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Conserved domains on  [gi|767952816|ref|XP_011515265|]
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mdm2-binding protein isoform X2 [Homo sapiens]

Protein Classification

MTBP_N and MTBP_mid domain-containing protein( domain architecture ID 10633035)

MTBP_N and MTBP_mid domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MTBP_N pfam14918
MDM2-binding; MTBP, or MDM2-binding protein, binds to MDM2. The MDM2 protein, through its ...
 1-270 9.84e-158

MDM2-binding; MTBP, or MDM2-binding protein, binds to MDM2. The MDM2 protein, through its interaction with p53, plays an important role in the regulation of the G1 checkpoint of the cell cycle. MTBP promotes MDM2-mediated ubiquitination and degradation of p53 and also MDM2 stabilization in an MDM2 RING finger-dependent manner. MTBP differentially regulates the E3 ubiquitin ligase activity of MDM2 towards two of its most critical targets (itself and p53) and in doing so significantly contributes to MDM2-dependent p53 homeostasis in unstressed cells. MTBP inhibits cancer cell migration by interacting with a protein involved in cell motility. This motility protein is alpha-actinin-4 (ACTN4). It is unclear which regions of MTBP interact with which binding-partner. See PF14919, PF14920.


:

Pssm-ID: 464374  Cd Length: 254  Bit Score: 447.65  E-value: 9.84e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952816    1 MDRYLLLVIWgegkfpsaasrEAEHGPEVSSGEGTENQPdftaANVYHLLKRSISASINPEDSTFPACSVGGIPGSKKWF 80
Cdd:pfam14918   1 MDRYVLLIIW-----------ERRFDGEFSSFSGLEETP----ENVYELLKRISTVSSNKYDSTFPACSLTGIPGSRKWF 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952816   81 FAVQAIYGFYQFCSSDWQEIHFDTEKDKIEDVLQTNIEECLGAVECFEEEDSNSRESLSLADLYEEAAENLHQLSDKLPA 160
Cdd:pfam14918  66 FAVQAICGSFQFCSSDWEELHFDSEKDDIEESLQTALEECLSALQCQEEEDSNSRESLSLTDLFEEAAENLHQLSDKLPA 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952816  161 PGRAMVDIILLLSDKDPPKLKDYLPTVGALKHLREWYSAKITIAGNHCEInCQKIAEYLSANVVSLEDLRNVIDSKELWR 240
Cdd:pfam14918 146 PGRAMLDVILLCSEPDTPKLKDCLPLIGALKHLKEWHSAKITIVTNHCEG-WQKIAGYLSATVVSLSDIKSCIDSRELWR 224

                         250       260       270
                  ....*....|....*....|....*....|
gi 767952816  241 GKIQIWERKFGFEISFPEFCLKGVTLKNFS 270
Cdd:pfam14918 225 GKIQIWERKFGSEVSFPEFCLRQVSPEKFL 254
MTBP_mid super family cl20805
MDM2-binding; MTBP, or MDM2-binding protein, binds to MDM2. The MDM2 protein, through its ...
 294-484 1.01e-128

MDM2-binding; MTBP, or MDM2-binding protein, binds to MDM2. The MDM2 protein, through its interaction with p53, plays an important role in the regulation of the G1 checkpoint of the cell cycle. MTBP promotes MDM2-mediated ubiquitination and degradation of p53 and also MDM2 stabilization in an MDM2 RING finger-dependent manner. MTBP differentially regulates the E3 ubiquitin ligase activity of MDM2 towards two of its most critical targets (itself and p53) and in doing so significantly contributes to MDM2-dependent p53 homeostasis in unstressed cells. MTBP inhibits cancer cell migration by interacting with a protein involved in cell motility. This motility protein is alpha-actinin-4 (ACTN4). It is unclear which regions of MTBP interact with which binding-partner. See PF14918, PF14920.


The actual alignment was detected with superfamily member pfam14919:

Pssm-ID: 464375  Cd Length: 336  Bit Score: 377.05  E-value: 1.01e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952816  294 KVFHYYGPALEFVQMIKLSDLPSCYMSDIEFELGLT-NSTKQNSVLLLEQISSLCSKVGALFVLPCTISNILIPPPNQLS 372
Cdd:pfam14919   1 EVFHYYGPVLDFVQMVKLSDLPSFLMSDSEFELGLTrNNKSQKSKLLLDQLSSLRGKVGALFSLPCTVSNIAIPPASQLS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952816  373 SRKWKEYIAKKPKTISVPDVEVKGECSSYYLLLQGNGNRRCKATLIHSANQINGSFALNLIHGKMKTKTEEAKLSFPFD- 451
Cdd:pfam14919  81 SRKWKEYMAKKPKSISVPDVEVKGESASYYLLVQGNGSGGCKATLLHSASQINGAAALATIHGKLLRETEEASSGFPVDn 160

                         170       180       190
                  ....*....|....*....|....*....|....
gi 767952816  452 -LLSLPHFSGEQIVQREKQLANVQVLALEECLKS 484
Cdd:pfam14919 161 fLRSLPCLSGEQLVQRERKLAQVQALALKEYLRR 194
 
Name Accession Description Interval E-value
MTBP_N pfam14918
MDM2-binding; MTBP, or MDM2-binding protein, binds to MDM2. The MDM2 protein, through its ...
 1-270 9.84e-158

MDM2-binding; MTBP, or MDM2-binding protein, binds to MDM2. The MDM2 protein, through its interaction with p53, plays an important role in the regulation of the G1 checkpoint of the cell cycle. MTBP promotes MDM2-mediated ubiquitination and degradation of p53 and also MDM2 stabilization in an MDM2 RING finger-dependent manner. MTBP differentially regulates the E3 ubiquitin ligase activity of MDM2 towards two of its most critical targets (itself and p53) and in doing so significantly contributes to MDM2-dependent p53 homeostasis in unstressed cells. MTBP inhibits cancer cell migration by interacting with a protein involved in cell motility. This motility protein is alpha-actinin-4 (ACTN4). It is unclear which regions of MTBP interact with which binding-partner. See PF14919, PF14920.


Pssm-ID: 464374  Cd Length: 254  Bit Score: 447.65  E-value: 9.84e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952816    1 MDRYLLLVIWgegkfpsaasrEAEHGPEVSSGEGTENQPdftaANVYHLLKRSISASINPEDSTFPACSVGGIPGSKKWF 80
Cdd:pfam14918   1 MDRYVLLIIW-----------ERRFDGEFSSFSGLEETP----ENVYELLKRISTVSSNKYDSTFPACSLTGIPGSRKWF 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952816   81 FAVQAIYGFYQFCSSDWQEIHFDTEKDKIEDVLQTNIEECLGAVECFEEEDSNSRESLSLADLYEEAAENLHQLSDKLPA 160
Cdd:pfam14918  66 FAVQAICGSFQFCSSDWEELHFDSEKDDIEESLQTALEECLSALQCQEEEDSNSRESLSLTDLFEEAAENLHQLSDKLPA 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952816  161 PGRAMVDIILLLSDKDPPKLKDYLPTVGALKHLREWYSAKITIAGNHCEInCQKIAEYLSANVVSLEDLRNVIDSKELWR 240
Cdd:pfam14918 146 PGRAMLDVILLCSEPDTPKLKDCLPLIGALKHLKEWHSAKITIVTNHCEG-WQKIAGYLSATVVSLSDIKSCIDSRELWR 224

                         250       260       270
                  ....*....|....*....|....*....|
gi 767952816  241 GKIQIWERKFGFEISFPEFCLKGVTLKNFS 270
Cdd:pfam14918 225 GKIQIWERKFGSEVSFPEFCLRQVSPEKFL 254
MTBP_mid pfam14919
MDM2-binding; MTBP, or MDM2-binding protein, binds to MDM2. The MDM2 protein, through its ...
 294-484 1.01e-128

MDM2-binding; MTBP, or MDM2-binding protein, binds to MDM2. The MDM2 protein, through its interaction with p53, plays an important role in the regulation of the G1 checkpoint of the cell cycle. MTBP promotes MDM2-mediated ubiquitination and degradation of p53 and also MDM2 stabilization in an MDM2 RING finger-dependent manner. MTBP differentially regulates the E3 ubiquitin ligase activity of MDM2 towards two of its most critical targets (itself and p53) and in doing so significantly contributes to MDM2-dependent p53 homeostasis in unstressed cells. MTBP inhibits cancer cell migration by interacting with a protein involved in cell motility. This motility protein is alpha-actinin-4 (ACTN4). It is unclear which regions of MTBP interact with which binding-partner. See PF14918, PF14920.


Pssm-ID: 464375  Cd Length: 336  Bit Score: 377.05  E-value: 1.01e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952816  294 KVFHYYGPALEFVQMIKLSDLPSCYMSDIEFELGLT-NSTKQNSVLLLEQISSLCSKVGALFVLPCTISNILIPPPNQLS 372
Cdd:pfam14919   1 EVFHYYGPVLDFVQMVKLSDLPSFLMSDSEFELGLTrNNKSQKSKLLLDQLSSLRGKVGALFSLPCTVSNIAIPPASQLS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952816  373 SRKWKEYIAKKPKTISVPDVEVKGECSSYYLLLQGNGNRRCKATLIHSANQINGSFALNLIHGKMKTKTEEAKLSFPFD- 451
Cdd:pfam14919  81 SRKWKEYMAKKPKSISVPDVEVKGESASYYLLVQGNGSGGCKATLLHSASQINGAAALATIHGKLLRETEEASSGFPVDn 160

                         170       180       190
                  ....*....|....*....|....*....|....
gi 767952816  452 -LLSLPHFSGEQIVQREKQLANVQVLALEECLKS 484
Cdd:pfam14919 161 fLRSLPCLSGEQLVQRERKLAQVQALALKEYLRR 194
 
Name Accession Description Interval E-value
MTBP_N pfam14918
MDM2-binding; MTBP, or MDM2-binding protein, binds to MDM2. The MDM2 protein, through its ...
 1-270 9.84e-158

MDM2-binding; MTBP, or MDM2-binding protein, binds to MDM2. The MDM2 protein, through its interaction with p53, plays an important role in the regulation of the G1 checkpoint of the cell cycle. MTBP promotes MDM2-mediated ubiquitination and degradation of p53 and also MDM2 stabilization in an MDM2 RING finger-dependent manner. MTBP differentially regulates the E3 ubiquitin ligase activity of MDM2 towards two of its most critical targets (itself and p53) and in doing so significantly contributes to MDM2-dependent p53 homeostasis in unstressed cells. MTBP inhibits cancer cell migration by interacting with a protein involved in cell motility. This motility protein is alpha-actinin-4 (ACTN4). It is unclear which regions of MTBP interact with which binding-partner. See PF14919, PF14920.


Pssm-ID: 464374  Cd Length: 254  Bit Score: 447.65  E-value: 9.84e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952816    1 MDRYLLLVIWgegkfpsaasrEAEHGPEVSSGEGTENQPdftaANVYHLLKRSISASINPEDSTFPACSVGGIPGSKKWF 80
Cdd:pfam14918   1 MDRYVLLIIW-----------ERRFDGEFSSFSGLEETP----ENVYELLKRISTVSSNKYDSTFPACSLTGIPGSRKWF 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952816   81 FAVQAIYGFYQFCSSDWQEIHFDTEKDKIEDVLQTNIEECLGAVECFEEEDSNSRESLSLADLYEEAAENLHQLSDKLPA 160
Cdd:pfam14918  66 FAVQAICGSFQFCSSDWEELHFDSEKDDIEESLQTALEECLSALQCQEEEDSNSRESLSLTDLFEEAAENLHQLSDKLPA 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952816  161 PGRAMVDIILLLSDKDPPKLKDYLPTVGALKHLREWYSAKITIAGNHCEInCQKIAEYLSANVVSLEDLRNVIDSKELWR 240
Cdd:pfam14918 146 PGRAMLDVILLCSEPDTPKLKDCLPLIGALKHLKEWHSAKITIVTNHCEG-WQKIAGYLSATVVSLSDIKSCIDSRELWR 224

                         250       260       270
                  ....*....|....*....|....*....|
gi 767952816  241 GKIQIWERKFGFEISFPEFCLKGVTLKNFS 270
Cdd:pfam14918 225 GKIQIWERKFGSEVSFPEFCLRQVSPEKFL 254
MTBP_mid pfam14919
MDM2-binding; MTBP, or MDM2-binding protein, binds to MDM2. The MDM2 protein, through its ...
 294-484 1.01e-128

MDM2-binding; MTBP, or MDM2-binding protein, binds to MDM2. The MDM2 protein, through its interaction with p53, plays an important role in the regulation of the G1 checkpoint of the cell cycle. MTBP promotes MDM2-mediated ubiquitination and degradation of p53 and also MDM2 stabilization in an MDM2 RING finger-dependent manner. MTBP differentially regulates the E3 ubiquitin ligase activity of MDM2 towards two of its most critical targets (itself and p53) and in doing so significantly contributes to MDM2-dependent p53 homeostasis in unstressed cells. MTBP inhibits cancer cell migration by interacting with a protein involved in cell motility. This motility protein is alpha-actinin-4 (ACTN4). It is unclear which regions of MTBP interact with which binding-partner. See PF14918, PF14920.


Pssm-ID: 464375  Cd Length: 336  Bit Score: 377.05  E-value: 1.01e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952816  294 KVFHYYGPALEFVQMIKLSDLPSCYMSDIEFELGLT-NSTKQNSVLLLEQISSLCSKVGALFVLPCTISNILIPPPNQLS 372
Cdd:pfam14919   1 EVFHYYGPVLDFVQMVKLSDLPSFLMSDSEFELGLTrNNKSQKSKLLLDQLSSLRGKVGALFSLPCTVSNIAIPPASQLS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767952816  373 SRKWKEYIAKKPKTISVPDVEVKGECSSYYLLLQGNGNRRCKATLIHSANQINGSFALNLIHGKMKTKTEEAKLSFPFD- 451
Cdd:pfam14919  81 SRKWKEYMAKKPKSISVPDVEVKGESASYYLLVQGNGSGGCKATLLHSASQINGAAALATIHGKLLRETEEASSGFPVDn 160

                         170       180       190
                  ....*....|....*....|....*....|....
gi 767952816  452 -LLSLPHFSGEQIVQREKQLANVQVLALEECLKS 484
Cdd:pfam14919 161 fLRSLPCLSGEQLVQRERKLAQVQALALKEYLRR 194
 
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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