 880 890 900
LTTYRKPVDG DNYVRRSNQR LQRPHVYLPI HLYGQLVHHK TGCHLLEVQN
910 920 930 940 950
IITELCRNVR TPDLDKWEEI KKLKASLWAL GNIGSSNWGL NLLQEENVIP
960 970 980 990 1000
DILKLAKQCE VLSIRGTCVY VLGLIAKTKQ GCDILKCHNW DAVRHSRKHL
1010 1020 1030 1040 1050
WPVVPDDVEQ LCNELSSIPS TLSLNSESTS SRHNSESESV PSSMFILEDD
1060 1070 1080 1090 1100
RFGSSSTSTF FLDINEDTEP TFYDRSGPIK DKNSFPFFAS SKLVKNRILN
1110 1120 1130 1140 1150
SLTLPNKKHR SSSDPKGGKL SSESKTSNRR IRTLTEPSVD FNHSDDFTPI
1160 1170 1180 1190 1200
STVQKTLQLE TSFMGNKHIE DTGSTPSIGE NDLKFTKNFG TENHRENTSR
1210 1220 1230 1240 1250
ERLVVESSTS SHMKIRSQSF NTDTTTSGIS SMSSSPSRET VGVDATTMDT
1260 1270 1280 1290 1300
DCGSMSTVVS TKTIKTSHYL TPQSNHLSLS KSNSVSLVPP GSSHTLPRRA
1310 1320 1330 1340 1350
QSLKAPSIAT IKSLADCNFS YTSSRDAFGY ATLKRLQQQR MHPSLSHSEA
1360 1370 1380 1390 1400
LASPAKDVLF TDTITMKANS FESRLTPSRF MKALSYASLD KEDLLSPINQ
1410 1420 1430 1440 1450
NTLQRSSSVR SMVSSATYGG SDDYIGLALP VDINDIFQVK DIPYFQTKNI
1460 1470 1480 1490 1500
PPHDDRGARA FAHDAGGLPS GTGGLVKNSF HLLRQQMSLT EIMNSIHSDA
1510 1520 1530 1540 1550
SLFLESTEDT GLQEHTDDNC LYCVCIEILG FQPSNQLSAI CSHSDFQDIP
1560 1570 1580 1590 1600
YSDWCEQTIH NPLEVVPSKF SGISGCSDGV SQEGSASSTK STELLLGVKT
1610 1620 1630 1640 1650
IPDDTPMCRI LLRKEVLRLV INLSSSVSTK CHETGLLTIK EKYPQTFDDI
1660 1670 1680 1690 1700
CLYSEVSHLL SHCTFRLPCR RFIQELFQDV QFLQMHEEAE AVLATPPKQP

IVDTSAES
Length:1,708
Mass (Da):192,218
Last modified:July 5, 2004 - v1
Checksum:iDB7B1E4A45DAE2AB
GO
Isoform 2 (identifier: Q6R327-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     252-257: RILAPY → NFSTLY
     258-1708: Missing.

Note: No experimental confirmation available. May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

Show »
Length:257
Mass (Da):28,988
Checksum:i57DCA4610207FA94
GO
Isoform 3 (identifier: Q6R327-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1379-1379: R → RIDFKKKHVGGIRSLRPTITNNLFR

Note: No experimental confirmation available.Curated

Show »
Length:1,732
Mass (Da):195,011
Checksum:i984F516A908EEC3A
GO

Sequence cautioni

The sequence CAH18135.1 differs from that shown. Reason: Wrong choice of CDS.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti545 – 5451E → G in CAH18135. (PubMed:17974005)Curated
Sequence conflicti815 – 8151F → L in CAH18135. (PubMed:17974005)Curated
Sequence conflicti1283 – 12831N → S in CAH18135. (PubMed:17974005)Curated
Sequence conflicti1699 – 16991Q → R in AAH51729. (PubMed:15489334)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti837 – 8371S → F.2 Publications
Corresponds to variant rs2043112 [ dbSNP | Ensembl ].
VAR_051320

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei252 – 2576RILAPY → NFSTLY in isoform 2. 1 PublicationVSP_038362
Alternative sequencei258 – 17081451Missing in isoform 2. 1 PublicationVSP_038363Add
BLAST
Alternative sequencei1379 – 13791R → RIDFKKKHVGGIRSLRPTIT NNLFR in isoform 3. 2 PublicationsVSP_052581

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY515854 mRNA. Translation: AAS79796.1.
AL834497 mRNA. Translation: CAD39155.1.
CR749280 mRNA. Translation: CAH18135.1. Sequence problems.
AC008964 Genomic DNA. No translation available.
AC109467 Genomic DNA. No translation available.
CH471119 Genomic DNA. Translation: EAW55980.1.
BC051729 mRNA. Translation: AAH51729.1.
BC137163 mRNA. Translation: AAI37164.1.
BC137164 mRNA. Translation: AAI37165.1.
BC144509 mRNA. Translation: AAI44510.1.
AB082530 mRNA. Translation: BAC02708.1.
CCDSiCCDS34148.1. [Q6R327-1]
CCDS68861.1. [Q6R327-3]
RefSeqiNP_001272368.1. NM_001285439.1. [Q6R327-3]
NP_001272369.1. NM_001285440.1.
NP_689969.2. NM_152756.4. [Q6R327-1]
UniGeneiHs.407926.

Genome annotation databases

EnsembliENST00000296782; ENSP00000296782; ENSG00000164327. [Q6R327-3]
ENST00000357387; ENSP00000349959; ENSG00000164327. [Q6R327-1]
ENST00000511516; ENSP00000423019; ENSG00000164327. [Q6R327-4]
GeneIDi253260.
KEGGihsa:253260.
UCSCiuc003jlo.2. human. [Q6R327-3]
uc003jlp.2. human. [Q6R327-1]

Polymorphism databases

DMDMi74710068.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY515854 mRNA. Translation: AAS79796.1 .
AL834497 mRNA. Translation: CAD39155.1 .
CR749280 mRNA. Translation: CAH18135.1 . Sequence problems.
AC008964 Genomic DNA. No translation available.
AC109467 Genomic DNA. No translation available.
CH471119 Genomic DNA. Translation: EAW55980.1 .
BC051729 mRNA. Translation: AAH51729.1 .
BC137163 mRNA. Translation: AAI37164.1 .
BC137164 mRNA. Translation: AAI37165.1 .
BC144509 mRNA. Translation: AAI44510.1 .
AB082530 mRNA. Translation: BAC02708.1 .
CCDSi CCDS34148.1. [Q6R327-1 ]
CCDS68861.1. [Q6R327-3 ]
RefSeqi NP_001272368.1. NM_001285439.1. [Q6R327-3 ]
NP_001272369.1. NM_001285440.1.
NP_689969.2. NM_152756.4. [Q6R327-1 ]
UniGenei Hs.407926.

3D structure databases

ProteinModelPortali Q6R327.
SMRi Q6R327. Positions 308-335, 399-428, 752-777, 890-975.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 128962. 55 interactions.
DIPi DIP-39479N.
IntActi Q6R327. 27 interactions.
MINTi MINT-3976651.
STRINGi 9606.ENSP00000349959.

Chemistry

ChEMBLi CHEMBL1795179.

PTM databases

PhosphoSitei Q6R327.

Polymorphism databases

DMDMi 74710068.

Proteomic databases

MaxQBi Q6R327.
PaxDbi Q6R327.
PRIDEi Q6R327.

Protocols and materials databases

DNASUi 253260.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000296782 ; ENSP00000296782 ; ENSG00000164327 . [Q6R327-3 ]
ENST00000357387 ; ENSP00000349959 ; ENSG00000164327 . [Q6R327-1 ]
ENST00000511516 ; ENSP00000423019 ; ENSG00000164327 . [Q6R327-4 ]
GeneIDi 253260.
KEGGi hsa:253260.
UCSCi uc003jlo.2. human. [Q6R327-3 ]
uc003jlp.2. human. [Q6R327-1 ]

Organism-specific databases

CTDi 253260.
GeneCardsi GC05M038939.
H-InvDB HIX0021738.
HGNCi HGNC:28611. RICTOR.
HPAi HPA037802.
MIMi 609022. gene.
neXtProti NX_Q6R327.
PharmGKBi PA165660455.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG305760.
GeneTreei ENSGT00390000002096.
HOGENOMi HOG000154126.
HOVERGENi HBG060827.
InParanoidi Q6R327.
KOi K08267.
OMAi RFHEMKK.
OrthoDBi EOG7SBNMS.
PhylomeDBi Q6R327.
TreeFami TF343656.

Enzyme and pathway databases

Reactomei REACT_147727. Constitutive PI3K/AKT Signaling in Cancer.
REACT_19358. CD28 dependent PI3K/Akt signaling.
REACT_75829. PIP3 activates AKT signaling.

Miscellaneous databases

GeneWikii RICTOR.
GenomeRNAii 253260.
NextBioi 92081.
PROi Q6R327.
SOURCEi Search...

Gene expression databases

Bgeei Q6R327.
ExpressionAtlasi Q6R327. baseline and differential.
Genevestigatori Q6R327.

Family and domain databases

Gene3Di 1.25.10.10. 4 hits.
InterProi IPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR028268. Pianissimo_fam.
IPR028267. Pianissimo_N.
IPR029453. Rictor_IV.
IPR029451. RICTOR_M.
IPR029259. RICTOR_phospho.
IPR029452. RICTOR_V.
[Graphical view ]
PANTHERi PTHR13298. PTHR13298. 1 hit.
Pfami PF14663. 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 ]
SUPFAMi SSF48371. SSF48371. 5 hits.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Rictor, a novel binding partner of mTOR, defines a rapamycin-insensitive and raptor-independent pathway that regulates the cytoskeleton."
    Sarbassov D.D., Ali S.M., Kim D.-H., Guertin D.A., Latek R.R., Erdjument-Bromage H., Tempst P., Sabatini D.M.
    Curr. Biol. 14:1296-1302(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, IDENTIFICATION IN THE TORC2 COMPLEX, INTERACTION WITH MTOR.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 932-1708 (ISOFORM 3), VARIANT PHE-837.
    Tissue: Amygdala.
  3. "The DNA sequence and comparative analysis of human chromosome 5."
    Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
    , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
    Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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] (ISOFORMS 1 AND 3), VARIANT PHE-837.
    Tissue: Brain and LymphImported.
  6. "Characterization of size-fractionated cDNA libraries generated by the in vitro recombination-assisted method."
    Ohara O., Nagase T., Mitsui G., Kohga H., Kikuno R., Hiraoka S., Takahashi Y., Kitajima S., Saga Y., Koseki H.
    DNA Res. 9:47-57(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 434-1708 (ISOFORM 1).
    Tissue: BrainImported.
  7. "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: FUNCTION, IDENTIFICATION IN THE TORC2 COMPLEX, PHOSPHORYLATION.
  8. "Phosphorylation and regulation of Akt/PKB by the rictor-mTOR complex."
    Sarbassov D.D., Guertin D.A., Ali S.M., Sabatini D.M.
    Science 307:1098-1101(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. Cited for: IDENTIFICATION IN THE TORC2 COMPLEX, INTERACTION WITH PRR5 AND PRR5L.
  11. "PRR5, a novel component of mTOR complex 2, regulates platelet-derived growth factor receptor beta expression and signaling."
    Woo S.-Y., Kim D.-H., Jun C.-B., Kim Y.-M., Haar E.V., Lee S.-I., Hegg J.W., Bandhakavi S., Griffin T.J., Kim D.-H.
    J. Biol. Chem. 282:25604-25612(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE TORC2 COMPLEX, INTERACTION WITH PRR5.
  12. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
    Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
    J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21 AND SER-1396, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-1282; SER-1388 AND SER-1396, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-1284; SER-1388 AND SER-1411, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  17. "mTORC1-activated S6K1 phosphorylates Rictor on threonine 1135 and regulates mTORC2 signaling."
    Julien L.A., Carriere A., Moreau J., Roux P.P.
    Mol. Cell. Biol. 30:908-921(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THR-1135.
  18. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21 AND SER-1591, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. "The Bardet-Biedl syndrome-related protein CCDC28B modulates mTORC2 function and interacts with SIN1 to control cilia length independently of the mTOR complex."
    Cardenas-Rodriguez M., Irigoin F., Osborn D.P., Gascue C., Katsanis N., Beales P.L., Badano J.L.
    Hum. Mol. Genet. 22:4031-4042(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CCDC28B.
  22. "Interaction between NBS1 and the mTOR/Rictor/SIN1 complex through specific domains."
    Wang J.Q., Chen J.H., Chen Y.C., Chen M.Y., Hsieh C.Y., Teng S.C., Wu K.J.
    PLoS ONE 8:E65586-E65586(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NBN.

Entry informationi

Entry nameiRICTR_HUMAN
AccessioniPrimary (citable) accession number: Q6R327
Secondary accession number(s): B2RNX0
, B7ZMF7, Q68DT5, Q86UB7, Q8N3A0, Q8NCM6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 23, 2007
Last sequence update: July 5, 2004
Last modified: October 29, 2014
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3