histone acetyltransferase HAC1 isoform X1 [Glycine max]
Protein Classification
ZnF_TAZ and PHD_HAC_like domain-containing protein( domain architecture ID 10651082)
protein containing domains ZnF_TAZ, PHD_HAC_like, HAT_KAT11, and ZZ
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||
| HAT_KAT11 super family | cl02120 | Histone acetylation protein; Histone acetylation is required in many cellular processes ... |
1151-1372 | 4.03e-45 | |||||
Histone acetylation protein; Histone acetylation is required in many cellular processes including transcription, DNA repair, and chromatin assembly. This family contains the fungal KAT11 protein (previously known as RTT109) which is required for H3K56 acetylation. Loss of KAT11 results in the loss of H3K56 acetylation, both on bulk histone and on chromatin. KAT11 and H3K56 acetylation appear to correlate with actively transcribed genes and associate with the elongating form of Pol II in yeast. This family also incorporates the p300/CBP histone acetyltransferase domain which has different catalytic properties and cofactor regulation to KAT11. The actual alignment was detected with superfamily member pfam08214: Pssm-ID: 413203 Cd Length: 348 Bit Score: 167.58 E-value: 4.03e-45
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| PHD_HAC_like | cd15614 | PHD finger found in Arabidopsis thaliana histone acetyltransferases (HATs) HAC and similar ... |
1020-1092 | 5.38e-37 | |||||
PHD finger found in Arabidopsis thaliana histone acetyltransferases (HATs) HAC and similar proteins; This family includes A. thaliana HACs (HAC1/2/4/5/12), which are histone acetyltransferases of the p300/CREB-binding protein (CBP) co-activator family. CBP-type HAT proteins are also found in animals, but absent in fungi. The domain architecture of CBP-type HAT proteins differs between plants and animals. Members in this family contain an N-terminal partially conserved KIX domain, a Zf-TAZ domain, a Cysteine rich CBP-type HAT domain that harbors a plant homeodomain (PHD) finger, a Zf-ZZ domain, and a Zf-TAZ domain. PHD fingers can recognize the unmodified and modified histone H3 tail, and some have been found to interact with non-histone proteins. : Pssm-ID: 277086 Cd Length: 73 Bit Score: 134.02 E-value: 5.38e-37
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| ZnF_TAZ | smart00551 | TAZ zinc finger, present in p300 and CBP; |
663-736 | 3.37e-26 | |||||
TAZ zinc finger, present in p300 and CBP; : Pssm-ID: 214717 Cd Length: 79 Bit Score: 103.21 E-value: 3.37e-26
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| ZnF_TAZ | smart00551 | TAZ zinc finger, present in p300 and CBP; |
1613-1689 | 3.97e-23 | |||||
TAZ zinc finger, present in p300 and CBP; : Pssm-ID: 214717 Cd Length: 79 Bit Score: 94.74 E-value: 3.97e-23
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| ZZ super family | cl00295 | Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ... |
1551-1596 | 1.94e-11 | |||||
Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ZZ motif coordinates one or two zinc ions and most likely participates in ligand binding or molecular scaffolding. Many proteins containing ZZ motifs have other zinc-binding motifs as well, and the majority serve as scaffolds in pathways involving acetyltransferase, protein kinase, or ubiqitin-related activity. ZZ proteins can be grouped into the following functional classes: chromatin modifying, cytoskeletal scaffolding, ubiquitin binding or conjugating, and membrane receptor or ion-channel modifying proteins. The actual alignment was detected with superfamily member cd02337: Pssm-ID: 412288 Cd Length: 41 Bit Score: 60.27 E-value: 1.94e-11
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| ZZ super family | cl00295 | Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ... |
1427-1461 | 2.71e-03 | |||||
Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ZZ motif coordinates one or two zinc ions and most likely participates in ligand binding or molecular scaffolding. Many proteins containing ZZ motifs have other zinc-binding motifs as well, and the majority serve as scaffolds in pathways involving acetyltransferase, protein kinase, or ubiqitin-related activity. ZZ proteins can be grouped into the following functional classes: chromatin modifying, cytoskeletal scaffolding, ubiquitin binding or conjugating, and membrane receptor or ion-channel modifying proteins. The actual alignment was detected with superfamily member smart00291: Pssm-ID: 412288 [Multi-domain] Cd Length: 44 Bit Score: 37.42 E-value: 2.71e-03
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| Name | Accession | Description | Interval | E-value | |||||
| HAT_KAT11 | pfam08214 | Histone acetylation protein; Histone acetylation is required in many cellular processes ... |
1151-1372 | 4.03e-45 | |||||
Histone acetylation protein; Histone acetylation is required in many cellular processes including transcription, DNA repair, and chromatin assembly. This family contains the fungal KAT11 protein (previously known as RTT109) which is required for H3K56 acetylation. Loss of KAT11 results in the loss of H3K56 acetylation, both on bulk histone and on chromatin. KAT11 and H3K56 acetylation appear to correlate with actively transcribed genes and associate with the elongating form of Pol II in yeast. This family also incorporates the p300/CBP histone acetyltransferase domain which has different catalytic properties and cofactor regulation to KAT11. Pssm-ID: 400497 Cd Length: 348 Bit Score: 167.58 E-value: 4.03e-45
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| PHD_HAC_like | cd15614 | PHD finger found in Arabidopsis thaliana histone acetyltransferases (HATs) HAC and similar ... |
1020-1092 | 5.38e-37 | |||||
PHD finger found in Arabidopsis thaliana histone acetyltransferases (HATs) HAC and similar proteins; This family includes A. thaliana HACs (HAC1/2/4/5/12), which are histone acetyltransferases of the p300/CREB-binding protein (CBP) co-activator family. CBP-type HAT proteins are also found in animals, but absent in fungi. The domain architecture of CBP-type HAT proteins differs between plants and animals. Members in this family contain an N-terminal partially conserved KIX domain, a Zf-TAZ domain, a Cysteine rich CBP-type HAT domain that harbors a plant homeodomain (PHD) finger, a Zf-ZZ domain, and a Zf-TAZ domain. PHD fingers can recognize the unmodified and modified histone H3 tail, and some have been found to interact with non-histone proteins. Pssm-ID: 277086 Cd Length: 73 Bit Score: 134.02 E-value: 5.38e-37
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| ZnF_TAZ | smart00551 | TAZ zinc finger, present in p300 and CBP; |
663-736 | 3.37e-26 | |||||
TAZ zinc finger, present in p300 and CBP; Pssm-ID: 214717 Cd Length: 79 Bit Score: 103.21 E-value: 3.37e-26
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| zf-TAZ | pfam02135 | TAZ zinc finger; The TAZ2 domain of CBP binds to other transcription factors such as the p53 ... |
664-733 | 8.07e-25 | |||||
TAZ zinc finger; The TAZ2 domain of CBP binds to other transcription factors such as the p53 tumour suppressor protein, E1A oncoprotein, MyoD, and GATA-1. The zinc coordinating motif that is necessary for binding to target DNA sequences consists of HCCC. Pssm-ID: 460457 Cd Length: 72 Bit Score: 99.38 E-value: 8.07e-25
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| ZnF_TAZ | smart00551 | TAZ zinc finger, present in p300 and CBP; |
1613-1689 | 3.97e-23 | |||||
TAZ zinc finger, present in p300 and CBP; Pssm-ID: 214717 Cd Length: 79 Bit Score: 94.74 E-value: 3.97e-23
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| zf-TAZ | pfam02135 | TAZ zinc finger; The TAZ2 domain of CBP binds to other transcription factors such as the p53 ... |
1617-1685 | 6.11e-18 | |||||
TAZ zinc finger; The TAZ2 domain of CBP binds to other transcription factors such as the p53 tumour suppressor protein, E1A oncoprotein, MyoD, and GATA-1. The zinc coordinating motif that is necessary for binding to target DNA sequences consists of HCCC. Pssm-ID: 460457 Cd Length: 72 Bit Score: 79.74 E-value: 6.11e-18
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| ZZ_CBP | cd02337 | Zinc finger, ZZ type. Zinc finger present in CBP/p300 and related proteins. The ZZ motif ... |
1551-1596 | 1.94e-11 | |||||
Zinc finger, ZZ type. Zinc finger present in CBP/p300 and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. CREB-binding protein (CBP) is a large multidomain protein that provides binding sites for transcriptional coactivators, the role of the ZZ domain in CBP/p300 is unclear. Pssm-ID: 239077 Cd Length: 41 Bit Score: 60.27 E-value: 1.94e-11
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| ZnF_ZZ | smart00291 | Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ... |
1549-1592 | 8.00e-05 | |||||
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain present in dystrophin-like proteins, and CREB-binding protein/p300 homologues. The ZZ in dystrophin appears to bind calmodulin. A missense mutation of one of the conserved cysteines in dystrophin results in a patient with Duchenne muscular dystrophy. Pssm-ID: 197633 [Multi-domain] Cd Length: 44 Bit Score: 41.66 E-value: 8.00e-05
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| PHD | smart00249 | PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in ... |
1050-1092 | 1.06e-04 | |||||
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: 41.43 E-value: 1.06e-04
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| PHD | pfam00628 | PHD-finger; PHD folds into an interleaved type of Zn-finger chelating 2 Zn ions in a similar ... |
1050-1092 | 1.45e-04 | |||||
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: 40.94 E-value: 1.45e-04
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| ZZ | pfam00569 | Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ... |
1549-1592 | 5.41e-04 | |||||
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds calmodulin. Putative zinc finger; binding not yet shown. Four to six cysteine residues in its sequence are responsible for coordinating zinc ions, to reinforce the structure. Pssm-ID: 395451 Cd Length: 45 Bit Score: 39.39 E-value: 5.41e-04
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| ZnF_ZZ | smart00291 | Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ... |
1427-1461 | 2.71e-03 | |||||
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain present in dystrophin-like proteins, and CREB-binding protein/p300 homologues. The ZZ in dystrophin appears to bind calmodulin. A missense mutation of one of the conserved cysteines in dystrophin results in a patient with Duchenne muscular dystrophy. Pssm-ID: 197633 [Multi-domain] Cd Length: 44 Bit Score: 37.42 E-value: 2.71e-03
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| Name | Accession | Description | Interval | E-value | |||||
| HAT_KAT11 | pfam08214 | Histone acetylation protein; Histone acetylation is required in many cellular processes ... |
1151-1372 | 4.03e-45 | |||||
Histone acetylation protein; Histone acetylation is required in many cellular processes including transcription, DNA repair, and chromatin assembly. This family contains the fungal KAT11 protein (previously known as RTT109) which is required for H3K56 acetylation. Loss of KAT11 results in the loss of H3K56 acetylation, both on bulk histone and on chromatin. KAT11 and H3K56 acetylation appear to correlate with actively transcribed genes and associate with the elongating form of Pol II in yeast. This family also incorporates the p300/CBP histone acetyltransferase domain which has different catalytic properties and cofactor regulation to KAT11. Pssm-ID: 400497 Cd Length: 348 Bit Score: 167.58 E-value: 4.03e-45
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| PHD_HAC_like | cd15614 | PHD finger found in Arabidopsis thaliana histone acetyltransferases (HATs) HAC and similar ... |
1020-1092 | 5.38e-37 | |||||
PHD finger found in Arabidopsis thaliana histone acetyltransferases (HATs) HAC and similar proteins; This family includes A. thaliana HACs (HAC1/2/4/5/12), which are histone acetyltransferases of the p300/CREB-binding protein (CBP) co-activator family. CBP-type HAT proteins are also found in animals, but absent in fungi. The domain architecture of CBP-type HAT proteins differs between plants and animals. Members in this family contain an N-terminal partially conserved KIX domain, a Zf-TAZ domain, a Cysteine rich CBP-type HAT domain that harbors a plant homeodomain (PHD) finger, a Zf-ZZ domain, and a Zf-TAZ domain. PHD fingers can recognize the unmodified and modified histone H3 tail, and some have been found to interact with non-histone proteins. Pssm-ID: 277086 Cd Length: 73 Bit Score: 134.02 E-value: 5.38e-37
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| RING_CBP-p300 | cd15802 | atypical RING domain found in CREB-binding protein and p300 histone acetyltransferases; CBP ... |
988-1056 | 7.42e-27 | |||||
atypical RING domain found in CREB-binding protein and p300 histone acetyltransferases; CBP and p300 (also known as CREBBP or KAT3A and EP300 or KAT3B, respectively) are two histone acetyltransferases (HATs) that associate with and acetylate transcriptional regulators and chromatin. The catalytic core of animal CBP-p300 contains a bromodomain, a CH2 region containing a discontinuous PHD domain interrupted by this RING domain, and a HAT domain. Bromodomain-RING-PHD forms a compact module in which the RING domain is juxtaposed with the HAT substrate-binding site. This ring domain contains only a single zinc ion-binding cluster instead of two; instead of a second zinc atom, a network of hydrophobic interactions stabilizes the domain. The RING domain has an inhibitory role. Disease mutations that disrupt RING attachment lead to upregulation of HAT activity. HAT regulation may require repositioning of the RING domain to facilitate access to an otherwise partially occluded HAT active site. Plant CBP-p300 type HATs lack a bromodomain whose role in the animal animal CBP-p300's is to bind acetylated histones; it has been suggested that these plant proteins may utilize a different domain or another bromodomain protein to perform this function. This RING domain has also been referred to as DUF902. Pssm-ID: 276805 Cd Length: 73 Bit Score: 105.06 E-value: 7.42e-27
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| ZnF_TAZ | smart00551 | TAZ zinc finger, present in p300 and CBP; |
663-736 | 3.37e-26 | |||||
TAZ zinc finger, present in p300 and CBP; Pssm-ID: 214717 Cd Length: 79 Bit Score: 103.21 E-value: 3.37e-26
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| zf-TAZ | pfam02135 | TAZ zinc finger; The TAZ2 domain of CBP binds to other transcription factors such as the p53 ... |
664-733 | 8.07e-25 | |||||
TAZ zinc finger; The TAZ2 domain of CBP binds to other transcription factors such as the p53 tumour suppressor protein, E1A oncoprotein, MyoD, and GATA-1. The zinc coordinating motif that is necessary for binding to target DNA sequences consists of HCCC. Pssm-ID: 460457 Cd Length: 72 Bit Score: 99.38 E-value: 8.07e-25
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| ZnF_TAZ | smart00551 | TAZ zinc finger, present in p300 and CBP; |
1613-1689 | 3.97e-23 | |||||
TAZ zinc finger, present in p300 and CBP; Pssm-ID: 214717 Cd Length: 79 Bit Score: 94.74 E-value: 3.97e-23
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| zf-TAZ | pfam02135 | TAZ zinc finger; The TAZ2 domain of CBP binds to other transcription factors such as the p53 ... |
1617-1685 | 6.11e-18 | |||||
TAZ zinc finger; The TAZ2 domain of CBP binds to other transcription factors such as the p53 tumour suppressor protein, E1A oncoprotein, MyoD, and GATA-1. The zinc coordinating motif that is necessary for binding to target DNA sequences consists of HCCC. Pssm-ID: 460457 Cd Length: 72 Bit Score: 79.74 E-value: 6.11e-18
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| PHD_TCF19_like | cd15517 | PHD finger found in Transcription factor 19 (TCF-19), Lysine-specific demethylase KDM5A and ... |
1051-1092 | 1.75e-11 | |||||
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: 60.64 E-value: 1.75e-11
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| ZZ_CBP | cd02337 | Zinc finger, ZZ type. Zinc finger present in CBP/p300 and related proteins. The ZZ motif ... |
1551-1596 | 1.94e-11 | |||||
Zinc finger, ZZ type. Zinc finger present in CBP/p300 and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. CREB-binding protein (CBP) is a large multidomain protein that provides binding sites for transcriptional coactivators, the role of the ZZ domain in CBP/p300 is unclear. Pssm-ID: 239077 Cd Length: 41 Bit Score: 60.27 E-value: 1.94e-11
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| ZZ | cd02249 | Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ... |
1552-1596 | 1.02e-05 | |||||
Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ZZ motif coordinates one or two zinc ions and most likely participates in ligand binding or molecular scaffolding. Many proteins containing ZZ motifs have other zinc-binding motifs as well, and the majority serve as scaffolds in pathways involving acetyltransferase, protein kinase, or ubiqitin-related activity. ZZ proteins can be grouped into the following functional classes: chromatin modifying, cytoskeletal scaffolding, ubiquitin binding or conjugating, and membrane receptor or ion-channel modifying proteins. Pssm-ID: 239069 [Multi-domain] Cd Length: 46 Bit Score: 43.96 E-value: 1.02e-05
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| PHD3_KDM5A_like | cd15610 | PHD finger 3 found in Lysine-specific demethylase 5A (KDM5A), 5B (KDM5B), and similar proteins; ... |
1058-1092 | 2.23e-05 | |||||
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: 43.47 E-value: 2.23e-05
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| ZnF_ZZ | smart00291 | Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ... |
1549-1592 | 8.00e-05 | |||||
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain present in dystrophin-like proteins, and CREB-binding protein/p300 homologues. The ZZ in dystrophin appears to bind calmodulin. A missense mutation of one of the conserved cysteines in dystrophin results in a patient with Duchenne muscular dystrophy. Pssm-ID: 197633 [Multi-domain] Cd Length: 44 Bit Score: 41.66 E-value: 8.00e-05
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| PHD | smart00249 | PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in ... |
1050-1092 | 1.06e-04 | |||||
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: 41.43 E-value: 1.06e-04
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| PHD | pfam00628 | PHD-finger; PHD folds into an interleaved type of Zn-finger chelating 2 Zn ions in a similar ... |
1050-1092 | 1.45e-04 | |||||
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: 40.94 E-value: 1.45e-04
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| PHD_ARID4_like | cd15615 | PHD finger found in Arabidopsis thaliana AT-rich interactive domain-containing protein 4 ... |
1046-1092 | 5.30e-04 | |||||
PHD finger found in Arabidopsis thaliana AT-rich interactive domain-containing protein 4 (ARID4) and similar proteins; This family includes A. thaliana ARID4 (ARID domain-containing protein 4) and similar proteins. Their biological roles remain unclear, but they all contain an AT-rich interactive domain (ARID) and a plant homeodomain (PHD) finger at the C-terminus. ARID is a helix-turn-helix motif-based DNA-binding domain conserved in all eukaryotes. PHD fingers can recognize the unmodified and modified histone H3 tail, and some have been found to interact with non-histone proteins. Pssm-ID: 277087 Cd Length: 57 Bit Score: 39.77 E-value: 5.30e-04
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| ZZ | pfam00569 | Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ... |
1549-1592 | 5.41e-04 | |||||
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds calmodulin. Putative zinc finger; binding not yet shown. Four to six cysteine residues in its sequence are responsible for coordinating zinc ions, to reinforce the structure. Pssm-ID: 395451 Cd Length: 45 Bit Score: 39.39 E-value: 5.41e-04
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| ZnF_ZZ | smart00291 | Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ... |
1427-1461 | 2.71e-03 | |||||
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain present in dystrophin-like proteins, and CREB-binding protein/p300 homologues. The ZZ in dystrophin appears to bind calmodulin. A missense mutation of one of the conserved cysteines in dystrophin results in a patient with Duchenne muscular dystrophy. Pssm-ID: 197633 [Multi-domain] Cd Length: 44 Bit Score: 37.42 E-value: 2.71e-03
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| PHD_MLL5 | cd15550 | PHD finger found in mixed lineage leukemia 5 (MLL5); MLL5 is a histone methyltransferase that ... |
1051-1072 | 5.82e-03 | |||||
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: 36.14 E-value: 5.82e-03
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| PHD_SF | cd15489 | PHD finger superfamily; The PHD finger superfamily includes a canonical plant homeodomain (PHD) ... |
1049-1092 | 5.87e-03 | |||||
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: 36.53 E-value: 5.87e-03
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| ZZ_NBR1_like | cd02340 | Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 ... |
1552-1590 | 6.59e-03 | |||||
Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Drosophila ref(2)P appears to control the multiplication of sigma rhabdovirus. NBR1 (Next to BRCA1 gene 1 protein) interacts with fasciculation and elongation protein zeta-1 (FEZ1) and calcium and integrin binding protein (CIB), and may function in cell signalling pathways. Sequestosome 1 is a phosphotyrosine independent ligand for the Lck SH2 domain and binds noncovalently to ubiquitin via its UBA domain. Pssm-ID: 239080 Cd Length: 43 Bit Score: 36.08 E-value: 6.59e-03
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| ZZ_Mind_bomb | cd02339 | Zinc finger, ZZ type. Zinc finger present in Drosophila Mind bomb (D-mib) and related proteins. ... |
1551-1584 | 8.02e-03 | |||||
Zinc finger, ZZ type. Zinc finger present in Drosophila Mind bomb (D-mib) and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Mind bomb is an E3 ubiqitin ligase that has been shown to regulate signaling by the Notch ligand Delta in Drosophila melanogaster. Pssm-ID: 239079 Cd Length: 45 Bit Score: 35.90 E-value: 8.02e-03
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