dbPTM

RPTOR_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RPTOR_HUMAN
UniProt AC	Q8N122
Protein Name	Regulatory-associated protein of mTOR
Gene Name	RPTOR
Organism	Homo sapiens (Human).
Sequence Length	1335
Subcellular Localization	Cytoplasm. Lysosome. Cytoplasmic granule . Targeting to lysosomes depends on amino acid availability. In arsenite-stressed cells, accumulates in stress granules when associated with SPAG5 and association with lysosomes is drastically decreased.
Protein Description	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..
Protein Sequence	MESEMLQSPLLGLGEEDEADLTDWNLPLAFMKKRHCEKIEGSKSLAQSWRMKDRMKTVSVALVLCLNVGVDPPDVVKTTPCARLECWIDPLSMGPQKALETIGANLQKQYENWQPRARYKQSLDPTVDEVKKLCTSLRRNAKEERVLFHYNGHGVPRPTVNGEVWVFNKNYTQYIPLSIYDLQTWMGSPSIFVYDCSNAGLIVKSFKQFALQREQELEVAAINPNHPLAQMPLPPSMKNCIQLAACEATELLPMIPDLPADLFTSCLTTPIKIALRWFCMQKCVSLVPGVTLDLIEKIPGRLNDRRTPLGELNWIFTAITDTIAWNVLPRDLFQKLFRQDLLVASLFRNFLLAERIMRSYNCTPVSSPRLPPTYMHAMWQAWDLAVDICLSQLPTIIEEGTAFRHSPFFAEQLTAFQVWLTMGVENRNPPEQLPIVLQVLLSQVHRLRALDLLGRFLDLGPWAVSLALSVGIFPYVLKLLQSSARELRPLLVFIWAKILAVDSSCQADLVKDNGHKYFLSVLADPYMPAEHRTMTAFILAVIVNSYHTGQEACLQGNLIAICLEQLNDPHPLLRQWVAICLGRIWQNFDSARWCGVRDSAHEKLYSLLSDPIPEVRCAAVFALGTFVGNSAERTDHSTTIDHNVAMMLAQLVSDGSPMVRKELVVALSHLVVQYESNFCTVALQFIEEEKNYALPSPATTEGGSLTPVRDSPCTPRLRSVSSYGNIRAVATARSLNKSLQNLSLTEESGGAVAFSPGNLSTSSSASSTLGSPENEEHILSFETIDKMRRASSYSSLNSLIGVSFNSVYTQIWRVLLHLAADPYPEVSDVAMKVLNSIAYKATVNARPQRVLDTSSLTQSAPASPTNKGVHIHQAGGSPPASSTSSSSLTNDVAKQPVSRDLPSGRPGTTGPAGAQYTPHSHQFPRTRKMFDKGPEQTADDADDAAGHKSFISATVQTGFCDWSARYFAQPVMKIPEEHDLESQIRKEREWRFLRNSRVRRQAQQVIQKGITRLDDQIFLNRNPGVPSVVKFHPFTPCIAVADKDSICFWDWEKGEKLDYFHNGNPRYTRVTAMEYLNGQDCSLLLTATDDGAIRVWKNFADLEKNPEMVTAWQGLSDMLPTTRGAGMVVDWEQETGLLMSSGDVRIVRIWDTDREMKVQDIPTGADSCVTSLSCDSHRSLIVAGLGDGSIRVYDRRMALSECRVMTYREHTAWVVKASLQKRPDGHIVSVSVNGDVRIFDPRMPESVNVLQIVKGLTALDIHPQADLIACGSVNQFTAIYNSSGELINNIKYYDGFMGQRVGAISCLAFHPHWPHLAVGSNDYYISVYSVEKRVR

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
3	Phosphorylation	-----MESEMLQSPL -----CCCHHHCCCC	39.92	29978859
8	Phosphorylation	MESEMLQSPLLGLGE CCCHHHCCCCCCCCC	17.35	21071439
22	Phosphorylation	EEDEADLTDWNLPLA CCCCCCCCCCCCCHH	39.24	29978859
43	Ubiquitination	CEKIEGSKSLAQSWR CHHHCCCHHHHHHHH	61.42	-
43	Ubiquitination	CEKIEGSKSLAQSWR CHHHCCCHHHHHHHH	61.42	-
48	Phosphorylation	GSKSLAQSWRMKDRM CCHHHHHHHHHHHHH	15.84	-
86	Glutathionylation	TPCARLECWIDPLSM CCCCEEEEEECCCCC	4.58	22555962
97	Ubiquitination	PLSMGPQKALETIGA CCCCCHHHHHHHHCH	59.06	-
97	Ubiquitination	PLSMGPQKALETIGA CCCCCHHHHHHHHCH	59.06	-
108	Ubiquitination	TIGANLQKQYENWQP HHCHHHHHHHHHCCC	59.00	-
108	Ubiquitination	TIGANLQKQYENWQP HHCHHHHHHHHHCCC	59.00	21906983
108 (in isoform 1)	Ubiquitination	-	59.00	21890473
108 (in isoform 2)	Ubiquitination	-	59.00	21890473
120	Ubiquitination	WQPRARYKQSLDPTV CCCCHHHHHHCCCCH	28.05	-
120	Malonylation	WQPRARYKQSLDPTV CCCCHHHHHHCCCCH	28.05	26320211
120	Ubiquitination	WQPRARYKQSLDPTV CCCCHHHHHHCCCCH	28.05	-
120 (in isoform 1)	Ubiquitination	-	28.05	21890473
120 (in isoform 2)	Ubiquitination	-	28.05	21890473
122	Phosphorylation	PRARYKQSLDPTVDE CCHHHHHHCCCCHHH	30.50	21406692
126	Phosphorylation	YKQSLDPTVDEVKKL HHHHCCCCHHHHHHH	40.01	21406692
131	Ubiquitination	DPTVDEVKKLCTSLR CCCHHHHHHHHHHHH	37.67	-
131	Ubiquitination	DPTVDEVKKLCTSLR CCCHHHHHHHHHHHH	37.67	21906983
131 (in isoform 1)	Ubiquitination	-	37.67	21890473
131 (in isoform 2)	Ubiquitination	-	37.67	21890473
132	Ubiquitination	PTVDEVKKLCTSLRR CCHHHHHHHHHHHHH	54.70	-
159	Phosphorylation	GHGVPRPTVNGEVWV CCCCCCCCCCCEEEE	28.08	-
207	Ubiquitination	GLIVKSFKQFALQRE CHHHHHHHHHHHHHH	52.15	-
297	Ubiquitination	VTLDLIEKIPGRLND CCHHHHHHCCCCCCC	47.40	-
335	Ubiquitination	LPRDLFQKLFRQDLL CCHHHHHHHHHHHHH	42.11	21890473
335	Ubiquitination	LPRDLFQKLFRQDLL CCHHHHHHHHHHHHH	42.11	21890473
335 (in isoform 1)	Ubiquitination	-	42.11	21890473
335 (in isoform 2)	Ubiquitination	-	42.11	21890473
511	Ubiquitination	SCQADLVKDNGHKYF CCCCEEECCCCCEEE	53.42	-
603	Ubiquitination	VRDSAHEKLYSLLSD CCCCHHHHHHHHHCC	42.74	21906983
603 (in isoform 1)	Ubiquitination	-	42.74	21890473
606	Phosphorylation	SAHEKLYSLLSDPIP CHHHHHHHHHCCCCC	33.02	-
682	Ubiquitination	ESNFCTVALQFIEEE CCCCHHHHHHHHHHH	4.22	-
692	Phosphorylation	FIEEEKNYALPSPAT HHHHHHCCCCCCCCC	22.15	21945579
696	Phosphorylation	EKNYALPSPATTEGG HHCCCCCCCCCCCCC	28.19	21945579
699	Phosphorylation	YALPSPATTEGGSLT CCCCCCCCCCCCCCC	28.85	21945579
700	O-linked_Glycosylation	ALPSPATTEGGSLTP CCCCCCCCCCCCCCC	34.44	30379171
700	Phosphorylation	ALPSPATTEGGSLTP CCCCCCCCCCCCCCC	34.44	21945579
704	Phosphorylation	PATTEGGSLTPVRDS CCCCCCCCCCCCCCC	39.67	21945579
706	Phosphorylation	TTEGGSLTPVRDSPC CCCCCCCCCCCCCCC	22.80	21945579
711	Phosphorylation	SLTPVRDSPCTPRLR CCCCCCCCCCCCCCC	16.00	21945579
714	Phosphorylation	PVRDSPCTPRLRSVS CCCCCCCCCCCCCCC	18.15	21945579
718	Methylation	SPCTPRLRSVSSYGN CCCCCCCCCCCCCCC	35.97	115490313
719	Phosphorylation	PCTPRLRSVSSYGNI CCCCCCCCCCCCCCH	30.83	22322096
721	Phosphorylation	TPRLRSVSSYGNIRA CCCCCCCCCCCCHHH	21.06	30266825
722	Phosphorylation	PRLRSVSSYGNIRAV CCCCCCCCCCCHHHH	34.60	25159151
723	Phosphorylation	RLRSVSSYGNIRAVA CCCCCCCCCCHHHHH	13.49	23927012
731	Phosphorylation	GNIRAVATARSLNKS CCHHHHHHHHHHCHH	18.92	29414761
734	Phosphorylation	RAVATARSLNKSLQN HHHHHHHHHCHHHHH	33.55	28102081
738	Phosphorylation	TARSLNKSLQNLSLT HHHHHCHHHHHCCCC	33.83	24275569
767	Phosphorylation	STSSSASSTLGSPEN CCCCCCCCCCCCCCC	27.63	26074081
768	Phosphorylation	TSSSASSTLGSPENE CCCCCCCCCCCCCCH	32.42	26074081
771	Phosphorylation	SASSTLGSPENEEHI CCCCCCCCCCCHHCE	31.95	26074081
774	Ubiquitination	STLGSPENEEHILSF CCCCCCCCHHCEECH	64.44	-
791	Phosphorylation	IDKMRRASSYSSLNS HHHHHHHCCCHHHHH	28.18	23663014
792	Phosphorylation	DKMRRASSYSSLNSL HHHHHHCCCHHHHHH	28.22	25072903
793	Phosphorylation	KMRRASSYSSLNSLI HHHHHCCCHHHHHHH	10.36	23663014
794	Phosphorylation	MRRASSYSSLNSLIG HHHHCCCHHHHHHHC	30.23	23663014
795	Phosphorylation	RRASSYSSLNSLIGV HHHCCCHHHHHHHCC	24.28	23663014
798	Phosphorylation	SSYSSLNSLIGVSFN CCCHHHHHHHCCCHH	27.02	23663014
803	Phosphorylation	LNSLIGVSFNSVYTQ HHHHHCCCHHHHHHH	17.31	25072903
806	Phosphorylation	LIGVSFNSVYTQIWR HHCCCHHHHHHHHHH	17.94	25072903
808	Phosphorylation	GVSFNSVYTQIWRVL CCCHHHHHHHHHHHH	7.86	25072903
809	Phosphorylation	VSFNSVYTQIWRVLL CCHHHHHHHHHHHHH	16.06	25072903
815	Ubiquitination	YTQIWRVLLHLAADP HHHHHHHHHHHHCCC	1.55	-
836	Phosphorylation	VAMKVLNSIAYKATV HHHHHHHHHHHHHCC	12.39	23312004
840	Ubiquitination	VLNSIAYKATVNARP HHHHHHHHHCCCCCC	28.67	-
850	Ubiquitination	VNARPQRVLDTSSLT CCCCCCEEECCCCCC	4.83	-
853	Phosphorylation	RPQRVLDTSSLTQSA CCCEEECCCCCCCCC	18.96	23927012
854	Phosphorylation	PQRVLDTSSLTQSAP CCEEECCCCCCCCCC	24.02	23927012
855	Phosphorylation	QRVLDTSSLTQSAPA CEEECCCCCCCCCCC	37.21	25159151
857	Phosphorylation	VLDTSSLTQSAPASP EECCCCCCCCCCCCC	23.56	29255136
859	Phosphorylation	DTSSLTQSAPASPTN CCCCCCCCCCCCCCC	30.86	29255136
863	Phosphorylation	LTQSAPASPTNKGVH CCCCCCCCCCCCCCE	31.06	19664994
865	Phosphorylation	QSAPASPTNKGVHIH CCCCCCCCCCCCEEE	47.25	29255136
867	Ubiquitination	APASPTNKGVHIHQA CCCCCCCCCCEEEEC	65.86	-
877	Phosphorylation	HIHQAGGSPPASSTS EEEECCCCCCCCCCC	27.13	29255136
881	Phosphorylation	AGGSPPASSTSSSSL CCCCCCCCCCCCCCC	39.66	30266825
882	Phosphorylation	GGSPPASSTSSSSLT CCCCCCCCCCCCCCC	34.12	30266825
883	Phosphorylation	GSPPASSTSSSSLTN CCCCCCCCCCCCCCC	30.08	30266825
884	Phosphorylation	SPPASSTSSSSLTND CCCCCCCCCCCCCCC	30.12	30266825
885	Phosphorylation	PPASSTSSSSLTNDV CCCCCCCCCCCCCCC	24.84	30266825
886	Phosphorylation	PASSTSSSSLTNDVA CCCCCCCCCCCCCCC	29.18	30266825
887	Phosphorylation	ASSTSSSSLTNDVAK CCCCCCCCCCCCCCC	40.95	22167270
889	Phosphorylation	STSSSSLTNDVAKQP CCCCCCCCCCCCCCC	31.18	23927012
894	Ubiquitination	SLTNDVAKQPVSRDL CCCCCCCCCCCCCCC	55.79	-
898	Ubiquitination	DVAKQPVSRDLPSGR CCCCCCCCCCCCCCC	27.10	-
898	Phosphorylation	DVAKQPVSRDLPSGR CCCCCCCCCCCCCCC	27.10	23927012
903	Phosphorylation	PVSRDLPSGRPGTTG CCCCCCCCCCCCCCC	55.52	29214152
908	Phosphorylation	LPSGRPGTTGPAGAQ CCCCCCCCCCCCCCC	31.12	23312004
909	Phosphorylation	PSGRPGTTGPAGAQY CCCCCCCCCCCCCCC	47.27	23312004
916	Phosphorylation	TGPAGAQYTPHSHQF CCCCCCCCCCCCCCC	23.00	28796482
917	Phosphorylation	GPAGAQYTPHSHQFP CCCCCCCCCCCCCCC	11.49	28796482
920	Phosphorylation	GAQYTPHSHQFPRTR CCCCCCCCCCCCCHH	21.86	23312004
932	Ubiquitination	RTRKMFDKGPEQTAD CHHHHHCCCCCCCCC	66.16	-
939	Ubiquitination	KGPEQTADDADDAAG CCCCCCCCCCCHHCC	55.83	21890473
939	Ubiquitination	KGPEQTADDADDAAG CCCCCCCCCCCHHCC	55.83	-
973	Ubiquitination	YFAQPVMKIPEEHDL HHHCCHHCCCCCCCH	56.17	21906983
973 (in isoform 1)	Ubiquitination	-	56.17	21890473
982	Phosphorylation	PEEHDLESQIRKERE CCCCCHHHHHHHHHH	37.90	-
999	Ubiquitination	FLRNSRVRRQAQQVI HHHHHHHHHHHHHHH	24.71	-
1008	Ubiquitination	QAQQVIQKGITRLDD HHHHHHHHCCCCCHH	40.95	21906983
1008 (in isoform 1)	Ubiquitination	-	40.95	21890473
1030	Ubiquitination	PGVPSVVKFHPFTPC CCCCCEEEECCCCCE	35.48	-
1053	Ubiquitination	ICFWDWEKGEKLDYF CEEECCCCCCCCEEC	69.02	-
1056	Ubiquitination	WDWEKGEKLDYFHNG ECCCCCCCCEECCCC	56.16	21906983
1056 (in isoform 1)	Ubiquitination	-	56.16	21890473
1063	Ubiquitination	KLDYFHNGNPRYTRV CCEECCCCCCCCEEE	36.63	-
1097	Ubiquitination	DGAIRVWKNFADLEK CCCEEEEECHHHHHH	39.05	21890473
1097 (in isoform 1)	Ubiquitination	-	39.05	21890473
1104	Ubiquitination	KNFADLEKNPEMVTA ECHHHHHHCHHHHHH	82.30	-
1116	Phosphorylation	VTAWQGLSDMLPTTR HHHHHHHHHHCCCCC	28.00	24114839
1121	Phosphorylation	GLSDMLPTTRGAGMV HHHHHCCCCCCCCEE	25.76	24114839
1122	Phosphorylation	LSDMLPTTRGAGMVV HHHHCCCCCCCCEEE	25.76	24114839
1157	Ubiquitination	WDTDREMKVQDIPTG EECCCCCCEEECCCC	31.80	-
1189	O-linked_Glycosylation	VAGLGDGSIRVYDRR EEECCCCCEEEECHH	16.38	30379171
1189	Phosphorylation	VAGLGDGSIRVYDRR EEECCCCCEEEECHH	16.38	-
1193	Phosphorylation	GDGSIRVYDRRMALS CCCCEEEECHHHHHH	8.22	-
1221	Ubiquitination	VVKASLQKRPDGHIV EEEHHHCCCCCCCEE	71.80	-
1243	Sulfoxidation	VRIFDPRMPESVNVL EEECCCCCCCCCCHH	5.41	21406390

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
8	S	Phosphorylation	Kinase	MAPK1	P28482	GPS
8	S	Phosphorylation	Kinase	MAPK3	P27361	GPS
606	S	Phosphorylation	Kinase	LATS2	Q9NRM7	PSP
606	S	Phosphorylation	Kinase	LATS1	O95835	PSP
696	S	Phosphorylation	Kinase	JNK1	P45983	PSP
696	S	Phosphorylation	Kinase	MAPK1	P28482	GPS
696	S	Phosphorylation	Kinase	MAPK3	P27361	GPS
696	S	Phosphorylation	Kinase	CDK1	P06493	PSP
706	T	Phosphorylation	Kinase	JNK1	P45983	PSP
706	T	Phosphorylation	Kinase	CDK1	P06493	PSP
719	S	Phosphorylation	Kinase	RSK-SUBFAMILY	-	GPS
719	S	Phosphorylation	Kinase	P90RSK	Q15418	PSP
719	S	Phosphorylation	Kinase	RPS6KA3	P51812	GPS
719	S	Phosphorylation	Kinase	RSK_GROUP	-	PhosphoELM
721	S	Phosphorylation	Kinase	DAPK2	Q9UIK4	PSP
721	S	Phosphorylation	Kinase	RSK-SUBFAMILY	-	GPS
721	S	Phosphorylation	Kinase	P90RSK	Q15418	PSP
721	S	Phosphorylation	Kinase	RPS6KA3	P51812	GPS
722	S	Phosphorylation	Kinase	AMPK-FAMILY	-	GPS
722	S	Phosphorylation	Kinase	RSK_GROUP	-	PhosphoELM
722	S	Phosphorylation	Kinase	RSK-SUBFAMILY	-	GPS
722	S	Phosphorylation	Kinase	AMPK	Q9Y478	Uniprot
722	S	Phosphorylation	Kinase	P90RSK	Q15418	PSP
722	S	Phosphorylation	Kinase	GSK3B	P49841	PSP
722	S	Phosphorylation	Kinase	PRKAA1	Q13131	GPS
722	S	Phosphorylation	Kinase	RPS6KA3	P51812	GPS
771	S	Phosphorylation	Kinase	MAPK11	Q15759	GPS
791	S	Phosphorylation	Kinase	PKACA	P17612	PSP
792	S	Phosphorylation	Kinase	ULK1	O75385	PSP
792	S	Phosphorylation	Kinase	AMPK	Q9Y478	Uniprot
792	S	Phosphorylation	Kinase	PRKAA1	Q13131	GPS
792	S	Phosphorylation	Kinase	GSK3B	P49841	PSP
792	S	Phosphorylation	Kinase	AMPK-FAMILY	-	GPS
792	S	Phosphorylation	Kinase	ULK2	Q8IYT8	PSP
855	S	Phosphorylation	Kinase	ULK1	O75385	PSP
855	S	Phosphorylation	Kinase	ULK2	Q8IYT8	PSP
859	S	Phosphorylation	Kinase	MTOR	P42345	Uniprot
859	S	Phosphorylation	Kinase	ULK1	O75385	PSP
859	S	Phosphorylation	Kinase	ULK2	Q8IYT8	PSP
859	S	Phosphorylation	Kinase	GSK3B	P49841	PSP
863	S	Phosphorylation	Kinase	MAPK1	P28482	GPS
863	S	Phosphorylation	Kinase	MTOR	P42345	Uniprot
863	S	Phosphorylation	Kinase	MAPK3	P27361	GPS
863	S	Phosphorylation	Kinase	GSK3B	P49841	PSP
863	S	Phosphorylation	Kinase	JNK1	P45983	PSP
863	S	Phosphorylation	Kinase	MAPK11	Q15759	GPS
863	S	Phosphorylation	Kinase	ULK1	O75385	PSP
863	S	Phosphorylation	Kinase	NLK	Q9UBE8	PSP
877	S	Phosphorylation	Kinase	GSK3B	P49841	PSP
877	S	Phosphorylation	Kinase	ULK1	O75385	PSP
908	T	Phosphorylation	Kinase	ICK	Q9UPZ9	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
696	S	Phosphorylation	19864431
Osmotic stress also induces phosphorylation at Ser-696, Thr-706 and Ser-863 by MAPK8.
706	T	Phosphorylation	19864431
Osmotic stress also induces phosphorylation at Ser-696, Thr-706 and Ser-863 by MAPK8.
719	S	Phosphorylation	18722121
In response to growth factors, phosphorylated at Ser-719, Ser-721 and Ser-722 by RPS6KA1, which stimulates mTORC1 activity.
721	S	Phosphorylation	18722121
In response to growth factors, phosphorylated at Ser-719, Ser-721 and Ser-722 by RPS6KA1, which stimulates mTORC1 activity.
722	S	Phosphorylation	18722121
In response to growth factors, phosphorylated at Ser-719, Ser-721 and Ser-722 by RPS6KA1, which stimulates mTORC1 activity.
855	S	Phosphorylation	19864431
Ser-863 phosphorylation is required for phosphorylation at Ser-855 and Ser-859.
859	S	Phosphorylation	18669648
Ser-863 phosphorylation is required for phosphorylation at Ser-855 and Ser-859.
863	S	Phosphorylation	16964243
Insulin-stimulated phosphorylation at Ser-863 by MTOR and MAPK8 up-regulates mTORC1 activity.
863	S	Phosphorylation	16964243
Osmotic stress also induces phosphorylation at Ser-696, Thr-706 and Ser-863 by MAPK8.
863	S	Phosphorylation	16964243
Ser-863 phosphorylation is required for phosphorylation at Ser-855 and Ser-859.

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of RPTOR_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
MTOR_HUMAN	MTOR	physical	15467718
MTOR_HUMAN	MTOR	physical	15268862
4EBP1_HUMAN	EIF4EBP1	physical	12747827
4EBP1_HUMAN	EIF4EBP1	physical	16837165
4EBP1_HUMAN	EIF4EBP1	physical	16824195
MTOR_HUMAN	MTOR	physical	12747827
MTOR_HUMAN	MTOR	physical	12150926
MTOR_HUMAN	MTOR	physical	16837165
MTOR_HUMAN	MTOR	physical	16798736
MTOR_HUMAN	MTOR	physical	16919458
MTOR_HUMAN	MTOR	physical	16631613
MTOR_HUMAN	MTOR	physical	16962653
PLD2_HUMAN	PLD2	physical	16837165
KS6B1_HUMAN	RPS6KB1	physical	15809305
KS6B1_HUMAN	RPS6KB1	physical	16837165
RHEB_MOUSE	Rheb	physical	16631613
RRAGA_HUMAN	RRAGA	physical	21816923
RRAGC_HUMAN	RRAGC	physical	21816923
MTOR_HUMAN	MTOR	physical	21045808
EIF3B_HUMAN	EIF3B	physical	21045808
RS6_HUMAN	RPS6	physical	21045808
RRAGB_HUMAN	RRAGB	physical	21981924
SQSTM_HUMAN	SQSTM1	physical	21981924
MK08_HUMAN	MAPK8	physical	22493283
MTOR_HUMAN	MTOR	physical	22493283
4EBP1_HUMAN	EIF4EBP1	physical	22493283
KS6B1_HUMAN	RPS6KB1	physical	22493283
MTOR_HUMAN	MTOR	physical	22356909
CCNB1_HUMAN	CCNB1	physical	20169205
MTOR_HUMAN	MTOR	physical	20169205
LST8_HUMAN	MLST8	physical	20169205
AKTS1_HUMAN	AKT1S1	physical	20169205
DPTOR_HUMAN	DEPTOR	physical	20169205
AKTS1_HUMAN	AKT1S1	physical	17386266
MTOR_HUMAN	MTOR	physical	17386266
IRS1_HUMAN	IRS1	physical	16354680
LST8_HUMAN	MLST8	physical	16798736
4EBP1_HUMAN	EIF4EBP1	physical	16798736
IF4E_HUMAN	EIF4E	physical	16798736
MTOR_HUMAN	MTOR	physical	21071439
KS6B1_HUMAN	RPS6KB1	physical	21071439
4EBP1_HUMAN	EIF4EBP1	physical	21071439
HSP74_HUMAN	HSPA4	physical	16962653
ULK1_HUMAN	ULK1	physical	21460630
MTOR_HUMAN	MTOR	physical	19145465
RICTR_HUMAN	RICTOR	physical	19145465
4EBP1_HUMAN	EIF4EBP1	physical	18722121
MTOR_HUMAN	MTOR	physical	18722121
4EBP1_HUMAN	EIF4EBP1	physical	12665511
IRS1_HUMAN	IRS1	physical	19561084
MTOR_HUMAN	MTOR	physical	21177249
MTOR_HUMAN	MTOR	physical	19875983
MTOR_HUMAN	MTOR	physical	23297343
CUL4A_HUMAN	CUL4A	physical	23297343
CUL4B_HUMAN	CUL4B	physical	23297343
DDB1_HUMAN	DDB1	physical	23297343
UCHL1_HUMAN	UCHL1	physical	23297343
4EBP1_HUMAN	EIF4EBP1	physical	18337751
MTOR_HUMAN	MTOR	physical	19446321
DPTOR_HUMAN	DEPTOR	physical	19446321
SIR1_HUMAN	SIRT1	physical	21471201
MTOR_HUMAN	MTOR	physical	17565979
PREX1_HUMAN	PREX1	physical	17565979
LST8_HUMAN	MLST8	physical	17565979
SYLC_HUMAN	LARS	physical	22424946
RRAGD_HUMAN	RRAGD	physical	22424946
RPTOR_HUMAN	RPTOR	physical	22424946
PDIA3_HUMAN	PDIA3	physical	21321085
MTOR_HUMAN	MTOR	physical	21321085
LST8_HUMAN	MLST8	physical	21321085
KS6B1_HUMAN	RPS6KB1	physical	23184942
MTOR_HUMAN	MTOR	physical	18505677
AMRA1_HUMAN	AMBRA1	physical	23524951
MTOR_HUMAN	MTOR	physical	24403073
RPTOR_HUMAN	RPTOR	physical	24403073
LST8_HUMAN	MLST8	physical	24403073
4EBP1_HUMAN	EIF4EBP1	physical	24403073
GBB1_HUMAN	GNB1	physical	24462769
RRAGC_HUMAN	RRAGC	physical	24337580
RRAGB_HUMAN	RRAGB	physical	24337580
MTOR_HUMAN	MTOR	physical	24337580
MTOR_HUMAN	MTOR	physical	18030348
AKTS1_HUMAN	AKT1S1	physical	18030348
IKKA_HUMAN	CHUK	physical	18519641
IKKB_HUMAN	IKBKB	physical	18519641
NEMO_HUMAN	IKBKG	physical	18519641
MTOR_HUMAN	MTOR	physical	18519641
MTOR_HUMAN	MTOR	physical	18570873
AKTS1_HUMAN	AKT1S1	physical	18570873
4EBP1_HUMAN	EIF4EBP1	physical	18955708
LST8_HUMAN	MLST8	physical	12408816
MTOR_HUMAN	MTOR	physical	12408816
KS6B1_HUMAN	RPS6KB1	physical	19402821
TF3C1_HUMAN	GTF3C1	physical	20543138
AKTS1_HUMAN	AKT1S1	physical	17277771
BAG3_HUMAN	BAG3	physical	26186194
FAF2_HUMAN	FAF2	physical	26186194
4EBP2_HUMAN	EIF4EBP2	physical	20347422
PDK1_HUMAN	PDK1	physical	24516643
MTOR_HUMAN	MTOR	physical	24516643
LST8_HUMAN	MLST8	physical	18030348
RAB1A_HUMAN	RAB1A	physical	25446900
ULK1_HUMAN	ULK1	physical	25686248
FAF2_HUMAN	FAF2	physical	28514442
BAG3_HUMAN	BAG3	physical	28514442
TCPH_HUMAN	CCT7	physical	28514442
KI13B_HUMAN	KIF13B	physical	27173435
CING_HUMAN	CGN	physical	27173435
SI1L1_HUMAN	SIPA1L1	physical	27173435
MAGI1_HUMAN	MAGI1	physical	27173435
TESK2_HUMAN	TESK2	physical	27173435
ESR1_HUMAN	ESR1	physical	26522726
MTOR_HUMAN	MTOR	physical	26522726
EP300_HUMAN	EP300	physical	29033323

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of RPTOR_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals 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). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-859; SER-863 ANDSER-877, AND MASS SPECTROMETRY.	19690332 [Abstract]
"Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-721; SER-722; SER-859;SER-863 AND SER-877, AND MASS SPECTROMETRY.	19369195 [Abstract]
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-722; SER-859; SER-863AND SER-877, AND MASS SPECTROMETRY.	19413330 [Abstract]
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-719; SER-722; SER-859;SER-863 AND SER-877, AND MASS SPECTROMETRY.	18669648 [Abstract]
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe 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). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-859; SER-863 ANDSER-877, AND MASS SPECTROMETRY.	18691976 [Abstract]
"AMPK phosphorylation of raptor mediates a metabolic checkpoint."; Gwinn D.M., Shackelford D.B., Egan D.F., Mihaylova M.M., Mery A.,Vasquez D.S., Turk B.E., Shaw R.J.; Mol. Cell 30:214-226(2008). Cited for: PHOSPHORYLATION AT SER-722 AND SER-792, MUTAGENESIS OF SER-722 ANDSER-792, AND INTERACTION WITH 14-3-3.	18439900 [Abstract]
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient 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). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-719 AND SER-722, ANDMASS SPECTROMETRY.	18220336 [Abstract]
"Oncogenic MAPK signaling stimulates mTORC1 activity by promoting RSK-mediated raptor phosphorylation."; Carriere A., Cargnello M., Julien L.A., Gao H., Bonneil E.,Thibault P., Roux P.P.; Curr. Biol. 18:1269-1277(2008). Cited for: PHOSPHORYLATION AT SER-719; SER-721 AND SER-722.	18722121 [Abstract]
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."; Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.; Anal. Sci. 24:161-166(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-863 AND THR-865, ANDMASS SPECTROMETRY.	18187866 [Abstract]

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