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Conserved domains on  [gi|6680582|ref|NP_032479|]
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Krueppel-like factor 3 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
KLF3_N cd21577
N-terminal domain of Kruppel-like factor 3; Kruppel-like factor 3 (KLF3; also called ...
49-259 2.83e-50

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: 166.75  E-value: 2.83e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680582   49 TPEGLTHGIQVEPVDLTVNKRGSPPAAGGSPSSLKFPShrrASPGLSMPSSSPPIKKYSPPSPGVQPFGVPLSMPPvMAA 128
Cdd:cd21577   9 TSFYSPSHSQLEPVDLSLSKRSSPPSSSSSSSSSSSSS---SSPSSRASPPSPYSKSSPPSPPQQRPLSPPLSLPP-PVA 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680582  129 ALSRHGIRSPGILPVIQPVVVQPVPFMYTSHLQQPLMVSLSEEMDN----SNSGMPVPVIESYEKPLLQKKIKIEPGIEP 204
Cdd:cd21577  85 PPPLSPGSVPGGLPVISPVMVQPVPVLYPPHLHQPIMVSSSPPPDDdhhhHKASSMKPSELGGDNHELHKPIKTEPRPEH 164
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 6680582  205 QRtDYYPEEMSPPLMNPVSPPQallqENHPSVIVQPGKRPLPVESPDTQRKRRIH 259
Cdd:cd21577 165 AQ-DPYSEEMSSSVISSPPEYE----SNTPSVIVHPGKRPLPVESPDTLKKRRIH 214
zf-H2C2_2 pfam13465
Zinc-finger double domain;
305-330 9.47e-07

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 44.67  E-value: 9.47e-07
                          10        20
                  ....*....|....*....|....*.
gi 6680582    305 ELTRHFRKHTGIKPFQCPDCDRSFSR 330
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
259-283 6.34e-04

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.


:

Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 36.51  E-value: 6.34e-04
                          10        20
                  ....*....|....*....|....*
gi 6680582    259 HRCDYdgCNKVYTKSSHLKAHRRTH 283
Cdd:pfam00096   1 YKCPD--CGKSFSRKSNLKRHLRTH 23
 
Name Accession Description Interval E-value
KLF3_N cd21577
N-terminal domain of Kruppel-like factor 3; Kruppel-like factor 3 (KLF3; also called ...
49-259 2.83e-50

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: 166.75  E-value: 2.83e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680582   49 TPEGLTHGIQVEPVDLTVNKRGSPPAAGGSPSSLKFPShrrASPGLSMPSSSPPIKKYSPPSPGVQPFGVPLSMPPvMAA 128
Cdd:cd21577   9 TSFYSPSHSQLEPVDLSLSKRSSPPSSSSSSSSSSSSS---SSPSSRASPPSPYSKSSPPSPPQQRPLSPPLSLPP-PVA 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680582  129 ALSRHGIRSPGILPVIQPVVVQPVPFMYTSHLQQPLMVSLSEEMDN----SNSGMPVPVIESYEKPLLQKKIKIEPGIEP 204
Cdd:cd21577  85 PPPLSPGSVPGGLPVISPVMVQPVPVLYPPHLHQPIMVSSSPPPDDdhhhHKASSMKPSELGGDNHELHKPIKTEPRPEH 164
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 6680582  205 QRtDYYPEEMSPPLMNPVSPPQallqENHPSVIVQPGKRPLPVESPDTQRKRRIH 259
Cdd:cd21577 165 AQ-DPYSEEMSSSVISSPPEYE----SNTPSVIVHPGKRPLPVESPDTLKKRRIH 214
zf-H2C2_2 pfam13465
Zinc-finger double domain;
305-330 9.47e-07

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 44.67  E-value: 9.47e-07
                          10        20
                  ....*....|....*....|....*.
gi 6680582    305 ELTRHFRKHTGIKPFQCPDCDRSFSR 330
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
169-331 3.94e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 45.07  E-value: 3.94e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680582  169 SEEMDNSNSGMPVPVIESYEKPLLQKKIKIEPGIEPQRTDYYPEEMSPPLMNPVSPPQALLQ----------------EN 232
Cdd:COG5048 182 SNLSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQspsslsssdssssaseSP 261
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680582  233 HPSVIVQPGKRPLPVESPDTQRKRRIHRCDYDGCNKVYTKSSHLKAHRRT--HTGE--KPYKCTWEGCTWKFARSDELTR 308
Cdd:COG5048 262 RSSLPTASSQSSSPNESDSSSEKGFSLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYSLCGKLFSRNDALKR 341
                       170       180
                ....*....|....*....|...
gi 6680582  309 HFRKHTGIKPFQCPDCDRSFSRS 331
Cdd:COG5048 342 HILLHTSISPAKEKLLNSSSKFS 364
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
259-283 6.34e-04

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 36.51  E-value: 6.34e-04
                          10        20
                  ....*....|....*....|....*
gi 6680582    259 HRCDYdgCNKVYTKSSHLKAHRRTH 283
Cdd:pfam00096   1 YKCPD--CGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
275-292 4.61e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.27  E-value: 4.61e-03
                          10
                  ....*....|....*...
gi 6680582    275 HLKAHRRTHTGEKPYKCT 292
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCP 18
ZnF_C2H2 smart00355
zinc finger;
319-341 6.57e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 33.59  E-value: 6.57e-03
                           10        20
                   ....*....|....*....|...
gi 6680582     319 FQCPDCDRSFSRSDHLALHRKRH 341
Cdd:smart00355   1 YRCPECGKVFKSKSALREHMRTH 23
 
Name Accession Description Interval E-value
KLF3_N cd21577
N-terminal domain of Kruppel-like factor 3; Kruppel-like factor 3 (KLF3; also called ...
49-259 2.83e-50

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: 166.75  E-value: 2.83e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680582   49 TPEGLTHGIQVEPVDLTVNKRGSPPAAGGSPSSLKFPShrrASPGLSMPSSSPPIKKYSPPSPGVQPFGVPLSMPPvMAA 128
Cdd:cd21577   9 TSFYSPSHSQLEPVDLSLSKRSSPPSSSSSSSSSSSSS---SSPSSRASPPSPYSKSSPPSPPQQRPLSPPLSLPP-PVA 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680582  129 ALSRHGIRSPGILPVIQPVVVQPVPFMYTSHLQQPLMVSLSEEMDN----SNSGMPVPVIESYEKPLLQKKIKIEPGIEP 204
Cdd:cd21577  85 PPPLSPGSVPGGLPVISPVMVQPVPVLYPPHLHQPIMVSSSPPPDDdhhhHKASSMKPSELGGDNHELHKPIKTEPRPEH 164
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 6680582  205 QRtDYYPEEMSPPLMNPVSPPQallqENHPSVIVQPGKRPLPVESPDTQRKRRIH 259
Cdd:cd21577 165 AQ-DPYSEEMSSSVISSPPEYE----SNTPSVIVHPGKRPLPVESPDTLKKRRIH 214
zf-H2C2_2 pfam13465
Zinc-finger double domain;
305-330 9.47e-07

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 44.67  E-value: 9.47e-07
                          10        20
                  ....*....|....*....|....*.
gi 6680582    305 ELTRHFRKHTGIKPFQCPDCDRSFSR 330
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
319-341 8.44e-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: 41.90  E-value: 8.44e-06
                          10        20
                  ....*....|....*....|...
gi 6680582    319 FQCPDCDRSFSRSDHLALHRKRH 341
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
169-331 3.94e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 45.07  E-value: 3.94e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680582  169 SEEMDNSNSGMPVPVIESYEKPLLQKKIKIEPGIEPQRTDYYPEEMSPPLMNPVSPPQALLQ----------------EN 232
Cdd:COG5048 182 SNLSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQspsslsssdssssaseSP 261
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680582  233 HPSVIVQPGKRPLPVESPDTQRKRRIHRCDYDGCNKVYTKSSHLKAHRRT--HTGE--KPYKCTWEGCTWKFARSDELTR 308
Cdd:COG5048 262 RSSLPTASSQSSSPNESDSSSEKGFSLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYSLCGKLFSRNDALKR 341
                       170       180
                ....*....|....*....|...
gi 6680582  309 HFRKHTGIKPFQCPDCDRSFSRS 331
Cdd:COG5048 342 HILLHTSISPAKEKLLNSSSKFS 364
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
259-283 6.34e-04

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 36.51  E-value: 6.34e-04
                          10        20
                  ....*....|....*....|....*
gi 6680582    259 HRCDYdgCNKVYTKSSHLKAHRRTH 283
Cdd:pfam00096   1 YKCPD--CGKSFSRKSNLKRHLRTH 23
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
257-339 1.06e-03

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 40.47  E-value: 1.06e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680582  257 RIHRCDYDGCNKVYTKSSHLKAHRRT-HTGEKPYKCTWEGCTWKFARSDeltrhfrkhtgiKPFQCPDCDRSFSRSDHLA 335
Cdd:COG5189 348 KPYKCPVEGCNKKYKNQNGLKYHMLHgHQNQKLHENPSPEKMNIFSAKD------------KPYRCEVCDKRYKNLNGLK 415

                ....
gi 6680582  336 LHRK 339
Cdd:COG5189 416 YHRK 419
zf-H2C2_2 pfam13465
Zinc-finger double domain;
275-292 4.61e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.27  E-value: 4.61e-03
                          10
                  ....*....|....*...
gi 6680582    275 HLKAHRRTHTGEKPYKCT 292
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCP 18
ZnF_C2H2 smart00355
zinc finger;
319-341 6.57e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 33.59  E-value: 6.57e-03
                           10        20
                   ....*....|....*....|...
gi 6680582     319 FQCPDCDRSFSRSDHLALHRKRH 341
Cdd:smart00355   1 YRCPECGKVFKSKSALREHMRTH 23
zf-C2H2_4 pfam13894
C2H2-type zinc finger; This family contains a number of divergent C2H2 type zinc fingers.
319-341 8.60e-03

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


Pssm-ID: 464025  Cd Length: 24  Bit Score: 33.39  E-value: 8.60e-03
                          10        20
                  ....*....|....*....|...
gi 6680582    319 FQCPDCDRSFSRSDHLALHRKRH 341
Cdd:pfam13894   1 FKCPICGKSFSSKKSLKRHLKTH 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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