Skip Header

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

Regulatory-associated protein of mTOR

Gene

Rptor

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

Functioni

Involved in the control of the mammalian target of rapamycin complex 1 (mTORC1) activity which regulates cell growth and survival, and autophagy in response to nutrient and hormonal signals; functions as a scaffold for recruiting mTORC1 substrates. mTORC1 is activated in response to growth factors or amino acids. Growth factor-stimulated mTORC1 activation involves a AKT1-mediated phosphorylation of TSC1-TSC2, which leads to the activation of the RHEB GTPase that potently activates the protein kinase activity of mTORC1. Amino acid-signaling to mTORC1 requires its relocalization to the lysosomes mediated by the Ragulator complex and the Rag GTPases. Activated mTORC1 up-regulates protein synthesis by phosphorylating key regulators of mRNA translation and ribosome synthesis. mTORC1 phosphorylates EIF4EBP1 and releases it from inhibiting the elongation initiation factor 4E (eiF4E). mTORC1 phosphorylates and activates S6K1 at 'Thr-389', which then promotes protein synthesis by phosphorylating PDCD4 and targeting it for degradation. Involved in ciliogenesis (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Regulatory-associated protein of mTOR
Short name:
Raptor
Alternative name(s):
p150 target of rapamycin (TOR)-scaffold protein
Gene namesi
Name:Rptor
Synonyms:Raptor
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:1921620. Rptor.

Subcellular locationi

  • Cytoplasm By similarity
  • Lysosome By similarity
  • Cytoplasmic granule By similarity

  • Note: Targeting to lysosomes depends on amino acid availability (By similarity). During oxidative stress, accumulates in stress granules when associated with SPAG5 and association with lysosomes is drastically decreased.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Lysosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi722 – 7221S → A: Abolishes AMPK-mediated phosphorylation; when associated with A-792. 1 Publication
Mutagenesisi792 – 7921S → A: Abolishes AMPK-mediated phosphorylation; when associated with A-722. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 13351335Regulatory-associated protein of mTORPRO_0000051201Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei696 – 6961Phosphoserine; by MAPK8By similarity
Modified residuei706 – 7061Phosphothreonine; by MAPK8By similarity
Modified residuei719 – 7191Phosphoserine; by RPS6KA1By similarity
Modified residuei721 – 7211Phosphoserine; by RPS6KA1By similarity
Modified residuei722 – 7221Phosphoserine; by AMPK and RPS6KA11 Publication
Modified residuei738 – 7381PhosphoserineBy similarity
Modified residuei792 – 7921Phosphoserine; by AMPK1 Publication
Modified residuei855 – 8551PhosphoserineBy similarity
Modified residuei859 – 8591Phosphoserine; by MTORCombined sources1 Publication
Modified residuei863 – 8631Phosphoserine; by MAPK8 and MTORCombined sources1 Publication
Modified residuei865 – 8651PhosphothreonineCombined sources
Modified residuei877 – 8771PhosphoserineCombined sources

Post-translational modificationi

Insulin-stimulated phosphorylation at Ser-863 by MTOR and MAPK8 up-regulates mTORC1 activity. Osmotic stress also induces phosphorylation at Ser-696, Thr-706 and Ser-863 by MAPK8. Ser-863 phosphorylation is required for phosphorylation at Ser-855 and Ser-859 (By similarity). In response to nutrient limitation, phosphorylated by AMPK; phosphorylation promotes interaction with 14-3-3 proteins, leading to negative regulation of the mTORC1 complex. In response to growth factors, phosphorylated at Ser-719, Ser-721 and Ser-722 by RPS6KA1, which stimulates mTORC1 activity.By similarity2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ8K4Q0.
MaxQBiQ8K4Q0.
PaxDbiQ8K4Q0.
PRIDEiQ8K4Q0.

PTM databases

iPTMnetiQ8K4Q0.
PhosphoSiteiQ8K4Q0.

Expressioni

Gene expression databases

CleanExiMM_4932417H02RIK.

Interactioni

Subunit structurei

Part of the mammalian target of rapamycin complex 1 (mTORC1) which contains MTOR, MLST8, RPTOR, AKT1S1/PRAS40 and DEPTOR. mTORC1 binds to and is inhibited by FKBP12-rapamycin. Binds directly 4EBP1 and RPS6KB1 independently of its association with MTOR. Binds preferentially to poorly or non-phosphorylated form of EIF4EBP1, and this binding is critical to the ability of MTOR to catalyze phosphorylation. Forms a complex with MTOR under both leucine-rich and -poor conditions. Interacts with ULK1 in a nutrient-dependent manner; the interaction is reduced during starvation. Interacts (when phosphorylated by AMPK) with 14-3-3 protein, leading to inhibit its activity. Interacts with SPAG5; SPAG5 competes with MTOR for RPTOR-binding, resulting in decreased mTORC1 formation. Interacts with G3BP1. The complex formed with G3BP1 AND SPAG5 is increased by oxidative stress (By similarity). Interacts with HTR6. Interacts with PIH1D1. Interacts with BRAT1 (By similarity).By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
MtorQ9JLN96EBI-4567273,EBI-1571628

GO - Molecular functioni

Protein-protein interaction databases

DIPiDIP-46324N.
IntActiQ8K4Q0. 3 interactions.
MINTiMINT-4607805.
STRINGi10090.ENSMUSP00000026671.

Structurei

3D structure databases

ProteinModelPortaliQ8K4Q0.
SMRiQ8K4Q0. Positions 474-670.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati1020 – 106142WD 1Add
BLAST
Repeati1065 – 110642WD 2Add
BLAST
Repeati1121 – 116040WD 3Add
BLAST
Repeati1164 – 120340WD 4Add
BLAST
Repeati1209 – 124941WD 5Add
BLAST
Repeati1251 – 129141WD 6Add
BLAST
Repeati1299 – 133537WD 7Add
BLAST

Sequence similaritiesi

Belongs to the WD repeat RAPTOR family.Curated
Contains 7 WD repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, WD repeat

Phylogenomic databases

eggNOGiKOG1517. Eukaryota.
ENOG410XQKJ. LUCA.
HOGENOMiHOG000184479.
HOVERGENiHBG059496.
InParanoidiQ8K4Q0.
PhylomeDBiQ8K4Q0.

Family and domain databases

Gene3Di1.25.10.10. 2 hits.
2.130.10.10. 3 hits.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR000357. HEAT.
IPR004083. Raptor.
IPR029347. Raptor_N.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR017986. WD40_repeat_dom.
[Graphical view]
PANTHERiPTHR12848. PTHR12848. 1 hit.
PfamiPF02985. HEAT. 1 hit.
PF14538. Raptor_N. 1 hit.
PF00400. WD40. 1 hit.
[Graphical view]
SMARTiSM01302. Raptor_N. 1 hit.
SM00320. WD40. 7 hits.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 2 hits.
SSF50978. SSF50978. 1 hit.
PROSITEiPS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8K4Q0-1) [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
MESEMLQSPL MGLGEEDEAD LTDWNLPLAF MKKRHCEKIE GSKSLAQSWR
60 70 80 90 100
MKDRMKTVSV ALVLCLNVGV DPPDVVKTTP CARLECWIDP LSMGPQKALE
110 120 130 140 150
TIGANLQKQY ENWQPRARYK QSLDPTVDEV KKLCTSLRRN AKEERVLFHY
160 170 180 190 200
NGHGVPRPTV NGEVWVFNKN YTQYIPLSIY DLQTWMGSPS IFVYDCSNAG
210 220 230 240 250
LIVKSFKQFA LQREQELEVA AINPNHPLAQ MPLPPSMKNC IQLAACEAHE
260 270 280 290 300
LLPMIPDLPA DLFTSCLTTP IKIALRWFCM QKCVSLVPGV TLDLIEKIPG
310 320 330 340 350
RLNDRRTPLG ELNWIFTAIT DTIAWNVLPR DLFQKLFRQD LLVASLFRNF
360 370 380 390 400
LLAERIMRSY NCTPVSSPRL PPTYMHAMWQ AWDLAVDICL SQLPTIIEEG
410 420 430 440 450
TAFRHSPFFA EQLTAFQVWL TMGVENRSPP EQLPIVLQVL LSQVHRLRAL
460 470 480 490 500
DLLGRFLDLG PWAVSLALSV GIFPYVLKLL QSSARELRPL LVFIWAKILA
510 520 530 540 550
VDSSCQADLV KDNGHKYFLS VLADPYMPAE HRTMTAFILA VIVNSYTTGQ
560 570 580 590 600
EACLQGNLIA ICLEQLSDPH PLLRQWVAIC LGRIWQNFDS ARWCGVRDSA
610 620 630 640 650
HEKLYSLLSD PIPEVRCAAV FALGTFVGNS AERTDHSTTI DHNVAMMLAQ
660 670 680 690 700
LINDGSPMVR KELVVALSHL VVQYESNFCT VALQFMEEEK NYPLPSPAAT
710 720 730 740 750
EGGSLTPVRD SPCTPRLRSV SSYGNIRAVT TARNLNKSLQ NLSLTEESGS
760 770 780 790 800
SVAFSPGNLS TSSSASSTLG SPENEEYILS FETIDKMRRV SSYSALNSLI
810 820 830 840 850
GVSFNSVYTQ IWRVLLHLAA DPYPDVSDLA MKVLNSIAYK ATVNARPQRI
860 870 880 890 900
LDTSSLTQSA PASPTNKGMH MHQVGGSPPA SSTSSCSLTN DVAKQTVSRD
910 920 930 940 950
LPSSRPGTAG PTGAQYTPHS HQFPRTRKMF DKGPDQTTDD ADDAAGHKSF
960 970 980 990 1000
ICASMQTGFC DWSARYFAQA VMKIPEEHDL ESQIRKEREW RFLRNTRVRK
1010 1020 1030 1040 1050
QAQQVIQKGI TRLDDQIFLN RNPGVPSVVK FHPFTPCIAV ADKDSICFWD
1060 1070 1080 1090 1100
WEKGEKLDYF HNGNPRYTRV TAMEYLNGQD CSLLLTATDD GAIRVWKNFA
1110 1120 1130 1140 1150
DLEKNPEMVT AWQGLSDMLP TTRGAGMVVD WEQETGLLMS SGDVRIVRIW
1160 1170 1180 1190 1200
DTDRETKVQD IPTGADSCVT SLSCDSHRSL IVAGLGDGSI RVYDRRMALS
1210 1220 1230 1240 1250
ECRVMTYREH TAWVVKAYLQ KHPEGHIVSV SVNGDVRFFD PRMPESVNVM
1260 1270 1280 1290 1300
QIVKGLTALD IHPQANLIAC GSMNQFTAIY NGNGELINNI KYYDGFMGQR
1310 1320 1330
VGAISCLAFH PHWPHLAVGS NDYYISVYSV EKRVR
Length:1,335
Mass (Da):149,471
Last modified:October 1, 2002 - v1
Checksum:i26702199FF7C8136
GO
Isoform 2 (identifier: Q8K4Q0-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-185: Missing.
     841-843: ATV → VCI
     844-1335: Missing.

Note: No experimental confirmation available.
Show »
Length:658
Mass (Da):73,194
Checksum:i3170963C4874A50D
GO
Isoform 3 (identifier: Q8K4Q0-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-421: Missing.
     701-728: EGGSLTPVRDSPCTPRLRSVSSYGNIRA → GTGVAGSLGPPSGPSPGQSVAWVQPGQV
     729-1335: Missing.

Note: No experimental confirmation available.
Show »
Length:307
Mass (Da):33,567
Checksum:i8ABB0CE761E60A62
GO
Isoform 4 (identifier: Q8K4Q0-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-954: Missing.
     1202-1202: C → W
     1203-1335: Missing.

Note: No experimental confirmation available.
Show »
Length:248
Mass (Da):28,444
Checksum:i089152673E6302F9
GO
Isoform 5 (identifier: Q8K4Q0-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     298-1335: Missing.

Note: No experimental confirmation available.
Show »
Length:297
Mass (Da):33,651
Checksum:i39AF4E83D6842EEA
GO

Sequence cautioni

The sequence AK029341 differs from that shown. Reason: Frameshift at position 22. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti630 – 6301S → F in AK029341 (PubMed:16141072).Curated
Sequence conflicti630 – 6301S → F in BAB30288 (PubMed:16141072).Curated
Sequence conflicti970 – 9701A → P in BAC30561 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 954954Missing in isoform 4. 1 PublicationVSP_010176Add
BLAST
Alternative sequencei1 – 421421Missing in isoform 3. 1 PublicationVSP_010177Add
BLAST
Alternative sequencei1 – 185185Missing in isoform 2. 1 PublicationVSP_010175Add
BLAST
Alternative sequencei298 – 13351038Missing in isoform 5. 1 PublicationVSP_010178Add
BLAST
Alternative sequencei701 – 72828EGGSL…GNIRA → GTGVAGSLGPPSGPSPGQSV AWVQPGQV in isoform 3. 1 PublicationVSP_010179Add
BLAST
Alternative sequencei729 – 1335607Missing in isoform 3. 1 PublicationVSP_010180Add
BLAST
Alternative sequencei841 – 8433ATV → VCI in isoform 2. 1 PublicationVSP_010181
Alternative sequencei844 – 1335492Missing in isoform 2. 1 PublicationVSP_010182Add
BLAST
Alternative sequencei1202 – 12021C → W in isoform 4. 1 PublicationVSP_010183
Alternative sequencei1203 – 1335133Missing in isoform 4. 1 PublicationVSP_010184Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB082952 mRNA. Translation: BAC06491.1.
AK016530 mRNA. Translation: BAB30288.1.
AK029341 mRNA. No translation available.
AK034306 mRNA. Translation: BAC28669.1.
AK040288 mRNA. Translation: BAC30561.1.
CCDSiCCDS25720.1. [Q8K4Q0-1]
UniGeneiMm.209933.
Mm.442144.
Mm.450470.
Mm.462932.

Genome annotation databases

UCSCiuc007mqw.1. mouse. [Q8K4Q0-5]
uc007mra.1. mouse. [Q8K4Q0-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB082952 mRNA. Translation: BAC06491.1.
AK016530 mRNA. Translation: BAB30288.1.
AK029341 mRNA. No translation available.
AK034306 mRNA. Translation: BAC28669.1.
AK040288 mRNA. Translation: BAC30561.1.
CCDSiCCDS25720.1. [Q8K4Q0-1]
UniGeneiMm.209933.
Mm.442144.
Mm.450470.
Mm.462932.

3D structure databases

ProteinModelPortaliQ8K4Q0.
SMRiQ8K4Q0. Positions 474-670.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-46324N.
IntActiQ8K4Q0. 3 interactions.
MINTiMINT-4607805.
STRINGi10090.ENSMUSP00000026671.

PTM databases

iPTMnetiQ8K4Q0.
PhosphoSiteiQ8K4Q0.

Proteomic databases

EPDiQ8K4Q0.
MaxQBiQ8K4Q0.
PaxDbiQ8K4Q0.
PRIDEiQ8K4Q0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

UCSCiuc007mqw.1. mouse. [Q8K4Q0-5]
uc007mra.1. mouse. [Q8K4Q0-1]

Organism-specific databases

MGIiMGI:1921620. Rptor.

Phylogenomic databases

eggNOGiKOG1517. Eukaryota.
ENOG410XQKJ. LUCA.
HOGENOMiHOG000184479.
HOVERGENiHBG059496.
InParanoidiQ8K4Q0.
PhylomeDBiQ8K4Q0.

Miscellaneous databases

ChiTaRSiRptor. mouse.
PROiQ8K4Q0.
SOURCEiSearch...

Gene expression databases

CleanExiMM_4932417H02RIK.

Family and domain databases

Gene3Di1.25.10.10. 2 hits.
2.130.10.10. 3 hits.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR000357. HEAT.
IPR004083. Raptor.
IPR029347. Raptor_N.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR017986. WD40_repeat_dom.
[Graphical view]
PANTHERiPTHR12848. PTHR12848. 1 hit.
PfamiPF02985. HEAT. 1 hit.
PF14538. Raptor_N. 1 hit.
PF00400. WD40. 1 hit.
[Graphical view]
SMARTiSM01302. Raptor_N. 1 hit.
SM00320. WD40. 7 hits.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 2 hits.
SSF50978. SSF50978. 1 hit.
PROSITEiPS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Raptor, a binding partner of target of rapamycin (TOR), mediates TOR action."
    Hara K., Maruki Y., Long X., Yoshino K., Oshiro N., Hidayat S., Tokunaga C., Avruch J., Yonezawa K.
    Cell 110:177-189(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "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] (ISOFORMS 2; 3; 4 AND 5).
    Strain: C57BL/6J.
    Tissue: Diencephalon, Head, Testis and Thymus.
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic brain.
  4. Cited for: PHOSPHORYLATION AT SER-722 AND SER-792, MUTAGENESIS OF SER-722 AND SER-792.
  5. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-859 AND SER-863, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. "Mammalian target of rapamycin complex 1 (mTORC1) activity is associated with phosphorylation of raptor by mTOR."
    Wang L., Lawrence J.C. Jr., Sturgill T.W., Harris T.E.
    J. Biol. Chem. 284:14693-14697(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-859 AND SER-863 BY MTOR.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-859; SER-863; THR-865 AND SER-877, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  8. "Tel2 structure and function in the Hsp90-dependent maturation of mTOR and ATR complexes."
    Takai H., Xie Y., de Lange T., Pavletich N.P.
    Genes Dev. 24:2019-2030(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MTOR.

Entry informationi

Entry nameiRPTOR_MOUSE
AccessioniPrimary (citable) accession number: Q8K4Q0
Secondary accession number(s): Q8C9W9
, Q8CBY4, Q8CDY8, Q9D4H3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: October 1, 2002
Last modified: May 11, 2016
This is version 129 of the entry and version 1 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.