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Conserved domains on  [gi|29243970|ref|NP_808271|]
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GSK-3-binding protein FRAT2 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
GSK-3_bind super family cl05090
Glycogen synthase kinase-3 binding; Glycogen synthase kinase-3 (GSK-3) sequentially ...
1-209 4.92e-80

Glycogen synthase kinase-3 binding; Glycogen synthase kinase-3 (GSK-3) sequentially phosphorylates four serine residues on glycogen synthase (GS), in the sequence SxxxSxxxSxxx-SxxxS(p), by recognising and phosphorylating the first serine in the sequence motif SxxxS(P) (where S(p) represents a phosphoserine). Interaction of GSK-3 with a peptide derived from GSK-3 binding protein (this family) prevents GSK-3 interaction with Axin. This interaction thereby inhibits the Axin-dependent phosphorylation of beta-catenin by GSK-3.


The actual alignment was detected with superfamily member pfam05350:

Pssm-ID: 428435  Cd Length: 237  Bit Score: 239.85  E-value: 4.92e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243970     1 MPCRREEEEEAGDEAEGEEDDDSFLLLQQSVTLGGSTDVDRLIVQIGETLQLDTAHDRPASPCAAPGPPPAPPRVLAALS 80
Cdd:pfam05350   1 MPCRREEEEEAGEEAEGEEEDDSFLLLQQSVTLGSSGEVDRLVAQIGETLQLDAAQDSPASPCAPPGPPLRPPRPLAAVP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243970    81 ADKTGTPARRLLRPTGSAETGDPAPPGAVRCVLGERGRVRGRSAPYCVAEIAPGASALP--------------------- 139
Cdd:pfam05350  81 ADKARSPARPLLLPPASAETGGPAPPGALRCALGDRGRVRGRAAPYCVAELAAGPSALSplppqpgldgppgagkqgipq 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 29243970   140 ---GPGRRGWLPGSVASHRIQQRRWTAGGARAADDDPHRLLQQLVLSGNLIKEAVRRLQRAVAAVAATSPASA 209
Cdd:pfam05350 161 plsGPCRRGWLRGAAASRRLQQRRGSQPETRTGDDDPHRLLQQLVLSGNLIKEAVRRLHSRRLQLHAKLPQHP 233
 
Name Accession Description Interval E-value
GSK-3_bind pfam05350
Glycogen synthase kinase-3 binding; Glycogen synthase kinase-3 (GSK-3) sequentially ...
1-209 4.92e-80

Glycogen synthase kinase-3 binding; Glycogen synthase kinase-3 (GSK-3) sequentially phosphorylates four serine residues on glycogen synthase (GS), in the sequence SxxxSxxxSxxx-SxxxS(p), by recognising and phosphorylating the first serine in the sequence motif SxxxS(P) (where S(p) represents a phosphoserine). Interaction of GSK-3 with a peptide derived from GSK-3 binding protein (this family) prevents GSK-3 interaction with Axin. This interaction thereby inhibits the Axin-dependent phosphorylation of beta-catenin by GSK-3.


Pssm-ID: 428435  Cd Length: 237  Bit Score: 239.85  E-value: 4.92e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243970     1 MPCRREEEEEAGDEAEGEEDDDSFLLLQQSVTLGGSTDVDRLIVQIGETLQLDTAHDRPASPCAAPGPPPAPPRVLAALS 80
Cdd:pfam05350   1 MPCRREEEEEAGEEAEGEEEDDSFLLLQQSVTLGSSGEVDRLVAQIGETLQLDAAQDSPASPCAPPGPPLRPPRPLAAVP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243970    81 ADKTGTPARRLLRPTGSAETGDPAPPGAVRCVLGERGRVRGRSAPYCVAEIAPGASALP--------------------- 139
Cdd:pfam05350  81 ADKARSPARPLLLPPASAETGGPAPPGALRCALGDRGRVRGRAAPYCVAELAAGPSALSplppqpgldgppgagkqgipq 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 29243970   140 ---GPGRRGWLPGSVASHRIQQRRWTAGGARAADDDPHRLLQQLVLSGNLIKEAVRRLQRAVAAVAATSPASA 209
Cdd:pfam05350 161 plsGPCRRGWLRGAAASRRLQQRRGSQPETRTGDDDPHRLLQQLVLSGNLIKEAVRRLHSRRLQLHAKLPQHP 233
 
Name Accession Description Interval E-value
GSK-3_bind pfam05350
Glycogen synthase kinase-3 binding; Glycogen synthase kinase-3 (GSK-3) sequentially ...
1-209 4.92e-80

Glycogen synthase kinase-3 binding; Glycogen synthase kinase-3 (GSK-3) sequentially phosphorylates four serine residues on glycogen synthase (GS), in the sequence SxxxSxxxSxxx-SxxxS(p), by recognising and phosphorylating the first serine in the sequence motif SxxxS(P) (where S(p) represents a phosphoserine). Interaction of GSK-3 with a peptide derived from GSK-3 binding protein (this family) prevents GSK-3 interaction with Axin. This interaction thereby inhibits the Axin-dependent phosphorylation of beta-catenin by GSK-3.


Pssm-ID: 428435  Cd Length: 237  Bit Score: 239.85  E-value: 4.92e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243970     1 MPCRREEEEEAGDEAEGEEDDDSFLLLQQSVTLGGSTDVDRLIVQIGETLQLDTAHDRPASPCAAPGPPPAPPRVLAALS 80
Cdd:pfam05350   1 MPCRREEEEEAGEEAEGEEEDDSFLLLQQSVTLGSSGEVDRLVAQIGETLQLDAAQDSPASPCAPPGPPLRPPRPLAAVP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29243970    81 ADKTGTPARRLLRPTGSAETGDPAPPGAVRCVLGERGRVRGRSAPYCVAEIAPGASALP--------------------- 139
Cdd:pfam05350  81 ADKARSPARPLLLPPASAETGGPAPPGALRCALGDRGRVRGRAAPYCVAELAAGPSALSplppqpgldgppgagkqgipq 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 29243970   140 ---GPGRRGWLPGSVASHRIQQRRWTAGGARAADDDPHRLLQQLVLSGNLIKEAVRRLQRAVAAVAATSPASA 209
Cdd:pfam05350 161 plsGPCRRGWLRGAAASRRLQQRRGSQPETRTGDDDPHRLLQQLVLSGNLIKEAVRRLHSRRLQLHAKLPQHP 233
 
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.
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