Q6QI06 (RICTR_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Rapamycin-insensitive companion of mTOR

Alternative name(s):
AVO3 homolog
Short name=mAVO3
Protein pianissimo

Gene names

Name:	Rictor
Synonyms:	Kiaa1999

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	1708 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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. Ref.2 Ref.7 Ref.8 Ref.9
Subunit structure	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. May interact with PRR5L.
Post-translational modification	Phosphorylated by MTOR; when part of mTORC2. Phosphorylated at Thr-1135 by RPS6KB1; phosphorylation of RICTOR inhibits mTORC2 and AKT1 signaling By similarity. Ref.10
Disruption phenotype	Mice develop normally until E9.5, and then display growth arrest and embryonic lethality by E11.5. Ref.2 Ref.9
Sequence similarities	Belongs to the pianissimo family.

Ontologies

Keywords
Coding sequence diversity	Alternative splicing
Molecular function	Developmental protein
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	actin cytoskeleton reorganization Inferred from sequence or structural similarity. Source: UniProtKB embryo development Inferred from mutant phenotype Ref.2. Source: UniProtKB positive regulation of actin filament polymerization Inferred from mutant phenotype Ref.1. Source: MGI positive regulation of peptidyl-tyrosine phosphorylation Inferred from mutant phenotype Ref.1. Source: MGI regulation of Rac GTPase activity Inferred from mutant phenotype Ref.1. Source: MGI regulation of protein kinase B signaling cascade Inferred from direct assay Ref.2. Source: UniProtKB
Molecular function	protein binding Inferred from physical interaction. Source: UniProtKB ribosome binding Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Mtor	Q9JLN9	2	EBI-4286572,EBI-1571628

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 Ref.1 Ref.2 (identifier: Q6QI06-1)

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.

Isoform 2 Ref.4 (identifier: Q6QI06-2)

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

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1708	1708	Rapamycin-insensitive companion of mTOR		PRO_0000308180
Amino acid modifications
	Modified residue	21	1	Phosphoserine Ref.10 UniProtKB Q6R327
	Modified residue	582	1	N6-acetyllysine By similarity
	Modified residue	1135	1	Phosphothreonine; by RPS6KB1 By similarity
	Modified residue	1174	1	Phosphothreonine By similarity
	Modified residue	1176	1	Phosphoserine Ref.10
	Modified residue	1281	1	Phosphoserine By similarity
	Modified residue	1283	1	Phosphoserine By similarity
	Modified residue	1294	1	Phosphothreonine By similarity
	Modified residue	1352	1	Phosphoserine By similarity
	Modified residue	1384	1	Phosphoserine By similarity
	Modified residue	1385	1	Phosphotyrosine By similarity
	Modified residue	1387	1	Phosphoserine By similarity
	Modified residue	1395	1	Phosphoserine By similarity
	Modified residue	1410	1	Phosphoserine By similarity
Natural variations
	Alternative sequence	1 – 152	152	Missing in isoform 2. Ref.4		VSP_052583
Experimental info
	Sequence conflict	15	1	I → V in AAR89074. Ref.1
	Sequence conflict	185	1	R → Q in AAR89074. Ref.1
	Sequence conflict	405	1	L → I in AAR89074. Ref.1
	Sequence conflict	698	1	I → L in AAS46920. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified July 27, 2011. Version 2. Checksum: 309CEE9B1404316D	FASTA	1,708	191,570
	10 20 30 40 50 60 MAAIGRGRSL KNLRIRGRND SGEENVPLDL TREPSDNLRE ILQNVAKLQG VSNMRKLGHL 70 80 90 100 110 120 NNFTKLLCDI GHSEEKLGFN YEDIIICLRL ALLNEAKEVR AAGLRALRYL IQDSSILQKV 130 140 150 160 170 180 LKLKVDYLIA RCIDIQQSNE VERTQALRLV RKMITVNASL FPSSVANSLI AVGNDGLQER 190 200 210 220 230 240 DRMVRACIAI ICELALQNPE VVALRGGLNT ILKNVIDCQL SRINEALITT ILHLLNHPKT 250 260 270 280 290 300 RQYVRADVEL ERILAPYTDF HYRHSPDTAE GQLKEDREAR FLASKMGIIA TFRSWAGIIN 310 320 330 340 350 360 LCKPGNSGIQ SLIGVLCIPN MEIRRGLLEV LYDIFRLPLP VVTDEFIEAL LSVDPGRFQD 370 380 390 400 410 420 SWRLSDGFVA AEAKTILPHR ARSRPDLMDN YLALILSAFI RNGLLEGLVE VITNSDDHIS 430 440 450 460 470 480 VRATILLGEL LHMANTILPH SHSHHLHCLP TLMNMAASFD IPKEKRLRAS AALNCLNRFH 490 500 510 520 530 540 EMKKRGPKPY SLHLDHIIQK AIATHHKRDQ YLRVQKDIFV LKDTEEALLI NLRDSQVLQH 550 560 570 580 590 600 KENLDWDWNL IGTILKWPNV NLRNYKDEQL HRFVRRLLYF YKPSSKLYAS LDLDLAKSKQ 610 620 630 640 650 660 LTVVGCQFTE FLLESEEDGQ GYLEDLVKDI VQWLNASSGV KPERSLQNNG LLTTLSQHYF 670 680 690 700 710 720 LFIGTLSCHP HGVKMLEKCS VFQCLLNLCS LKNQDHLIKL TVSSLDYSRD GLARVILSKI 730 740 750 760 770 780 LTAATDACRL YATKHLRVLL RANVEFFNNW GIELLVTQLH DKNKTISSEA LDILDEACED 790 800 810 820 830 840 KANLHALIQM KPALSHLGDK GLLLLLRFLS IPKGFSYLNE RGYVAKQLEK WHKEYNSKYV 850 860 870 880 890 900 DLIEEQLNEA LTTYRKPIDG DNYVRRSNQR LQRPHVYLPV HLYGQLVHHK TGCHLLEVQS 910 920 930 940 950 960 IITELCHNVR TPDLDKWEDI KKLKASLWAL GNIGSSNWGL NLLQEENVIP DILKLAKQCE 970 980 990 1000 1010 1020 VLSIRGTCVY VLGLIAKTKQ GCDILKCHSW DSVRHSRKHL WPVVPDDVEQ LCNELSSVPS 1030 1040 1050 1060 1070 1080 TLSLNSESTS SRHNSESESA PSSMFMLEDD RFGSTSTSTF FLDINEDAEP AFYDRPGPIK 1090 1100 1110 1120 1130 1140 DKNSFPFFGS SKLVKNRILN SLTLPTKKHR SSSDPKGGKL SSENKTSNRR IRTLTEPSVD 1150 1160 1170 1180 1190 1200 LNHSEDFTSS SAQKSLQLEP SFVGNKHLED AGSTPSIGEN DLKFPKSFGT ETHRENTSRE 1210 1220 1230 1240 1250 1260 RLVVEGSASS HIKIRSQSFN TDTTTSGISS MSSSPSRETV AVDPTAMDTD CGSLSTVVST 1270 1280 1290 1300 1310 1320 KTVKTSHYLT PQSNHLSLSK SNSVSLVPPG SSHTLPRRAQ SLKAPSIATI KSLADCNFSY 1330 1340 1350 1360 1370 1380 TSSRDAFGYA TLKRLQQQRM HPSLSHSEAL ASPAKDVLFT DTITMKANSF ESRLTPSRFM 1390 1400 1410 1420 1430 1440 KALSYASLDK EDLLSPINHN TLQRSSSVRS MVSSATYGGS DDYIGLALPV DINDIFQIKD 1450 1460 1470 1480 1490 1500 VPYFQSKHVP PPDDRGARMF SHDGAGLSSG AGGLVKNSFH LLRQQMSLTE IMNSVHSDAS 1510 1520 1530 1540 1550 1560 LFLESTEDTG LQEHTDDNCL YCVCIELLGF QPSNQLSSIC SHSDLQDIPY SDWCEQTIHN 1570 1580 1590 1600 1610 1620 PLEVVPSKFS GISGCSDGAS QEEGSASSTK STELLLGVKT IPDDTPMCRI LLRKEVLRLV 1630 1640 1650 1660 1670 1680 VNLSSSVSTK CHETGLLTIK EKYPQTFDDI CLYSEVSHLL SHCTFRLQCR RFIQELFQDV 1690 1700 QFLQMHEEAE AVLAIPPIQP IVDESAES
	Isoform 2 [UniParc]. Checksum: 80A368FADB2B90EC	FASTA	1,556	174,268
	10 20 30 40 50 60 MITVNASLFP SSVANSLIAV GNDGLQERDR MVRACIAIIC ELALQNPEVV ALRGGLNTIL 70 80 90 100 110 120 KNVIDCQLSR INEALITTIL HLLNHPKTRQ YVRADVELER ILAPYTDFHY RHSPDTAEGQ 130 140 150 160 170 180 LKEDREARFL ASKMGIIATF RSWAGIINLC KPGNSGIQSL IGVLCIPNME IRRGLLEVLY 190 200 210 220 230 240 DIFRLPLPVV TDEFIEALLS VDPGRFQDSW RLSDGFVAAE AKTILPHRAR SRPDLMDNYL 250 260 270 280 290 300 ALILSAFIRN GLLEGLVEVI TNSDDHISVR ATILLGELLH MANTILPHSH SHHLHCLPTL 310 320 330 340 350 360 MNMAASFDIP KEKRLRASAA LNCLNRFHEM KKRGPKPYSL HLDHIIQKAI ATHHKRDQYL 370 380 390 400 410 420 RVQKDIFVLK DTEEALLINL RDSQVLQHKE NLDWDWNLIG TILKWPNVNL RNYKDEQLHR 430 440 450 460 470 480 FVRRLLYFYK PSSKLYASLD LDLAKSKQLT VVGCQFTEFL LESEEDGQGY LEDLVKDIVQ 490 500 510 520 530 540 WLNASSGVKP ERSLQNNGLL TTLSQHYFLF IGTLSCHPHG VKMLEKCSVF QCLLNLCSLK 550 560 570 580 590 600 NQDHLIKLTV SSLDYSRDGL ARVILSKILT AATDACRLYA TKHLRVLLRA NVEFFNNWGI 610 620 630 640 650 660 ELLVTQLHDK NKTISSEALD ILDEACEDKA NLHALIQMKP ALSHLGDKGL LLLLRFLSIP 670 680 690 700 710 720 KGFSYLNERG YVAKQLEKWH KEYNSKYVDL IEEQLNEALT TYRKPIDGDN YVRRSNQRLQ 730 740 750 760 770 780 RPHVYLPVHL YGQLVHHKTG CHLLEVQSII TELCHNVRTP DLDKWEDIKK LKASLWALGN 790 800 810 820 830 840 IGSSNWGLNL LQEENVIPDI LKLAKQCEVL SIRGTCVYVL GLIAKTKQGC DILKCHSWDS 850 860 870 880 890 900 VRHSRKHLWP VVPDDVEQLC NELSSVPSTL SLNSESTSSR HNSESESAPS SMFMLEDDRF 910 920 930 940 950 960 GSTSTSTFFL DINEDAEPAF YDRPGPIKDK NSFPFFGSSK LVKNRILNSL TLPTKKHRSS 970 980 990 1000 1010 1020 SDPKGGKLSS ENKTSNRRIR TLTEPSVDLN HSEDFTSSSA QKSLQLEPSF VGNKHLEDAG 1030 1040 1050 1060 1070 1080 STPSIGENDL KFPKSFGTET HRENTSRERL VVEGSASSHI KIRSQSFNTD TTTSGISSMS 1090 1100 1110 1120 1130 1140 SSPSRETVAV DPTAMDTDCG SLSTVVSTKT VKTSHYLTPQ SNHLSLSKSN SVSLVPPGSS 1150 1160 1170 1180 1190 1200 HTLPRRAQSL KAPSIATIKS LADCNFSYTS SRDAFGYATL KRLQQQRMHP SLSHSEALAS 1210 1220 1230 1240 1250 1260 PAKDVLFTDT ITMKANSFES RLTPSRFMKA LSYASLDKED LLSPINHNTL QRSSSVRSMV 1270 1280 1290 1300 1310 1320 SSATYGGSDD YIGLALPVDI NDIFQIKDVP YFQSKHVPPP DDRGARMFSH DGAGLSSGAG 1330 1340 1350 1360 1370 1380 GLVKNSFHLL RQQMSLTEIM NSVHSDASLF LESTEDTGLQ EHTDDNCLYC VCIELLGFQP 1390 1400 1410 1420 1430 1440 SNQLSSICSH SDLQDIPYSD WCEQTIHNPL EVVPSKFSGI SGCSDGASQE EGSASSTKST 1450 1460 1470 1480 1490 1500 ELLLGVKTIP DDTPMCRILL RKEVLRLVVN LSSSVSTKCH ETGLLTIKEK YPQTFDDICL 1510 1520 1530 1540 1550 YSEVSHLLSH CTFRLQCRRF IQELFQDVQF LQMHEEAEAV LAIPPIQPIV DESAES

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 15467718] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), IDENTIFICATION IN TORC2 COMPLEX. Strain: C3H.
[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: 16962829] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, IDENTIFICATION IN TORC2 COMPLEX, DISRUPTION PHENOTYPE. Strain: LAF1.
[3]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed: 19468303] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6.
[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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Strain: C57BL/6. Tissue: Brain.
[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: 16141072] [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/6J. Tissue: Cerebellum and Embryo.
[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: 15368895] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 826-1708 (ISOFORM 1/2). Tissue: Thymus.
[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: 16221682] [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: 16962653] [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: 17141160] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[10]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed: 19367708] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21 AND SER-1176, MASS SPECTROMETRY. Tissue: Melanoma.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00399440. IPI00869420.
RefSeq	NP_084444.3. NM_030168.3.
UniGene	Mm.275811.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-46323N.
IntAct	Q6QI06. 2 interactions.
STRING	Q6QI06.
PTM databases
PhosphoSite	Q6QI06.
Proteomic databases
PRIDE	Q6QI06.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000061656; ENSMUSP00000051809; ENSMUSG00000050310.
GeneID	78757.
KEGG	mmu:78757.
UCSC	uc007vdr.2. mouse. uc011zrb.1. mouse.
Organism-specific databases
CTD	253260.
MGI	MGI:1926007. Rictor.
Rouge	Search...
Phylogenomic databases
HOVERGEN	HBG060827.
InParanoid	Q6QI06.
OrthoDB	EOG43XV2K.
PhylomeDB	Q6QI06.
Gene expression databases
ArrayExpress	Q6QI06.
Bgee	Q6QI06.
CleanEx	MM_4921505C17RIK.
Genevestigator	Q6QI06.
Family and domain databases
InterPro	IPR011989. ARM-like. IPR016024. ARM-type_fold. [Graphical view]
Gene3D	G3DSA:1.25.10.10. ARM-like. 3 hits.
KO	K08267.
SUPFAM	SSF48371. ARM-type_fold. 2 hits.
ProtoNet	Search...
Other
NextBio	349448.
SOURCE	Search...

Entry information

Entry name

RICTR_MOUSE

Accession

Primary (citable) accession number: Q6QI06
Secondary accession number(s): E9QPE0 , Q0VAV4, Q69Z40, Q6PDL2, Q6RI74, Q8BPH9, Q8CBF2

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 23, 2007
Last sequence update:	July 27, 2011
Last modified:	January 25, 2012
This is version 61 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program