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Conserved domains on  [gi|2462494358|ref|XP_054186750|]
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phostensin isoform X1 [Homo sapiens]

Protein Classification

Phostensin_N and Phostensin domain-containing protein( domain architecture ID 10621602)

Phostensin_N and Phostensin domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Phostensin pfam13914
Phostensin PP1-binding and SH3-binding region; Phostensin has been identified as a PP1 ...
 523-628 1.20e-35

Phostensin PP1-binding and SH3-binding region; Phostensin has been identified as a PP1 regulatory protein binding PP1 at the KISF motif. The domain also appears to carry an incomplete incomplete SH3-binding domain PxRxP further upstream. It is likely that Phostensin targets PP1 to the F-actin cytoskeleton. Phostensin binds to actin and decreases the elongation and depolymerization rates of actin filament pointed ends.


:

Pssm-ID: 464038 [Multi-domain]  Cd Length: 138  Bit Score: 131.22  E-value: 1.20e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462494358 523 GVKAGPGVGAPR-------RSGHTFTVNPRR----------SVPPATPATPTSPAT----VDAAVPGAGKKRYPTAEEIL 581
Cdd:pfam13914  14 PLQYFPHPGGPShsselqhRGGNTFTVVPRRkpgglqsqanSEPPSQPTAEEEEAPslvgPDATLGGTLKKRYPTVHEIE 93

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2462494358 582 VLGGYLRLSRSCLAKGSPERhhKQLKISFSETALETTYQYPSESSVL 628
Cdd:pfam13914  94 VIGGYLALDKSCLVKAGSSR--KKMKISFNEKSLETTFEYPSESSLL 138
Phostensin_N pfam13916
PP1-regulatory protein, Phostensin N-terminal; Phostensin has been identified as a PP1 ...
 96-184 2.21e-16

PP1-regulatory protein, Phostensin N-terminal; Phostensin has been identified as a PP1 regulatory protein binding protein. This domain is N-terminal to the PP1- and SH3-binding regions though may carry an additional SH3-binding motif. It is likely that Phostensin targets PP1 to the F-actin cytoskeleton. Phostensin binds to actin and decreases the elongation and depolymerization rates of actin filament pointed ends.


:

Pssm-ID: 464039  Cd Length: 84  Bit Score: 74.49  E-value: 2.21e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462494358  96 AERERLSqMPAWKRGLLERRRAKLGLSPGEPSPVlgtvEAGPPDPDESAVLLEAIGPVHQNRFIRQERQQQQQQQQRSEE 175
Cdd:pfam13916   1 GPGPRTA-MPAWKREILERRRAKLAALGGGAGPG----AAEPAGPDERLVLAESLGPLHENPFMRLESERRRQGQAPAQQ 75


                  ....*....
gi 2462494358 176 LLAERKPGP 184
Cdd:pfam13916  76 LLEDYRRVP 84
 
Name Accession Description Interval E-value
Phostensin pfam13914
Phostensin PP1-binding and SH3-binding region; Phostensin has been identified as a PP1 ...
 523-628 1.20e-35

Phostensin PP1-binding and SH3-binding region; Phostensin has been identified as a PP1 regulatory protein binding PP1 at the KISF motif. The domain also appears to carry an incomplete incomplete SH3-binding domain PxRxP further upstream. It is likely that Phostensin targets PP1 to the F-actin cytoskeleton. Phostensin binds to actin and decreases the elongation and depolymerization rates of actin filament pointed ends.


Pssm-ID: 464038 [Multi-domain]  Cd Length: 138  Bit Score: 131.22  E-value: 1.20e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462494358 523 GVKAGPGVGAPR-------RSGHTFTVNPRR----------SVPPATPATPTSPAT----VDAAVPGAGKKRYPTAEEIL 581
Cdd:pfam13914  14 PLQYFPHPGGPShsselqhRGGNTFTVVPRRkpgglqsqanSEPPSQPTAEEEEAPslvgPDATLGGTLKKRYPTVHEIE 93

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2462494358 582 VLGGYLRLSRSCLAKGSPERhhKQLKISFSETALETTYQYPSESSVL 628
Cdd:pfam13914  94 VIGGYLALDKSCLVKAGSSR--KKMKISFNEKSLETTFEYPSESSLL 138
Phostensin_N pfam13916
PP1-regulatory protein, Phostensin N-terminal; Phostensin has been identified as a PP1 ...
 96-184 2.21e-16

PP1-regulatory protein, Phostensin N-terminal; Phostensin has been identified as a PP1 regulatory protein binding protein. This domain is N-terminal to the PP1- and SH3-binding regions though may carry an additional SH3-binding motif. It is likely that Phostensin targets PP1 to the F-actin cytoskeleton. Phostensin binds to actin and decreases the elongation and depolymerization rates of actin filament pointed ends.


Pssm-ID: 464039  Cd Length: 84  Bit Score: 74.49  E-value: 2.21e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462494358  96 AERERLSqMPAWKRGLLERRRAKLGLSPGEPSPVlgtvEAGPPDPDESAVLLEAIGPVHQNRFIRQERQQQQQQQQRSEE 175
Cdd:pfam13916   1 GPGPRTA-MPAWKREILERRRAKLAALGGGAGPG----AAEPAGPDERLVLAESLGPLHENPFMRLESERRRQGQAPAQQ 75


                  ....*....
gi 2462494358 176 LLAERKPGP 184
Cdd:pfam13916  76 LLEDYRRVP 84
 
Name Accession Description Interval E-value
Phostensin pfam13914
Phostensin PP1-binding and SH3-binding region; Phostensin has been identified as a PP1 ...
 523-628 1.20e-35

Phostensin PP1-binding and SH3-binding region; Phostensin has been identified as a PP1 regulatory protein binding PP1 at the KISF motif. The domain also appears to carry an incomplete incomplete SH3-binding domain PxRxP further upstream. It is likely that Phostensin targets PP1 to the F-actin cytoskeleton. Phostensin binds to actin and decreases the elongation and depolymerization rates of actin filament pointed ends.


Pssm-ID: 464038 [Multi-domain]  Cd Length: 138  Bit Score: 131.22  E-value: 1.20e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462494358 523 GVKAGPGVGAPR-------RSGHTFTVNPRR----------SVPPATPATPTSPAT----VDAAVPGAGKKRYPTAEEIL 581
Cdd:pfam13914  14 PLQYFPHPGGPShsselqhRGGNTFTVVPRRkpgglqsqanSEPPSQPTAEEEEAPslvgPDATLGGTLKKRYPTVHEIE 93

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2462494358 582 VLGGYLRLSRSCLAKGSPERhhKQLKISFSETALETTYQYPSESSVL 628
Cdd:pfam13914  94 VIGGYLALDKSCLVKAGSSR--KKMKISFNEKSLETTFEYPSESSLL 138
Phostensin_N pfam13916
PP1-regulatory protein, Phostensin N-terminal; Phostensin has been identified as a PP1 ...
 96-184 2.21e-16

PP1-regulatory protein, Phostensin N-terminal; Phostensin has been identified as a PP1 regulatory protein binding protein. This domain is N-terminal to the PP1- and SH3-binding regions though may carry an additional SH3-binding motif. It is likely that Phostensin targets PP1 to the F-actin cytoskeleton. Phostensin binds to actin and decreases the elongation and depolymerization rates of actin filament pointed ends.


Pssm-ID: 464039  Cd Length: 84  Bit Score: 74.49  E-value: 2.21e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462494358  96 AERERLSqMPAWKRGLLERRRAKLGLSPGEPSPVlgtvEAGPPDPDESAVLLEAIGPVHQNRFIRQERQQQQQQQQRSEE 175
Cdd:pfam13916   1 GPGPRTA-MPAWKREILERRRAKLAALGGGAGPG----AAEPAGPDERLVLAESLGPLHENPFMRLESERRRQGQAPAQQ 75


                  ....*....
gi 2462494358 176 LLAERKPGP 184
Cdd:pfam13916  76 LLEDYRRVP 84
 
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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