Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
ASCOP2B SuperfamilyFKBP12-rapamycin-binding domain of FKBP-rapamycin-associated protein (FRAP)8036936 3001600 SCOP2B (2022-06-29)
BSCOP2B SuperfamilyFKBP12-rapamycin-binding domain of FKBP-rapamycin-associated protein (FRAP)8036936 3001600 SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
CPF00400e6zwmC1 A: beta duplicates or obligate multimersX: beta-propeller-likeH: beta-propellerT: 7-bladedF: PF00400ECOD (1.6)
DPF00400e6zwmD1 A: beta duplicates or obligate multimersX: beta-propeller-likeH: beta-propellerT: 7-bladedF: PF00400ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
A, B
PF02260FATC domain (FATC)FATC domain- Family
A, B
PF08771FKBP12-rapamycin binding domain (FRB_dom)FKBP12-rapamycin binding domainThe macrolide antibiotic rapamycin and the cytosol protein FKBP12 can form a complex which specifically inhibits the TORC1 complex, leading to growth arrest. The FKBP12-rapamycin complex interferes with TORC1 function by binding to the FKBP12-rapa ...The macrolide antibiotic rapamycin and the cytosol protein FKBP12 can form a complex which specifically inhibits the TORC1 complex, leading to growth arrest. The FKBP12-rapamycin complex interferes with TORC1 function by binding to the FKBP12-rapamycin binding domain (FRB) of the TOR proteins. This entry represents the FRB domain [1, 2].
Domain
A, B
PF00454Phosphatidylinositol 3- and 4-kinase (PI3_PI4_kinase)Phosphatidylinositol 3- and 4-kinase- Family
A, B
PF11865Domain of unknown function (DUF3385) (DUF3385)Domain of unknown function (DUF3385)- Repeat
A, B
PF02259FAT domain (FAT)FAT domain- Repeat
C, D
PF00400WD domain, G-beta repeat (WD40)WD domain, G-beta repeat- Repeat
E, F
PF14663Rapamycin-insensitive companion of mTOR RasGEF_N domain (RasGEF_N_2)Rapamycin-insensitive companion of mTOR RasGEF_N domainRictor appears to serve as a scaffolding protein that is important for maintaining mTORC2 integrity. The mammalian target of rapamycin (mTOR) is a conserved Ser/Thr kinase that forms two functionally distinct complexes, mTROC1 and mTORC2, important f ...Rictor appears to serve as a scaffolding protein that is important for maintaining mTORC2 integrity. The mammalian target of rapamycin (mTOR) is a conserved Ser/Thr kinase that forms two functionally distinct complexes, mTROC1 and mTORC2, important for nutrient and growth-factor signalling. This region is the more conserved central section that may include several individual domains. Rictor can be inhibited in the short-term by rapamycin.
Domain
E, F
PF14664Rapamycin-insensitive companion of mTOR, N-term (RICTOR_N)Rapamycin-insensitive companion of mTOR, N-termRictor appears to serve as a scaffolding protein that is important for maintaining mTORC2 integrity. The mammalian target of rapamycin (mTOR) is a conserved Ser/Thr kinase that forms two functionally distinct complexes, mTROC1 and mTORC2, important f ...Rictor appears to serve as a scaffolding protein that is important for maintaining mTORC2 integrity. The mammalian target of rapamycin (mTOR) is a conserved Ser/Thr kinase that forms two functionally distinct complexes, mTROC1 and mTORC2, important for nutrient and growth-factor signalling. This region is the N-terminal conserved section that may include several individual domains. Rictor can be inhibited in the short-term by rapamycin.
Domain
E, F
PF14666Rapamycin-insensitive companion of mTOR, middle domain (RICTOR_M)Rapamycin-insensitive companion of mTOR, middle domainRictor appears to serve as a scaffolding protein that is important for maintaining mTORC2 integrity. The mammalian target of rapamycin (mTOR) is a conserved Ser/Thr kinase that forms two functionally distinct complexes, mTROC1 and mTORC2, important f ...Rictor appears to serve as a scaffolding protein that is important for maintaining mTORC2 integrity. The mammalian target of rapamycin (mTOR) is a conserved Ser/Thr kinase that forms two functionally distinct complexes, mTROC1 and mTORC2, important for nutrient and growth-factor signalling. This region is the more conserved central section that may include several individual domains. Rictor can be inhibited in the short-term by rapamycin.
Domain
E, F
PF14668Rapamycin-insensitive companion of mTOR, domain 5 (RICTOR_V)Rapamycin-insensitive companion of mTOR, domain 5Rictor appears to serve as a scaffolding protein that is important for maintaining mTORC2 integrity. The mammalian target of rapamycin (mTOR) is a conserved Ser/Thr kinase that forms two functionally distinct complexes, mTROC1 and mTORC2, important f ...Rictor appears to serve as a scaffolding protein that is important for maintaining mTORC2 integrity. The mammalian target of rapamycin (mTOR) is a conserved Ser/Thr kinase that forms two functionally distinct complexes, mTROC1 and mTORC2, important for nutrient and growth-factor signalling. These long eukaryotic proteins carry several well-conserved domains, and this is No.5.
Domain
G, H
PF05422Stress-activated map kinase interacting protein 1 (SIN1) (SIN1)Stress-activated map kinase interacting protein 1 (SIN1)- Family
G, H
PF16978SAPK-interacting protein 1 (Sin1), middle CRIM domain (CRIM)SAPK-interacting protein 1 (Sin1), middle CRIM domain- Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
A, B
Serine/threonine-protein kinase mTOR
C, D
Target of rapamycin complex subunit LST8
E, F
Rapamycin-insensitive companion of mTOR
G, H
Target of rapamycin complex 2 subunit MAPKAP1

InterPro: Protein Family Classification InterPro Database Homepage

ChainsAccessionNameType
A, B
IPR016024Armadillo-type foldHomologous Superfamily
A, B
IPR009076FKBP12-rapamycin binding domainDomain
A, B
IPR011990Tetratricopeptide-like helical domain superfamilyHomologous Superfamily
A, B
IPR018936Phosphatidylinositol 3/4-kinase, conserved siteConserved Site
A, B
IPR036940Phosphatidylinositol 3-/4-kinase, catalytic domain superfamilyHomologous Superfamily
A, B
IPR014009PIK-related kinaseDomain
A, B
IPR026683Serine/threonine-protein kinase TOR, catalytic domainDomain
A, B
IPR003151PIK-related kinase, FATDomain
A, B
IPR036738FKBP12-rapamycin binding domain superfamilyHomologous Superfamily
A, B
IPR003152FATC domainDomain
A, B
IPR024585Serine/threonine-protein kinase mTOR domainDomain
A, B
IPR011989Armadillo-like helicalHomologous Superfamily
A, B
IPR000403Phosphatidylinositol 3-/4-kinase, catalytic domainDomain
A, B
IPR011009Protein kinase-like domain superfamilyHomologous Superfamily
C, D
IPR019775WD40 repeat, conserved siteConserved Site
C, D
IPR011047Quinoprotein alcohol dehydrogenase-like superfamilyHomologous Superfamily
C, D
IPR015943WD40/YVTN repeat-like-containing domain superfamilyHomologous Superfamily
C, D
IPR001680WD40 repeatRepeat
C, D
IPR037588Target of rapamycin complex subunit LST8Family
C, D
IPR020472G-protein beta WD-40 repeatRepeat
E, F
IPR028267Rapamycin-insensitive companion of mTOR, N-terminal domainDomain
E, F
IPR029451Rapamycin-insensitive companion of mTOR, middle domainDomain
E, F
IPR016024Armadillo-type foldHomologous Superfamily
E, F
IPR029259Rapamycin-insensitive companion of mTOR, phosphorylation-sitePTM
E, F
IPR029453Rapamycin-insensitive companion of mTOR, domain 4Domain
E, F
IPR029452Rapamycin-insensitive companion of mTOR, domain 5Domain
E, F
IPR028268Pianissimo familyFamily
G, H
IPR032679Sin1, N-terminalDomain
G, H
IPR031313SAPK-interacting protein 1, Pleckstrin-homology domainDomain
G, H
IPR011993PH-like domain superfamilyHomologous Superfamily
G, H
IPR031567Sin1, middle CRIM domainDomain
G, H
IPR008828TORC2 component Sin1/Avo1Family

Pharos: Disease Associations Pharos Homepage Annotation

ChainsDrug Target  Associated Disease
A, B
PharosP42345
C, D
PharosQ9BVC4
E, F
PharosQ6R327
G, H
PharosQ9BPZ7