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Conserved domains on  [gi|568986864|ref|XP_006518688|]
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Krueppel-like factor 12 isoform X3 [Mus musculus]

Protein Classification

C2H2-type zinc finger protein( domain architecture ID 15347866)

Cys2His2 (C2H2)-type zinc finger protein may be involved in transcriptional regulation

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
KLF12_N cd21441
N-terminal domain of Kruppel-like factor 12; Kruppel-like factor 12 (also known as ...
 8-205 5.01e-94

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: 279.59  E-value: 5.01e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568986864   8 PAVRVKTELVESEQGSPNVHNYPDMEAVPLLLNNVKGEPPEDSLPVDHFQTQTEPVDLSINKARTSPTAASSSPVSMTAS 87
Cdd:cd21441    1 PAVRVKTELLESEQGSPNVHNYPDMEAVPLLLNNVKAEPPEDSLSTDHFQTQTEPVDLSINKARTSPTAVSSSPVSMTAS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568986864  88 ASSPSSTSTSSSSSSRPASSpTVITSVSSASSSSTVLSPGPLVASASGVGGQQFLHIIHPVPPSSPMNLQSNKLSHVHRI 167
Cdd:cd21441   81 ASPSSSSSSSSSSSRPASSP-TVITSVSSASSVPTVLTPGPLVASASGVGGQQFLHIIHPVPPSSPMNLQSNKLSHVHRI 159

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 568986864 168 PVVVQSVPVVYTAVRSPGNVNNTIVVPLLEDGRSHGKA 205
Cdd:cd21441  160 PVVVQSVPVVYTAVRSPGNVNNTIVVPLLEDGRSHGKA 197
zf-H2C2_2 pfam13465
Zinc-finger double domain;
344-369 9.06e-06

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 41.97  E-value: 9.06e-06
                          10        20
                  ....*....|....*....|....*.
gi 568986864  344 ELTRHYRKHTGVKPFKCADCDRSFSR 369
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
206-382 6.80e-05

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 44.69  E-value: 6.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568986864 206 QMEPRGLSPRQSKSDSDDDDLPNVTLDSVNETGSTALSIARAVQEVHPSPVSRVRGNRMNNQkfaCSISPFSIESTRRQR 285
Cdd:COG5048  233 SQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASSQSSSPNESDSSSEKGFSLPIKSKQ---CNISFSRSSPLTRHL 309

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568986864 286 RSESPDSRKRRIHRCDFEGCNKVYTKSSHLKAHRRTHTGEKPYKCTWEGCTWKF-----ARSDELTRHYRKHTGVKPFKC 360
Cdd:COG5048  310 RSVNHSGESLKPFSCPYSLCGKLFSRNDALKRHILLHTSISPAKEKLLNSSSKFspllnNEPPQSLQQYKDLKNDKKSET 389

                        170       180
                 ....*....|....*....|....
gi 568986864 361 AD--CDRSFSRSDHLALHRRRHML 382
Cdd:COG5048  390 LSnsCIRNFKRDSNLSLHIITHLS 413
 
Name Accession Description Interval E-value
KLF12_N cd21441
N-terminal domain of Kruppel-like factor 12; Kruppel-like factor 12 (also known as ...
 8-205 5.01e-94

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: 279.59  E-value: 5.01e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568986864   8 PAVRVKTELVESEQGSPNVHNYPDMEAVPLLLNNVKGEPPEDSLPVDHFQTQTEPVDLSINKARTSPTAASSSPVSMTAS 87
Cdd:cd21441    1 PAVRVKTELLESEQGSPNVHNYPDMEAVPLLLNNVKAEPPEDSLSTDHFQTQTEPVDLSINKARTSPTAVSSSPVSMTAS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568986864  88 ASSPSSTSTSSSSSSRPASSpTVITSVSSASSSSTVLSPGPLVASASGVGGQQFLHIIHPVPPSSPMNLQSNKLSHVHRI 167
Cdd:cd21441   81 ASPSSSSSSSSSSSRPASSP-TVITSVSSASSVPTVLTPGPLVASASGVGGQQFLHIIHPVPPSSPMNLQSNKLSHVHRI 159

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 568986864 168 PVVVQSVPVVYTAVRSPGNVNNTIVVPLLEDGRSHGKA 205
Cdd:cd21441  160 PVVVQSVPVVYTAVRSPGNVNNTIVVPLLEDGRSHGKA 197
zf-H2C2_2 pfam13465
Zinc-finger double domain;
344-369 9.06e-06

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 41.97  E-value: 9.06e-06
                          10        20
                  ....*....|....*....|....*.
gi 568986864  344 ELTRHYRKHTGVKPFKCADCDRSFSR 369
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
206-382 6.80e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 44.69  E-value: 6.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568986864 206 QMEPRGLSPRQSKSDSDDDDLPNVTLDSVNETGSTALSIARAVQEVHPSPVSRVRGNRMNNQkfaCSISPFSIESTRRQR 285
Cdd:COG5048  233 SQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASSQSSSPNESDSSSEKGFSLPIKSKQ---CNISFSRSSPLTRHL 309

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568986864 286 RSESPDSRKRRIHRCDFEGCNKVYTKSSHLKAHRRTHTGEKPYKCTWEGCTWKF-----ARSDELTRHYRKHTGVKPFKC 360
Cdd:COG5048  310 RSVNHSGESLKPFSCPYSLCGKLFSRNDALKRHILLHTSISPAKEKLLNSSSKFspllnNEPPQSLQQYKDLKNDKKSET 389

                        170       180
                 ....*....|....*....|....
gi 568986864 361 AD--CDRSFSRSDHLALHRRRHML 382
Cdd:COG5048  390 LSnsCIRNFKRDSNLSLHIITHLS 413
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 298-322 5.41e-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: 34.20  E-value: 5.41e-03
                          10        20
                  ....*....|....*....|....*
gi 568986864  298 HRCdfEGCNKVYTKSSHLKAHRRTH 322
Cdd:pfam00096   1 YKC--PDCGKSFSRKSNLKRHLRTH 23
 
Name Accession Description Interval E-value
KLF12_N cd21441
N-terminal domain of Kruppel-like factor 12; Kruppel-like factor 12 (also known as ...
 8-205 5.01e-94

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: 279.59  E-value: 5.01e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568986864   8 PAVRVKTELVESEQGSPNVHNYPDMEAVPLLLNNVKGEPPEDSLPVDHFQTQTEPVDLSINKARTSPTAASSSPVSMTAS 87
Cdd:cd21441    1 PAVRVKTELLESEQGSPNVHNYPDMEAVPLLLNNVKAEPPEDSLSTDHFQTQTEPVDLSINKARTSPTAVSSSPVSMTAS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568986864  88 ASSPSSTSTSSSSSSRPASSpTVITSVSSASSSSTVLSPGPLVASASGVGGQQFLHIIHPVPPSSPMNLQSNKLSHVHRI 167
Cdd:cd21441   81 ASPSSSSSSSSSSSRPASSP-TVITSVSSASSVPTVLTPGPLVASASGVGGQQFLHIIHPVPPSSPMNLQSNKLSHVHRI 159

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 568986864 168 PVVVQSVPVVYTAVRSPGNVNNTIVVPLLEDGRSHGKA 205
Cdd:cd21441  160 PVVVQSVPVVYTAVRSPGNVNNTIVVPLLEDGRSHGKA 197
KLF8_12_N cd21093
N-terminal domain of Kruppel-like factor (KLF) 8, KLF12, and similar proteins; Kruppel-like ...
 23-205 8.96e-62

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: 196.15  E-value: 8.96e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568986864  23 SPNVHNYPDMEaVPLLLNNVKGEPPEDSLPVDHFQTQTEPVDLSINKARTSPTAASSSPVSMTASASSPSSTSTSSSSSS 102
Cdd:cd21093    1 SPNLLNYPDME-VPLLLNNIKTEPPEELLSSDHSQPQTEPVDLSINKARTSPTAVSSSPVSMSSSISSSSSSSPRPASSP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568986864 103 rpasspTVITSVSSASSSSTVLSPGPLVASASGVGGQQFLHIIHPVPPSSpmnlQSNKLSHVHRIPVVVQSVPVVYTAVR 182
Cdd:cd21093   80 ------TVITSVSSASAIPTVLSPGSILASAQGVGGQQILHVIHTVPSVS----LPNKMSHLHTIPVVVQSLPVVYTAVR 149

                        170       180
                 ....*....|....*....|....
gi 568986864 183 SPGNVnNTIVVPLLE-DGRSHGKA 205
Cdd:cd21093  150 SDGNT-ATITVPLIGgDGKSHGKV 172
KLF8_N cd21440
N-terminal domain of Kruppel-like factor 8; Kruppel-like factor 8 (also known as Krueppel-like ...
 36-203 3.43e-19

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: 84.12  E-value: 3.43e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568986864  36 PLLLNNVKGEPPEDSLPVDHFQTQTEPVDLSINKARTSPTAASSSPVSMTASASSPSSTSTSSSSSSRPASSPTVItsvs 115
Cdd:cd21440   13 PALLSDIKTEPPEELLASDCSQPQAEPVDLSLHKPKAPLQPPSVLSPSPMILSVSPSAPQSLVSSTGTGMGTTSAI---- 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568986864 116 sasssSTVLSPGPLVASASGVGGQQFLHIIHPVPpssPMNLQSnKLSHVHRIPVVVQSVPVVYTAVRSPGnVNNTIVVPL 195
Cdd:cd21440   89 -----PAVLSPGSILASSQGSGGQQILHVIHTIP---SVNLPS-KMGNLQTIPVVVQSLPVVYTTLPTDG-VTAAITVPL 158


                 ....*....
gi 568986864 196 L-EDGRSHG 203
Cdd:cd21440  159 IgGDGKNAG 167
zf-H2C2_2 pfam13465
Zinc-finger double domain;
344-369 9.06e-06

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 41.97  E-value: 9.06e-06
                          10        20
                  ....*....|....*....|....*.
gi 568986864  344 ELTRHYRKHTGVKPFKCADCDRSFSR 369
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
206-382 6.80e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 44.69  E-value: 6.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568986864 206 QMEPRGLSPRQSKSDSDDDDLPNVTLDSVNETGSTALSIARAVQEVHPSPVSRVRGNRMNNQkfaCSISPFSIESTRRQR 285
Cdd:COG5048  233 SQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASSQSSSPNESDSSSEKGFSLPIKSKQ---CNISFSRSSPLTRHL 309

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568986864 286 RSESPDSRKRRIHRCDFEGCNKVYTKSSHLKAHRRTHTGEKPYKCTWEGCTWKF-----ARSDELTRHYRKHTGVKPFKC 360
Cdd:COG5048  310 RSVNHSGESLKPFSCPYSLCGKLFSRNDALKRHILLHTSISPAKEKLLNSSSKFspllnNEPPQSLQQYKDLKNDKKSET 389

                        170       180
                 ....*....|....*....|....
gi 568986864 361 AD--CDRSFSRSDHLALHRRRHML 382
Cdd:COG5048  390 LSnsCIRNFKRDSNLSLHIITHLS 413
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 358-380 8.98e-05

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: 39.21  E-value: 8.98e-05
                          10        20
                  ....*....|....*....|...
gi 568986864  358 FKCADCDRSFSRSDHLALHRRRH 380
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 296-377 3.77e-03

Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division and chromosome partitioning];


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 39.32  E-value: 3.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568986864 296 RIHRCDFEGCNKVYTKSSHLKAHRRT-HTGEKPYKCTWEGCTWKFARSDeltrhyrkhtgvKPFKCADCDRSFSRSDHLA 374
Cdd:COG5189  348 KPYKCPVEGCNKKYKNQNGLKYHMLHgHQNQKLHENPSPEKMNIFSAKD------------KPYRCEVCDKRYKNLNGLK 415


                 ...
gi 568986864 375 LHR 377
Cdd:COG5189  416 YHR 418
KLF3_N cd21577
N-terminal domain of Kruppel-like factor 3; Kruppel-like factor 3 (KLF3; also called ...
 47-81 4.14e-03

N-terminal domain of Kruppel-like factor 3; Kruppel-like factor 3 (KLF3; also called Krueppel-like factor 3 and originally called Basic Kruppel-like Factor/BKLF), was the third member of the KLF family of zinc finger transcription factors to be discovered. KLF3 possesses a wide range of biological impacts on regulating apoptosis, differentiation, and proliferation in various tissues during the entire progression process. It has been proposed as a tumor suppressor in colorectal cancer. It appears to function predominantly as a repressor of transcription, turning genes off by recruiting the C-terminal Binding Protein co-repressors CtBP1 and CtBP2. CtBP docks onto a short motif (residues 61-65) in the N-terminus of KLF3, through the Proline-X-Aspartate-Leucine-Serine (PXDLS) motif. CtBP in turn recruits histone modifying enzymes to alter chromatin and repress gene expression. KLF3 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 KLF3.


Pssm-ID: 410554 [Multi-domain]  Cd Length: 214  Bit Score: 38.10  E-value: 4.14e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 568986864  47 PEDSLPVDHfQTQTEPVDLSINKaRTSPTAASSSP 81
Cdd:cd21577    7 METSFYSPS-HSQLEPVDLSLSK-RSSPPSSSSSS 39
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 298-322 5.41e-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: 34.20  E-value: 5.41e-03
                          10        20
                  ....*....|....*....|....*
gi 568986864  298 HRCdfEGCNKVYTKSSHLKAHRRTH 322
Cdd:pfam00096   1 YKC--PDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
314-331 9.14e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 33.50  E-value: 9.14e-03
                          10
                  ....*....|....*...
gi 568986864  314 HLKAHRRTHTGEKPYKCT 331
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCP 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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