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Conserved domains on  [gi|18390325|ref|NP_083144|]
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CXXC-type zinc finger protein 1 isoform 1 [Mus musculus]

Protein Classification

CXXC-type zinc finger protein 1( domain architecture ID 10203964)

CXXC-type zinc finger protein 1 acts as a transcriptional activator that exhibits a unique DNA binding specificity for CpG unmethylated motifs with a preference for CpGG

Gene Ontology:  GO:0008270|GO:0003677
PubMed:  16297627

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CpG_bind_C pfam12269
CpG binding protein C-terminal domain; CpG-binding protein is a transcriptional activator that ...
404-640 1.67e-150

CpG binding protein C-terminal domain; CpG-binding protein is a transcriptional activator that exhibits a DNA binding specificity for unmethylated CpG motifs. CpG is made of a PHD1, an acidic, a basic, a coiled-coil, and a PHD2 domains. This protein contains three cysteine-rich domains identified at the N-terminal, central region and C-terminal of the protein, where the central cysteine-rich domain is located within the DNA-binding domain, found between PHD1 and the acidic domains. This domain is found in eukaryotes, and is approximately 240 amino acids in length. It is found at the C-terminal of the CpG-binding protein containing the coiled-coil and PHD2 domains.


:

Pssm-ID: 463514  Cd Length: 235  Bit Score: 434.81  E-value: 1.67e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390325   404 AANRIYEILPQRIQQWQQSPCIAEEHGKKLLERIRREQQSARTRLQEMERRFHELEAIILRAKQQAVREDEENNENDsDD 483
Cdd:pfam12269   1 ATNRIYEILPQRIQEWQLSPCVAEEENKKKLEKIRKEQQEAREALKELDARHQELDAIIERAKKLPVDTEEEENDDE-DD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390325   484 TDLQIFCVSCGHPINPRVALRHMERCYAKYESQTSFGSMYPTRIEGAtRLFCDVYNPQSKTYCKRLQVLCPEHSRDPKVP 563
Cdd:pfam12269  80 DELSIYCVTCGHEIHSRTAIKHMEKCFNKYESQTSFGSIYKTRIEGN-SMFCDFYNPQQKTYCKRLKVLCPEHTKEPKIP 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18390325   564 ADEVCGCPLVRDVFELTGDFCRLPKRQCNRHYCWEKLRRAEVDLERVRVWYKLDELFEQERNVRTAMTNRAGLLALM 640
Cdd:pfam12269 159 DTEVCGCPLVRNVFDPTGEFCRAPKKKCVKHYCWEKLRRAEIDLERVRQWLKLDELFEQERQIRTAMANRAGVLGLM 235
PHD_Cfp1 cd15553
PHD finger found in CXXC-type zinc finger protein 1 (Cfp1); Cfp1, also termed CpG-binding ...
28-73 3.82e-27

PHD finger found in CXXC-type zinc finger protein 1 (Cfp1); Cfp1, also termed CpG-binding protein, or PHD finger and CXXC domain-containing protein 1 (PCCX1), is a specificity factor that binds to unmethylated CpGs and links H3K4me3 with CpG islands (CGIs). It integrates both promoter CpG content and gene activity for accurate trimethylation of histone H3 Lys 4 (H3K4me3) deposition in embryonic stem cells. Moreover, Cfp1 is an essential component of the SETD1 histone H3K4 methyltransferase complex and functions as a critical regulator of histone methylation, cytosine methylation, cellular differentiation, and vertebrate development. Cfp1 contains a plant homeodomain (PHD) finger, a CXXC domain, and a CpG binding protein zinc finger C-terminal domain. Its CXXC domain selectively binds to non-methylated CpG islands, following by a preference for a guanosine nucleotide.


:

Pssm-ID: 277028  Cd Length: 46  Bit Score: 103.61  E-value: 3.82e-27
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 18390325  28 YCICRKPDINCFMIGCDNCNEWFHGDCIRITEKMAKAIREWYCREC 73
Cdd:cd15553   1 YCICRSSDISRFMIGCDNCEEWYHGDCINITEKEAKAIKEWYCQQC 46
zf-CXXC pfam02008
CXXC zinc finger domain; This domain contains eight conserved cysteine residues that bind to ...
166-212 2.90e-16

CXXC zinc finger domain; This domain contains eight conserved cysteine residues that bind to two zinc ions. The CXXC domain is found in a variety of chromatin-associated proteins. This domain binds to nonmethyl-CpG dinucleotides. The domain is characterized by two repeats, and shows a peculiar internal duplication in which the second unit is inserted into the first one. Each of these units is characterized by four conserved cysteines, displaying a CXXCXXCX(n)C motif that chelate a Zn+2 ion. The DNA binding interface has been identified by NMR. In eukaryotes, the CXXC domain is found in stramenopiles, plants and metazoans. Plants possess a mono-CXXC domain that is present in distinct chromatin proteins. Structural comparisons show that the mono-CXXC is homologous to the structural-zinc binding domain of medium chain dehydrogenases.


:

Pssm-ID: 366873  Cd Length: 48  Bit Score: 72.77  E-value: 2.90e-16
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 18390325   166 IKRSARMCGECEACRRTEDCGHCDFCRDMKKFGGPNKIRQKCRLRQC 212
Cdd:pfam02008   2 NRRKRRRCGVCEGCQRPEDCGQCSFCLDMPKFGGPGKKKQKCRLRRC 48
 
Name Accession Description Interval E-value
CpG_bind_C pfam12269
CpG binding protein C-terminal domain; CpG-binding protein is a transcriptional activator that ...
404-640 1.67e-150

CpG binding protein C-terminal domain; CpG-binding protein is a transcriptional activator that exhibits a DNA binding specificity for unmethylated CpG motifs. CpG is made of a PHD1, an acidic, a basic, a coiled-coil, and a PHD2 domains. This protein contains three cysteine-rich domains identified at the N-terminal, central region and C-terminal of the protein, where the central cysteine-rich domain is located within the DNA-binding domain, found between PHD1 and the acidic domains. This domain is found in eukaryotes, and is approximately 240 amino acids in length. It is found at the C-terminal of the CpG-binding protein containing the coiled-coil and PHD2 domains.


Pssm-ID: 463514  Cd Length: 235  Bit Score: 434.81  E-value: 1.67e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390325   404 AANRIYEILPQRIQQWQQSPCIAEEHGKKLLERIRREQQSARTRLQEMERRFHELEAIILRAKQQAVREDEENNENDsDD 483
Cdd:pfam12269   1 ATNRIYEILPQRIQEWQLSPCVAEEENKKKLEKIRKEQQEAREALKELDARHQELDAIIERAKKLPVDTEEEENDDE-DD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390325   484 TDLQIFCVSCGHPINPRVALRHMERCYAKYESQTSFGSMYPTRIEGAtRLFCDVYNPQSKTYCKRLQVLCPEHSRDPKVP 563
Cdd:pfam12269  80 DELSIYCVTCGHEIHSRTAIKHMEKCFNKYESQTSFGSIYKTRIEGN-SMFCDFYNPQQKTYCKRLKVLCPEHTKEPKIP 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18390325   564 ADEVCGCPLVRDVFELTGDFCRLPKRQCNRHYCWEKLRRAEVDLERVRVWYKLDELFEQERNVRTAMTNRAGLLALM 640
Cdd:pfam12269 159 DTEVCGCPLVRNVFDPTGEFCRAPKKKCVKHYCWEKLRRAEIDLERVRQWLKLDELFEQERQIRTAMANRAGVLGLM 235
PHD_Cfp1 cd15553
PHD finger found in CXXC-type zinc finger protein 1 (Cfp1); Cfp1, also termed CpG-binding ...
28-73 3.82e-27

PHD finger found in CXXC-type zinc finger protein 1 (Cfp1); Cfp1, also termed CpG-binding protein, or PHD finger and CXXC domain-containing protein 1 (PCCX1), is a specificity factor that binds to unmethylated CpGs and links H3K4me3 with CpG islands (CGIs). It integrates both promoter CpG content and gene activity for accurate trimethylation of histone H3 Lys 4 (H3K4me3) deposition in embryonic stem cells. Moreover, Cfp1 is an essential component of the SETD1 histone H3K4 methyltransferase complex and functions as a critical regulator of histone methylation, cytosine methylation, cellular differentiation, and vertebrate development. Cfp1 contains a plant homeodomain (PHD) finger, a CXXC domain, and a CpG binding protein zinc finger C-terminal domain. Its CXXC domain selectively binds to non-methylated CpG islands, following by a preference for a guanosine nucleotide.


Pssm-ID: 277028  Cd Length: 46  Bit Score: 103.61  E-value: 3.82e-27
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 18390325  28 YCICRKPDINCFMIGCDNCNEWFHGDCIRITEKMAKAIREWYCREC 73
Cdd:cd15553   1 YCICRSSDISRFMIGCDNCEEWYHGDCINITEKEAKAIKEWYCQQC 46
zf-CXXC pfam02008
CXXC zinc finger domain; This domain contains eight conserved cysteine residues that bind to ...
166-212 2.90e-16

CXXC zinc finger domain; This domain contains eight conserved cysteine residues that bind to two zinc ions. The CXXC domain is found in a variety of chromatin-associated proteins. This domain binds to nonmethyl-CpG dinucleotides. The domain is characterized by two repeats, and shows a peculiar internal duplication in which the second unit is inserted into the first one. Each of these units is characterized by four conserved cysteines, displaying a CXXCXXCX(n)C motif that chelate a Zn+2 ion. The DNA binding interface has been identified by NMR. In eukaryotes, the CXXC domain is found in stramenopiles, plants and metazoans. Plants possess a mono-CXXC domain that is present in distinct chromatin proteins. Structural comparisons show that the mono-CXXC is homologous to the structural-zinc binding domain of medium chain dehydrogenases.


Pssm-ID: 366873  Cd Length: 48  Bit Score: 72.77  E-value: 2.90e-16
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 18390325   166 IKRSARMCGECEACRRTEDCGHCDFCRDMKKFGGPNKIRQKCRLRQC 212
Cdd:pfam02008   2 NRRKRRRCGVCEGCQRPEDCGQCSFCLDMPKFGGPGKKKQKCRLRRC 48
PHD pfam00628
PHD-finger; PHD folds into an interleaved type of Zn-finger chelating 2 Zn ions in a similar ...
29-76 4.42e-10

PHD-finger; PHD folds into an interleaved type of Zn-finger chelating 2 Zn ions in a similar manner to that of the RING and FYVE domains. Several PHD fingers have been identified as binding modules of methylated histone H3.


Pssm-ID: 425785 [Multi-domain]  Cd Length: 51  Bit Score: 55.58  E-value: 4.42e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 18390325    29 CICRKPDINCFMIGCDNCNEWFHGDCIRIT-EKMAKAIREWYCRECREK 76
Cdd:pfam00628   3 AVCGKSDDGGELVQCDGCDDWFHLACLGPPlDPAEIPSGEWLCPECKPK 51
PHD smart00249
PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in ...
29-73 2.44e-09

PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in nuclear proteins thought to be involved in epigenetics and chromatin-mediated transcriptional regulation. The PHD finger binds two zinc ions using the so-called 'cross-brace' motif and is thus structurally related to the RING finger and the FYVE finger. It is not yet known if PHD fingers have a common molecular function. Several reports suggest that it can function as a protein-protein interacton domain and it was recently demonstrated that the PHD finger of p300 can cooperate with the adjacent BROMO domain in nucleosome binding in vitro. Other reports suggesting that the PHD finger is a ubiquitin ligase have been refuted as these domains were RING fingers misidentified as PHD fingers.


Pssm-ID: 214584 [Multi-domain]  Cd Length: 47  Bit Score: 53.37  E-value: 2.44e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 18390325     29 CICRKPDINCFMIGCDNCNEWFHGDCIRITEKMAKAIREWYCREC 73
Cdd:smart00249   3 SVCGKPDDGGELLQCDGCDRWYHQTCLGPPLLEEEPDGKWYCPKC 47
TNG2 COG5034
Chromatin remodeling protein, contains PhD zinc finger [Chromatin structure and dynamics];
2-76 3.31e-09

Chromatin remodeling protein, contains PhD zinc finger [Chromatin structure and dynamics];


Pssm-ID: 227367 [Multi-domain]  Cd Length: 271  Bit Score: 58.41  E-value: 3.31e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390325   2 EGDGSDLEPPDAGDDSKSENGEnaPIYCICRKPDINCfMIGCDNCN---EWFHGDCIRITE--KMAkaireWYCRECREK 76
Cdd:COG5034 199 EGNNGGSTKSRGVSSEDNSEGE--ELYCFCQQVSYGQ-MVACDNANckrEWFHLECVGLKEppKGK-----WYCPECKKA 270
 
Name Accession Description Interval E-value
CpG_bind_C pfam12269
CpG binding protein C-terminal domain; CpG-binding protein is a transcriptional activator that ...
404-640 1.67e-150

CpG binding protein C-terminal domain; CpG-binding protein is a transcriptional activator that exhibits a DNA binding specificity for unmethylated CpG motifs. CpG is made of a PHD1, an acidic, a basic, a coiled-coil, and a PHD2 domains. This protein contains three cysteine-rich domains identified at the N-terminal, central region and C-terminal of the protein, where the central cysteine-rich domain is located within the DNA-binding domain, found between PHD1 and the acidic domains. This domain is found in eukaryotes, and is approximately 240 amino acids in length. It is found at the C-terminal of the CpG-binding protein containing the coiled-coil and PHD2 domains.


Pssm-ID: 463514  Cd Length: 235  Bit Score: 434.81  E-value: 1.67e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390325   404 AANRIYEILPQRIQQWQQSPCIAEEHGKKLLERIRREQQSARTRLQEMERRFHELEAIILRAKQQAVREDEENNENDsDD 483
Cdd:pfam12269   1 ATNRIYEILPQRIQEWQLSPCVAEEENKKKLEKIRKEQQEAREALKELDARHQELDAIIERAKKLPVDTEEEENDDE-DD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390325   484 TDLQIFCVSCGHPINPRVALRHMERCYAKYESQTSFGSMYPTRIEGAtRLFCDVYNPQSKTYCKRLQVLCPEHSRDPKVP 563
Cdd:pfam12269  80 DELSIYCVTCGHEIHSRTAIKHMEKCFNKYESQTSFGSIYKTRIEGN-SMFCDFYNPQQKTYCKRLKVLCPEHTKEPKIP 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18390325   564 ADEVCGCPLVRDVFELTGDFCRLPKRQCNRHYCWEKLRRAEVDLERVRVWYKLDELFEQERNVRTAMTNRAGLLALM 640
Cdd:pfam12269 159 DTEVCGCPLVRNVFDPTGEFCRAPKKKCVKHYCWEKLRRAEIDLERVRQWLKLDELFEQERQIRTAMANRAGVLGLM 235
PHD_Cfp1 cd15553
PHD finger found in CXXC-type zinc finger protein 1 (Cfp1); Cfp1, also termed CpG-binding ...
28-73 3.82e-27

PHD finger found in CXXC-type zinc finger protein 1 (Cfp1); Cfp1, also termed CpG-binding protein, or PHD finger and CXXC domain-containing protein 1 (PCCX1), is a specificity factor that binds to unmethylated CpGs and links H3K4me3 with CpG islands (CGIs). It integrates both promoter CpG content and gene activity for accurate trimethylation of histone H3 Lys 4 (H3K4me3) deposition in embryonic stem cells. Moreover, Cfp1 is an essential component of the SETD1 histone H3K4 methyltransferase complex and functions as a critical regulator of histone methylation, cytosine methylation, cellular differentiation, and vertebrate development. Cfp1 contains a plant homeodomain (PHD) finger, a CXXC domain, and a CpG binding protein zinc finger C-terminal domain. Its CXXC domain selectively binds to non-methylated CpG islands, following by a preference for a guanosine nucleotide.


Pssm-ID: 277028  Cd Length: 46  Bit Score: 103.61  E-value: 3.82e-27
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 18390325  28 YCICRKPDINCFMIGCDNCNEWFHGDCIRITEKMAKAIREWYCREC 73
Cdd:cd15553   1 YCICRSSDISRFMIGCDNCEEWYHGDCINITEKEAKAIKEWYCQQC 46
zf-CXXC pfam02008
CXXC zinc finger domain; This domain contains eight conserved cysteine residues that bind to ...
166-212 2.90e-16

CXXC zinc finger domain; This domain contains eight conserved cysteine residues that bind to two zinc ions. The CXXC domain is found in a variety of chromatin-associated proteins. This domain binds to nonmethyl-CpG dinucleotides. The domain is characterized by two repeats, and shows a peculiar internal duplication in which the second unit is inserted into the first one. Each of these units is characterized by four conserved cysteines, displaying a CXXCXXCX(n)C motif that chelate a Zn+2 ion. The DNA binding interface has been identified by NMR. In eukaryotes, the CXXC domain is found in stramenopiles, plants and metazoans. Plants possess a mono-CXXC domain that is present in distinct chromatin proteins. Structural comparisons show that the mono-CXXC is homologous to the structural-zinc binding domain of medium chain dehydrogenases.


Pssm-ID: 366873  Cd Length: 48  Bit Score: 72.77  E-value: 2.90e-16
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 18390325   166 IKRSARMCGECEACRRTEDCGHCDFCRDMKKFGGPNKIRQKCRLRQC 212
Cdd:pfam02008   2 NRRKRRRCGVCEGCQRPEDCGQCSFCLDMPKFGGPGKKKQKCRLRRC 48
PHD_PHF3_like cd15552
PHD finger found in PHD finger protein 3 (PHF3), and death-inducer obliterator variants Dido1, ...
28-73 2.89e-15

PHD finger found in PHD finger protein 3 (PHF3), and death-inducer obliterator variants Dido1, Dido2, and Dido3; PHF3 is a human homolog of yeast protein bypass of Ess1 (Bye1), a nuclear protein with a domain resembling the central domain in the transcription elongation factor TFIIS. It is ubiquitously expressed in normal tissues including brain, but its expression is significantly reduced or lost in glioblastomas. PHF3 contains an N-terminal plant homeodomain (PHD) finger, a central RNA polymerase II (Pol II)-binding TFIIS-like domain (TLD) domain, and a C-terminal Spen paralogue and orthologue C-terminal (SPOC) domain. This family also includes Dido gene encoding three alternative splicing variants (Dido1, 2, and 3), which have been implicated in a number of cellular processes such as apoptosis and chromosomal segregation, particularly in the hematopoietic system. Dido1 is important for maintaining embryonic stem (ES) cells and directly regulates the expression of pluripotency factors. It is the shortest isoform that contains only a highly conserved PHD finger responsible for the binding of histone H3 with a higher affinity for trimethylated lysine4 (H3K4me3). Gene Dido1 is a Bone morphogenetic protein (BMP) target gene and promotes BMP-induced melanoma progression. It also triggers apoptosis after nuclear translocation and caspase upregulation. Dido3 is the largest isoform and is ubiquitously expressed in all human tissues. It is dispensable for ES cell self-renewal and pluripotency, but is involved in the maintenance of stem cell genomic stability and tumorigenesis. Dido3 contains a PHD finger, a transcription elongation factor S-II subunit M (TFSIIM) domain, a SPOC module, and a long C-terminal region (CT) of unknown homology.


Pssm-ID: 277027  Cd Length: 50  Bit Score: 70.12  E-value: 2.89e-15
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 18390325  28 YCICRKPDINCFMIGCDNCNEWFHGDCIRITE----KMAKAIREWYCREC 73
Cdd:cd15552   1 YCICRKPHNNRFMICCDRCEEWFHGDCVGITEaqgkEMEENIEEYVCPKC 50
PHD2_3_BPTF cd15560
PHD finger 2 and 3 found in bromodomain and PHD finger-containing transcription factor (BPTF); ...
28-73 5.55e-13

PHD finger 2 and 3 found in bromodomain and PHD finger-containing transcription factor (BPTF); BPTF, also termed nucleosome-remodeling factor subunit BPTF, or fetal Alz-50 clone 1 protein (FAC1), or fetal Alzheimer antigen, functions as a transcriptional regulator that exhibits altered expression and subcellular localization during neuronal development and neurodegenerative diseases such as Alzheimer's disease. It interacts with the human orthologue of the Kelch-like Ech-associated protein (Keap1). Its function and subcellular localization can be regulated by Keap1. Moreover, BPTF is a novel DNA-binding protein that recognizes the DNA sequence CACAACAC and represses transcription through this site in a phosphorylation-dependent manner. Furthermore, BPTF interacts with the Myc-associated zinc finger protein (ZF87/MAZ) and alters its transcriptional activity, which has been implicated in gene regulation in neurodegeneration. Some family members contain two or three plant homeodomain (PHD) fingers, which may be involved in complex formation with histone H3 trimethylated at K4 (H3K4me3). This family corresponds to the second and third PHD fingers.


Pssm-ID: 277035  Cd Length: 47  Bit Score: 63.52  E-value: 5.55e-13
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 18390325  28 YCICRKP-DINCFMIGCDNCNEWFHGDCIRITEKMAKAIREWYCREC 73
Cdd:cd15560   1 YCICRTPyDESQFYIGCDRCQDWFHGRCVGILQSEAEKIDEYVCPQC 47
PHD_KDM7 cd15640
PHD finger found in lysine-specific demethylase 7 (KDM7); KDM7, also termed JmjC ...
28-73 1.03e-11

PHD finger found in lysine-specific demethylase 7 (KDM7); KDM7, also termed JmjC domain-containing histone demethylation protein 1D (JHDM1D), or KIAA1718, is a dual histone demethylase that catalyzes demethylation of monomethylated and dimethylated H3K9 (H3K9me2/me1) and H3K27 (H3K27me2/me1), which functions as an eraser of silencing marks on chromatin during brain development. It also plays a tumor-suppressive role by regulating angiogenesis. KDM7 contains a plant homeodomain (PHD) that binds Lys4-trimethylated histone 3 (H3K4me3) and a jumonji domain that demethylates either H3K9me2 or H3K27me2.


Pssm-ID: 277110  Cd Length: 50  Bit Score: 60.00  E-value: 1.03e-11
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 18390325  28 YCICRKP-DINCFMIGCDNCNEWFHGDCIRITEKMAKAIREWYCREC 73
Cdd:cd15640   1 YCVCRQPyDVNRFMIECDICKDWFHGSCVQVEEHHAADIDLYHCPNC 47
PHD_SPP1 cd16039
PHD finger found in Set1 complex component SPP1; Set1C component SPP1, also called COMPASS ...
28-73 1.16e-11

PHD finger found in Set1 complex component SPP1; Set1C component SPP1, also called COMPASS component Spp1, or Complex proteins associated with set1 protein Spp1, or Suppressor of PRP protein 1, is a component of the COMPASS complex that links histone methylation to initiation of meiotic recombination. It induces double-strand break (DSB) formation by tethering to recombinationally cold regions. SPP1 interacts with H3K4me3 and Mer2, a protein required for DSB formation, to promote recruitment of potential meiotic DSB sites to the chromosomal axis. SPP1 contains a PHD finger, a zinc binding motif.


Pssm-ID: 277186  Cd Length: 46  Bit Score: 59.80  E-value: 1.16e-11
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 18390325  28 YCICRKPDINCFMIGCDNCNEWFHGDCIRITEKMAKAIREWYCREC 73
Cdd:cd16039   1 YCICQKPDDGRWMIACDGCDEWYHFTCVNIPEADVELVDSFFCPPC 46
PHD_PHF2_like cd15554
PHD finger found in PHF2, PHF8 and KDM7; This family includes PHF2, PHF8, KDM7, and similar ...
28-73 4.39e-11

PHD finger found in PHF2, PHF8 and KDM7; This family includes PHF2, PHF8, KDM7, and similar proteins. PHF2, also termed GRC5, or PHD finger protein 2, is a histone lysine demethylase ubiquitously expressed in various tissues. PHF8, also termed PHD finger protein 8, or KDM7B, is a monomethylated histone H4 lysine 20(H4K20me1) demethylase that transcriptionally regulates many cell cycle genes. It also preferentially acts on H3K9me2 and H3K9me1. PHF8 is modulated by CDC20-containing anaphase-promoting complex (APC (cdc20)) and plays an important role in the G2/M transition. It acts as a critical molecular sensor for mediating retinoic acid (RA) treatment response in RAR alpha-fusion-induced leukemia. Moreover, PHF8 is essential for cytoskeleton dynamics and is associated with X-linked mental retardation. KDM7, also termed JmjC domain-containing histone demethylation protein 1D (JHDM1D), or KIAA1718, is a dual histone demethylase that catalyzes demethylation of monomethylated and dimethylated H3K9 (H3K9me2/me1) and H3K27 (H3K27me2/me1), which functions as an eraser of silencing marks on chromatin during brain development. It also plays a tumor-suppressive role by regulating angiogenesis. All family members contain a plant homeodomain (PHD) finger and a JmjC domain.


Pssm-ID: 277029  Cd Length: 47  Bit Score: 58.16  E-value: 4.39e-11
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 18390325  28 YCICRKP-DINCFMIGCDNCNEWFHGDCIRITEKMAKAIREWYCREC 73
Cdd:cd15554   1 YCICRQPyDVTRFMIECDVCKDWFHGSCVGVEEHQANDIERYHCPNC 47
PHD pfam00628
PHD-finger; PHD folds into an interleaved type of Zn-finger chelating 2 Zn ions in a similar ...
29-76 4.42e-10

PHD-finger; PHD folds into an interleaved type of Zn-finger chelating 2 Zn ions in a similar manner to that of the RING and FYVE domains. Several PHD fingers have been identified as binding modules of methylated histone H3.


Pssm-ID: 425785 [Multi-domain]  Cd Length: 51  Bit Score: 55.58  E-value: 4.42e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 18390325    29 CICRKPDINCFMIGCDNCNEWFHGDCIRIT-EKMAKAIREWYCRECREK 76
Cdd:pfam00628   3 AVCGKSDDGGELVQCDGCDDWFHLACLGPPlDPAEIPSGEWLCPECKPK 51
PHD_DIDO1_like cd15639
PHD finger found in death-inducer obliterator variants Dido1, Dido2, and Dido3; This family ...
27-73 1.99e-09

PHD finger found in death-inducer obliterator variants Dido1, Dido2, and Dido3; This family includes three alternative splicing variants (Dido1, 2, and 3) encoded by the Dido gene, which have been implicated in a number of cellular processes such as apoptosis and chromosomal segregation, particularly in the hematopoietic system. Dido1, also termed DIO-1, or death-associated transcription factor 1 (DATF-1), is important for maintaining embryonic stem (ES) cells and directly regulates the expression of pluripotency factors. It is the shortest isoform that contains only a highly conserved plant homeodomain (PHD) finger responsible for the binding of histone H3 with a higher affinity for trimethylated lysine 4 (H3K4me3). Gene Dido is a Bonemorphogenetic protein (BMP) target gene, which promotes BMP-induced melanoma progression. It also triggers apoptosis after nuclear translocation and caspase upregulation. Dido3 is the largest isoform ubiquitously expressed in all human tissues. It is dispensable for ES cell self-renewal and pluripotency, but involved in the maintenance of stem cell genomic stability and tumorigenesis. Dido3 contains a PHD finger, a transcription elongation factor S-II subunit M (TFSIIM) domain, aspen paralog and ortholog (SPOC) module, and a long C-terminal region (CT) of unknown homology. Its PHD finger interacts with H3K4me3.


Pssm-ID: 277109  Cd Length: 54  Bit Score: 53.82  E-value: 1.99e-09
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 18390325  27 IYCICRKPDINCFMIGCDNCNEWFHGDCIRITEKMAKAI----REWYCREC 73
Cdd:cd15639   4 LYCICRQPHNNRFMICCDRCEEWFHGDCVGITEARGRLLerngEDYICPNC 54
PHD smart00249
PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in ...
29-73 2.44e-09

PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in nuclear proteins thought to be involved in epigenetics and chromatin-mediated transcriptional regulation. The PHD finger binds two zinc ions using the so-called 'cross-brace' motif and is thus structurally related to the RING finger and the FYVE finger. It is not yet known if PHD fingers have a common molecular function. Several reports suggest that it can function as a protein-protein interacton domain and it was recently demonstrated that the PHD finger of p300 can cooperate with the adjacent BROMO domain in nucleosome binding in vitro. Other reports suggesting that the PHD finger is a ubiquitin ligase have been refuted as these domains were RING fingers misidentified as PHD fingers.


Pssm-ID: 214584 [Multi-domain]  Cd Length: 47  Bit Score: 53.37  E-value: 2.44e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 18390325     29 CICRKPDINCFMIGCDNCNEWFHGDCIRITEKMAKAIREWYCREC 73
Cdd:smart00249   3 SVCGKPDDGGELLQCDGCDRWYHQTCLGPPLLEEEPDGKWYCPKC 47
TNG2 COG5034
Chromatin remodeling protein, contains PhD zinc finger [Chromatin structure and dynamics];
2-76 3.31e-09

Chromatin remodeling protein, contains PhD zinc finger [Chromatin structure and dynamics];


Pssm-ID: 227367 [Multi-domain]  Cd Length: 271  Bit Score: 58.41  E-value: 3.31e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390325   2 EGDGSDLEPPDAGDDSKSENGEnaPIYCICRKPDINCfMIGCDNCN---EWFHGDCIRITE--KMAkaireWYCRECREK 76
Cdd:COG5034 199 EGNNGGSTKSRGVSSEDNSEGE--ELYCFCQQVSYGQ-MVACDNANckrEWFHLECVGLKEppKGK-----WYCPECKKA 270
PHD_ING cd15505
PHD finger found in the inhibitor of growth (ING) protein family; The ING family includes a ...
28-73 1.99e-08

PHD finger found in the inhibitor of growth (ING) protein family; The ING family includes a group of tumor suppressors, ING1-5, which act as readers and writers of the histone epigenetic code, affecting DNA damage response, chromatin remodeling, cellular senescence, differentiation, cell cycle regulation and apoptosis. They may have a general role in mediating the cellular response to genotoxic stress through binding to and regulating the activities of histone acetyltransferase (HAT) and histone deacetylase (HDAC) chromatin remodeling complexes. All ING proteins contain an N-terminal ING domain and a C-terminal plant homeodomain (PHD) finger.


Pssm-ID: 276980 [Multi-domain]  Cd Length: 45  Bit Score: 50.37  E-value: 1.99e-08
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 18390325  28 YCICRKPDINcFMIGCDNCN---EWFHGDCIRITEKMAKairEWYCREC 73
Cdd:cd15505   1 YCICNQVSYG-EMVACDNPNcpiEWFHFECVGLTAKPKG---KWYCPEC 45
PHD_PHF8 cd15642
PHD finger found in histone lysine demethylase PHF8; PHF8, also termed PHD finger protein 8, ...
27-74 6.49e-08

PHD finger found in histone lysine demethylase PHF8; PHF8, also termed PHD finger protein 8, or KDM7B, is a monomethylated histone H4 lysine 20 (H4K20me1) demethylase that transcriptionally regulates many cell cycle genes. It also preferentially acts on H3K9me2 and H3K9me1. PHF8 is modulated by CDC20-containing anaphase-promoting complex (APC (cdc20)) and plays an important role in the G2/M transition. It acts as a critical molecular sensor for mediating retinoic acid (RA) treatment response in RAR alpha-fusion-induced leukemia. Moreover, PHF8 is essential for cytoskeleton dynamics and is associated with X-linked mental retardation. PHF8 contains an N-terminal plant homeodomain (PHD) finger followed by a JmjC domain. The PHD finger mediates binding to nucleosomes at active gene promoters and the JmjC domain catalyzes the demethylation of mono- or dimethyl-lysines.


Pssm-ID: 277112  Cd Length: 52  Bit Score: 49.25  E-value: 6.49e-08
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 18390325  27 IYCICRKP-DINCFMIGCDNCNEWFHGDCIRITEKMAKAIREWYCRECR 74
Cdd:cd15642   1 VYCLCRLPyDVTRFMIECDVCQDWFHGSCVGVEEEKAAEIDLYHCPNCQ 49
PHD_PHF2 cd15641
PHD finger found in lysine-specific demethylase PHF2; PHF2, also termed GRC5, or PHD finger ...
28-75 8.49e-08

PHD finger found in lysine-specific demethylase PHF2; PHF2, also termed GRC5, or PHD finger protein 2, is a histone lysine demethylase ubiquitously expressed in various tissues. It contains a plant homeodomain (PHD) finger and a JmjC domain and plays an important role in adipogenesis. The PHD finger domain can recognize trimethylated histone H3 lysine 4 (H3K4me3). PHF2 also has dimethylated histone H3 lysine 9(H3K9me2) demethylase activity and acts as a coactivator of several metabolism-related transcription factors. Moreover, it can demethylate ARID5B and further forms a complex with demethylated ARD5B to bind the promoter regions of target genes. The overexpression of PHF2 is involved in the progression of esophageal squamous cell carcinoma (ESCC).


Pssm-ID: 277111  Cd Length: 50  Bit Score: 48.86  E-value: 8.49e-08
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 18390325  28 YCICRKP-DINCFMIGCDNCNEWFHGDCIRITEKMAKAIREWYCRECRE 75
Cdd:cd15641   1 YCICRLPyDVTRFMIECDACKDWFHGSCVGVEEEEAPDIDIYHCPNCEK 49
PHD_PHF3 cd15638
PHD finger found in PHD finger protein 3 (PHF3); PHF3 is a human homolog of yeast protein ...
30-73 1.49e-07

PHD finger found in PHD finger protein 3 (PHF3); PHF3 is a human homolog of yeast protein bypass of Ess1 (Bye1), a nuclear protein with a domain resembling the central domain in the transcription elongation factor TFIIS. It is ubiquitously expressed in normal tissues including brain, but its expression is significantly reduced or lost in glioblastomas. PHF3 contains an N-terminal plant homeodomain (PHD) finger, a central RNA polymerase II (Pol II)-binding TFIIS-like domain (TLD) domain, and a C-terminal Spen paralogue and orthologue C-terminal (SPOC) domain.


Pssm-ID: 277108  Cd Length: 51  Bit Score: 48.38  E-value: 1.49e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 18390325  30 ICRKPDINCFMIGCDNCNEWFHGDCIRIT----EKMAKAIREWYCREC 73
Cdd:cd15638   4 FCKKPHGNRFMVGCGRCDDWFHGDCVGLSlsqaQQMEEEDKEYVCVKC 51
PHD_SF cd15489
PHD finger superfamily; The PHD finger superfamily includes a canonical plant homeodomain (PHD) ...
29-73 1.82e-07

PHD finger superfamily; The PHD finger superfamily includes a canonical plant homeodomain (PHD) finger typically characterized as Cys4HisCys3, and a non-canonical extended PHD finger, characterized as Cys2HisCys5HisCys2His. Variations include the RAG2 PHD finger characterized by Cys3His2Cys2His and the PHD finger 5 found in nuclear receptor-binding SET domain-containing proteins characterized by Cys4HisCys2His. The PHD finger is also termed LAP (leukemia-associated protein) motif or TTC (trithorax consensus) domain. Single or multiple copies of PHD fingers have been found in a variety of eukaryotic proteins involved in the control of gene transcription and chromatin dynamics. PHD fingers can recognize the unmodified and modified histone H3 tail, and some have been found to interact with non-histone proteins. They also function as epigenome readers controlling gene expression through molecular recruitment of multi-protein complexes of chromatin regulators and transcription factors. The PHD finger domain SF is structurally similar to the RING and FYVE_like superfamilies.


Pssm-ID: 276966 [Multi-domain]  Cd Length: 48  Bit Score: 48.08  E-value: 1.82e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 18390325  29 CICRKPDINC-FMIGCDNCNEWFHGDCIRITEKMAKAIREWYCREC 73
Cdd:cd15489   3 IVCGKGGDLGgELLQCDGCGKWFHADCLGPPLSSFVPNGKWICPVC 48
PHD_TCF19_like cd15517
PHD finger found in Transcription factor 19 (TCF-19), Lysine-specific demethylase KDM5A and ...
30-73 6.66e-07

PHD finger found in Transcription factor 19 (TCF-19), Lysine-specific demethylase KDM5A and KDM5B, and other similar proteins; TCF-19 was identified as a putative trans-activating factor with expression beginning at the late G1-S boundary in dividing cells. It functions as a novel islet factor necessary for proliferation and survival in the INS-1 beta cell line. It plays an important role in susceptibility to both Type 1 Diabetes Mellitus (T1DM) and Type 2 Diabetes Mellitus (T2DM); it has been suggested that it may positively impact beta cell mass under conditions of beta cell stress and increased insulin demand. KDM5A was originally identified as a retinoblastoma protein (Rb)-binding partner and its inactivation may be important for Rb to promote differentiation. It is involved in transcription through interaction with TBP, p107, nuclear receptors, Myc, Sin3/HDAC, Mad1, RBP-J, CLOCK, and BMAL1. KDM5B has a restricted expression pattern in the testis, ovary, and transiently in the mammary gland of the pregnant female and has been shown to be upregulated in breast cancer, prostate cancer, and lung cancer, suggesting a potential role in tumorigenesis. Both KDM5A and KDM5B function as trimethylated histone H3 lysine 4 (H3K4me3) demethylases. This family also includes Caenorhabditis elegans Lysine-specific demethylase 7 homolog (ceKDM7A). ceKDM7A (also termed JmjC domain-containing protein 1.2, PHD finger protein 8 homolog, or PHF8 homolog) is a plant homeodomain (PHD)- and JmjC domain-containing protein that functions as a histone demethylase specific for H3K9me2 and H3K27me2. The binding of the PHD finger to H3K4me3 guides H3K9me2- and H3K27me2-specific demethylation by its catalytic JmjC domain in a trans-histone regulation mechanism. In addition, this family includes plant protein OBERON 1 and OBERON 2, Alfin1-like (AL) proteins, histone acetyltransferases (HATs) HAC, and AT-rich interactive domain-containing protein 4 (ARID4).


Pssm-ID: 276992 [Multi-domain]  Cd Length: 49  Bit Score: 46.39  E-value: 6.66e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 18390325  30 ICRKPDI--NCFMIGCDNCNEWFHGDCIRITEKMAKAIREWYCREC 73
Cdd:cd15517   4 ICNLETAavDELWVQCDGCDKWFHQFCLGLSNERYADEDKFKCPNC 49
PHD_MLL5 cd15550
PHD finger found in mixed lineage leukemia 5 (MLL5); MLL5 is a histone methyltransferase that ...
29-73 9.50e-07

PHD finger found in mixed lineage leukemia 5 (MLL5); MLL5 is a histone methyltransferase that plays a key role in hematopoiesis, spermatogenesis and cell cycle progression. It contains a single plant homeodomain (PHD) finger followed by a catalytic SET domain. MLL5 can be recruited to E2F1-responsive promoters to stimulate H3K4 trimethylation and transcriptional activation by binding to the cell cycle regulator host cell factor (HCF-1), thereby facilitating the cell cycle G1 to S phase transition. It is also involved in mitotic fidelity and genomic integrity by modulating the stability of the chromosomal passenger complex (CPC) via the interaction with Borealin. Moreover, MLL5 is a component of a complex associated with retinoic acid receptor that requires GlcN Acylation of its SET domain in order to activate its histone lysine methyltransferase activity. It also participates in the camptothecin (CPT)-induced p53 activation. Furthermore, MLL5 indirectly regulates H3K4 methylation, represses cyclin A2 (CycA) expression, and promotes myogenic differentiation.


Pssm-ID: 277025 [Multi-domain]  Cd Length: 44  Bit Score: 45.77  E-value: 9.50e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 18390325  29 CICRKPDINCFMIGCDNCNEWFHGDCIRITEKMAKaiREWYCREC 73
Cdd:cd15550   2 CICGFEHDDGFMICCDKCSVWQHGDCMGIDRENIP--DSYLCEQC 44
PHD_Ecm5p_Lid2p_like cd15518
PHD finger found in Saccharomyces cerevisiae extracellular matrix protein 5 (Ecm5p), ...
28-73 2.72e-06

PHD finger found in Saccharomyces cerevisiae extracellular matrix protein 5 (Ecm5p), Schizosaccharomyces pombe Lid2 complex component Lid2p, and similar proteins; The family includes Saccharomyces cerevisiae Ecm5p, Schizosaccharomyces pombe Lid2 complex component Lid2p, and similar proteins. Ecm5p is a JmjC domain-containing protein that directly removes histone lysine methylation via a hydroxylation reaction. It associates with the yeast Snt2p and Rpd3 deacetylase, which may play a role in regulating transcription in response to oxidative stress. Ecm5p promotes oxidative stress tolerance, while Snt2p ultimately decreases tolerance. Ecm5p contains an N-terminal ARID domain, a JmjC domain, and a C-terminal plant homeodomain (PHD) finger. Lid2p is a trimethyl H3K4 (H3K4me3) demethylase responsible for H3K4 hypomethylation in heterochromatin. It interacts with the histone lysine-9 methyltransferase, Clr4, through the Dos1/Clr8-Rik1 complex, and mediates H3K9 methylation and small RNA production. It also acts cooperatively with the histone modification enzymes Set1 and Lsd1 and plays an essential role in cross-talk between H3K4 and H3K9 methylation in euchromatin. Lid2p contains a JmjC domain, three PHD fingers and a JmjN domain. This model includes the second PHD finger of Lid2p.


Pssm-ID: 276993  Cd Length: 45  Bit Score: 44.65  E-value: 2.72e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 18390325  28 YCICRKPDiNCFMIGCDNCNEWFHGDCIRITEKMAKAIREWYCREC 73
Cdd:cd15518   1 YCFCRQGE-GGTMIECEICKEWYHVKCIKNGRWKLDDDDKFVCPIC 45
PHD_AL_plant cd15613
PHD finger found in plant Alfin1-like (AL) proteins; AL proteins are ubiquitously expressed ...
39-76 5.01e-06

PHD finger found in plant Alfin1-like (AL) proteins; AL proteins are ubiquitously expressed nuclear proteins existing only in plants. They are involved in chromatin regulation by binding to tri- and dimethylated histone H3 at lysine 4 (H3K4me3/2), the active histone markers, through their plant homeodomain (PHD) fingers.


Pssm-ID: 277085  Cd Length: 51  Bit Score: 44.02  E-value: 5.01e-06
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 18390325  39 FMIGCDNCNEWFHGDCIRITEKMAKAIREWYCRECREK 76
Cdd:cd15613  14 FWICCDVCEKWYHGKCVKITPAKAEHIKQYKCPSCSNK 51
PHD_TAF3 cd15522
PHD finger found in transcription initiation factor TFIID subunit 3 (TAF3); TAF3 (also termed ...
28-73 7.91e-06

PHD finger found in transcription initiation factor TFIID subunit 3 (TAF3); TAF3 (also termed 140 kDa TATA box-binding protein-associated factor, TBP-associated factor 3, transcription initiation factor TFIID 140 kDa subunit (TAF140), or TAFII-140, is an integral component of TFIID) is a general initiation factor (GTF) that plays a key role in preinitiation complex (PIC) assembly through core promoter recognition. The interaction of H3K4me3 with TAF3 directs global TFIID recruitment to active genes, which regulates gene-selective functions of p53 in response to genotoxic stress. TAF3 is highly enriched in embryonic stem cells and is required for endoderm lineage differentiation and prevents premature specification of neuroectoderm and mesoderm. Moreover, TAF3, along with TRF3, forms a complex that is essential for myogenic differentiation. TAF3 contains a plant homeodomain (PHD) finger. This family also includes Drosophila melanogaster BIP2 (Bric-a-brac interacting protein 2) protein, which functions as an interacting partner of D. melanogaster p53 (Dmp53).


Pssm-ID: 276997 [Multi-domain]  Cd Length: 46  Bit Score: 43.43  E-value: 7.91e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 18390325  28 YC-ICRKPDINCFMIGCDNCNEWFHGDCIRITEKMAKaIREWYCREC 73
Cdd:cd15522   1 ICpICKKPDDGSPMIGCDECDDWYHWECVGITDEPPE-EDDWFCPKC 46
PHD2_KDM5A cd15606
PHD finger 2 found in Lysine-specific demethylase 5A (KDM5A); KDM5A (also termed Histone ...
28-55 3.60e-05

PHD finger 2 found in Lysine-specific demethylase 5A (KDM5A); KDM5A (also termed Histone demethylase JARID1A, Jumonji/ARID domain-containing protein 1A, or Retinoblastoma-binding protein 2 (RBBP-2 or RBP2)) was originally identified as a retinoblastoma protein (Rb)-binding partner and its inactivation may be important for Rb to promote differentiation. It is involved in transcription through interacting with TBP, p107, nuclear receptors, Myc, Sin3/HDAC, Mad1, RBP-J, CLOCK, and BMAL1. KDM5A functions as a trimethylated histone H3 lysine 4 (H3K4me3) demethylase that belongs to the JARID subfamily within the JmjC proteins. It also displays DNA-binding activities that can recognize the specific DNA sequence CCGCCC. KDM5A contains the catalytic JmjC domain, JmjN, the BRIGHT domain, which is an AT-rich interacting domain (ARID), and a Cys5HisCys2 zinc finger, as well as three plant homeodomain (PHD) fingers. This model corresponds to the second PHD finger.


Pssm-ID: 277079  Cd Length: 56  Bit Score: 41.65  E-value: 3.60e-05
                        10        20
                ....*....|....*....|....*...
gi 18390325  28 YCICRKPDINcFMIGCDNCNEWFHGDCI 55
Cdd:cd15606   1 YCICRKPFSG-FMLQCELCKDWFHSSCV 27
PHD_Bye1p_SIZ1_like cd15570
PHD domain found in Saccharomyces cerevisiae bypass of ESS1 protein 1 (Bye1p), the E3 Sumo ...
29-73 4.44e-05

PHD domain found in Saccharomyces cerevisiae bypass of ESS1 protein 1 (Bye1p), the E3 Sumo Ligase SIZ1, and similar proteins; Yeast Bye1p is a nuclear transcription factor with a domain resembling the central domain in the transcription elongation factor TFIIS and plays an inhibitory role during transcription elongation. It functions as a multicopy suppressor of Ess1, a peptidyl-prolyl cis-trans isomerase involved in proline isomerization of the C-terminal domain (CTD) of RNA polymerase II (Pol II). Bye1p contains an N-terminal plant homeodomain (PHD) finger, a central Pol II-binding TFIIS-like domain (TLD) domain, and a C-terminal Spen paralogue and orthologue C-terminal (SPOC) domain. The PHD domain binds to a histone H3 tail peptide containing trimethylated lysine 4 (H3K4me3). The TLD domain is responsible for the association with chromatin. Plant SIZ1 protein is a SUMO (small ubiquitin-related modifier) E3 ligase that facilitates conjugation of SUMO to substrate target proteins (sumoylation) and belongs to the protein inhibitor of activated STAT (PIAS) protein family. It negatively regulates abscisic acid (ABA) signaling, which is dependent on the bZIP transcripton factor ABI5. It also modulates plant growth and plays a role in drought stress response likely through the regulation of gene expression. SIZ1 functions as a floral repressor that not only represses the salicylic acid (SA)-dependent pathway, but also promotes FLOWERING LOCUS C (FLC) expression by repressing FLOWERING LOCUS D (FLD) activity through sumoylation. SIZ1 contains a PHD finger, which specifically binds methylated histone H3 at lysine 4 and arginine 2.


Pssm-ID: 277045  Cd Length: 50  Bit Score: 41.29  E-value: 4.44e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 18390325  29 CICRKPDINCFMIGCDNCNEWFHGDCIRITEKMAKAIRE----WYCREC 73
Cdd:cd15570   2 CPCGSSMEDGSMIQCEGCKTWQHMDCVLIPDKPADGLPElpskFYCELC 50
PHD_Yng1p_like cd15587
PHD finger found in yeast orthologs of ING tumor suppressor family; The yeast orthologs of the ...
28-75 7.68e-05

PHD finger found in yeast orthologs of ING tumor suppressor family; The yeast orthologs of the plant homeodomain (PHD) finger-containing ING tumor suppressor family consists of chromatin modification-related protein YNG1 (Yng1p), YNG2 (Yng2p), and transcriptional regulatory protein PHO23 (Pho23p). Yng1p, also termed ING1 homolog 1, is one of the components of the NuA3 histone acetyltransferase (HAT) complex. Its PHD finger binding to H3 Trimethylated at K4 (H3K4me3) promotes NuA3 H3 HAT activity at K14 of H3 on chromatin. Yng2p, also termed ESA1-associated factor 4, or ING1 homolog 2, is a subunit of the NuA4 HAT complex. It plays a critical role in intra-S-phase DNA damage response. Pho23p is part of the Rpd3/Sin3 histone deacetylase (HDAC) complex. It is required for the normal function of Rpd3 in the silencing of rDNA, telomeric, and mating-type loci. Yng1p and Pho23p inhibit p53-dependent transcription. In contrast, Yng2p has the opposite effect. All family members contain an N-terminal ING histone-binding domain and a C-terminal PHD finger.


Pssm-ID: 277062 [Multi-domain]  Cd Length: 47  Bit Score: 40.48  E-value: 7.68e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 18390325  28 YCICRKPDINcFMIGCDN--CN-EWFHGDCIRITEKMAKairEWYCRECRE 75
Cdd:cd15587   1 YCYCRRVSFG-EMVACDNpdCKiEWFHFECVGLTETPKG---KWYCSDCKV 47
PHD3_KDM5A_like cd15610
PHD finger 3 found in Lysine-specific demethylase 5A (KDM5A), 5B (KDM5B), and similar proteins; ...
31-73 3.84e-04

PHD finger 3 found in Lysine-specific demethylase 5A (KDM5A), 5B (KDM5B), and similar proteins; The family includes KDM5A and KDM5B, both of which belong to the JARID subfamily within the JmjC proteins. KDM5A, also termed Histone demethylase JARID1A, or Jumonji/ARID domain-containing protein 1A, or Retinoblastoma-binding protein 2 (RBBP-2 or RBP2), was originally identified as a retinoblastoma protein (Rb)-binding partner and its inactivation may be important for Rb to promote differentiation. It is involved in transcription through interacting with TBP, p107, nuclear receptors, Myc, Sin3/HDAC, Mad1, RBP-J, CLOCK and BMAL1. KDM5A functions as the trimethylated histone H3 lysine 4 (H3K4me3) demethylase. It also displays DNA-binding activities that can recognize the specific DNA sequence CCGCCC. KDM5B, also termed Cancer/testis antigen 31 (CT31), or Histone demethylase JARID1B, or Jumonji/ARID domain-containing protein 1B (JARID1B), or PLU-1, or retinoblastoma-binding protein 2 homolog 1 (RBP2-H1 or RBBP2H1A), has a restricted expression pattern in the testis, ovary, and transiently in the mammary gland of the pregnant female and has been shown to be upregulated in breast cancer, prostate cancer, and lung cancer, suggesting a potential role in tumorigenesis. KDM5B acts as a histone demethylase that catalyzes the removal of trimethylation of lysine 4 on histone H3 (H3K4me3), induced by polychlorinated biphenyls (PCBs). It also mediates demethylation of H3K4me2 and H3K4me1. Moreover, KDM5B functions as a negative regulator of hematopoietic stem cell (HSC) self-renewal and progenitor cell activity. KDM5B has also been shown to interact with the DNA binding transcription factors BF-1 and PAX9, as well asTIEG1/KLF10 (transforming growth factor-beta inducible early gene-1/Kruppel-like transcription factor 10), and possibly function as a transcriptional corepressor. The family also includes the Drosophila melanogaster protein little imaginal discs (Lid) that functions as a JmjC-dependent trimethyl histone H3K4 (H3K4me3) demethylase, which is required for dMyc-induced cell growth. It positively regulates Hox gene expression in S2 cells. Members in this family contain the catalytic JmjC domain, JmjN, the BRIGHT domain, which is an AT-rich interacting domain (ARID), and a Cys5HisCys2 zinc finger, as well as three plant homeodomain (PHD) fingers. This model corresponds to the third PHD finger.


Pssm-ID: 277083 [Multi-domain]  Cd Length: 50  Bit Score: 38.46  E-value: 3.84e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 18390325  31 CRKP---DINCFMigCDNCNEWFHGDCIRITEKMAKAIREWYCREC 73
Cdd:cd15610   7 CLKPtgdEVNWVQ--CDGCEEWFHLLCVGLSPEEVAEDEDYICPSC 50
PHD_ING3 cd15585
PHD finger found in inhibitor of growth protein 3 (ING3) and similar proteins; ING3, also ...
28-73 1.22e-03

PHD finger found in inhibitor of growth protein 3 (ING3) and similar proteins; ING3, also termed p47ING3, is one member of the inhibitor of growth (ING) family of type II tumor suppressors. It is ubiquitously expressed and has been implicated in transcription modulation, cell cycle control, and the induction of apoptosis. It is an important subunit of human NuA4 histone acetyltransferase complex, which regulates the acetylation of histones H2A and H4. Moreover, ING3 promotes ultraviolet (UV)-induced apoptosis through the Fas/caspase-8-dependent pathway in melanoma cells. It physically interacts with subunits of E3 ligase Skp1-Cullin-F-boxprotein complex (SCF complex) and is degraded by the SCF (F-box protein S-phase kinase-associated protein 2, Skp2)-mediated ubiquitin-proteasome system. It also acts as a suppression factor during tumorigenesis and progression of hepatocellular carcinoma (HCC). ING3 contains an N-terminal ING domain and a C-terminal plant homeodomain (PHD) finger.


Pssm-ID: 277060 [Multi-domain]  Cd Length: 45  Bit Score: 37.05  E-value: 1.22e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 18390325  28 YCICRKPDINcFMIGCDNCN---EWFHGDCIRITEKMAKairEWYCREC 73
Cdd:cd15585   1 YCICNQVSYG-EMVGCDNDDcpiEWFHYGCVGLTEAPKG---KWYCPQC 45
PHD_ING1_2 cd15584
PHD finger found in inhibitor of growth protein 1 (ING1) and 2 (ING2); ING1 is an epigenetic ...
28-73 2.16e-03

PHD finger found in inhibitor of growth protein 1 (ING1) and 2 (ING2); ING1 is an epigenetic regulator and a type II tumor suppressor that impacts cell growth, aging, apoptosis, and DNA repair, by affecting chromatin conformation and gene expression. It acts as a reader of the active chromatin mark, the trimethylation of histone H3 lysine 4 (H3K4me3). It binds and directs Growth arrest and DNA damage inducible protein 45 a (Gadd45a) to target sites, thus linking the histone code with DNA demethylation. It interacts with the proliferating cell nuclear antigen (PCNA) via the PCNA-interacting protein (PIP) domain in a UV-inducible manner. It also interacts with a PCNA-interacting protein, p15 (PAF). Moreover, ING1 associates with members of the 14-3-3 family, which is necessary for cytoplasmic relocalization. Endogenous ING1 protein specifically interacts with the pro-apoptotic BCL2 family member BAX and colocalizes with BAX in a UV-inducible manner. It stabilizes the p53 tumor suppressor by inhibiting polyubiquitination of multi-monoubiquitinated forms via interaction with and colocalization of the herpesvirus-associated ubiquitin-specific protease (HAUSP)-deubiquitinase with p53. It is also involved in trichostatin A-induced apoptosis and caspase 3 signaling in p53-deficient glioblastoma cells. In addition, tyrosine kinase Src can bind and phosphorylate ING1 and further regulates its activity. ING2, also termed inhibitor of growth 1-like protein (ING1Lp), or p32, or p33ING2, belongs to the inhibitor of growth (ING) family of type II tumor suppressors. It is a core component of a multi-factor chromatin-modifying complex containing the transcriptional co-repressor SIN3A and histone deacetylase 1 (HDAC1). It has been implicated in the control of cell cycle, in genome stability, and in muscle differentiation. ING2 independently interacts with H3K4me3 (Histone H3 trimethylated on lysine 4) and PtdIns(5)P, and modulates crosstalk between lysine methylation and lysine acetylation on histone proteins through association with chromatin in the presence of DNA damage. It collaborates with SnoN to mediate transforming growth factor (TGF)-beta-induced Smad-dependent transcription and cellular responses. It is upregulated in colon cancer and increases invasion by enhanced MMP13 expression. It also acts as a cofactor of p300 for p53 acetylation and plays a positive regulatory role during p53-mediated replicative senescence. Both ING1 and ING2 contain an N-terminal ING domain and a C-terminal plant homeodomain (PHD) finger.


Pssm-ID: 277059 [Multi-domain]  Cd Length: 45  Bit Score: 36.27  E-value: 2.16e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 18390325  28 YCICRKPDINcFMIGCDN--CN-EWFHGDCIRITEKMAKairEWYCREC 73
Cdd:cd15584   1 YCLCNQVSYG-EMIGCDNdeCPiEWFHFSCVGLTHKPKG---KWYCPKC 45
PHD_ING4_5 cd15586
PHD finger found in inhibitor of growth protein 4 (ING4) and 5 (ING5); ING4, also termed ...
28-73 3.14e-03

PHD finger found in inhibitor of growth protein 4 (ING4) and 5 (ING5); ING4, also termed p29ING4, and ING5, also termed p28ING5, belong to the inhibitor of growth (ING) family of type II tumor suppressors. ING4 acts as an E3 ubiquitin ligase to induce ubiquitination of the p65 subunit of NF-kappaB and inhibit the transactivation of NF-kappaB target genes. It also induces apoptosis through a p53 dependent pathway, including increasing p53 acetylation, inhibiting Mdm2-mediated degradation of p53 and enhancing the expression of p53 responsive genes both at the transcriptional and post-translational levels. Moreover, ING4 can inhibit the translation of proto-oncogene MYC by interacting with AUF1. It also regulates other transcription factors, such as hypoxia-inducible factor (HIF). ING5 is a Tip60 cofactor that acetylates p53 at K120 and subsequently activates the expression of p53-dependent apoptotic genes in response to DNA damage. Aberrant ING5 expression may contribute to pathogenesis, growth, and invasion of gastric carcinomas and colorectal cancer. ING5 can physically interact with p300 and p53 in vivo, and its overexpression induces apoptosis in colorectal cancer cells. It also associates with cyclin A1 (INCA1) and functions as a growth suppressor with suppressed expression in Acute Myeloid Leukemia (AML). Moreover, ING5 translocation from the nucleus to the cytoplasm might be a critical event for carcinogenesis and tumor progression in human head and neck squamous cell carcinoma. Both ING4 and ING5 contain an N-terminal ING histone-binding domain and a C-terminal plant homeodomain (PHD) finger. They associate with histone acetyltransferase (HAT) complexes containing MOZ (monocytic leukemia zinc finger protein)/MORF (MOZ-related factor) and HBO1, and further direct the MOZ/MORF and HBO1 complexes to chromatin.


Pssm-ID: 277061 [Multi-domain]  Cd Length: 45  Bit Score: 36.01  E-value: 3.14e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 18390325  28 YCICRKPDINcFMIGCDNCN---EWFHGDCIRITEKMAKairEWYCREC 73
Cdd:cd15586   1 YCLCHQVSYG-EMIGCDNPDcpiEWFHFACVGLTTKPKG---KWFCPRC 45
PHD3_Lid2p_like cd15520
PHD finger 3 found in Schizosaccharomyces pombe Lid2 complex component Lid2p and similar ...
29-73 3.50e-03

PHD finger 3 found in Schizosaccharomyces pombe Lid2 complex component Lid2p and similar proteins; Lid2p is a trimethyl H3K4 (H3K4me3) demethylase responsible for H3K4 hypomethylation in heterochromatin. It interacts with the histone lysine-9 methyltransferase, Clr4, through the Dos1/Clr8-Rik1 complex, and mediates H3K9 methylation and small RNA production. It also acts cooperatively with the histone modification enzymes Set1 and Lsd1, and plays an essential role in cross-talk between H3K4 and H3K9 methylation in euchromatin. Lid2p contains a JmjC domain, three PHD fingers and a JmjN domain. The family corresponds to the third PHD finger.


Pssm-ID: 276995  Cd Length: 47  Bit Score: 36.04  E-value: 3.50e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 18390325  29 CICRKPD-INCFMIGCDNCNEWFHGDCIRITEKMAKAIREWYCREC 73
Cdd:cd15520   2 CGCGEGFnIADRMIFCDRCERTVHLDCVGLSDRIVDSPSEFFCPEC 47
PHD_ING2 cd15683
PHD finger found in inhibitor of growth protein 2 (ING2); ING2, also termed inhibitor of ...
28-74 4.10e-03

PHD finger found in inhibitor of growth protein 2 (ING2); ING2, also termed inhibitor of growth 1-like protein (ING1Lp), or p32, or p33ING2, is one member of the inhibitor of growth (ING) family of type II tumor suppressors. It is a core component of a multi-factor chromatin-modifying complex containing the transcriptional co-repressor SIN3A and histone deacetylase 1 (HDAC1). It has been implicated in the control of cell cycle, in genome stability, and in muscle differentiation. ING2 independently interacts with H3K4me3 (Histone H3 trimethylated on lysine 4) and PtdIns(5)P, and modulates crosstalk between lysine methylation and lysine acetylation on histone proteins through association with chromatin in the presence of DNA damage. It collaborates with SnoN to mediate transforming growth factor (TGF)-beta-induced Smad-dependent transcription and cellular responses. It is upregulated in colon cancer and increases invasion by enhanced MMP13 expression. It also acts as a cofactor of p300 for p53 acetylation and plays a positive regulatory role during p53-mediated replicative senescence. ING2 contains an N-terminal ING domain and a C-terminal plant homeodomain (PHD) finger.


Pssm-ID: 277153 [Multi-domain]  Cd Length: 49  Bit Score: 35.77  E-value: 4.10e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 18390325  28 YCICRKPDINcFMIGCDNCN---EWFHGDCIRITEKMAKairEWYCRECR 74
Cdd:cd15683   2 YCLCNQVSYG-EMIGCDNEQcpiEWFHFSCVGLTYKPKG---KWYCPKCR 47
PHD_ING1 cd15682
PHD finger found in inhibitor of growth protein 1 (ING1); ING1 is an epigenetic regulator and ...
28-74 6.08e-03

PHD finger found in inhibitor of growth protein 1 (ING1); ING1 is an epigenetic regulator and a type II tumor suppressor that impacts cell growth, aging, apoptosis, and DNA repair, by affecting chromatin conformation and gene expression. It acts as a reader of the active chromatin mark, the trimethylation of histone H3 lysine 4 (H3K4me3). It binds and directs Growth arrest and DNA damage inducible protein 45 a (Gadd45a) to target sites, thus linking the histone code with DNA demethylation. It interacts with the proliferating cell nuclear antigen (PCNA) via the PCNA-interacting protein (PIP) domain in a UV-inducible manner. It also interacts with a PCNA-interacting protein, p15 (PAF). Moreover, ING1 associates with members of the 14-3-3 family, which is necessary for the cytoplasmic relocalization. Endogenous ING1 protein specifically interacts with the pro-apoptotic BCL2 family member BAX and colocalizes with BAX in a UV-inducible manner. It stabilizes the p53 tumor suppressor by inhibiting polyubiquitination of multi-monoubiquitinated forms via interaction with and colocalization of the herpesvirus-associated ubiquitin-specific protease (HAUSP)-deubiquitinase with p53. It is also involved in trichostatin A-induced apoptosis and caspase 3 signaling in p53-deficient glioblastoma cells. In addition, tyrosine kinase Src can bind phosphorylate ING1 and further regulates its activity. ING1 contains an N-terminal ING domain and a C-terminal plant homeodomain (PHD) finger.


Pssm-ID: 277152 [Multi-domain]  Cd Length: 49  Bit Score: 35.37  E-value: 6.08e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 18390325  28 YCICRKPDINcFMIGCDNCN---EWFHGDCIRITEKMAKairEWYCRECR 74
Cdd:cd15682   2 YCLCNQVSYG-EMIGCDNDEcpiEWFHFSCVGLNHKPKG---KWYCPKCR 47
PHD_PHF13 cd15632
PHD finger found in PHD finger protein 13 (PHF13); PHF13, also termed survival time-associated ...
27-74 6.90e-03

PHD finger found in PHD finger protein 13 (PHF13); PHF13, also termed survival time-associated PHD finger protein in ovarian cancer 1 (SPOC1), is a novel plant homeodomain (PHD) finger-containing protein that shows strong expression in spermatogonia and ovarian cancer cells, modulates chromatin structure and mitotic chromosome condensation, and is important for proper cell division. It is also required for spermatogonial stem cell differentiation and sustained spermatogenesis. The overexpression of PHF13 associates with unresectable carcinomas and shorter survival in ovarian cancer.


Pssm-ID: 277102  Cd Length: 47  Bit Score: 35.02  E-value: 6.90e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 18390325  27 IYCICRKPDINCFMIGCDNCNEWFHGDCIRITEKMAKAIreWYCRECR 74
Cdd:cd15632   2 VTCFCMKPFAGRPMIECNECHTWIHLSCAKIRKSNVPEV--YVCQKCR 47
 
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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