N-terminal domain of Kruppel-like factor 8; Kruppel-like factor 8 (also known as Krueppel-like transcription factor 8, KLF8) is a CACCC-box binding protein that associates with C-terminal Binding Protein (CtBP) and represses transcription. It plays an essential role in the regulation of the cell cycle, apoptosis, and differentiation. It has been identified as a key component of the transcription factor network that controls terminal differentiation during adipogenesis. It also plays an important role in the formation of several human tumors, including the promotion of tumorigenesis, invasion, and metastasis of colorectal cancer cells, and the progression of pancreatic cancer. KLF8 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. Although these factors bind to similar elements in vitro, they have distinct activities in vivo depending on their expression profile and the sequence of the N-terminal activation/repression domain, which differ between members. KLF8 contains an N-terminal repression domain that is related to that of KLF12.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022943159  45 SPTLLDANPMENPALFNDIKIEPPEELLASDFSLPQVEPVDLSFHKPKAPLQPASMLQA-PIRPPKPQSSPQTLVVSTST 123
Cdd:cd21440     1 SSSLLAASPAETPALLSDIKTEPPEELLASDCSQPQAEPVDLSLHKPKAPLQPPSVLSPsPMILSVSPSAPQSLVSSTGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022943159 124 SDMSTsANIPTVLTPGSVLTSSQSTGSQQILHVIHTIPSVSLPNKMGGLKTIPVVVQSLPMVYTTLPADGGPAAITVPLI 203
Cdd:cd21440    81 GMGTT-SAIPAVLSPGSILASSQGSGGQQILHVIHTIPSVNLPSKMGNLQTIPVVVQSLPVVYTTLPTDGVTAAITVPLI 159

                         170
                  ....*....|
gi 1022943159 204 GGDGKNAGSV 213
Cdd:cd21440   160 GGDGKNAGSV 169

FOG: Zn-finger [General function prediction only];

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1022943159 269 RIHQCDFagCSKVYTKSSHLKAHRRIHTGEKPYKCTWDGCSWKFARSDELTRHFRKHTGIKPFRCTDCNRS 339
Cdd:COG5048    32 RPDSCPN--CTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPL 100

N-terminal domain of Kruppel-like factor 8; Kruppel-like factor 8 (also known as Krueppel-like transcription factor 8, KLF8) is a CACCC-box binding protein that associates with C-terminal Binding Protein (CtBP) and represses transcription. It plays an essential role in the regulation of the cell cycle, apoptosis, and differentiation. It has been identified as a key component of the transcription factor network that controls terminal differentiation during adipogenesis. It also plays an important role in the formation of several human tumors, including the promotion of tumorigenesis, invasion, and metastasis of colorectal cancer cells, and the progression of pancreatic cancer. KLF8 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. Although these factors bind to similar elements in vitro, they have distinct activities in vivo depending on their expression profile and the sequence of the N-terminal activation/repression domain, which differ between members. KLF8 contains an N-terminal repression domain that is related to that of KLF12.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022943159  45 SPTLLDANPMENPALFNDIKIEPPEELLASDFSLPQVEPVDLSFHKPKAPLQPASMLQA-PIRPPKPQSSPQTLVVSTST 123
Cdd:cd21440     1 SSSLLAASPAETPALLSDIKTEPPEELLASDCSQPQAEPVDLSLHKPKAPLQPPSVLSPsPMILSVSPSAPQSLVSSTGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022943159 124 SDMSTsANIPTVLTPGSVLTSSQSTGSQQILHVIHTIPSVSLPNKMGGLKTIPVVVQSLPMVYTTLPADGGPAAITVPLI 203
Cdd:cd21440    81 GMGTT-SAIPAVLSPGSILASSQGSGGQQILHVIHTIPSVNLPSKMGNLQTIPVVVQSLPVVYTTLPTDGVTAAITVPLI 159

                         170
                  ....*....|
gi 1022943159 204 GGDGKNAGSV 213
Cdd:cd21440   160 GGDGKNAGSV 169

FOG: Zn-finger [General function prediction only];

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1022943159 269 RIHQCDFagCSKVYTKSSHLKAHRRIHTGEKPYKCTWDGCSWKFARSDELTRHFRKHTGIKPFRCTDCNRS 339
Cdd:COG5048    32 RPDSCPN--CTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPL 100

zinc finger;

                           10        20
                   ....*....|....*....|...
gi 1022943159  331 FRCTDCNRSFSRSDHLSLHRRRH 353
Cdd:smart00355   1 YRCPECGKVFKSKSALREHMRTH 23

N-terminal domain of Kruppel-like factor 8; Kruppel-like factor 8 (also known as Krueppel-like transcription factor 8, KLF8) is a CACCC-box binding protein that associates with C-terminal Binding Protein (CtBP) and represses transcription. It plays an essential role in the regulation of the cell cycle, apoptosis, and differentiation. It has been identified as a key component of the transcription factor network that controls terminal differentiation during adipogenesis. It also plays an important role in the formation of several human tumors, including the promotion of tumorigenesis, invasion, and metastasis of colorectal cancer cells, and the progression of pancreatic cancer. KLF8 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. Although these factors bind to similar elements in vitro, they have distinct activities in vivo depending on their expression profile and the sequence of the N-terminal activation/repression domain, which differ between members. KLF8 contains an N-terminal repression domain that is related to that of KLF12.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022943159  45 SPTLLDANPMENPALFNDIKIEPPEELLASDFSLPQVEPVDLSFHKPKAPLQPASMLQA-PIRPPKPQSSPQTLVVSTST 123
Cdd:cd21440     1 SSSLLAASPAETPALLSDIKTEPPEELLASDCSQPQAEPVDLSLHKPKAPLQPPSVLSPsPMILSVSPSAPQSLVSSTGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022943159 124 SDMSTsANIPTVLTPGSVLTSSQSTGSQQILHVIHTIPSVSLPNKMGGLKTIPVVVQSLPMVYTTLPADGGPAAITVPLI 203
Cdd:cd21440    81 GMGTT-SAIPAVLSPGSILASSQGSGGQQILHVIHTIPSVNLPSKMGNLQTIPVVVQSLPVVYTTLPTDGVTAAITVPLI 159

                         170
                  ....*....|
gi 1022943159 204 GGDGKNAGSV 213
Cdd:cd21440   160 GGDGKNAGSV 169

N-terminal domain of Kruppel-like factor 12; Kruppel-like factor 12 (also known as Krueppel-like transcription factor 12, KLF12) regulates, by transcriptionally repressing Nur77 expression, endometrial decidualization, which is a prerequisite for successful implantation and the establishment of pregnancy. It is involved in the maturation processes of kidney collecting ducts after birth, and is able to increase the promoter activity of the UT-A1 urea transporter promoter by binding to the CACCC motif. KLF12 has also been found to promote colorectal cancer growth is also involved in the invasion and apoptosis of basal-like breast carcinoma. KLF12 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. Although these factors bind to similar elements in vitro, they have distinct activities in vivo depending on their expression profile and the sequence of the N-terminal activation/repression domain, which differ between members. KLF12 contains an N-terminal domain that is related to the N-terminal repression domain of KLF8.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022943159  41 SNMTSPTLLDANPMEN-PALFNDIKIEPPEELLASDFSLPQVEPVDLSFHKPK--------APLQPASMLQAPIRPPKPQ 111
Cdd:cd21441    12 SEQGSPNVHNYPDMEAvPLLLNNVKAEPPEDSLSTDHFQTQTEPVDLSINKARtsptavssSPVSMTASASPSSSSSSSS 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022943159 112 SSPQTLVVSTSTSDMSTSANIPTVLTPGSVLTSSQSTGSQQILHVIHTIPSVS----LPNKMGGLKTIPVVVQSLPMVYT 187
Cdd:cd21441    92 SSSRPASSPTVITSVSSASSVPTVLTPGPLVASASGVGGQQFLHIIHPVPPSSpmnlQSNKLSHVHRIPVVVQSVPVVYT 171

                         170       180
                  ....*....|....*....|....*..
gi 1022943159 188 TLPADGG-PAAITVPLIgGDGKNAGSV 213
Cdd:cd21441   172 AVRSPGNvNNTIVVPLL-EDGRSHGKA 197

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.

                          10        20
                  ....*....|....*....|...
gi 1022943159 331 FRCTDCNRSFSRSDHLSLHRRRH 353
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23

FOG: Zn-finger [General function prediction only];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022943159 217 PTSMSPLEIPSDSEESTIESGSSALQSLQGLQQEPAAMAQMQGEESLDL--KRRRIHQCDFAGCSKVYTKSSHLKAHRR- 293
Cdd:COG5048   232 NSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASSQSSSPNESDSssEKGFSLPIKSKQCNISFSRSSPLTRHLRs 311

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1022943159 294 -IHTGE--KPYKCTWDGCSWKFARSDELTRHFRKHTGIKPFRCTDCNRSFSRS 343
Cdd:COG5048   312 vNHSGEslKPFSCPYSLCGKLFSRNDALKRHILLHTSISPAKEKLLNSSSKFS 364

zinc finger;

                           10        20
                   ....*....|....*....|...
gi 1022943159  331 FRCTDCNRSFSRSDHLSLHRRRH 353
Cdd:smart00355   1 YRCPECGKVFKSKSALREHMRTH 23

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.

                          10        20
                  ....*....|....*....|....*
gi 1022943159 301 YKCTwdGCSWKFARSDELTRHFRKH 325
Cdd:pfam00096   1 YKCP--DCGKSFSRKSNLKRHLRTH 23