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Protein Page:
Raptor (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
Raptor 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. Interacts with MTOR. 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 to 4EBP1 and RPS6KB1 independently of its association with MTOR. Binds preferentially to poorly or non-phosphorylated forms 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. Highly expressed in skeletal muscle, and in a lesser extent in brain, lung, small intestine, kidney and placenta. Belongs to the WD repeat RAPTOR family. 2 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: Adaptor/scaffold
Cellular Component: lysosomal membrane; lysosome; cytoplasm; cytosol
Molecular Function: protein binding; protein complex binding; protein kinase binding
Biological Process: cellular response to nutrient levels; TOR signaling pathway; insulin receptor signaling pathway; positive regulation of transcription from RNA polymerase III promoter; positive regulation of endothelial cell proliferation; cell cycle arrest; cell growth; regulation of cell size; positive regulation of TOR signaling pathway
Reference #:  Q8N122 (UniProtKB)
Alt. Names/Synonyms: KIAA1303; KOG1; Mip1; p150 target of rapamycin (TOR)-scaffold protein; p150 target of rapamycin (TOR)-scaffold protein containing WD-repeats; RAPTOR; regulatory associated protein of MTOR, complex 1; Regulatory-associated protein of mTOR; RPTOR
Gene Symbols: RPTOR
Molecular weight: 149,038 Da
Basal Isoelectric point: 6.43  Predict pI for various phosphorylation states
CST Pathways:  AMPK Signaling  |  Autophagy Signaling  |  Insulin Receptor Signaling  |  mTOR Signaling  |  PI3K/Akt Signaling  |  T Cell Receptor Signaling  |  Translation: eIF4E and p70S6K
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
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Raptor

Protein Structure Not Found.


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Sites Implicated In
activity, induced: S771‑p, S863‑p, T908‑p
phosphorylation: S696‑p, S863‑p
protein conformation: S863‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
1 0 S8-p MESEMLQsPLLGLGE
0 1 K43 CEKIEGSKSLAQSWR
0 2 K108-ub TIGANLQkQYENWQP
0 1 K120-ub WQPRARYkQSLDPTV
0 1 K131-ub DPTVDEVkKLCTSLR
0 1 T159-p GHGVPRPtVNGEVWV
0 4 K335-ub LPRDLFQkLFRQDLL
0 1 K603-ub VRDSAHEkLYSLLSD
0 1 Y692-p FIEEEKNyALPsPAt
7 7 S696-p EKNyALPsPAttEGG
0 2 T699-p yALPsPAttEGGsLt
0 1 T700-p ALPsPAttEGGsLtP
1 1 S704-p PAttEGGsLtPVRDs
7 5 T706-p ttEGGsLtPVRDsPC
1 3 S711-p sLtPVRDsPCtPRLR
0 2 T714-p PVRDsPCtPRLRsVs
1 19 S719-p PCtPRLRsVssyGNI
1 7 S721-p tPRLRsVssyGNIRA
6 34 S722-p PRLRsVssyGNIRAV
0 5 Y723-p RLRsVssyGNIRAVA
0 2 S738-p TARSLNKsLQNLSLT
2 1 S771-p SASSTLGsPENEEHI
16 1 S792-p DKMRRASsYSsLNSL
0 1 S795-p RRASsYSsLNSLIGV
0 2 T853-p RPQRVLDtssLtQsA
0 2 S854-p PQRVLDtssLtQsAP
2 3 S855-p QRVLDtssLtQsAPA
1 9 T857-p VLDtssLtQsAPAsP
4 39 S859-p DtssLtQsAPAsPtN
9 61 S863-p LtQsAPAsPtNKGVH
1 12 T865-p QsAPAsPtNKGVHIH
6 28 S877-p HIHQAGGsPPAssts
0 3 S881-p AGGsPPAsstsSssL
1 1 S882-p GGsPPAsstsSssLt
0 3 T883-p GsPPAsstsSssLtN
0 2 S884-p sPPAsstsSssLtND
0 3 S886-p PAsstsSssLtNDVA
1 2 S887-p AsstsSssLtNDVAK
0 3 T889-p stsSssLtNDVAKQP
1 1 T908-p LPSGRPGtTGPAGAQ
0 3 Y916-p TGPAGAQytPHSHQF
0 1 T917-p GPAGAQytPHSHQFP
0 1 K973-ub YFAQPVMkIPEEHDL
0 1 S982-p PEEHDLEsQIRKERE
0 2 K1008-ub QAQQVIQkGITRLDD
0 1 K1056-ub WDWEKGEkLDYFHNG
0 2 K1097-ub DGAIRVWkNFADLEK
0 1 S1189-p VAGLGDGsIRVyDRR
0 1 Y1193-p GDGsIRVyDRRMALS
2083 : Phospho-Raptor (Ser792) Antibody
  mouse

 
S8 MESEMLQSPLMGLGE
K43-ub CEKIEGSkSLAQSWR
K108-ub TIGANLQkQYENWQP
K120 WQPRARYKQSLDPTV
K131 DPTVDEVKKLCTSLR
T159 GHGVPRPTVNGEVWV
K335 LPRDLFQKLFRQDLL
K603 VRDSAHEKLYSLLSD
Y692 FMEEEKNYPLPsPAA
S696-p EKNYPLPsPAATEGG
A699 YPLPsPAATEGGsLt
T700 PLPsPAATEGGsLtP
S704-p PAATEGGsLtPVRDS
T706-p ATEGGsLtPVRDSPC
S711 sLtPVRDSPCTPRLR
T714 PVRDSPCTPRLRsVs
S719-p PCTPRLRsVssyGNI
S721-p TPRLRsVssyGNIRA
S722-p PRLRsVssyGNIRAV
Y723-p RLRsVssyGNIRAVT
S738 TARNLNKSLQNLSLT
S771 SASSTLGSPENEEYI
S792-p DKMRRVSsYSALNSL
A795 RRVSsYSALNSLIGV
T853 RPQRILDTssLtQsA
S854-p PQRILDTssLtQsAP
S855-p QRILDTssLtQsAPA
T857-p ILDTssLtQsAPAsP
S859-p DTssLtQsAPAsPtN
S863-p LtQsAPAsPtNKGMH
T865-p QsAPAsPtNKGMHMH
S877-p HMHQVGGsPPASsts
S881 VGGsPPASstsSCsL
S882-p GGsPPASstsSCsLT
T883-p GsPPASstsSCsLTN
S884-p sPPASstsSCsLTND
C886 PASstsSCsLTNDVA
S887-p ASstsSCsLTNDVAK
T889 stsSCsLTNDVAKQT
T908 LPSSRPGTAGPTGAQ
Y916 AGPTGAQYTPHSHQF
T917 GPTGAQYTPHSHQFP
K973 YFAQAVMKIPEEHDL
S982 PEEHDLESQIRKERE
K1008-ub QAQQVIQkGITRLDD
K1056 WDWEKGEKLDYFHNG
K1097 DGAIRVWKNFADLEK
S1189 VAGLGDGSIRVYDRR
Y1193 GDGSIRVYDRRMALS
2083 : Phospho-Raptor (Ser792) Antibody
  rat

 
S8 MESEMLQSPLMGLGE
K43 CEKIEGSKSLAQSWR
K108 TIGANLQKQYENWQP
K120 WQPRARYKQSLDPTV
K131 DPTVDEVKKLCTSLR
T159 GHGVPRPTVNGEVWV
K335 LPRDLFQKLFRQDLL
K603 VRDSAHEKLYSLLSD
Y692 FMEEEKNYPLPSPAA
S696 EKNYPLPSPAATEGG
A699 YPLPSPAATEGGSLT
T700 PLPSPAATEGGSLTP
S704 PAATEGGSLTPVRDS
T706 ATEGGSLTPVRDSPC
S711 SLTPVRDSPCTPRLR
T714 PVRDSPCTPRLRsVS
S719-p PCTPRLRsVSsyGNI
S721 TPRLRsVSsyGNIRA
S722-p PRLRsVSsyGNIRAV
Y723-p RLRsVSsyGNIRAVT
S738 TARNLNKSLQNLSLT
S771 SASSTLGSPENEEYI
S792 DKMRRVSSYSALNSL
A795 RRVSSYSALNSLIGV
T853 RPQRILDTSSLTQsA
S854 PQRILDTSSLTQsAP
S855 QRILDTSSLTQsAPA
T857 ILDTSSLTQsAPAsP
S859-p DTSSLTQsAPAsPTN
S863-p LTQsAPAsPTNKGMH
T865 QsAPAsPTNKGMHIH
S877-p HIHQVGGsPPASSTS
S881 VGGsPPASSTSSCSL
S882 GGsPPASSTSSCSLT
T883 GsPPASSTSSCSLTN
S884 sPPASSTSSCSLTND
C886 PASSTSSCSLTNDVA
S887 ASSTSSCSLTNDVAK
T889 STSSCSLTNDVAKQT
T908 LPSSRPGTAGPTGAQ
Y916 AGPTGAQYTPHSHQF
T917 GPTGAQYTPHSHQFP
K973 YFAQPVMKIPEEHDL
S982 PEEHDLESQIRKERE
K1008 QAQQVIQKGITRLDD
K1056 WDWEKGEKLDYFHNG
K1097 DGAIRVWKNFADLEK
S1189 VAGLGDGSIRVYDRR
Y1193 GDGSIRVYDRRMALS
2083 : Phospho-Raptor (Ser792) Antibody
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