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Conserved domains on  [gi|1030311311|ref|NP_001313471|]
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transcription factor Sp4 isoform 2 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SP4_N cd22536
N-terminal domain of transcription factor Specificity Protein (SP) 4; Specificity Proteins ...
 15-631 0e+00

N-terminal domain of transcription factor Specificity Protein (SP) 4; Specificity Proteins (SPs) are transcription factors that are involved in many cellular processes, including cell differentiation, cell growth, apoptosis, immune responses, response to DNA damage, and chromatin remodeling. Human SP4 is a risk gene of multiple psychiatric disorders including schizophrenia, bipolar disorder, and major depression. SP4 belongs to a family of proteins, called the SP/Kruppel or Krueppel-like Factor (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. SP factors preferentially bind GC boxes, while KLFs bind CACCC boxes. Another characteristic hallmark of SP factors is the presence of the Buttonhead (BTD) box CXCPXC, just N-terminal to the zinc fingers. The function of the BTD box is unknown, but it is thought to play an important physiological role. Another feature of most SP factors is the presence of a conserved amino acid stretch, the so-called SP box, located close to the N-terminus. SP factors may be separated into three groups based on their domain architecture and the similarity of their N-terminal transactivation domains: SP1-4, SP5, and SP6-9. The transactivation domains between the three groups are not homologous to one another. SP1-4 have similar N-terminal transactivation domains characterized by glutamine-rich regions, which, in most cases, have adjacent serine/threonine-rich regions. This model represents the N-terminal domain of SP4.


:

Pssm-ID: 411773 [Multi-domain]  Cd Length: 623  Bit Score: 740.58  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030311311  15 NKKPKTSGSQDSQPSPLALLAATCSKIGTPGENQATGQ-QQIIIDPSQGLVQLQNQPQQLELVTTQLAGNAWQLVASTPP 93
Cdd:cd22536     1 NKKGKTSGSQDSQPSPLALLAATCSKIGTPGENQGAGQqQQIIIDPSQGLVQLQNQPQQLELVTTQLAGNAWQIVAAAPP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030311311  94 ASKENNVSQP----ASSSSSSSSSNNGSASPTKTKSGNS--STPGQFQVIQVQ---NPSGSVQYQVIPQLQTVEGQQIQI 164
Cdd:cd22536    81 TSKENNVAQQgvsaATSSAAPSSSNNGSTSPTKVKAGNSnaSAPGQFQVIQVQnmqNPSGSVQYQVIPQIQTVEGQQIQI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030311311 165 NPTSSSSLQDLQGQIQLISAGNNQAILTAANRTASGNILAQNLANQTVPVQIRPGVSIPLQLQTLPGTQAQVVTTLPINI 244
Cdd:cd22536   161 SPANATALQDLQGQIQLIPAGNNQAILTTPNRTASGNIIAQNLANQTVPVQIRPGVSIPLQLQTIPGAQAQVVTTLPINI 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030311311 245 GGVTLALPVINNVAAGGGTGQVGQPAataDSGTSNGNQLVSTPTnTTTSASTMPESPSSSTTCTTTASTSLTSSDTLVSS 324
Cdd:cd22536   241 GGVTLALPVINNVAAGGGSGQLVQPS---DGGVSNGNQLVSTPI-TTASVSTMPESPSSSTTCTTTASTSLTSSDTLVSS 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030311311 325 ADTGQYASTSASSsERTIEESQTPAAtESEAQSSSQLQPNGMQNAQDQSNSLQQVQIVGQPILQQIQIQQPQQQIIQAIP 404
Cdd:cd22536   317 AETGQYASTAASS-ERTEEEPQTSAA-ESEAQSSSQLQSNGLQNVQDQSNSLQQVQIVGQPILQQIQIQQPQQQIIQAIQ 394

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030311311 405 PQSFQLQSGQTIQTIQQQPLQNVQLQAV-NPTQVLIRAPTLTPSGQISWQTVQVQNIQSLSNLQVQNAGLSQQLTITPVS 483
Cdd:cd22536   395 PQSFQLQSGQTIQTIQQQPLQNVQLQAVqSPTQVLIRAPTLTPSGQISWQTVQVQNIQSLSNLQVQNAGLPQQLTLTPVS 474

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030311311 484 SS-GGTTLAQIAPVAVAGAPITLNTAQLASVPNLQTVSVANLGAAGVQVQGVPVTITSVAGQQQGQDGVKVQQATIAPVT 562
Cdd:cd22536   475 SSaGGTTIAQIAPVAVAGTPITLNAAQLASVPNLQTVNVANLGAAGVQVQGVPVTITSVAGQQQGQDGVKVQQATIAPVT 554

                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1030311311 563 VAVGGIANATIGAVSPDQLTQVHLQQGQQTSDQEVQPGKRLRRVACSCPNCREGEGRGSNEPGKKKQHI 631
Cdd:cd22536   555 VAVGNIANATIGAVSPDQITQVQLQQAQQASDQEVQPGKRLRRVACSCPNCREGEGRGSSEPGKKKQHI 623
zf-H2C2_2 pfam13465
Zinc-finger double domain;
676-699 1.46e-08

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 50.83  E-value: 1.46e-08
                          10        20
                  ....*....|....*....|....
gi 1030311311 676 ELQRHRRTHTGEKRFECPECSKRF 699
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 690-712 2.56e-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: 41.52  E-value: 2.56e-05
                          10        20
                  ....*....|....*....|...
gi 1030311311 690 FECPECSKRFMRSDHLSKHVKTH 712
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 660-684 4.74e-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: 40.75  E-value: 4.74e-05
                          10        20
                  ....*....|....*....|....*
gi 1030311311 660 FICNwmFCGKRFTRSDELQRHRRTH 684
Cdd:pfam00096   1 YKCP--DCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 630-654 8.92e-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: 8.92e-03
                          10        20
                  ....*....|....*....|....*
gi 1030311311 630 HICHIegCGKVYGKTSHLRAHLRWH 654
Cdd:pfam00096   1 YKCPD--CGKSFSRKSNLKRHLRTH 23
 
Name Accession Description Interval E-value
SP4_N cd22536
N-terminal domain of transcription factor Specificity Protein (SP) 4; Specificity Proteins ...
 15-631 0e+00

N-terminal domain of transcription factor Specificity Protein (SP) 4; Specificity Proteins (SPs) are transcription factors that are involved in many cellular processes, including cell differentiation, cell growth, apoptosis, immune responses, response to DNA damage, and chromatin remodeling. Human SP4 is a risk gene of multiple psychiatric disorders including schizophrenia, bipolar disorder, and major depression. SP4 belongs to a family of proteins, called the SP/Kruppel or Krueppel-like Factor (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. SP factors preferentially bind GC boxes, while KLFs bind CACCC boxes. Another characteristic hallmark of SP factors is the presence of the Buttonhead (BTD) box CXCPXC, just N-terminal to the zinc fingers. The function of the BTD box is unknown, but it is thought to play an important physiological role. Another feature of most SP factors is the presence of a conserved amino acid stretch, the so-called SP box, located close to the N-terminus. SP factors may be separated into three groups based on their domain architecture and the similarity of their N-terminal transactivation domains: SP1-4, SP5, and SP6-9. The transactivation domains between the three groups are not homologous to one another. SP1-4 have similar N-terminal transactivation domains characterized by glutamine-rich regions, which, in most cases, have adjacent serine/threonine-rich regions. This model represents the N-terminal domain of SP4.


Pssm-ID: 411773 [Multi-domain]  Cd Length: 623  Bit Score: 740.58  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030311311  15 NKKPKTSGSQDSQPSPLALLAATCSKIGTPGENQATGQ-QQIIIDPSQGLVQLQNQPQQLELVTTQLAGNAWQLVASTPP 93
Cdd:cd22536     1 NKKGKTSGSQDSQPSPLALLAATCSKIGTPGENQGAGQqQQIIIDPSQGLVQLQNQPQQLELVTTQLAGNAWQIVAAAPP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030311311  94 ASKENNVSQP----ASSSSSSSSSNNGSASPTKTKSGNS--STPGQFQVIQVQ---NPSGSVQYQVIPQLQTVEGQQIQI 164
Cdd:cd22536    81 TSKENNVAQQgvsaATSSAAPSSSNNGSTSPTKVKAGNSnaSAPGQFQVIQVQnmqNPSGSVQYQVIPQIQTVEGQQIQI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030311311 165 NPTSSSSLQDLQGQIQLISAGNNQAILTAANRTASGNILAQNLANQTVPVQIRPGVSIPLQLQTLPGTQAQVVTTLPINI 244
Cdd:cd22536   161 SPANATALQDLQGQIQLIPAGNNQAILTTPNRTASGNIIAQNLANQTVPVQIRPGVSIPLQLQTIPGAQAQVVTTLPINI 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030311311 245 GGVTLALPVINNVAAGGGTGQVGQPAataDSGTSNGNQLVSTPTnTTTSASTMPESPSSSTTCTTTASTSLTSSDTLVSS 324
Cdd:cd22536   241 GGVTLALPVINNVAAGGGSGQLVQPS---DGGVSNGNQLVSTPI-TTASVSTMPESPSSSTTCTTTASTSLTSSDTLVSS 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030311311 325 ADTGQYASTSASSsERTIEESQTPAAtESEAQSSSQLQPNGMQNAQDQSNSLQQVQIVGQPILQQIQIQQPQQQIIQAIP 404
Cdd:cd22536   317 AETGQYASTAASS-ERTEEEPQTSAA-ESEAQSSSQLQSNGLQNVQDQSNSLQQVQIVGQPILQQIQIQQPQQQIIQAIQ 394

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030311311 405 PQSFQLQSGQTIQTIQQQPLQNVQLQAV-NPTQVLIRAPTLTPSGQISWQTVQVQNIQSLSNLQVQNAGLSQQLTITPVS 483
Cdd:cd22536   395 PQSFQLQSGQTIQTIQQQPLQNVQLQAVqSPTQVLIRAPTLTPSGQISWQTVQVQNIQSLSNLQVQNAGLPQQLTLTPVS 474

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030311311 484 SS-GGTTLAQIAPVAVAGAPITLNTAQLASVPNLQTVSVANLGAAGVQVQGVPVTITSVAGQQQGQDGVKVQQATIAPVT 562
Cdd:cd22536   475 SSaGGTTIAQIAPVAVAGTPITLNAAQLASVPNLQTVNVANLGAAGVQVQGVPVTITSVAGQQQGQDGVKVQQATIAPVT 554

                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1030311311 563 VAVGGIANATIGAVSPDQLTQVHLQQGQQTSDQEVQPGKRLRRVACSCPNCREGEGRGSNEPGKKKQHI 631
Cdd:cd22536   555 VAVGNIANATIGAVSPDQITQVQLQQAQQASDQEVQPGKRLRRVACSCPNCREGEGRGSSEPGKKKQHI 623
zf-H2C2_2 pfam13465
Zinc-finger double domain;
676-699 1.46e-08

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 50.83  E-value: 1.46e-08
                          10        20
                  ....*....|....*....|....
gi 1030311311 676 ELQRHRRTHTGEKRFECPECSKRF 699
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 690-712 2.56e-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: 41.52  E-value: 2.56e-05
                          10        20
                  ....*....|....*....|...
gi 1030311311 690 FECPECSKRFMRSDHLSKHVKTH 712
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 660-684 4.74e-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: 40.75  E-value: 4.74e-05
                          10        20
                  ....*....|....*....|....*
gi 1030311311 660 FICNwmFCGKRFTRSDELQRHRRTH 684
Cdd:pfam00096   1 YKCP--DCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
646-673 1.05e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.66  E-value: 1.05e-04
                          10        20
                  ....*....|....*....|....*...
gi 1030311311 646 HLRAHLRWHTGERPFICnwMFCGKRFTR 673
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKC--PECGKSFKS 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
645-716 2.76e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 44.30  E-value: 2.76e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1030311311 645 SHLRAHLRW--HTGE--RPFICNWMFCGKRFTRSDELQRHRRTHTGEKRFECP--ECSKRFMRSDHLSKHVKTHQNKK 716
Cdd:COG5048   303 SPLTRHLRSvnHSGEslKPFSCPYSLCGKLFSRNDALKRHILLHTSISPAKEKllNSSSKFSPLLNNEPPQSLQQYKD 380
ZnF_C2H2 smart00355
zinc finger;
690-712 3.91e-04

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 38.22  E-value: 3.91e-04
                           10        20
                   ....*....|....*....|...
gi 1030311311  690 FECPECSKRFMRSDHLSKHVKTH 712
Cdd:smart00355   1 YRCPECGKVFKSKSALREHMRTH 23
ZnF_C2H2 smart00355
zinc finger;
660-684 1.95e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 36.29  E-value: 1.95e-03
                           10        20
                   ....*....|....*....|....*
gi 1030311311  660 FICNWmfCGKRFTRSDELQRHRRTH 684
Cdd:smart00355   1 YRCPE--CGKVFKSKSALREHMRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 630-654 8.92e-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: 8.92e-03
                          10        20
                  ....*....|....*....|....*
gi 1030311311 630 HICHIegCGKVYGKTSHLRAHLRWH 654
Cdd:pfam00096   1 YKCPD--CGKSFSRKSNLKRHLRTH 23
 
Name Accession Description Interval E-value
SP4_N cd22536
N-terminal domain of transcription factor Specificity Protein (SP) 4; Specificity Proteins ...
 15-631 0e+00

N-terminal domain of transcription factor Specificity Protein (SP) 4; Specificity Proteins (SPs) are transcription factors that are involved in many cellular processes, including cell differentiation, cell growth, apoptosis, immune responses, response to DNA damage, and chromatin remodeling. Human SP4 is a risk gene of multiple psychiatric disorders including schizophrenia, bipolar disorder, and major depression. SP4 belongs to a family of proteins, called the SP/Kruppel or Krueppel-like Factor (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. SP factors preferentially bind GC boxes, while KLFs bind CACCC boxes. Another characteristic hallmark of SP factors is the presence of the Buttonhead (BTD) box CXCPXC, just N-terminal to the zinc fingers. The function of the BTD box is unknown, but it is thought to play an important physiological role. Another feature of most SP factors is the presence of a conserved amino acid stretch, the so-called SP box, located close to the N-terminus. SP factors may be separated into three groups based on their domain architecture and the similarity of their N-terminal transactivation domains: SP1-4, SP5, and SP6-9. The transactivation domains between the three groups are not homologous to one another. SP1-4 have similar N-terminal transactivation domains characterized by glutamine-rich regions, which, in most cases, have adjacent serine/threonine-rich regions. This model represents the N-terminal domain of SP4.


Pssm-ID: 411773 [Multi-domain]  Cd Length: 623  Bit Score: 740.58  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030311311  15 NKKPKTSGSQDSQPSPLALLAATCSKIGTPGENQATGQ-QQIIIDPSQGLVQLQNQPQQLELVTTQLAGNAWQLVASTPP 93
Cdd:cd22536     1 NKKGKTSGSQDSQPSPLALLAATCSKIGTPGENQGAGQqQQIIIDPSQGLVQLQNQPQQLELVTTQLAGNAWQIVAAAPP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030311311  94 ASKENNVSQP----ASSSSSSSSSNNGSASPTKTKSGNS--STPGQFQVIQVQ---NPSGSVQYQVIPQLQTVEGQQIQI 164
Cdd:cd22536    81 TSKENNVAQQgvsaATSSAAPSSSNNGSTSPTKVKAGNSnaSAPGQFQVIQVQnmqNPSGSVQYQVIPQIQTVEGQQIQI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030311311 165 NPTSSSSLQDLQGQIQLISAGNNQAILTAANRTASGNILAQNLANQTVPVQIRPGVSIPLQLQTLPGTQAQVVTTLPINI 244
Cdd:cd22536   161 SPANATALQDLQGQIQLIPAGNNQAILTTPNRTASGNIIAQNLANQTVPVQIRPGVSIPLQLQTIPGAQAQVVTTLPINI 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030311311 245 GGVTLALPVINNVAAGGGTGQVGQPAataDSGTSNGNQLVSTPTnTTTSASTMPESPSSSTTCTTTASTSLTSSDTLVSS 324
Cdd:cd22536   241 GGVTLALPVINNVAAGGGSGQLVQPS---DGGVSNGNQLVSTPI-TTASVSTMPESPSSSTTCTTTASTSLTSSDTLVSS 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030311311 325 ADTGQYASTSASSsERTIEESQTPAAtESEAQSSSQLQPNGMQNAQDQSNSLQQVQIVGQPILQQIQIQQPQQQIIQAIP 404
Cdd:cd22536   317 AETGQYASTAASS-ERTEEEPQTSAA-ESEAQSSSQLQSNGLQNVQDQSNSLQQVQIVGQPILQQIQIQQPQQQIIQAIQ 394

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030311311 405 PQSFQLQSGQTIQTIQQQPLQNVQLQAV-NPTQVLIRAPTLTPSGQISWQTVQVQNIQSLSNLQVQNAGLSQQLTITPVS 483
Cdd:cd22536   395 PQSFQLQSGQTIQTIQQQPLQNVQLQAVqSPTQVLIRAPTLTPSGQISWQTVQVQNIQSLSNLQVQNAGLPQQLTLTPVS 474

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030311311 484 SS-GGTTLAQIAPVAVAGAPITLNTAQLASVPNLQTVSVANLGAAGVQVQGVPVTITSVAGQQQGQDGVKVQQATIAPVT 562
Cdd:cd22536   475 SSaGGTTIAQIAPVAVAGTPITLNAAQLASVPNLQTVNVANLGAAGVQVQGVPVTITSVAGQQQGQDGVKVQQATIAPVT 554

                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1030311311 563 VAVGGIANATIGAVSPDQLTQVHLQQGQQTSDQEVQPGKRLRRVACSCPNCREGEGRGSNEPGKKKQHI 631
Cdd:cd22536   555 VAVGNIANATIGAVSPDQITQVQLQQAQQASDQEVQPGKRLRRVACSCPNCREGEGRGSSEPGKKKQHI 623
SP3_N cd22537
N-terminal domain of transcription factor Specificity Protein (SP) 3; Specificity Proteins ...
 20-631 1.56e-58

N-terminal domain of transcription factor Specificity Protein (SP) 3; Specificity Proteins (SPs) are transcription factors that are involved in many cellular processes, including cell differentiation, cell growth, apoptosis, immune responses, response to DNA damage, and chromatin remodeling. SP1 and SP3 can interact with and recruit a large number of proteins including the transcription initiation complex, histone modifying enzymes, and chromatin remodeling complexes, which strongly suggest that SP1 and SP3 are important transcription factors in remodeling chromatin and the regulation of gene expression. SP3 belongs to a family of proteins, called the SP/Kruppel or Krueppel-like Factor (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. SP factors preferentially bind GC boxes, while KLFs bind CACCC boxes. Another characteristic hallmark of SP factors is the presence of the Buttonhead (BTD) box CXCPXC, just N-terminal to the zinc fingers. The function of the BTD box is unknown, but it is thought to play an important physiological role. Another feature of most SP factors is the presence of a conserved amino acid stretch, the so-called SP box, located close to the N-terminus. SP factors may be separated into three groups based on their domain architecture and the similarity of their N-terminal transactivation domains: SP1-4, SP5, and SP6-9. The transactivation domains between the three groups are not homologous to one another. SP1-4 have similar N-terminal transactivation domains characterized by glutamine-rich regions, which, in most cases, have adjacent serine/threonine-rich regions. This model represents the N-terminal domain of SP3.


Pssm-ID: 411774 [Multi-domain]  Cd Length: 574  Bit Score: 209.03  E-value: 1.56e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030311311  20 TSGSQDSQPSPLALLAATCSKIGTPGENqatgqqqiiiDPSQGLVQLQNQPQQLELVTTQLAG--NAWQLVASTPPASKE 97
Cdd:cd22537     1 GAAEQDTQPSPLALLAATCSKIGSPSPG----------DDAAAAGNAASAGQTGDLASAQLTGapNRWEVLTPTPTTIKD 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030311311  98 NNVSQPASSSSSSSSSNNGSASPTKTKSGNSstpgQFQVIQVQNPSG----SVQYQVIPQLQTVEGQQIQINPTSSS--- 170
Cdd:cd22537    71 EAGNLVQIPGGGTVTSSGQYVLPLQSLQNQQ----IFSVAPGSDASNgtvpNVQYQVIPQIQTTDGQQVQLGFATSSdnt 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030311311 171 SLQDLQGQIQLISaGNNQAILTAANRTASgnilAQNLANQTVPVQIrPGVSIPlqlQTLPGTQAQVVTTLPINIGGVTLA 250
Cdd:cd22537   147 GLQQEGGQIQIIP-GSNQTIIASGTPSAV----QQLLSQSGHVVQI-QGVSIG---GSSFPGQTQVVANVPLGLPGNITF 217

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030311311 251 LPvINNVAAG----GGTGQVGQPAATADSGTSNGNQLVSTPTNTTTSASTMPESPSSST--------TCTTTASTSLTSS 318
Cdd:cd22537   218 VP-INSVDLDslglSGTSQTMTTGITADGQLINTGQAVQSSDNSGESGKVSPDINETNTnadlfvptSSSSQLPVTIDST 296

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030311311 319 DTLVSSADTGQYASTSASSSERTIEESQTPAATESEAQS---SSQLQPNGMQNAQDQSNSLQQVQIVgqpilqqiqiqqp 395
Cdd:cd22537   297 GILQQNASSLTTVSGQVHTSDLQGNYIQAPVSDETQAQNiqvSTAQPSVQQIQLHESQQPTSQAQIV------------- 363

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030311311 396 qqqiiQAIPPQSFQLQSGQTIQTIQQQPLQNVQLQAVNPTQVLIRAPTLTPSGQISWQTVQVQNIQSLSNLQVQNAGlSQ 475
Cdd:cd22537   364 -----QGITQQAIQGVQALGAQAIPQQALQNLQLQLLNPGTFLIQAQTVTPSGQITWQTFQVQGVQNLQNLQIQNAP-AQ 437

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030311311 476 QLTITPVSSsggTTLAQI-APVAVAGAPITLNTAQLasvPNLQTVSVANLGAAGVQVQgvpvtitsvagqqQGQDGVKVQ 554
Cdd:cd22537   438 QITLTPVQT---LTLGQVgAGGAITSTPVSLSTGQL---PNLQTVTVNSIDSAGIQLQ-------------QSENADSPA 498

                         570       580       590       600       610       620       630
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1030311311 555 QATIAPVTVAVGGIANATIGAVSPDQLTQVHLQQGQQTSDQEVQPGKRLRRVACSCPNCREGEGRGSNEpGKKKQHI 631
Cdd:cd22537   499 DIQIKEEEPDSEEWQLSGDSTLNTNDLTHLRVQLVEEEGDQPHQEGKRLRRVACTCPNCKEGGGRGSNL-GKKKQHI 574
SP1_N cd22539
N-terminal domain of transcription factor Specificity Protein (SP) 1; Specificity Proteins ...
 21-631 1.40e-44

N-terminal domain of transcription factor Specificity Protein (SP) 1; Specificity Proteins (SPs) are transcription factors that are involved in many cellular processes, including cell differentiation, cell growth, apoptosis, immune responses, response to DNA damage, and chromatin remodeling. SP1 has been shown to interact with a variety of proteins including myogenin, SMAD3, SUMO1, SF1, TAL1, and UBC. Some 12,000 SP1 binding sites are found in the human genome. SP1 belongs to a family of proteins, called the SP/Kruppel or Krueppel-like Factor (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. SP factors preferentially bind GC boxes, while KLF bind CACCC boxes. Another characteristic hallmark of SP factors is the presence of the Buttonhead (BTD) box CXCPXC, just N-terminal to the zinc fingers. The function of the BTD box is unknown, but it is thought to play an important physiological role. Another feature of most SP factors is the presence of a conserved amino acid stretch, the so-called SP box, located close to the N-terminus. SP factors may be separated into three groups based on their domain architecture and the similarity of their N-terminal transactivation domains: SP1-4, SP5, and SP6-9. The transactivation domains between the three groups are not homologous to one another. SP1-4 have similar N-terminal transactivation domains characterized by glutamine-rich regions, which, in most cases, have adjacent serine/threonine-rich regions. This model represents the N-terminal domain of SP1.


Pssm-ID: 411775  Cd Length: 433  Bit Score: 166.23  E-value: 1.40e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030311311  21 SGSQDSQPSPLALLAATCSKIGTPGENQATGQQQiiidpsqglvQLQNQPQQLELVTTQLA--GNAWQLVASTPPASKEN 98
Cdd:cd22539     2 SGGQESQPSPLALLAATCSRIESPNENSNSSQQQ----------QQQQGELELDLTQAQIAqsANGWQIIPTGSQAPTPS 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030311311  99 NvSQPASSSSSSSSSNNGSASPTKTKSGNSSTPGQFQVIQVQNPSGSVQYQVIPQLQTVEGQQIQINPTSSSSLQDLQGQ 178
Cdd:cd22539    72 K-EQSGDSSTADSSKKSRVATAGYVVVAAPNLQNQQVLTSLPGVMPNIQYQVIPQFQTVDGQQLQFATTQAQVQQDASGQ 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030311311 179 IQLISAGNNQAIltAANRTASGNILAQ-NLANQTVPVQirpgvSIPLQLQTLPGtQAQVVTTLPINIGGVTLALPViNNV 257
Cdd:cd22539   151 LQIIPGTNQQII--TTNRSGSGNIITMpNLLQQAVPIQ-----GLGLANNVLPG-QTQFVANVPVALNGNITLLPV-SSV 221

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030311311 258 AAgggtgqvgqpaatadSGTSNGNQLVSTptnTTTSAStmpespsssttctttastsltssdtlvssadtgqyastsass 337
Cdd:cd22539   222 TA---------------SFFTNANSYSTT---TTTSNM------------------------------------------ 241

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030311311 338 sertieesqtpaateSEAQSSSQLQPNGMQNAQdQSNSLQQVQIVGqpilqqiqiqqpqqqiiqaippQSFQLQSgqtiq 417
Cdd:cd22539   242 ---------------GQQQQQILIQPQLVQGGQ-TIQALQAASLPG----------------------QTFTTQT----- 278

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030311311 418 tIQQQPLQNVQLQAV-NPTQVLIRAPtLTPSGQISWQTVQVQNIQSlsnlqvqnaglsqqltitpvsssggttlaqiapv 496
Cdd:cd22539   279 -ISQEALQNLQIQTVpNSGPIIIRTP-VGPNGQVSWQTIQLQNLQT---------------------------------- 322

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030311311 497 avagapITLNTAQLASVPNLQTVSVANLGAAGVQV---QGVPVTITSVAGQQQGQDGVKvqqatiapvtvAVGGIANATI 573
Cdd:cd22539   323 ------VTVNAAQLSSMPGLQTINLNALGASGIQVhqlQGLPLTIANATGEHGAQLGLH-----------GAGGDGLHDD 385

                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1030311311 574 GAVspdqltqvhlQQGQQTSDQEVQPGKRLRRVACSCPNCREGEGRGSNEPGKKKQHI 631
Cdd:cd22539   386 SAA----------EEGETEPDPQPQPGRRTRREACTCPYCKDGEGRDSGDPGKKKQHI 433
SP2_N cd22540
N-terminal domain of transcription factor Specificity Protein (SP) 2; Specificity Proteins ...
 17-628 5.28e-29

N-terminal domain of transcription factor Specificity Protein (SP) 2; Specificity Proteins (SPs) are transcription factors that are involved in many cellular processes, including cell differentiation, cell growth, apoptosis, immune responses, response to DNA damage, and chromatin remodeling. SP2 contains the least conserved DNA-binding domain within the SP subfamily of proteins, and its DNA sequence specificity differs from the other SP proteins. It localizes primarily within subnuclear foci associated with the nuclear matrix, and can activate, or in some cases, repress expression from different promoters. The transcription factor SP2 serves as a paradigm for indirect genomic binding. It does not require its DNA-binding domain for genomic DNA binding and occupies target promoters independently of whether they contain a cognate DNA-binding motif. SP2 belongs to a family of proteins, called the SP/Kruppel or Krueppel-like Factor (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. SP factors preferentially bind GC boxes, while KLFs bind CACCC boxes. Another characteristic hallmark of SP factors is the presence of the Buttonhead (BTD) box CXCPXC, just N-terminal to the zinc fingers. The function of the BTD box is unknown, but it is thought to play an important physiological role. Another feature of most SP factors is the presence of a conserved amino acid stretch, the so-called SP box, located close to the N-terminus. SP factors may be separated into three groups based on their domain architecture and the similarity of their N-terminal transactivation domains: SP1-4, SP5, and SP6-9. The transactivation domains between the three groups are not homologous to one another. SP1-4 have similar N-terminal transactivation domains characterized by glutamine-rich regions, which, in most cases, have adjacent serine/threonine-rich regions. This model represents the N-terminal domain of SP2.


Pssm-ID: 411776 [Multi-domain]  Cd Length: 511  Bit Score: 121.96  E-value: 5.28e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030311311  17 KPKTSGSQDSQPSPLALLAATCSKIGTPGenqatgqQQIIIDPSQGLvqlqnQPQQLELVTtqlagnawQLVASTPPASK 96
Cdd:cd22540    13 QPAASTTQDSQPSPLALLAATCSKIGPPA-------VEAAVTPPAPP-----QPTPRKLVP--------IKPAPLPLGPG 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030311311  97 ENNVSQPASSSSSSSSSNNGsasptktksGNSSTPGQFQVIQVQNP-----------SGSVQYQVIPQLQTvegqqiqin 165
Cdd:cd22540    73 KNSIGFLSAKGNIIQLQGSQ---------LSSSAPGGQQVFAIQNPtmiikgsqtrsSTNQQYQISPQIQA--------- 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030311311 166 ptssSSLQDLQGQIQLISaGNNQAILTAANRTASGNILAQnlanqtvPVQIRPGVSIPLQLQTLPGTQAQVVTTLPINiG 245
Cdd:cd22540   135 ----AGQINNSGQIQIIP-GTNQAIITPVQVLQQPQQAHK-------PVPIKPAPLQTSNTNSASLQVPGNVIKLQSG-G 201

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030311311 246 GVTLALPVINNVAAGGGTGQVGQPAATADSGTSNGNQlvstptntttsastmpespsssttctttastsltssdtlvsSA 325
Cdd:cd22540   202 NVALTLPVNNLVGTQDGATQLQLAAAPSKPSKKIRKK-----------------------------------------SA 240

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030311311 326 DTGQYASTSASSSERTIEESQTPAATESEAQSSSQLQPNGMQNAQdqsnsLQQVQIVgqpilqqIQIQQPQQQIIQAIPP 405
Cdd:cd22540   241 QAAQPAVTVAEQVETVLIETTADNIIQAGNNLLIVQSPGTGQPAV-----LQQVQVL-------QPKQEQQVVQIPQQAL 308

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030311311 406 QSFQLQSgQTIQTIQQQPLQNVQLQAVN--PTQVLIRaptlTPSGQISWQTVQVQNI----QSLSNLQVQNAGLSQQLTI 479
Cdd:cd22540   309 RVVQAAS-ATLPTVPQKPLQNIQIQNSEptPTQVYIK----TPSGEVQTVLLQEAPAatatPSSSTSTVQQQVTANNGTG 383

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030311311 480 TPVSSSG---GTTLAQIAPvavAGAPITLNTAQLASVPN-LQTVSVanlgaAGVQVQGVPVTITSVAGQQQGqdgvkvqq 555
Cdd:cd22540   384 TSKPNYNvrkERTLPKIAP---AGGIISLNAAQLAAAAQaIQTINI-----NGVQVQGVPVTITNAGGQQQL-------- 447

                         570       580       590       600       610       620       630
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1030311311 556 atiapVTVAVGGiANATIGAVSPDQLTqvhlQQGQQTSDQEVQPGKRLRRVACSCPNCREGEGRgSNEPGKKK 628
Cdd:cd22540   448 -----TVQTVSS-NNLTISGLSPTQIQ----LQMEQALEIETQPGEKRRRMACTCPNCKDGEKR-SGEQGKKK 509
SP1-4_N cd22545
N-terminal domain of transcription factor Specificity Proteins (SP) 1-4; Specificity Proteins ...
 591-631 4.21e-15

N-terminal domain of transcription factor Specificity Proteins (SP) 1-4; Specificity Proteins (SPs) are transcription factors that are involved in many cellular processes, including cell differentiation, cell growth, apoptosis, immune responses, response to DNA damage, and chromatin remodeling. There are many SPs in vertebrates (9 SPs in humans and mice, 7 SPs in chicken, and 11 SPs in teleost fish), but arthropods only have 3 SPs. SPs belong to a family of proteins, called the SP/Kruppel or Krueppel-like Factor (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. SP factors preferentially bind GC boxes, while KLFs bind CACCC boxes. Another characteristic hallmark of SP factors is the presence of the Buttonhead (BTD) box CXCPXC, just N-terminal to the zinc fingers. The function of the BTD box is unknown, but it is thought to play an important physiological role. Another feature of most SP factors is the presence of a conserved amino acid stretch, the so-called SP box, located close to the N-terminus. SP factors may be separated into three groups based on their domain architecture and the similarity of their N-terminal transactivation domains: SP1-4, SP5, and SP6-9. The transactivation domains between the three groups are not homologous to one another. SP1-4 have similar N-terminal transactivation domains characterized by glutamine-rich regions, which, in most cases, have adjacent serine/threonine-rich regions. This model represents the N-terminal domain of SP1-4.


Pssm-ID: 411777 [Multi-domain]  Cd Length: 82  Bit Score: 70.94  E-value: 4.21e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1030311311 591 QTSDQEVQPGKRLRRVACSCPNCREGEGRGSNEpGKKKQHI 631
Cdd:cd22545    43 QFQDQEPQPGKRLRRVACTCPNCKDGEGRGSED-GKKKQHI 82
SP1-4_N cd22545
N-terminal domain of transcription factor Specificity Proteins (SP) 1-4; Specificity Proteins ...
 20-55 5.68e-11

N-terminal domain of transcription factor Specificity Proteins (SP) 1-4; Specificity Proteins (SPs) are transcription factors that are involved in many cellular processes, including cell differentiation, cell growth, apoptosis, immune responses, response to DNA damage, and chromatin remodeling. There are many SPs in vertebrates (9 SPs in humans and mice, 7 SPs in chicken, and 11 SPs in teleost fish), but arthropods only have 3 SPs. SPs belong to a family of proteins, called the SP/Kruppel or Krueppel-like Factor (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. SP factors preferentially bind GC boxes, while KLFs bind CACCC boxes. Another characteristic hallmark of SP factors is the presence of the Buttonhead (BTD) box CXCPXC, just N-terminal to the zinc fingers. The function of the BTD box is unknown, but it is thought to play an important physiological role. Another feature of most SP factors is the presence of a conserved amino acid stretch, the so-called SP box, located close to the N-terminus. SP factors may be separated into three groups based on their domain architecture and the similarity of their N-terminal transactivation domains: SP1-4, SP5, and SP6-9. The transactivation domains between the three groups are not homologous to one another. SP1-4 have similar N-terminal transactivation domains characterized by glutamine-rich regions, which, in most cases, have adjacent serine/threonine-rich regions. This model represents the N-terminal domain of SP1-4.


Pssm-ID: 411777 [Multi-domain]  Cd Length: 82  Bit Score: 58.99  E-value: 5.68e-11
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1030311311  20 TSGSQDSQPSPLALLAATCSKIGTPGENQATGQQQI 55
Cdd:cd22545     1 TSSAQDSQPSPLALLAATCSKIGSPAENSTGPGGNI 36
zf-H2C2_2 pfam13465
Zinc-finger double domain;
676-699 1.46e-08

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 50.83  E-value: 1.46e-08
                          10        20
                  ....*....|....*....|....
gi 1030311311 676 ELQRHRRTHTGEKRFECPECSKRF 699
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
SP1-4_arthropods_N cd22553
N-terminal domain of transcription factor Specificity Protein (SP) 1-4 from arthropods; ...
 445-631 4.43e-07

N-terminal domain of transcription factor Specificity Protein (SP) 1-4 from arthropods; Specificity Proteins (SPs) are transcription factors that are involved in many cellular processes, including cell differentiation, cell growth, apoptosis, immune responses, response to DNA damage, and chromatin remodeling. There are many SPs in vertebrates (9 SPs in humans and mice, 7 SPs in the chicken, and 11 SPs in teleost fish), but arthropods only have 3 SPs. One SP is clade SP1-4, which is expressed ubiquitously throughout development. SP1-4 belongs to a family of proteins, called the SP/Kruppel or Krueppel-like Factor (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. SP factors preferentially bind GC boxes, while KLFs bind CACCC boxes. Another characteristic hallmark of SP factors is the presence of the Buttonhead (BTD) box CXCPXC, just N-terminal to the zinc fingers. The function of the BTD box is unknown, but it is thought to play an important physiological role. Another feature of most SP factors is the presence of a conserved amino acid stretch, the so-called SP box, located close to the N-terminus. This model represents the N-terminal domain of SP1-4 from arthropods.


Pssm-ID: 411778 [Multi-domain]  Cd Length: 384  Bit Score: 52.72  E-value: 4.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030311311 445 TPSGQISWQTVqVQNIQSLSNLQVQNAGLSQQLTITPVSSSGGTTLAQIAPVAVAGAPITLNTAQLASVPNLQTVSVANL 524
Cdd:cd22553   216 QVSSQGYIQQI-PANASQQQPQMVQQGPNQSGQIIGQVASASSIQAAAIPLTVYTGALAGQNGSNQQQVGQIVTSPIQGM 294

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030311311 525 gaagvqVQGVPVTITSVAGQQQGQdgvkvQQATIAPVTVAVGGIANATIGAVSPDQLTQvhlqqGQQTSDQEVQPGKRLR 604
Cdd:cd22553   295 ------TQGLTAPASSSIPTVVQQ-----QAIQGNPLPPGTQIIAAGQQLQQDPNDPTK-----WQVVADGTPGSKKRLR 358

                         170       180
                  ....*....|....*....|....*..
gi 1030311311 605 RVACSCPNCREGEGRGSNEpGKKKQHI 631
Cdd:cd22553   359 RVACTCPNCRDGDGTRNGE-NKKKQHI 384
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 690-712 2.56e-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: 41.52  E-value: 2.56e-05
                          10        20
                  ....*....|....*....|...
gi 1030311311 690 FECPECSKRFMRSDHLSKHVKTH 712
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 660-684 4.74e-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: 40.75  E-value: 4.74e-05
                          10        20
                  ....*....|....*....|....*
gi 1030311311 660 FICNwmFCGKRFTRSDELQRHRRTH 684
Cdd:pfam00096   1 YKCP--DCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
646-673 1.05e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.66  E-value: 1.05e-04
                          10        20
                  ....*....|....*....|....*...
gi 1030311311 646 HLRAHLRWHTGERPFICnwMFCGKRFTR 673
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKC--PECGKSFKS 26
zf-C2H2_4 pfam13894
C2H2-type zinc finger; This family contains a number of divergent C2H2 type zinc fingers.
 690-712 1.64e-04

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


Pssm-ID: 464025  Cd Length: 24  Bit Score: 39.16  E-value: 1.64e-04
                          10        20
                  ....*....|....*....|...
gi 1030311311 690 FECPECSKRFMRSDHLSKHVKTH 712
Cdd:pfam13894   1 FKCPICGKSFSSKKSLKRHLKTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
645-716 2.76e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 44.30  E-value: 2.76e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1030311311 645 SHLRAHLRW--HTGE--RPFICNWMFCGKRFTRSDELQRHRRTHTGEKRFECP--ECSKRFMRSDHLSKHVKTHQNKK 716
Cdd:COG5048   303 SPLTRHLRSvnHSGEslKPFSCPYSLCGKLFSRNDALKRHILLHTSISPAKEKllNSSSKFSPLLNNEPPQSLQQYKD 380
ZnF_C2H2 smart00355
zinc finger;
690-712 3.91e-04

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 38.22  E-value: 3.91e-04
                           10        20
                   ....*....|....*....|...
gi 1030311311  690 FECPECSKRFMRSDHLSKHVKTH 712
Cdd:smart00355   1 YRCPECGKVFKSKSALREHMRTH 23
SP5_N cd22541
N-terminal domain of transcription factor Specificity Protein (SP) 5; Specificity Proteins ...
 526-631 3.97e-04

N-terminal domain of transcription factor Specificity Protein (SP) 5; Specificity Proteins (SPs) are transcription factors that are involved in many cellular processes, including cell differentiation, cell growth, apoptosis, immune responses, response to DNA damage, and chromatin remodeling. There are many SPs in vertebrates (9 SPs in humans and mice, 7 SPs in the chicken, and 11 SPs in teleost fish), but arthropods only have 3 SPs. All of them contain clade SP5, which plays a potential role in human cancers and was found in several human tumors including hepatocellular carcinoma, gastric cancer, and colon cancer. Leukemia inhibitor factor/Stat3 and Wnt/beta-catenin signaling pathways converge on SP5 to promote mouse embryonic stem cell self-renewal. SP5 belongs to a family of proteins, called the SP/Kruppel or Krueppel-like Factor (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. SP factors preferentially bind GC boxes, while KLFs bind CACCC boxes. Another characteristic hallmark of SP factors is the presence of the Buttonhead (BTD) box CXCPXC, just N-terminal to the zinc fingers. The function of the BTD box is unknown, but it is thought to play an important physiological role. Another feature of most SP factors is the presence of a conserved amino acid stretch, the so-called SP box, located close to the N-terminus. SP factors may be separated into three groups based on their domain architecture and the similarity of their N-terminal transactivation domains: SP1-4, SP5, and SP6-9. The transactivation domains between the three groups are not homologous to one another. This model represents the N-terminal domain of SP5.


Pssm-ID: 412096 [Multi-domain]  Cd Length: 143  Bit Score: 41.40  E-value: 3.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030311311 526 AAGVQVQGVPVTITSVAGQQQGQDGVK------VQQATIAPVTVAVGGIANATiGAVSPDQLTqvHLQQGQQTSDQEVQP 599
Cdd:cd22541    40 AASAPPHPSPVSSPTQQPQQLPPNPADdipwwsIQQSNPAHPPSTSTPLGHPT-FAGYQPQIA--ALLQTKSPAASLSTT 116

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1030311311 600 gKRLRRvaCSCPNCREGEGrgSNEPGKKKQHI 631
Cdd:cd22541   117 -RRCRR--CRCPNCQNPST--SSEPGKKKQHI 143
ZnF_C2H2 smart00355
zinc finger;
660-684 1.95e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 36.29  E-value: 1.95e-03
                           10        20
                   ....*....|....*....|....*
gi 1030311311  660 FICNWmfCGKRFTRSDELQRHRRTH 684
Cdd:smart00355   1 YRCPE--CGKVFKSKSALREHMRTH 23
zf-C2H2_4 pfam13894
C2H2-type zinc finger; This family contains a number of divergent C2H2 type zinc fingers.
 660-684 7.47e-03

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


Pssm-ID: 464025  Cd Length: 24  Bit Score: 34.54  E-value: 7.47e-03
                          10        20
                  ....*....|....*....|....*
gi 1030311311 660 FICNwmFCGKRFTRSDELQRHRRTH 684
Cdd:pfam13894   1 FKCP--ICGKSFSSKKSLKRHLKTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 630-654 8.92e-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: 8.92e-03
                          10        20
                  ....*....|....*....|....*
gi 1030311311 630 HICHIegCGKVYGKTSHLRAHLRWH 654
Cdd:pfam00096   1 YKCPD--CGKSFSRKSNLKRHLRTH 23
 
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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