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Conserved domains on  [gi|323668328|ref|NP_001191120|]
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tumor protein p73 isoform g [Homo sapiens]

Protein Classification

P53 and P53_tetramer domain-containing protein( domain architecture ID 10170144)

protein containing domains P53, P53_tetramer, and SAM_superfamily

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
P53 cd08367
P53 DNA-binding domain; P53 is a tumor suppressor gene product; mutations in p53 or lack of ...
 78-257 2.57e-99

P53 DNA-binding domain; P53 is a tumor suppressor gene product; mutations in p53 or lack of expression are found associated with a large fraction of all human cancers. P53 is activated by DNA damage and acts as a regulator of gene expression that ultimatively blocks progression through the cell cycle. P53 binds to DNA as a tetrameric transcription factor. In its inactive form, p53 is bound to the ring finger protein Mdm2, which promotes its ubiquitinylation and subsequent proteosomal degradation. Phosphorylation of p53 disrupts the Mdm2-p53 complex, while the stable and active p53 binds to regulatory regions of its target genes, such as the cyclin-kinase inhibitor p21, which complexes and inactivates cdk2 and other cyclin complexes.


:

Pssm-ID: 176262  Cd Length: 179  Bit Score: 296.10  E-value: 2.57e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323668328  78 FEVTFQQSSTAKSATWTYSPLLKKLYCQIAKTCPIQIKVSTPPPPGTAIRAMPVYKKAEHVTDVVKRCPNHELGRDfneG 157
Cdd:cd08367    1 FEVTLDESGVAKSSTWTYSPKLNKLFVKMAKTCPIQFKVNPSPPPGLYVRAMLVYKDPEHVKEPVERCPNHRQGDD---G 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323668328 158 QSAPASHLIRVEgNNLSQYVDDPVTGRQSVVVPYEPPQVGTEFTTILYNFMCNSSCVGGMNRRPILIIITLEMRDGQVLG 237
Cdd:cd08367   78 HTAPNSHVIRCE-NPQAEYVGDAFTGRLSVVVPLEPPQVGSEYVTVLLQFMCQNSCPGGINRRPIQLVFTLEDENGNVLG 156

                        170       180
                 ....*....|....*....|
gi 323668328 238 RRSFEGRICACPGRDRKADE 257
Cdd:cd08367  157 RRVIEVRVCACPGRDRKNEE 176
SAM_superfamily super family cl15755
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 351-406 2.71e-38

SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of approximately 70 amino acids. This domain is found in the Fungi/Metazoa group and in a restricted number of bacteria. Proteins with SAM domains are represented by a wide variety of domain architectures and have different intracellular localization, including nucleus, cytoplasm and membranes. SAM domains have diverse functions. They can interact with proteins, RNAs and membrane lipids, contain site of phosphorylation and/or kinase docking site, and play a role in protein homo and hetero dimerization/oligomerization in processes ranging from signal transduction to regulation of transcription. Mutations in SAM domains have been linked to several diseases.


The actual alignment was detected with superfamily member cd09571:

Pssm-ID: 472832  Cd Length: 65  Bit Score: 133.94  E-value: 2.71e-38
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 323668328 351 FLTGLGCPNCIEYFTSQGLQSIYHLQNLTIEDLGALKIPEQYRMTIWRGLQDLKQG 406
Cdd:cd09571   10 FLTGLGCPNCIDYFTSQGLQSIYHLQNLTIEDLGALKIPEQYRMAIWRGLQELKQG 65
P53_tetramer pfam07710
P53 tetramerization motif;
296-335 6.80e-17

P53 tetramerization motif;


:

Pssm-ID: 462238  Cd Length: 42  Bit Score: 74.24  E-value: 6.80e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 323668328  296 KKRRHGDEDTYYLQVRGRENFEILMKLKESLELMELVPQP 335
Cdd:pfam07710   2 KRPLSSDEEEFTLPVRGRENYEMLKKIKESLELLDMVPQS 41
 
Name Accession Description Interval E-value
P53 cd08367
P53 DNA-binding domain; P53 is a tumor suppressor gene product; mutations in p53 or lack of ...
 78-257 2.57e-99

P53 DNA-binding domain; P53 is a tumor suppressor gene product; mutations in p53 or lack of expression are found associated with a large fraction of all human cancers. P53 is activated by DNA damage and acts as a regulator of gene expression that ultimatively blocks progression through the cell cycle. P53 binds to DNA as a tetrameric transcription factor. In its inactive form, p53 is bound to the ring finger protein Mdm2, which promotes its ubiquitinylation and subsequent proteosomal degradation. Phosphorylation of p53 disrupts the Mdm2-p53 complex, while the stable and active p53 binds to regulatory regions of its target genes, such as the cyclin-kinase inhibitor p21, which complexes and inactivates cdk2 and other cyclin complexes.


Pssm-ID: 176262  Cd Length: 179  Bit Score: 296.10  E-value: 2.57e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323668328  78 FEVTFQQSSTAKSATWTYSPLLKKLYCQIAKTCPIQIKVSTPPPPGTAIRAMPVYKKAEHVTDVVKRCPNHELGRDfneG 157
Cdd:cd08367    1 FEVTLDESGVAKSSTWTYSPKLNKLFVKMAKTCPIQFKVNPSPPPGLYVRAMLVYKDPEHVKEPVERCPNHRQGDD---G 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323668328 158 QSAPASHLIRVEgNNLSQYVDDPVTGRQSVVVPYEPPQVGTEFTTILYNFMCNSSCVGGMNRRPILIIITLEMRDGQVLG 237
Cdd:cd08367   78 HTAPNSHVIRCE-NPQAEYVGDAFTGRLSVVVPLEPPQVGSEYVTVLLQFMCQNSCPGGINRRPIQLVFTLEDENGNVLG 156

                        170       180
                 ....*....|....*....|
gi 323668328 238 RRSFEGRICACPGRDRKADE 257
Cdd:cd08367  157 RRVIEVRVCACPGRDRKNEE 176
P53 pfam00870
P53 DNA-binding domain; This family contains one anomalous member, viz: Zea mays (Q6JAD8). ...
 68-260 7.55e-92

P53 DNA-binding domain; This family contains one anomalous member, viz: Zea mays (Q6JAD8). This sequence is identical to human P53 and would appear to be a a human contaminant within the Zea mays sampling effort.


Pssm-ID: 459972 [Multi-domain]  Cd Length: 191  Bit Score: 277.63  E-value: 7.55e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323668328   68 SNTDYPGPHHFEVTFQQSSTAKSATWTYSPLLKKLYCQIAKTCPIQIKVSTPPPPGTAIRAMPVYKKAEHVTDVVKRCPN 147
Cdd:pfam00870   1 SEEDYPGSLNFNVLLDESKEAKKSSWTYSPKLNKLFVKMNKSCPFNFKTDPPPPPGLYIRAMLVYSKSEHANDPVERCPN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323668328  148 HELGRDFNEGQSAPasHLIRVEgNNLSQYV-DDPVTGRQSVVVPYEPPQVGTEFTTILYNFMCNSSCVGGMNRRPILIII 226
Cdd:pfam00870  81 HRAKDDGNNDPIRE--HVIRCE-NPDAEYVgTDEGDERLSVVVPLEHPQAGSESVTLLLKFMCKSSCPGGINRRPTALVF 157

                         170       180       190
                  ....*....|....*....|....*....|....
gi 323668328  227 TLEMRDGQVLGRRSFEGRICACPGRDRKADEDHY 260
Cdd:pfam00870 158 TLEDPDGQVLGRQSISVKVCSCPKRDRRKEEKAL 191
SAM_tumor-p73 cd09571
SAM domain of tumor-p73 proteins; SAM (sterile alpha motif) domain of p73 proteins is a ...
 351-406 2.71e-38

SAM domain of tumor-p73 proteins; SAM (sterile alpha motif) domain of p73 proteins is a putative protein-protein interaction and lipid-binding domain. p73 is a homolog to the tumor suppressor p53. p73 has a C-terminal SAM domain in the longest spliced alpha form, while p53 doesn't have it. p73 knockout mouse shows significant developmental abnormalities but no increased cancer susceptibility, suggesting that p73 plays a role in regulation of normal development. It was shown that SAM domain of p73 is able to bind some membrane lipids. The structural rearrangements in SAM are necessary to accomplish the binding. No evidence for homooligomerization through SAM domains was found for the p73 subfamily. It was suggested that the partner proteins should be either more distantly related SAM-containing domain proteins or proteins without the SAM domain.


Pssm-ID: 188970  Cd Length: 65  Bit Score: 133.94  E-value: 2.71e-38
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 323668328 351 FLTGLGCPNCIEYFTSQGLQSIYHLQNLTIEDLGALKIPEQYRMTIWRGLQDLKQG 406
Cdd:cd09571   10 FLTGLGCPNCIDYFTSQGLQSIYHLQNLTIEDLGALKIPEQYRMAIWRGLQELKQG 65
P53_tetramer pfam07710
P53 tetramerization motif;
296-335 6.80e-17

P53 tetramerization motif;


Pssm-ID: 462238  Cd Length: 42  Bit Score: 74.24  E-value: 6.80e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 323668328  296 KKRRHGDEDTYYLQVRGRENFEILMKLKESLELMELVPQP 335
Cdd:pfam07710   2 KRPLSSDEEEFTLPVRGRENYEMLKKIKESLELLDMVPQS 41
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
351-404 1.62e-09

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 53.81  E-value: 1.62e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 323668328  351 FLTGLGCPNCIEYFTSQGLQSIYHLQNLTIEDLGALKIPEQY-RMTIWRGLQDLK 404
Cdd:pfam07647  12 WLRSIGLEQYTDNFRDQGITGAELLLRLTLEDLKRLGITSVGhRRKILKKIQELK 66
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 351-405 7.41e-05

Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.


Pssm-ID: 197735  Cd Length: 68  Bit Score: 40.74  E-value: 7.41e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 323668328   351 FLTGLGCPNCIEYFTSQGLQSIYHLQNLTIEDLGALKI-PEQYRMTIWRGLQDLKQ 405
Cdd:smart00454  12 WLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGItKLGHRKKILKAIQKLKE 67
 
Name Accession Description Interval E-value
P53 cd08367
P53 DNA-binding domain; P53 is a tumor suppressor gene product; mutations in p53 or lack of ...
 78-257 2.57e-99

P53 DNA-binding domain; P53 is a tumor suppressor gene product; mutations in p53 or lack of expression are found associated with a large fraction of all human cancers. P53 is activated by DNA damage and acts as a regulator of gene expression that ultimatively blocks progression through the cell cycle. P53 binds to DNA as a tetrameric transcription factor. In its inactive form, p53 is bound to the ring finger protein Mdm2, which promotes its ubiquitinylation and subsequent proteosomal degradation. Phosphorylation of p53 disrupts the Mdm2-p53 complex, while the stable and active p53 binds to regulatory regions of its target genes, such as the cyclin-kinase inhibitor p21, which complexes and inactivates cdk2 and other cyclin complexes.


Pssm-ID: 176262  Cd Length: 179  Bit Score: 296.10  E-value: 2.57e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323668328  78 FEVTFQQSSTAKSATWTYSPLLKKLYCQIAKTCPIQIKVSTPPPPGTAIRAMPVYKKAEHVTDVVKRCPNHELGRDfneG 157
Cdd:cd08367    1 FEVTLDESGVAKSSTWTYSPKLNKLFVKMAKTCPIQFKVNPSPPPGLYVRAMLVYKDPEHVKEPVERCPNHRQGDD---G 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323668328 158 QSAPASHLIRVEgNNLSQYVDDPVTGRQSVVVPYEPPQVGTEFTTILYNFMCNSSCVGGMNRRPILIIITLEMRDGQVLG 237
Cdd:cd08367   78 HTAPNSHVIRCE-NPQAEYVGDAFTGRLSVVVPLEPPQVGSEYVTVLLQFMCQNSCPGGINRRPIQLVFTLEDENGNVLG 156

                        170       180
                 ....*....|....*....|
gi 323668328 238 RRSFEGRICACPGRDRKADE 257
Cdd:cd08367  157 RRVIEVRVCACPGRDRKNEE 176
P53 pfam00870
P53 DNA-binding domain; This family contains one anomalous member, viz: Zea mays (Q6JAD8). ...
 68-260 7.55e-92

P53 DNA-binding domain; This family contains one anomalous member, viz: Zea mays (Q6JAD8). This sequence is identical to human P53 and would appear to be a a human contaminant within the Zea mays sampling effort.


Pssm-ID: 459972 [Multi-domain]  Cd Length: 191  Bit Score: 277.63  E-value: 7.55e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323668328   68 SNTDYPGPHHFEVTFQQSSTAKSATWTYSPLLKKLYCQIAKTCPIQIKVSTPPPPGTAIRAMPVYKKAEHVTDVVKRCPN 147
Cdd:pfam00870   1 SEEDYPGSLNFNVLLDESKEAKKSSWTYSPKLNKLFVKMNKSCPFNFKTDPPPPPGLYIRAMLVYSKSEHANDPVERCPN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323668328  148 HELGRDFNEGQSAPasHLIRVEgNNLSQYV-DDPVTGRQSVVVPYEPPQVGTEFTTILYNFMCNSSCVGGMNRRPILIII 226
Cdd:pfam00870  81 HRAKDDGNNDPIRE--HVIRCE-NPDAEYVgTDEGDERLSVVVPLEHPQAGSESVTLLLKFMCKSSCPGGINRRPTALVF 157

                         170       180       190
                  ....*....|....*....|....*....|....
gi 323668328  227 TLEMRDGQVLGRRSFEGRICACPGRDRKADEDHY 260
Cdd:pfam00870 158 TLEDPDGQVLGRQSISVKVCSCPKRDRRKEEKAL 191
SAM_tumor-p73 cd09571
SAM domain of tumor-p73 proteins; SAM (sterile alpha motif) domain of p73 proteins is a ...
 351-406 2.71e-38

SAM domain of tumor-p73 proteins; SAM (sterile alpha motif) domain of p73 proteins is a putative protein-protein interaction and lipid-binding domain. p73 is a homolog to the tumor suppressor p53. p73 has a C-terminal SAM domain in the longest spliced alpha form, while p53 doesn't have it. p73 knockout mouse shows significant developmental abnormalities but no increased cancer susceptibility, suggesting that p73 plays a role in regulation of normal development. It was shown that SAM domain of p73 is able to bind some membrane lipids. The structural rearrangements in SAM are necessary to accomplish the binding. No evidence for homooligomerization through SAM domains was found for the p73 subfamily. It was suggested that the partner proteins should be either more distantly related SAM-containing domain proteins or proteins without the SAM domain.


Pssm-ID: 188970  Cd Length: 65  Bit Score: 133.94  E-value: 2.71e-38
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 323668328 351 FLTGLGCPNCIEYFTSQGLQSIYHLQNLTIEDLGALKIPEQYRMTIWRGLQDLKQG 406
Cdd:cd09571   10 FLTGLGCPNCIDYFTSQGLQSIYHLQNLTIEDLGALKIPEQYRMAIWRGLQELKQG 65
SAM_tumor-p63,p73 cd09503
SAM domain of tumor-p63,p73 proteins; SAM (sterile alpha motif) domain of p63, p73 ...
 351-406 9.99e-28

SAM domain of tumor-p63,p73 proteins; SAM (sterile alpha motif) domain of p63, p73 transcriptional factors is a putative protein-protein interaction domain and lipid-binding domain. p63 and p73 are homologs to the tumor suppressor p53. They have a C-terminal SAM domain in their longest spliced alpha forms, while p53 doesn't have it. p63 or p73 knockout mice show significant developmental abnormalities but no increased cancer susceptibility, suggesting that p63 and p73 play a role in regulation of normal development. It was shown that SAM domain of p73 is able to bind some membrane lipids. The structural rearrangements in SAM are necessary to accomplish the binding. No evidence for homooligomerization through SAM domains was found for p63/p73 subfamily. It was suggested that the partner proteins should be either more distantly related SAM-containing domain proteins or proteins without the SAM domain.


Pssm-ID: 188902  Cd Length: 65  Bit Score: 105.09  E-value: 9.99e-28
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 323668328 351 FLTGLGCPNCIEYFTSQGLQSIYHLQNLTIEDLGALKIPEQYRMTIWRGLQDLKQG 406
Cdd:cd09503   10 WLTKLGCSNYIDNFHQQGLLSIFQLDEFTLEDLAAMKIPEQHRNKIWKGLLEYRQA 65
SAM_tumor-p63 cd09572
SAM domain of tumor-p63 proteins; SAM (sterile alpha motif) domain of p63 proteins is a ...
 351-405 8.93e-18

SAM domain of tumor-p63 proteins; SAM (sterile alpha motif) domain of p63 proteins is a putative protein-protein interaction domain. p63 is homolog to the tumor suppressor p53. p63 has a C-terminal SAM domain in the longest spliced alpha form, while p53 doesn't have it. p63 knockout mice show significant developmental abnormalities but no increased cancer susceptibility, suggesting that p63 plays a role in regulation of normal development. No evidence for homooligomerization through SAM domains was found for the p63 subfamily. It was suggested that the partner proteins should be either more distantly related SAM-containing domain proteins or proteins without the SAM domain. Mutations in the SAM domain of p63 are found in AEC syndrome patients.


Pssm-ID: 188971  Cd Length: 65  Bit Score: 77.32  E-value: 8.93e-18
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 323668328 351 FLTGLGCPNCIEYFTSQGLQSIYHLQNLTIEDLGALKIPEQYRMTIWRGLQDLKQ 405
Cdd:cd09572   10 FLARLGCSSCLDYFTTQGLTTIYQIEHYSMDDLSSLKIPEQFRHAIWKGILDHRQ 64
P53_tetramer pfam07710
P53 tetramerization motif;
296-335 6.80e-17

P53 tetramerization motif;


Pssm-ID: 462238  Cd Length: 42  Bit Score: 74.24  E-value: 6.80e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 323668328  296 KKRRHGDEDTYYLQVRGRENFEILMKLKESLELMELVPQP 335
Cdd:pfam07710   2 KRPLSSDEEEFTLPVRGRENYEMLKKIKESLELLDMVPQS 41
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
351-404 1.62e-09

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 53.81  E-value: 1.62e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 323668328  351 FLTGLGCPNCIEYFTSQGLQSIYHLQNLTIEDLGALKIPEQY-RMTIWRGLQDLK 404
Cdd:pfam07647  12 WLRSIGLEQYTDNFRDQGITGAELLLRLTLEDLKRLGITSVGhRRKILKKIQELK 66
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 351-405 7.41e-05

Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.


Pssm-ID: 197735  Cd Length: 68  Bit Score: 40.74  E-value: 7.41e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 323668328   351 FLTGLGCPNCIEYFTSQGLQSIYHLQNLTIEDLGALKI-PEQYRMTIWRGLQDLKQ 405
Cdd:smart00454  12 WLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGItKLGHRKKILKAIQKLKE 67
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 351-402 6.44e-04

SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of approximately 70 amino acids. This domain is found in the Fungi/Metazoa group and in a restricted number of bacteria. Proteins with SAM domains are represented by a wide variety of domain architectures and have different intracellular localization, including nucleus, cytoplasm and membranes. SAM domains have diverse functions. They can interact with proteins, RNAs and membrane lipids, contain site of phosphorylation and/or kinase docking site, and play a role in protein homo and hetero dimerization/oligomerization in processes ranging from signal transduction to regulation of transcription. Mutations in SAM domains have been linked to several diseases.


Pssm-ID: 188886 [Multi-domain]  Cd Length: 56  Bit Score: 37.60  E-value: 6.44e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 323668328 351 FLTGLGCPNCIEYFTSQGLqSIYHLQNLTIEDLGALKI-PEQYRMTIWRGLQD 402
Cdd:cd09487    5 WLESLGLEQYADLFRKNEI-DGDALLLLTDEDLKELGItSPGHRKKILRAIQR 56
 
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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