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Krueppel-like factor 5 isoform 2 [Homo sapiens]
List of domain hits
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Name | Accession | Description | Interval | E-value | |||||
KLF5_N | cd21579 | N-terminal domain of Kruppel-like factor 5; Kruppel-like factor 5 (KLF5; also known as also ... |
1-279 | 2.36e-91 | |||||
N-terminal domain of Kruppel-like factor 5; Kruppel-like factor 5 (KLF5; also known as also known as Krueppel-like factor 5; intestinal enriched Kruppel-like factor/IKLF; basic transcription element binding protein 2/BTEB2) a protein that in humans is encoded by the KLF5 gene. KLF5 is involved in numerous functions in eukaryotic cells, such as proliferation, migration, and differentiation. The loss of KLF5 expression is associated with tumors of the breast, cervix, endometrium, ovary, and prostate. KLF5 mediates the expression of several genes essential for proper cardiac structure and function, and plays a role in familial dilated cardiomyopathy. It functions as a transcriptional activator. KLF5 exhibits both transcriptional activation activity as well as trans-activating function. It belongs to a family of proteins called the Specificity Protein (SP)/KLF family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. Members of the KLF family can act as activators or repressors of transcription depending on cell and promoter context. KLFs regulate various cellular functions, such as proliferation, differentiation, and apoptosis, as well as the development and homeostasis of several types of tissue. In addition to the C-terminal DNA-binding domain, each KLF also has a unique N-terminal activation/repression domain that confers specificity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the N-terminal domain of KLF5. : Pssm-ID: 410335 Cd Length: 273 Bit Score: 274.86 E-value: 2.36e-91
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zf-C2H2 | pfam00096 | Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ... |
342-364 | 1.16e-04 | |||||
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter. : Pssm-ID: 395048 [Multi-domain] Cd Length: 23 Bit Score: 38.82 E-value: 1.16e-04
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zf-H2C2_2 | pfam13465 | Zinc-finger double domain; |
328-353 | 5.02e-04 | |||||
Zinc-finger double domain; : Pssm-ID: 463886 [Multi-domain] Cd Length: 26 Bit Score: 36.97 E-value: 5.02e-04
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COG5048 super family | cl34881 | FOG: Zn-finger [General function prediction only]; |
268-342 | 1.29e-03 | |||||
FOG: Zn-finger [General function prediction only]; The actual alignment was detected with superfamily member COG5048: Pssm-ID: 227381 [Multi-domain] Cd Length: 467 Bit Score: 40.45 E-value: 1.29e-03
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Name | Accession | Description | Interval | E-value | |||||
KLF5_N | cd21579 | N-terminal domain of Kruppel-like factor 5; Kruppel-like factor 5 (KLF5; also known as also ... |
1-279 | 2.36e-91 | |||||
N-terminal domain of Kruppel-like factor 5; Kruppel-like factor 5 (KLF5; also known as also known as Krueppel-like factor 5; intestinal enriched Kruppel-like factor/IKLF; basic transcription element binding protein 2/BTEB2) a protein that in humans is encoded by the KLF5 gene. KLF5 is involved in numerous functions in eukaryotic cells, such as proliferation, migration, and differentiation. The loss of KLF5 expression is associated with tumors of the breast, cervix, endometrium, ovary, and prostate. KLF5 mediates the expression of several genes essential for proper cardiac structure and function, and plays a role in familial dilated cardiomyopathy. It functions as a transcriptional activator. KLF5 exhibits both transcriptional activation activity as well as trans-activating function. It belongs to a family of proteins called the Specificity Protein (SP)/KLF family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. Members of the KLF family can act as activators or repressors of transcription depending on cell and promoter context. KLFs regulate various cellular functions, such as proliferation, differentiation, and apoptosis, as well as the development and homeostasis of several types of tissue. In addition to the C-terminal DNA-binding domain, each KLF also has a unique N-terminal activation/repression domain that confers specificity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the N-terminal domain of KLF5. Pssm-ID: 410335 Cd Length: 273 Bit Score: 274.86 E-value: 2.36e-91
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zf-C2H2 | pfam00096 | Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ... |
342-364 | 1.16e-04 | |||||
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter. Pssm-ID: 395048 [Multi-domain] Cd Length: 23 Bit Score: 38.82 E-value: 1.16e-04
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zf-H2C2_2 | pfam13465 | Zinc-finger double domain; |
328-353 | 5.02e-04 | |||||
Zinc-finger double domain; Pssm-ID: 463886 [Multi-domain] Cd Length: 26 Bit Score: 36.97 E-value: 5.02e-04
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COG5048 | COG5048 | FOG: Zn-finger [General function prediction only]; |
268-342 | 1.29e-03 | |||||
FOG: Zn-finger [General function prediction only]; Pssm-ID: 227381 [Multi-domain] Cd Length: 467 Bit Score: 40.45 E-value: 1.29e-03
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zf-H2C2_2 | pfam13465 | Zinc-finger double domain; |
298-325 | 2.12e-03 | |||||
Zinc-finger double domain; Pssm-ID: 463886 [Multi-domain] Cd Length: 26 Bit Score: 35.04 E-value: 2.12e-03
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Name | Accession | Description | Interval | E-value | |||||
KLF5_N | cd21579 | N-terminal domain of Kruppel-like factor 5; Kruppel-like factor 5 (KLF5; also known as also ... |
1-279 | 2.36e-91 | |||||
N-terminal domain of Kruppel-like factor 5; Kruppel-like factor 5 (KLF5; also known as also known as Krueppel-like factor 5; intestinal enriched Kruppel-like factor/IKLF; basic transcription element binding protein 2/BTEB2) a protein that in humans is encoded by the KLF5 gene. KLF5 is involved in numerous functions in eukaryotic cells, such as proliferation, migration, and differentiation. The loss of KLF5 expression is associated with tumors of the breast, cervix, endometrium, ovary, and prostate. KLF5 mediates the expression of several genes essential for proper cardiac structure and function, and plays a role in familial dilated cardiomyopathy. It functions as a transcriptional activator. KLF5 exhibits both transcriptional activation activity as well as trans-activating function. It belongs to a family of proteins called the Specificity Protein (SP)/KLF family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. Members of the KLF family can act as activators or repressors of transcription depending on cell and promoter context. KLFs regulate various cellular functions, such as proliferation, differentiation, and apoptosis, as well as the development and homeostasis of several types of tissue. In addition to the C-terminal DNA-binding domain, each KLF also has a unique N-terminal activation/repression domain that confers specificity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the N-terminal domain of KLF5. Pssm-ID: 410335 Cd Length: 273 Bit Score: 274.86 E-value: 2.36e-91
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zf-C2H2 | pfam00096 | Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ... |
342-364 | 1.16e-04 | |||||
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter. Pssm-ID: 395048 [Multi-domain] Cd Length: 23 Bit Score: 38.82 E-value: 1.16e-04
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zf-H2C2_2 | pfam13465 | Zinc-finger double domain; |
328-353 | 5.02e-04 | |||||
Zinc-finger double domain; Pssm-ID: 463886 [Multi-domain] Cd Length: 26 Bit Score: 36.97 E-value: 5.02e-04
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COG5048 | COG5048 | FOG: Zn-finger [General function prediction only]; |
268-342 | 1.29e-03 | |||||
FOG: Zn-finger [General function prediction only]; Pssm-ID: 227381 [Multi-domain] Cd Length: 467 Bit Score: 40.45 E-value: 1.29e-03
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zf-H2C2_2 | pfam13465 | Zinc-finger double domain; |
298-325 | 2.12e-03 | |||||
Zinc-finger double domain; Pssm-ID: 463886 [Multi-domain] Cd Length: 26 Bit Score: 35.04 E-value: 2.12e-03
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COG5048 | COG5048 | FOG: Zn-finger [General function prediction only]; |
240-360 | 2.91e-03 | |||||
FOG: Zn-finger [General function prediction only]; Pssm-ID: 227381 [Multi-domain] Cd Length: 467 Bit Score: 39.29 E-value: 2.91e-03
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zf-C2H2 | pfam00096 | Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ... |
312-336 | 6.75e-03 | |||||
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter. Pssm-ID: 395048 [Multi-domain] Cd Length: 23 Bit Score: 33.81 E-value: 6.75e-03
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SFP1 | COG5189 | Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ... |
269-362 | 9.65e-03 | |||||
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division and chromosome partitioning]; Pssm-ID: 227516 [Multi-domain] Cd Length: 423 Bit Score: 37.78 E-value: 9.65e-03
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Blast search parameters | ||||
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