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Conserved domains on  [gi|1022943138|ref|NP_001311029|]
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Krueppel-like factor 8 isoform 4 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
KLF8_N cd21440
N-terminal domain of Kruppel-like factor 8; Kruppel-like factor 8 (also known as Krueppel-like ...
48-215 1.44e-89

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.


:

Pssm-ID: 410607 [Multi-domain]  Cd Length: 169  Bit Score: 263.24  E-value: 1.44e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022943138  48 SPTLLDANPMENPALFNDIKIEPPEELLASDFSLPQVEPVDLSFHKPKAPLQPASMLQA-PIRPPKPQSSPQTLVVSTST 126
Cdd:cd21440     1 SSSLLAASPAETPALLSDIKTEPPEELLASDCSQPQAEPVDLSLHKPKAPLQPPSVLSPsPMILSVSPSAPQSLVSSTGT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022943138 127 SDMSTsANIPTVLTPGSVLTSSQSTGSQQILHVIHTIPSVSLPNKMGGLKTIPVVVQSLPMVYTTLPADGGPAAITVPLI 206
Cdd:cd21440    81 GMGTT-SAIPAVLSPGSILASSQGSGGQQILHVIHTIPSVNLPSKMGNLQTIPVVVQSLPVVYTTLPTDGVTAAITVPLI 159

                  ....*....
gi 1022943138 207 GGDGKNAGS 215
Cdd:cd21440   160 GGDGKNAGS 168
zf-H2C2_2 pfam13465
Zinc-finger double domain;
236-261 7.23e-07

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 44.67  E-value: 7.23e-07
                          10        20
                  ....*....|....*....|....*.
gi 1022943138 236 ELTRHFRKHTGIKPFRCTDCNRSFSR 261
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
220-244 1.60e-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: 35.35  E-value: 1.60e-03
                          10        20
                  ....*....|....*....|....*
gi 1022943138 220 YKCTwdGCSWKFARSDELTRHFRKH 244
Cdd:pfam00096   1 YKCP--DCGKSFSRKSNLKRHLRTH 23
 
Name Accession Description Interval E-value
KLF8_N cd21440
N-terminal domain of Kruppel-like factor 8; Kruppel-like factor 8 (also known as Krueppel-like ...
48-215 1.44e-89

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.


Pssm-ID: 410607 [Multi-domain]  Cd Length: 169  Bit Score: 263.24  E-value: 1.44e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022943138  48 SPTLLDANPMENPALFNDIKIEPPEELLASDFSLPQVEPVDLSFHKPKAPLQPASMLQA-PIRPPKPQSSPQTLVVSTST 126
Cdd:cd21440     1 SSSLLAASPAETPALLSDIKTEPPEELLASDCSQPQAEPVDLSLHKPKAPLQPPSVLSPsPMILSVSPSAPQSLVSSTGT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022943138 127 SDMSTsANIPTVLTPGSVLTSSQSTGSQQILHVIHTIPSVSLPNKMGGLKTIPVVVQSLPMVYTTLPADGGPAAITVPLI 206
Cdd:cd21440    81 GMGTT-SAIPAVLSPGSILASSQGSGGQQILHVIHTIPSVNLPSKMGNLQTIPVVVQSLPVVYTTLPTDGVTAAITVPLI 159

                  ....*....
gi 1022943138 207 GGDGKNAGS 215
Cdd:cd21440   160 GGDGKNAGS 168
zf-H2C2_2 pfam13465
Zinc-finger double domain;
236-261 7.23e-07

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 44.67  E-value: 7.23e-07
                          10        20
                  ....*....|....*....|....*.
gi 1022943138 236 ELTRHFRKHTGIKPFRCTDCNRSFSR 261
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
ZnF_C2H2 smart00355
zinc finger;
250-272 1.06e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 35.52  E-value: 1.06e-03
                           10        20
                   ....*....|....*....|...
gi 1022943138  250 FRCTDCNRSFSRSDHLSLHRRRH 272
Cdd:smart00355   1 YRCPECGKVFKSKSALREHMRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
220-244 1.60e-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: 35.35  E-value: 1.60e-03
                          10        20
                  ....*....|....*....|....*
gi 1022943138 220 YKCTwdGCSWKFARSDELTRHFRKH 244
Cdd:pfam00096   1 YKCP--DCGKSFSRKSNLKRHLRTH 23
 
Name Accession Description Interval E-value
KLF8_N cd21440
N-terminal domain of Kruppel-like factor 8; Kruppel-like factor 8 (also known as Krueppel-like ...
48-215 1.44e-89

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.


Pssm-ID: 410607 [Multi-domain]  Cd Length: 169  Bit Score: 263.24  E-value: 1.44e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022943138  48 SPTLLDANPMENPALFNDIKIEPPEELLASDFSLPQVEPVDLSFHKPKAPLQPASMLQA-PIRPPKPQSSPQTLVVSTST 126
Cdd:cd21440     1 SSSLLAASPAETPALLSDIKTEPPEELLASDCSQPQAEPVDLSLHKPKAPLQPPSVLSPsPMILSVSPSAPQSLVSSTGT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022943138 127 SDMSTsANIPTVLTPGSVLTSSQSTGSQQILHVIHTIPSVSLPNKMGGLKTIPVVVQSLPMVYTTLPADGGPAAITVPLI 206
Cdd:cd21440    81 GMGTT-SAIPAVLSPGSILASSQGSGGQQILHVIHTIPSVNLPSKMGNLQTIPVVVQSLPVVYTTLPTDGVTAAITVPLI 159

                  ....*....
gi 1022943138 207 GGDGKNAGS 215
Cdd:cd21440   160 GGDGKNAGS 168
KLF8_12_N cd21093
N-terminal domain of Kruppel-like factor (KLF) 8, KLF12, and similar proteins; Kruppel-like ...
48-215 2.32e-85

N-terminal domain of Kruppel-like factor (KLF) 8, KLF12, and similar proteins; Kruppel-like transcription factors (also known as Krueppel-like transcription factors, KLFs) belong 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. This model represents the related N-terminal activation/repression domains of KLF8 and KLF12.


Pssm-ID: 410606 [Multi-domain]  Cd Length: 172  Bit Score: 252.39  E-value: 2.32e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022943138  48 SPTLLDANPMENPALFNDIKIEPPEELLASDFSLPQVEPVDLSFHKPKAPLQPASMLQA---PIRPPKPQSSPQTLVVST 124
Cdd:cd21093     1 SPNLLNYPDMEVPLLLNNIKTEPPEELLSSDHSQPQTEPVDLSINKARTSPTAVSSSPVsmsSSISSSSSSSPRPASSPT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022943138 125 STSDMSTSANIPTVLTPGSVLTSSQSTGSQQILHVIHTIPSVSLPNKMGGLKTIPVVVQSLPMVYTTLPADGGPAAITVP 204
Cdd:cd21093    81 VITSVSSASAIPTVLSPGSILASAQGVGGQQILHVIHTVPSVSLPNKMSHLHTIPVVVQSLPVVYTAVRSDGNTATITVP 160
                         170
                  ....*....|.
gi 1022943138 205 LIGGDGKNAGS 215
Cdd:cd21093   161 LIGGDGKSHGK 171
KLF12_N cd21441
N-terminal domain of Kruppel-like factor 12; Kruppel-like factor 12 (also known as ...
44-214 2.38e-27

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.


Pssm-ID: 410608 [Multi-domain]  Cd Length: 197  Bit Score: 104.70  E-value: 2.38e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022943138  44 SNMTSPTLLDANPMEN-PALFNDIKIEPPEELLASDFSLPQVEPVDLSFHKPK--------APLQPASMLQAPIRPPKPQ 114
Cdd:cd21441    12 SEQGSPNVHNYPDMEAvPLLLNNVKAEPPEDSLSTDHFQTQTEPVDLSINKARtsptavssSPVSMTASASPSSSSSSSS 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022943138 115 SSPQTLVVSTSTSDMSTSANIPTVLTPGSVLTSSQSTGSQQILHVIHTIPSVS----LPNKMGGLKTIPVVVQSLPMVYT 190
Cdd:cd21441    92 SSSRPASSPTVITSVSSASSVPTVLTPGPLVASASGVGGQQFLHIIHPVPPSSpmnlQSNKLSHVHRIPVVVQSVPVVYT 171
                         170       180
                  ....*....|....*....|....*
gi 1022943138 191 TLPADGG-PAAITVPLIgGDGKNAG 214
Cdd:cd21441   172 AVRSPGNvNNTIVVPLL-EDGRSHG 195
zf-H2C2_2 pfam13465
Zinc-finger double domain;
236-261 7.23e-07

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 44.67  E-value: 7.23e-07
                          10        20
                  ....*....|....*....|....*.
gi 1022943138 236 ELTRHFRKHTGIKPFRCTDCNRSFSR 261
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
250-272 1.45e-06

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: 43.83  E-value: 1.45e-06
                          10        20
                  ....*....|....*....|...
gi 1022943138 250 FRCTDCNRSFSRSDHLSLHRRRH 272
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
ZnF_C2H2 smart00355
zinc finger;
250-272 1.06e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 35.52  E-value: 1.06e-03
                           10        20
                   ....*....|....*....|...
gi 1022943138  250 FRCTDCNRSFSRSDHLSLHRRRH 272
Cdd:smart00355   1 YRCPECGKVFKSKSALREHMRTH 23
zf-C2H2_4 pfam13894
C2H2-type zinc finger; This family contains a number of divergent C2H2 type zinc fingers.
250-272 1.27e-03

C2H2-type zinc finger; This family contains a number of divergent C2H2 type zinc fingers.


Pssm-ID: 464025  Cd Length: 24  Bit Score: 35.70  E-value: 1.27e-03
                          10        20
                  ....*....|....*....|...
gi 1022943138 250 FRCTDCNRSFSRSDHLSLHRRRH 272
Cdd:pfam13894   1 FKCPICGKSFSSKKSLKRHLKTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
220-244 1.60e-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: 35.35  E-value: 1.60e-03
                          10        20
                  ....*....|....*....|....*
gi 1022943138 220 YKCTwdGCSWKFARSDELTRHFRKH 244
Cdd:pfam00096   1 YKCP--DCGKSFSRKSNLKRHLRTH 23
zf-H2C2_5 pfam13909
C2H2-type zinc-finger domain;
220-246 3.65e-03

C2H2-type zinc-finger domain;


Pssm-ID: 404746 [Multi-domain]  Cd Length: 25  Bit Score: 34.06  E-value: 3.65e-03
                          10        20
                  ....*....|....*....|....*..
gi 1022943138 220 YKCtwDGCSWKFARSDELTRHFRKHTG 246
Cdd:pfam13909   1 YKC--SQCDYSTAWKSNLKRHLRKHTG 25
 
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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