NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|21312878|ref|NP_080546|]
View 

proline-rich AKT1 substrate 1 isoform b [Mus musculus]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
PRAS super family cl24384
Proline-rich AKT1 substrate 1; This domain family is found in eukaryotes, and is typically ...
128-252 1.33e-46

Proline-rich AKT1 substrate 1; This domain family is found in eukaryotes, and is typically between 117 and 132 amino acids in length. PRAS domain family is found in eukaryotes, and is typically between 117 and 132 amino acids in length. It is a proline-rich family that can be phosphorylated by AKT, and in the phosphorylated state binds to 14-3-3. The AKT signalling pathway contributes to regulation of apoptosis after a variety of cell death stimuli, and PRAS is found to be a substrate. PRAS plays an important role in regulating cell survival downstream of the PI3-K/Akt pathway after re-perfusion injury after transient focal cerebral ischemia. Copper/zinc-SOD (SOD1), a cytosolic isoenzyme of superoxide dismutase, SOD, is highly protective against ischemia and re-perfusion injury after transient focal cerebral ischemia, and SOD1 thus contributes to the inhibition of direct oxidation of PRAS and the activation of its signalling pathway. PRAS is also a mTOR binding partner, and PRAS phosphorylation by AKT and its association with 14-3-3, a cytosolic anchor protein, are crucial for insulin to stimulate mTOR (mammalian target of rapamycin).


The actual alignment was detected with superfamily member pfam15798:

Pssm-ID: 406279  Cd Length: 123  Bit Score: 151.56  E-value: 1.33e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312878   128 GLFMMDEDATLQDLPPFCESD-PESTDDGSLSEETPAGPtacpQPPATALPtQQYAKSLPVSVPVWAFKEKRTEARSSDE 206
Cdd:pfam15798   1 GVFSMDEDSPSRDCEPFFESDgEEESTDGSLSEDAPPPS----RPFAQGHP-LQYARSLPVSVPVWGFKENRQSADQSDG 75
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 21312878   207 ENGP-PSSPDLDRIAASMRALVLREAED-TQVFGDLPRPRLNTSDFQK 252
Cdd:pfam15798  76 DEGErPGSADLEHIAASMKALLVPGATDgTEMFGDLPRPRLNTGDFSL 123
 
Name Accession Description Interval E-value
PRAS pfam15798
Proline-rich AKT1 substrate 1; This domain family is found in eukaryotes, and is typically ...
128-252 1.33e-46

Proline-rich AKT1 substrate 1; This domain family is found in eukaryotes, and is typically between 117 and 132 amino acids in length. PRAS domain family is found in eukaryotes, and is typically between 117 and 132 amino acids in length. It is a proline-rich family that can be phosphorylated by AKT, and in the phosphorylated state binds to 14-3-3. The AKT signalling pathway contributes to regulation of apoptosis after a variety of cell death stimuli, and PRAS is found to be a substrate. PRAS plays an important role in regulating cell survival downstream of the PI3-K/Akt pathway after re-perfusion injury after transient focal cerebral ischemia. Copper/zinc-SOD (SOD1), a cytosolic isoenzyme of superoxide dismutase, SOD, is highly protective against ischemia and re-perfusion injury after transient focal cerebral ischemia, and SOD1 thus contributes to the inhibition of direct oxidation of PRAS and the activation of its signalling pathway. PRAS is also a mTOR binding partner, and PRAS phosphorylation by AKT and its association with 14-3-3, a cytosolic anchor protein, are crucial for insulin to stimulate mTOR (mammalian target of rapamycin).


Pssm-ID: 406279  Cd Length: 123  Bit Score: 151.56  E-value: 1.33e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312878   128 GLFMMDEDATLQDLPPFCESD-PESTDDGSLSEETPAGPtacpQPPATALPtQQYAKSLPVSVPVWAFKEKRTEARSSDE 206
Cdd:pfam15798   1 GVFSMDEDSPSRDCEPFFESDgEEESTDGSLSEDAPPPS----RPFAQGHP-LQYARSLPVSVPVWGFKENRQSADQSDG 75
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 21312878   207 ENGP-PSSPDLDRIAASMRALVLREAED-TQVFGDLPRPRLNTSDFQK 252
Cdd:pfam15798  76 DEGErPGSADLEHIAASMKALLVPGATDgTEMFGDLPRPRLNTGDFSL 123
 
Name Accession Description Interval E-value
PRAS pfam15798
Proline-rich AKT1 substrate 1; This domain family is found in eukaryotes, and is typically ...
128-252 1.33e-46

Proline-rich AKT1 substrate 1; This domain family is found in eukaryotes, and is typically between 117 and 132 amino acids in length. PRAS domain family is found in eukaryotes, and is typically between 117 and 132 amino acids in length. It is a proline-rich family that can be phosphorylated by AKT, and in the phosphorylated state binds to 14-3-3. The AKT signalling pathway contributes to regulation of apoptosis after a variety of cell death stimuli, and PRAS is found to be a substrate. PRAS plays an important role in regulating cell survival downstream of the PI3-K/Akt pathway after re-perfusion injury after transient focal cerebral ischemia. Copper/zinc-SOD (SOD1), a cytosolic isoenzyme of superoxide dismutase, SOD, is highly protective against ischemia and re-perfusion injury after transient focal cerebral ischemia, and SOD1 thus contributes to the inhibition of direct oxidation of PRAS and the activation of its signalling pathway. PRAS is also a mTOR binding partner, and PRAS phosphorylation by AKT and its association with 14-3-3, a cytosolic anchor protein, are crucial for insulin to stimulate mTOR (mammalian target of rapamycin).


Pssm-ID: 406279  Cd Length: 123  Bit Score: 151.56  E-value: 1.33e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312878   128 GLFMMDEDATLQDLPPFCESD-PESTDDGSLSEETPAGPtacpQPPATALPtQQYAKSLPVSVPVWAFKEKRTEARSSDE 206
Cdd:pfam15798   1 GVFSMDEDSPSRDCEPFFESDgEEESTDGSLSEDAPPPS----RPFAQGHP-LQYARSLPVSVPVWGFKENRQSADQSDG 75
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 21312878   207 ENGP-PSSPDLDRIAASMRALVLREAED-TQVFGDLPRPRLNTSDFQK 252
Cdd:pfam15798  76 DEGErPGSADLEHIAASMKALLVPGATDgTEMFGDLPRPRLNTGDFSL 123
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH