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histone acetyltransferase KAT6B isoform 5 [Homo sapiens]
List of domain hits
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Name | Accession | Description | Interval | E-value | |||
MOZ_SAS super family | cl38061 | MOZ/SAS family; This region of these proteins has been suggested to be homologous to ... |
283-390 | 3.66e-60 | |||
MOZ/SAS family; This region of these proteins has been suggested to be homologous to acetyltransferases. The actual alignment was detected with superfamily member pfam01853: Pssm-ID: 460362 [Multi-domain] Cd Length: 179 Bit Score: 204.20 E-value: 3.66e-60
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PHD1_MOZ_MORF | cd15618 | PHD finger 1 found in monocytic leukemia zinc-finger protein (MOZ) and its factor (MORF); MOZ ... |
212-269 | 1.89e-33 | |||
PHD finger 1 found in monocytic leukemia zinc-finger protein (MOZ) and its factor (MORF); MOZ (also termed histone acetyltransferase KAT6A, YBF2/SAS3, SAS2 and TIP60protein 3 (MYST-3), runt-related transcription factor-binding protein 2, or zinc finger protein 220) is a MYST-type histone acetyltransferase (HAT) that functions as a coactivator for acute myeloid leukemia 1 protein (AML1)- and p53-dependent transcription. It possesses intrinsic HAT activity to acetylate both itself and lysine (K) residues on histone H2B, histone H3 (K14) and histone H4 (K5, K8, K12 and K16) in vitro and H3K9 in vivo. MOZ-related factor (MORF), also termed MOZ2, or histone acetyltransferase KAT6B, or MOZ, YBF2/SAS3, SAS2 and TIP60 protein 4 (MYST4), is a ubiquitously expressed transcriptional regulator with intrinsic HAT activity. It can interact with the Runt-domain transcription factor Runx2 and form a tetrameric complex with BRPFs, ING5, and EAF6. Both MOZ and MORF are catalytic subunits of HAT complexes that are required for normal developmental programs, such as hematopoiesis, neurogenesis, and skeletogenesis, and are also implicated in human leukemias. MOZ is also the catalytic subunit of a tetrameric inhibitor of growth 5 (ING5) complex, which specifically acetylates nucleosomal histone H3K14. Moreover, MOZ and MORF are involved in regulating transcriptional activation mediated by Runx2 (or Cbfa1), a Runt-domain transcription factor known to play important roles in T cell lymphomagenesis and bone development, and its homologs. MOZ contains a linker histone 1 and histone 5 domains and two plant homeodomain (PHD) fingers. In contrast, MORF contains an N-terminal region containing two PHD fingers, a putative HAT domain, an acidic region, and a C-terminal Ser/Met-rich domain. The model corresponds to the first PHD finger. : Pssm-ID: 277090 Cd Length: 58 Bit Score: 123.37 E-value: 1.89e-33
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H15 | smart00526 | Domain in histone families 1 and 5; |
113-167 | 1.41e-09 | |||
Domain in histone families 1 and 5; : Pssm-ID: 197772 [Multi-domain] Cd Length: 66 Bit Score: 55.66 E-value: 1.41e-09
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Name | Accession | Description | Interval | E-value | |||
MOZ_SAS | pfam01853 | MOZ/SAS family; This region of these proteins has been suggested to be homologous to ... |
283-390 | 3.66e-60 | |||
MOZ/SAS family; This region of these proteins has been suggested to be homologous to acetyltransferases. Pssm-ID: 460362 [Multi-domain] Cd Length: 179 Bit Score: 204.20 E-value: 3.66e-60
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SAS2 | COG5027 | Histone acetyltransferase (MYST family) [Chromatin structure and dynamics]; |
283-424 | 1.75e-42 | |||
Histone acetyltransferase (MYST family) [Chromatin structure and dynamics]; Pssm-ID: 227360 [Multi-domain] Cd Length: 395 Bit Score: 161.09 E-value: 1.75e-42
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PLN00104 | PLN00104 | MYST -like histone acetyltransferase; Provisional |
283-426 | 2.31e-41 | |||
MYST -like histone acetyltransferase; Provisional Pssm-ID: 215056 [Multi-domain] Cd Length: 450 Bit Score: 159.15 E-value: 2.31e-41
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PHD1_MOZ_MORF | cd15618 | PHD finger 1 found in monocytic leukemia zinc-finger protein (MOZ) and its factor (MORF); MOZ ... |
212-269 | 1.89e-33 | |||
PHD finger 1 found in monocytic leukemia zinc-finger protein (MOZ) and its factor (MORF); MOZ (also termed histone acetyltransferase KAT6A, YBF2/SAS3, SAS2 and TIP60protein 3 (MYST-3), runt-related transcription factor-binding protein 2, or zinc finger protein 220) is a MYST-type histone acetyltransferase (HAT) that functions as a coactivator for acute myeloid leukemia 1 protein (AML1)- and p53-dependent transcription. It possesses intrinsic HAT activity to acetylate both itself and lysine (K) residues on histone H2B, histone H3 (K14) and histone H4 (K5, K8, K12 and K16) in vitro and H3K9 in vivo. MOZ-related factor (MORF), also termed MOZ2, or histone acetyltransferase KAT6B, or MOZ, YBF2/SAS3, SAS2 and TIP60 protein 4 (MYST4), is a ubiquitously expressed transcriptional regulator with intrinsic HAT activity. It can interact with the Runt-domain transcription factor Runx2 and form a tetrameric complex with BRPFs, ING5, and EAF6. Both MOZ and MORF are catalytic subunits of HAT complexes that are required for normal developmental programs, such as hematopoiesis, neurogenesis, and skeletogenesis, and are also implicated in human leukemias. MOZ is also the catalytic subunit of a tetrameric inhibitor of growth 5 (ING5) complex, which specifically acetylates nucleosomal histone H3K14. Moreover, MOZ and MORF are involved in regulating transcriptional activation mediated by Runx2 (or Cbfa1), a Runt-domain transcription factor known to play important roles in T cell lymphomagenesis and bone development, and its homologs. MOZ contains a linker histone 1 and histone 5 domains and two plant homeodomain (PHD) fingers. In contrast, MORF contains an N-terminal region containing two PHD fingers, a putative HAT domain, an acidic region, and a C-terminal Ser/Met-rich domain. The model corresponds to the first PHD finger. Pssm-ID: 277090 Cd Length: 58 Bit Score: 123.37 E-value: 1.89e-33
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H15 | smart00526 | Domain in histone families 1 and 5; |
113-167 | 1.41e-09 | |||
Domain in histone families 1 and 5; Pssm-ID: 197772 [Multi-domain] Cd Length: 66 Bit Score: 55.66 E-value: 1.41e-09
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PHD | pfam00628 | PHD-finger; PHD folds into an interleaved type of Zn-finger chelating 2 Zn ions in a similar ... |
215-272 | 4.19e-08 | |||
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: 50.95 E-value: 4.19e-08
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PHD | smart00249 | PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in ... |
215-269 | 2.61e-06 | |||
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: 45.67 E-value: 2.61e-06
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H15 | cd00073 | linker histone 1 and histone 5 domains; the basic subunit of chromatin is the nucleosome, ... |
114-167 | 1.96e-03 | |||
linker histone 1 and histone 5 domains; the basic subunit of chromatin is the nucleosome, consisting of an octamer of core histones, two full turns of DNA, a linker histone (H1 or H5) and a variable length of linker DNA; H1/H5 are chromatin-associated proteins that bind to the exterior of nucleosomes and dramatically stabilize the highly condensed states of chromatin fibers; stabilization of higher order folding occurs through electrostatic neutralization of the linker DNA segments, through a highly positively charged carboxy- terminal domain known as the AKP helix (Ala, Lys, Pro); thought to be involved in specific protein-protein and protein-DNA interactions and play a role in suppressing core histone tail domain acetylation in the chromatin fiber Pssm-ID: 238028 [Multi-domain] Cd Length: 88 Bit Score: 38.76 E-value: 1.96e-03
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Name | Accession | Description | Interval | E-value | ||||
MOZ_SAS | pfam01853 | MOZ/SAS family; This region of these proteins has been suggested to be homologous to ... |
283-390 | 3.66e-60 | ||||
MOZ/SAS family; This region of these proteins has been suggested to be homologous to acetyltransferases. Pssm-ID: 460362 [Multi-domain] Cd Length: 179 Bit Score: 204.20 E-value: 3.66e-60
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SAS2 | COG5027 | Histone acetyltransferase (MYST family) [Chromatin structure and dynamics]; |
283-424 | 1.75e-42 | ||||
Histone acetyltransferase (MYST family) [Chromatin structure and dynamics]; Pssm-ID: 227360 [Multi-domain] Cd Length: 395 Bit Score: 161.09 E-value: 1.75e-42
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PLN00104 | PLN00104 | MYST -like histone acetyltransferase; Provisional |
283-426 | 2.31e-41 | ||||
MYST -like histone acetyltransferase; Provisional Pssm-ID: 215056 [Multi-domain] Cd Length: 450 Bit Score: 159.15 E-value: 2.31e-41
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PLN03238 | PLN03238 | probable histone acetyltransferase MYST; Provisional |
283-427 | 3.87e-38 | ||||
probable histone acetyltransferase MYST; Provisional Pssm-ID: 215642 [Multi-domain] Cd Length: 290 Bit Score: 145.00 E-value: 3.87e-38
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PHD1_MOZ_MORF | cd15618 | PHD finger 1 found in monocytic leukemia zinc-finger protein (MOZ) and its factor (MORF); MOZ ... |
212-269 | 1.89e-33 | ||||
PHD finger 1 found in monocytic leukemia zinc-finger protein (MOZ) and its factor (MORF); MOZ (also termed histone acetyltransferase KAT6A, YBF2/SAS3, SAS2 and TIP60protein 3 (MYST-3), runt-related transcription factor-binding protein 2, or zinc finger protein 220) is a MYST-type histone acetyltransferase (HAT) that functions as a coactivator for acute myeloid leukemia 1 protein (AML1)- and p53-dependent transcription. It possesses intrinsic HAT activity to acetylate both itself and lysine (K) residues on histone H2B, histone H3 (K14) and histone H4 (K5, K8, K12 and K16) in vitro and H3K9 in vivo. MOZ-related factor (MORF), also termed MOZ2, or histone acetyltransferase KAT6B, or MOZ, YBF2/SAS3, SAS2 and TIP60 protein 4 (MYST4), is a ubiquitously expressed transcriptional regulator with intrinsic HAT activity. It can interact with the Runt-domain transcription factor Runx2 and form a tetrameric complex with BRPFs, ING5, and EAF6. Both MOZ and MORF are catalytic subunits of HAT complexes that are required for normal developmental programs, such as hematopoiesis, neurogenesis, and skeletogenesis, and are also implicated in human leukemias. MOZ is also the catalytic subunit of a tetrameric inhibitor of growth 5 (ING5) complex, which specifically acetylates nucleosomal histone H3K14. Moreover, MOZ and MORF are involved in regulating transcriptional activation mediated by Runx2 (or Cbfa1), a Runt-domain transcription factor known to play important roles in T cell lymphomagenesis and bone development, and its homologs. MOZ contains a linker histone 1 and histone 5 domains and two plant homeodomain (PHD) fingers. In contrast, MORF contains an N-terminal region containing two PHD fingers, a putative HAT domain, an acidic region, and a C-terminal Ser/Met-rich domain. The model corresponds to the first PHD finger. Pssm-ID: 277090 Cd Length: 58 Bit Score: 123.37 E-value: 1.89e-33
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PHD1_MORF | cd15689 | PHD finger 1 found in monocytic leukemia zinc finger protein-related factor (MORF); MORF, also ... |
212-270 | 2.03e-33 | ||||
PHD finger 1 found in monocytic leukemia zinc finger protein-related factor (MORF); MORF, also termed MOZ2, or histone acetyltransferase KAT6B, or MOZ, YBF2/SAS3, SAS2 and TIP60 protein 4 (MYST4), is a ubiquitously expressed transcriptional regulator with intrinsic histone acetyltransferase (HAT) activity. It can interact with the Runt-domain transcription factor Runx2 and form a tetrameric complex with BRPFs, ING5, and EAF6. MORF and monocytic leukemia zinc-finger protein (MOZ) are catalytic subunits of HAT complexes that are required for normal developmental programs, such as hematopoiesis, neurogenesis, and skeletogenesis, and are also implicated in human leukemias. MORF contains an N-terminal region containing two plant homeodomain (PHD) fingers, a putative HAT domain, an acidic region, and a C-terminal Ser/Met-rich domain. The model corresponds to the first PHD finger. Pssm-ID: 277159 Cd Length: 59 Bit Score: 123.23 E-value: 2.03e-33
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PLN03239 | PLN03239 | histone acetyltransferase; Provisional |
283-426 | 9.05e-32 | ||||
histone acetyltransferase; Provisional Pssm-ID: 178777 [Multi-domain] Cd Length: 351 Bit Score: 128.23 E-value: 9.05e-32
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PHD1_MOZ | cd15688 | PHD finger 1 found in monocytic leukemia zinc-finger protein (MOZ); MOZ, also termed histone ... |
212-270 | 1.19e-31 | ||||
PHD finger 1 found in monocytic leukemia zinc-finger protein (MOZ); MOZ, also termed histone acetyltransferase KAT6A, YBF2/SAS3, SAS2 and TIP60 protein 3 (MYST-3), or runt-related transcription factor-binding protein 2, or zinc finger protein 220, is a MYST-type histone acetyltransferase (HAT) that functions as a coactivator for acute myeloid leukemia 1 protein (AML1)- and p53-dependent transcription. It possesses intrinsic HAT activity to acetylate both itself and lysine (K) residues on histone H2B, histone H3 (K14) and histone H4 (K5, K8, K12 and K16) in vitro and H3K9 in vivo. MOZ and MOZ-related factor (MORF) are catalytic subunits of histone acetyltransferase (HAT) complexes that are required for normal developmental programs, such as hematopoiesis, neurogenesis, and skeletogenesis, and implicated in human leukemias. It is also the catalytic subunit of a tetrameric inhibitor of growth 5 (ING5) complex, which specifically acetylates nucleosomal histone H3K14. Moreover, MOZ and MORF are involved in regulating transcriptional activation mediated by Runx2 (or Cbfa1), a Runt-domain transcription factor known to play important roles in T cell lymphomagenesis and bone development, and its homologs. MOZ contains a linker histone 1 and histone 5 domains and two plant homeodomain (PHD) fingers. The model corresponds to the first PHD finger. Pssm-ID: 277158 Cd Length: 59 Bit Score: 118.26 E-value: 1.19e-31
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PHD1_MOZ_d4 | cd15526 | PHD finger 1 found in monocytic leukemia zinc-finger protein (MOZ), its factor (MORF), and d4 ... |
215-269 | 4.57e-27 | ||||
PHD finger 1 found in monocytic leukemia zinc-finger protein (MOZ), its factor (MORF), and d4 gene family proteins; MOZ is a MYST-type histone acetyltransferase (HAT) that functions as a coactivator for acute myeloid leukemia 1 protein (AML1)- and p53-dependent transcription. It possesses intrinsic HAT activity and to acetylate both itself and lysine (K) residues on histone H2B, histone H3 (K14) and histone H4 (K5, K8, K12 and K16) in vitro and H3K9 in vivo. MOZ-related factor (MORF) is a ubiquitously expressed transcriptional regulator with intrinsic HAT activity. It can interact with the Runt-domain transcription factor Runx2 and form a tetrameric complex with BRPFs, ING5, and EAF6. Both MOZ and MORF are catalytic subunits of HAT complexes that are required for normal developmental programs, such as hematopoiesis, neurogenesis, and skeletogenesis, and are implicated in human leukemias. MOZ is also the catalytic subunit of a tetrameric inhibitor of growth 5 (ING5) complex, which specifically acetylates nucleosomal histone H3K14. Moreover, MOZ and MORF are involved in regulating transcriptional activation mediated by Runx2 (or Cbfa1), a Runt-domain transcription factor known to play important roles in T cell lymphoma genesis and bone development, and its homologs. This family also includes three members of the d4 gene family, DPF1 (neuro-d4), DPF2 (ubi-d4/Requiem), and DPF3 (cer-d4), which function as transcription factors and are involved in transcriptional regulation of genes via changing the condensed/decondensed state of chromatin in nucleus. DPF2 is ubiquitously expressed and it acts as a transcription factor that may participate in developmentally programmed cell death. DPF1 and DPF3 are expressed predominantly in neural tissues, and they may be involved in the transcription regulation of neuro specific gene clusters. All family members contain two plant homeodomain (PHD) fingers. This model corresponds to the first PHD finger. Pssm-ID: 277001 Cd Length: 56 Bit Score: 104.74 E-value: 4.57e-27
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PHD1_d4 | cd15619 | PHD finger 1 found in d4 gene family proteins; The family includes proteins coded by three ... |
216-269 | 1.65e-20 | ||||
PHD finger 1 found in d4 gene family proteins; The family includes proteins coded by three members of the d4 gene family, DPF1 (neuro-d4), DPF2 (ubi-d4/Requiem), and DPF3 (cer-d4), which function as transcription factors and are involved in transcriptional regulation of genes by changing the condensed/decondensed state of chromatin in the nucleus. DPF2 is ubiquitously expressed and it acts as a transcription factor that may participate in developmentally programmed cell death. DPF1 and DPF3 are expressed predominantly in neural tissues, and they may be involved in the transcription regulation of neuro-specific gene clusters. The d4 family proteins show distinct domain organization with domain 2/3 in the N-terminal region, a Cys2His2 (C2H2) zinc finger or Kruppel-type zinc finger in the central part and two adjacent plant homeodomain (PHD) fingers (d4-domain) in the C-terminal part of the molecule. This model corresponds to the first PHD finger. Pssm-ID: 277091 Cd Length: 56 Bit Score: 86.36 E-value: 1.65e-20
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PHD1_DPF2_like | cd15691 | PHD finger 1 found in D4, zinc and double PHD fingers family 2 (DPF2); DPF2 (also termed zinc ... |
216-269 | 1.39e-19 | ||||
PHD finger 1 found in D4, zinc and double PHD fingers family 2 (DPF2); DPF2 (also termed zinc finger protein ubi-d4, apoptosis response zinc finger protein, BRG1-associated factor 45D (BAF45D), or protein requiem) is a transcription factor that is encoded by the ubiquitously expressed gene, ubi-d4, and may be involved in leukemia or other cancers with other genes connected with cancer. It recognizes acetylated histone H3 and suppresses the function of estrogen-related receptor alpha (ERRalpha) through histone deacetylase 1 (HDAC1). Moreover, DPF2 functions as a linker protein between the SWI/SNF complex and RelB/p52 NF-kappaB heterodimer and plays important roles in NF-kappaB transactivation via its non-canonical pathway. It is also required as a transcriptional coactivator in SWI/SNF complex-dependent activation of NF-kappaB RelA/p50 heterodimer. DPF2 contains a nuclear localization signal in the N-terminal region, a Cys2His2 (C2H2) zinc finger or Kruppel-type zinc-finger and a sequence of negatively charged amino acids in the central region, and a cysteine/histidine-rich region that is composed of two adjacent plant homeodomain (PHD) fingers (d4-domain) in the C-terminal part of the molecule. This subfamily also includes DPF3 from zebrafish. This model describes the first PHD finger. Pssm-ID: 277161 Cd Length: 56 Bit Score: 83.53 E-value: 1.39e-19
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PHD1_DPF3 | cd15692 | PHD finger 1 found in D4, zinc and double PHD fingers family 3 (DPF3); DPF3, also termed ... |
216-270 | 2.14e-19 | ||||
PHD finger 1 found in D4, zinc and double PHD fingers family 3 (DPF3); DPF3, also termed BRG1-associated factor 45C (BAF45C), or zinc finger protein cer-d4, is encoded by a neuro-specific gene, cer-d4. It functions as a new epigenetic key factor for heart and muscle development and may be involved in the transcription regulation of neuro-specific gene clusters. It interacts with the BAF chromatin remodeling complex and binds methylated and acetylated lysine residues of histone 3 and 4. DPF3 contains a nuclear localization signal in the N-terminal region, a Cys2His2 (C2H2) zinc finger or Kruppel-type zinc-finger and a sequence of negatively charged amino acids in the central region, and a cysteine/histidine-rich region that is composed of two adjacent plant homeodomain (PHD) fingers (d4-domain) in the C-terminal part of the molecule. This model corresponds to the first PHD finger. Pssm-ID: 277162 Cd Length: 57 Bit Score: 83.20 E-value: 2.14e-19
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PTZ00064 | PTZ00064 | histone acetyltransferase; Provisional |
275-426 | 8.99e-19 | ||||
histone acetyltransferase; Provisional Pssm-ID: 173359 [Multi-domain] Cd Length: 552 Bit Score: 92.00 E-value: 8.99e-19
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PHD1_DPF1 | cd15690 | PHD finger 1 found in D4, zinc and double PHD fingers family 1 (DPF1); DPF1, also termed zinc ... |
212-270 | 1.49e-16 | ||||
PHD finger 1 found in D4, zinc and double PHD fingers family 1 (DPF1); DPF1, also termed zinc finger protein neuro-d4, or BRG1-associated factor 45B (BAF45B), is encoded by a neuro specific gene, neuro-d4. It may be involved in the transcription regulation of neuro specific gene clusters. DPF1 contains a nuclear localization signal in the N-terminal region, a Cys2His2 (C2H2) zinc finger or Kruppel-type zinc-finger and a sequence of negatively charged amino acids in the central, and a cysteine/histidine-rich region that is composed of two adjacent plant homeodomain (PHD)-fingers (d4-domain) in the C-terminal part of the molecule. The family corresponds to the first PHD finger. Pssm-ID: 277160 Cd Length: 58 Bit Score: 75.08 E-value: 1.49e-16
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PHD1_PHF10 | cd15528 | PHD finger 1 found in PHD finger protein 10 (PHF10) and similar proteins; PHF10, also termed ... |
215-269 | 1.35e-14 | ||||
PHD finger 1 found in PHD finger protein 10 (PHF10) and similar proteins; PHF10, also termed BRG1-associated factor 45a (BAF45a), or XAP135, is a ubiquitously expressed transcriptional regulator that is required for maintaining the undifferentiated status of neuroblasts. It contains a SAY (supporter of activation of yellow) domain and two adjacent plant homeodomain (PHD) fingers. This model corresponds to the first PHD finger. Pssm-ID: 277003 Cd Length: 54 Bit Score: 69.36 E-value: 1.35e-14
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H15 | smart00526 | Domain in histone families 1 and 5; |
113-167 | 1.41e-09 | ||||
Domain in histone families 1 and 5; Pssm-ID: 197772 [Multi-domain] Cd Length: 66 Bit Score: 55.66 E-value: 1.41e-09
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PHD | pfam00628 | PHD-finger; PHD folds into an interleaved type of Zn-finger chelating 2 Zn ions in a similar ... |
215-272 | 4.19e-08 | ||||
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: 50.95 E-value: 4.19e-08
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PHD | smart00249 | PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in ... |
215-269 | 2.61e-06 | ||||
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: 45.67 E-value: 2.61e-06
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PHD_SF | cd15489 | PHD finger superfamily; The PHD finger superfamily includes a canonical plant homeodomain (PHD) ... |
215-269 | 7.74e-04 | ||||
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: 38.84 E-value: 7.74e-04
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H15 | cd00073 | linker histone 1 and histone 5 domains; the basic subunit of chromatin is the nucleosome, ... |
114-167 | 1.96e-03 | ||||
linker histone 1 and histone 5 domains; the basic subunit of chromatin is the nucleosome, consisting of an octamer of core histones, two full turns of DNA, a linker histone (H1 or H5) and a variable length of linker DNA; H1/H5 are chromatin-associated proteins that bind to the exterior of nucleosomes and dramatically stabilize the highly condensed states of chromatin fibers; stabilization of higher order folding occurs through electrostatic neutralization of the linker DNA segments, through a highly positively charged carboxy- terminal domain known as the AKP helix (Ala, Lys, Pro); thought to be involved in specific protein-protein and protein-DNA interactions and play a role in suppressing core histone tail domain acetylation in the chromatin fiber Pssm-ID: 238028 [Multi-domain] Cd Length: 88 Bit Score: 38.76 E-value: 1.96e-03
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Blast search parameters | ||||
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