RHEB_HUMAN - dbPTM
RHEB_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RHEB_HUMAN
UniProt AC Q15382
Protein Name GTP-binding protein Rheb
Gene Name RHEB
Organism Homo sapiens (Human).
Sequence Length 184
Subcellular Localization Endomembrane system
Lipid-anchor
Cytoplasmic side . Golgi apparatus membrane
Lipid-anchor
Cytoplasmic side . Cytoplasm, cytosol . Endoplasmic reticulum membrane
Lipid-anchor
Cytoplasmic side .
Protein Description Activates the protein kinase activity of mTORC1, and thereby plays a role in the regulation of apoptosis. Stimulates the phosphorylation of S6K1 and EIF4EBP1 through activation of mTORC1 signaling. Has low intrinsic GTPase activity..
Protein Sequence MPQSKSRKIAILGYRSVGKSSLTIQFVEGQFVDSYDPTIENTFTKLITVNGQEYHLQLVDTAGQDEYSIFPQTYSIDINGYILVYSVTSIKSFEVIKVIHGKLLDMVGKVQIPIMLVGNKKDLHMERVISYEEGKALAESWNAAFLESSAKENQTAVDVFRRIILEAEKMDGAASQGKSSCSVM
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
14PhosphorylationRKIAILGYRSVGKSS
CCEEEECEEECCCCE
9.0328102081
16PhosphorylationIAILGYRSVGKSSLT
EEEECEEECCCCEEE
27.0925159151
102UbiquitinationVIKVIHGKLLDMVGK
EEEEECCHHHHHHCC
31.54-
109UbiquitinationKLLDMVGKVQIPIML
HHHHHHCCEEEEEEE
21.40-
120UbiquitinationPIMLVGNKKDLHMER
EEEEECCCCCCCEEE
41.5621890473
1202-HydroxyisobutyrylationPIMLVGNKKDLHMER
EEEEECCCCCCCEEE
41.56-
121UbiquitinationIMLVGNKKDLHMERV
EEEECCCCCCCEEEE
70.31-
1212-HydroxyisobutyrylationIMLVGNKKDLHMERV
EEEECCCCCCCEEEE
70.31-
130PhosphorylationLHMERVISYEEGKAL
CCEEEEEEHHHHHHH
24.5121336308
135UbiquitinationVISYEEGKALAESWN
EEEHHHHHHHHHHHH
43.4321890473
140PhosphorylationEGKALAESWNAAFLE
HHHHHHHHHHHHHHH
21.7420068231
151UbiquitinationAFLESSAKENQTAVD
HHHHHHHCCCHHHHH
60.1821890473
169UbiquitinationRIILEAEKMDGAASQ
HHHHHHHHHCCCHHC
49.7121890473
170SulfoxidationIILEAEKMDGAASQG
HHHHHHHHCCCHHCC
4.2928183972
175PhosphorylationEKMDGAASQGKSSCS
HHHCCCHHCCCCCCC
38.6429214152
181FarnesylationASQGKSSCSVM----
HHCCCCCCCCC----
4.6022002721
181FarnesylationASQGKSSCSVM----
HHCCCCCCCCC----
4.6022002721
181MethylationASQGKSSCSVM----
HHCCCCCCCCC----
4.6022002721

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
130SPhosphorylationKinaseMAPKAPK5Q8IW41
Uniprot
130SPhosphorylationKinaseMAPKAPK5O54992
PSP
-KUbiquitinationE3 ubiquitin ligaseRNF152Q8N8N0
PMID:32296023

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RHEB_HUMAN !!

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 RHEB_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TSC2_HUMANTSC2physical
12842888
ATM_HUMANATMphysical
15854902
ATR_HUMANATRphysical
15854902
MTOR_HUMANMTORphysical
15854902
MTOR_HUMANMTORphysical
15878852
MTOR_HUMANMTORphysical
15772076
MTOR_HUMANMTORphysical
16915281
RASH_HUMANHRASphysical
15854902
RAF1_HUMANRAF1physical
15854902
RAF1_HUMANRAF1physical
15150271
RAP1A_HUMANRAP1Aphysical
15854902
TSC2_HUMANTSC2physical
15854902
RAB7A_HUMANRAB7Aphysical
15809346
RAB9A_HUMANRAB9Aphysical
15809346
RPTOR_HUMANRPTORphysical
15854902
RAF1_HUMANRAF1physical
9001246
BNIP3_HUMANBNIP3physical
17928295
BNI3L_HUMANBNIP3Lphysical
17928295
PRAF1_HUMANRABAC1physical
17928295
DP13A_MOUSEAppl1physical
20368287
GO45_MOUSEBlzf1physical
20368287
TRAF2_HUMANTRAF2physical
20368287
TRAF2_MOUSETraf2physical
20368287
FKBP8_HUMANFKBP8physical
17991864
RPTOR_HUMANRPTORphysical
24337580
PLD1_HUMANPLD1physical
18550814
MTOR_HUMANMTORphysical
18550814
RPTOR_HUMANRPTORphysical
25446900
UBB_HUMANUBBphysical
28514442
LAMP2_HUMANLAMP2physical
28514442
SRPRB_HUMANSRPRBphysical
28514442
HD_HUMANHTTphysical
25351248
MTOR_HUMANMTORphysical
25351248

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 RHEB_HUMAN

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Related Literatures of Post-Translational Modification
Prenylation
ReferencePubMed
"A tagging-via-substrate technology for detection and proteomics offarnesylated proteins.";
Kho Y., Kim S.C., Jiang C., Barma D., Kwon S.W., Cheng J.,Jaunbergs J., Weinbaum C., Tamanoi F., Falck J., Zhao Y.;
Proc. Natl. Acad. Sci. U.S.A. 101:12479-12484(2004).
Cited for: ISOPRENYLATION AT CYS-181.

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