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Conserved domains on  [gi|1734342231|ref|NP_001359465|]
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protein C-ets-1 isoform 5 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Ets1_N_flank pfam19525
Ets1 N-terminal flanking region of Ets domain; Ets1 is a member of the Ets family of ...
 80-267 1.55e-129

Ets1 N-terminal flanking region of Ets domain; Ets1 is a member of the Ets family of transcription factors in which the DNA-binding activity is in an autoinhibited state. The autoinhibition of Ets1 is mediated by structural coupling of the regions flanking the Ets domain. The inhibitory regions are folded as helices HI1 and HI2 N-terminal to the ETS domain and as H4 C-terminal to the ETS domain, which are packed together to form an inhibitory module. This domain represents the N-terminal flanking region of Ets domain which contains the residues forming HI1 and HI2 helices and additional residues(244-301) N-terminal to HI1. HI1 and HI2 exert the autoinhibitory function by directing the inhibitory residues N-terminal to HI1 to mask the Ets domain DNA-binding surface. These residues are flexible and function by masking the DNA-binding surface of the Ets domain. Phosphorylation of serine residues present in this region enhances autoinhibition dramatically. These inhibitory sequences are required for cooperative DNA binding.


:

Pssm-ID: 466113  Cd Length: 188  Bit Score: 368.93  E-value: 1.55e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734342231  80 PTYPESCYTSDYFISYGIEHAQCVPPSEFSEPSFITESYQTLHPISSEELLSLKYENDYPSVILQDPLQTDTLQTDYFAI 159
Cdd:pfam19525   1 TTYPESRYTSDYFISYGIEHAQCVPPSEFSEPSFITESYQTLHPISSEELLSLKYENDYPSVILRDPPQTDALQTDYFSI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734342231 160 KQEVLTPDNMCLGRASRGKLGGQDSFESVESYDSCDRLTQSWSSQSSFNSLQRVPSYDSFDYEDYPAALPNHKPKGTFKD 239
Cdd:pfam19525  81 KQEVVTPDNMCMGRASRGKLGGQDSFESIESYDSCDRLTQSWSSQSSFQSLQRVPSYDSFDSEDYPAALPSHKPKGTFKD 160

                         170       180
                  ....*....|....*....|....*...
gi 1734342231 240 YVRDRADLNKDKPVIPAAALAGYTGSGP 267
Cdd:pfam19525 161 YVRDRADLNKDKPVIPAAALAGYTGRMM 188
ETS smart00413
erythroblast transformation specific domain; variation of the helix-turn-helix motif
 267-351 4.38e-50

erythroblast transformation specific domain; variation of the helix-turn-helix motif


:

Pssm-ID: 197710  Cd Length: 87  Bit Score: 162.82  E-value: 4.38e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734342231  267 PIQLWQFLLELLTDKSCQSFISWTG-DGWEFKLSDPDEVARRWGKRKNKPKMNYEKLSRGLRYYYDKNIIHKTAGKRYVY 345
Cdd:smart00413   1 GIQLWQFLLDLLLDPENSDIIKWTDrDEGEFKLVDPEEVARLWGQRKNKPNMNYEKLSRALRYYYKKNILEKVPGKRLVY 80


                   ....*.
gi 1734342231  346 RFVCDL 351
Cdd:smart00413  81 KFVKNP 86
SAM_superfamily super family cl15755
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 51-68 1.40e-05

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 cd08542:

Pssm-ID: 472832  Cd Length: 88  Bit Score: 43.05  E-value: 1.40e-05
                          10
                  ....*....|....*...
gi 1734342231  51 ATFSGFTKEQQRLGIPKE 68
Cdd:cd08542     1 ATFSGFTKEQQRLGIPKD 18
 
Name Accession Description Interval E-value
Ets1_N_flank pfam19525
Ets1 N-terminal flanking region of Ets domain; Ets1 is a member of the Ets family of ...
 80-267 1.55e-129

Ets1 N-terminal flanking region of Ets domain; Ets1 is a member of the Ets family of transcription factors in which the DNA-binding activity is in an autoinhibited state. The autoinhibition of Ets1 is mediated by structural coupling of the regions flanking the Ets domain. The inhibitory regions are folded as helices HI1 and HI2 N-terminal to the ETS domain and as H4 C-terminal to the ETS domain, which are packed together to form an inhibitory module. This domain represents the N-terminal flanking region of Ets domain which contains the residues forming HI1 and HI2 helices and additional residues(244-301) N-terminal to HI1. HI1 and HI2 exert the autoinhibitory function by directing the inhibitory residues N-terminal to HI1 to mask the Ets domain DNA-binding surface. These residues are flexible and function by masking the DNA-binding surface of the Ets domain. Phosphorylation of serine residues present in this region enhances autoinhibition dramatically. These inhibitory sequences are required for cooperative DNA binding.


Pssm-ID: 466113  Cd Length: 188  Bit Score: 368.93  E-value: 1.55e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734342231  80 PTYPESCYTSDYFISYGIEHAQCVPPSEFSEPSFITESYQTLHPISSEELLSLKYENDYPSVILQDPLQTDTLQTDYFAI 159
Cdd:pfam19525   1 TTYPESRYTSDYFISYGIEHAQCVPPSEFSEPSFITESYQTLHPISSEELLSLKYENDYPSVILRDPPQTDALQTDYFSI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734342231 160 KQEVLTPDNMCLGRASRGKLGGQDSFESVESYDSCDRLTQSWSSQSSFNSLQRVPSYDSFDYEDYPAALPNHKPKGTFKD 239
Cdd:pfam19525  81 KQEVVTPDNMCMGRASRGKLGGQDSFESIESYDSCDRLTQSWSSQSSFQSLQRVPSYDSFDSEDYPAALPSHKPKGTFKD 160

                         170       180
                  ....*....|....*....|....*...
gi 1734342231 240 YVRDRADLNKDKPVIPAAALAGYTGSGP 267
Cdd:pfam19525 161 YVRDRADLNKDKPVIPAAALAGYTGRMM 188
ETS smart00413
erythroblast transformation specific domain; variation of the helix-turn-helix motif
 267-351 4.38e-50

erythroblast transformation specific domain; variation of the helix-turn-helix motif


Pssm-ID: 197710  Cd Length: 87  Bit Score: 162.82  E-value: 4.38e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734342231  267 PIQLWQFLLELLTDKSCQSFISWTG-DGWEFKLSDPDEVARRWGKRKNKPKMNYEKLSRGLRYYYDKNIIHKTAGKRYVY 345
Cdd:smart00413   1 GIQLWQFLLDLLLDPENSDIIKWTDrDEGEFKLVDPEEVARLWGQRKNKPNMNYEKLSRALRYYYKKNILEKVPGKRLVY 80


                   ....*.
gi 1734342231  346 RFVCDL 351
Cdd:smart00413  81 KFVKNP 86
Ets pfam00178
Ets-domain;
269-347 2.00e-46

Ets-domain;


Pssm-ID: 459700  Cd Length: 80  Bit Score: 153.04  E-value: 2.00e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734342231 269 QLWQFLLELLTDKSCQSFISWT-GDGWEFKLSDPDEVARRWGKRKNKPKMNYEKLSRGLRYYYDKNIIHKTAGKRYVYRF 347
Cdd:pfam00178   1 QLWQFLLDLLTDPEYSDIIKWTdKEEGEFRLVDPEAVARLWGKRKGNPKMTYEKLSRALRYYYKKGILEKVPGKRLTYRF 80
SAM_PNT-ETS-1 cd08542
Sterile alpha motif (SAM)/Pointed domain of ETS-1; SAM Pointed domain of ETS-1 subfamily of ...
 51-68 1.40e-05

Sterile alpha motif (SAM)/Pointed domain of ETS-1; SAM Pointed domain of ETS-1 subfamily of ETS transcriptional activators is a protein-protein interaction domain. The ETS-1 activator is regulated by phosphorylation. It contains a docking site for the ERK2 MAP (Mitogen Activated Protein) kinase, while the ERK2 phosphorylation site is located in the N-terminal disordered region upstream of the SAM Pointed domain. Mutations of the kinase docking site residues inhibit phosphorylation. ETS-1 activators play a role in a number of different physiological processes, and they are expressed during embryonic development, including blood vessel formation, hematopoietic, lymphoid, neuronal and osteogenic differentiation. The Ets-1 gene is a proto-oncogene involved in progression of different tumors (including breast cancer, meningioma, and prostate cancer). Members of this subfamily are potential molecular targets for selective cancer therapy.


Pssm-ID: 176092  Cd Length: 88  Bit Score: 43.05  E-value: 1.40e-05
                          10
                  ....*....|....*...
gi 1734342231  51 ATFSGFTKEQQRLGIPKE 68
Cdd:cd08542     1 ATFSGFTKEQQRLGIPKD 18
 
Name Accession Description Interval E-value
Ets1_N_flank pfam19525
Ets1 N-terminal flanking region of Ets domain; Ets1 is a member of the Ets family of ...
 80-267 1.55e-129

Ets1 N-terminal flanking region of Ets domain; Ets1 is a member of the Ets family of transcription factors in which the DNA-binding activity is in an autoinhibited state. The autoinhibition of Ets1 is mediated by structural coupling of the regions flanking the Ets domain. The inhibitory regions are folded as helices HI1 and HI2 N-terminal to the ETS domain and as H4 C-terminal to the ETS domain, which are packed together to form an inhibitory module. This domain represents the N-terminal flanking region of Ets domain which contains the residues forming HI1 and HI2 helices and additional residues(244-301) N-terminal to HI1. HI1 and HI2 exert the autoinhibitory function by directing the inhibitory residues N-terminal to HI1 to mask the Ets domain DNA-binding surface. These residues are flexible and function by masking the DNA-binding surface of the Ets domain. Phosphorylation of serine residues present in this region enhances autoinhibition dramatically. These inhibitory sequences are required for cooperative DNA binding.


Pssm-ID: 466113  Cd Length: 188  Bit Score: 368.93  E-value: 1.55e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734342231  80 PTYPESCYTSDYFISYGIEHAQCVPPSEFSEPSFITESYQTLHPISSEELLSLKYENDYPSVILQDPLQTDTLQTDYFAI 159
Cdd:pfam19525   1 TTYPESRYTSDYFISYGIEHAQCVPPSEFSEPSFITESYQTLHPISSEELLSLKYENDYPSVILRDPPQTDALQTDYFSI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734342231 160 KQEVLTPDNMCLGRASRGKLGGQDSFESVESYDSCDRLTQSWSSQSSFNSLQRVPSYDSFDYEDYPAALPNHKPKGTFKD 239
Cdd:pfam19525  81 KQEVVTPDNMCMGRASRGKLGGQDSFESIESYDSCDRLTQSWSSQSSFQSLQRVPSYDSFDSEDYPAALPSHKPKGTFKD 160

                         170       180
                  ....*....|....*....|....*...
gi 1734342231 240 YVRDRADLNKDKPVIPAAALAGYTGSGP 267
Cdd:pfam19525 161 YVRDRADLNKDKPVIPAAALAGYTGRMM 188
ETS smart00413
erythroblast transformation specific domain; variation of the helix-turn-helix motif
 267-351 4.38e-50

erythroblast transformation specific domain; variation of the helix-turn-helix motif


Pssm-ID: 197710  Cd Length: 87  Bit Score: 162.82  E-value: 4.38e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734342231  267 PIQLWQFLLELLTDKSCQSFISWTG-DGWEFKLSDPDEVARRWGKRKNKPKMNYEKLSRGLRYYYDKNIIHKTAGKRYVY 345
Cdd:smart00413   1 GIQLWQFLLDLLLDPENSDIIKWTDrDEGEFKLVDPEEVARLWGQRKNKPNMNYEKLSRALRYYYKKNILEKVPGKRLVY 80


                   ....*.
gi 1734342231  346 RFVCDL 351
Cdd:smart00413  81 KFVKNP 86
Ets pfam00178
Ets-domain;
269-347 2.00e-46

Ets-domain;


Pssm-ID: 459700  Cd Length: 80  Bit Score: 153.04  E-value: 2.00e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734342231 269 QLWQFLLELLTDKSCQSFISWT-GDGWEFKLSDPDEVARRWGKRKNKPKMNYEKLSRGLRYYYDKNIIHKTAGKRYVYRF 347
Cdd:pfam00178   1 QLWQFLLDLLTDPEYSDIIKWTdKEEGEFRLVDPEAVARLWGKRKGNPKMTYEKLSRALRYYYKKGILEKVPGKRLTYRF 80
SAM_PNT-ETS-1 cd08542
Sterile alpha motif (SAM)/Pointed domain of ETS-1; SAM Pointed domain of ETS-1 subfamily of ...
 51-68 1.40e-05

Sterile alpha motif (SAM)/Pointed domain of ETS-1; SAM Pointed domain of ETS-1 subfamily of ETS transcriptional activators is a protein-protein interaction domain. The ETS-1 activator is regulated by phosphorylation. It contains a docking site for the ERK2 MAP (Mitogen Activated Protein) kinase, while the ERK2 phosphorylation site is located in the N-terminal disordered region upstream of the SAM Pointed domain. Mutations of the kinase docking site residues inhibit phosphorylation. ETS-1 activators play a role in a number of different physiological processes, and they are expressed during embryonic development, including blood vessel formation, hematopoietic, lymphoid, neuronal and osteogenic differentiation. The Ets-1 gene is a proto-oncogene involved in progression of different tumors (including breast cancer, meningioma, and prostate cancer). Members of this subfamily are potential molecular targets for selective cancer therapy.


Pssm-ID: 176092  Cd Length: 88  Bit Score: 43.05  E-value: 1.40e-05
                          10
                  ....*....|....*...
gi 1734342231  51 ATFSGFTKEQQRLGIPKE 68
Cdd:cd08542     1 ATFSGFTKEQQRLGIPKD 18
 
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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