SET and MYND domain containing 1b [Salmo salar]
histone-lysine N-methyltransferase SMYD1( domain architecture ID 14410430)
histone-lysine N-methyltransferase SMYD1 methylates histone H3 at 'Lys-4' (H3K4me), seems able to perform both mono-, di-, and trimethylation
List of domain hits
Name | Accession | Description | Interval | E-value | |||||
SET_SMYD1 | cd10526 | SET domain (including post-SET domain) found in SET and MYND domain-containing protein 1 ... |
3-269 | 6.25e-125 | |||||
SET domain (including post-SET domain) found in SET and MYND domain-containing protein 1 (SMYD1) and similar proteins; SMYD1 (EC 2.1.1.43), also termed BOP, is a heart and muscle specific SET-MYND domain containing protein, which functions as a histone methyltransferase and regulates downstream gene transcription. It methylates histone H3 at 'Lys-4' (H3K4me), seems able to perform both mono-, di-, and trimethylation. SMYD1 plays a critical role in cardiomyocyte differentiation, cardiac morphogenesis and myofibril organization, as well as in the regulation of endothelial cells (ECs). It is expressed in vascular endothelial cells, it has beenshown that knockdown of SMYD1 in endothelial cells impairs EC migration and tube formation. : Pssm-ID: 380924 [Multi-domain] Cd Length: 210 Bit Score: 355.18 E-value: 6.25e-125
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zf-MYND | pfam01753 | MYND finger; |
47-85 | 4.12e-14 | |||||
MYND finger; : Pssm-ID: 460312 Cd Length: 39 Bit Score: 65.13 E-value: 4.12e-14
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Name | Accession | Description | Interval | E-value | |||||
SET_SMYD1 | cd10526 | SET domain (including post-SET domain) found in SET and MYND domain-containing protein 1 ... |
3-269 | 6.25e-125 | |||||
SET domain (including post-SET domain) found in SET and MYND domain-containing protein 1 (SMYD1) and similar proteins; SMYD1 (EC 2.1.1.43), also termed BOP, is a heart and muscle specific SET-MYND domain containing protein, which functions as a histone methyltransferase and regulates downstream gene transcription. It methylates histone H3 at 'Lys-4' (H3K4me), seems able to perform both mono-, di-, and trimethylation. SMYD1 plays a critical role in cardiomyocyte differentiation, cardiac morphogenesis and myofibril organization, as well as in the regulation of endothelial cells (ECs). It is expressed in vascular endothelial cells, it has beenshown that knockdown of SMYD1 in endothelial cells impairs EC migration and tube formation. Pssm-ID: 380924 [Multi-domain] Cd Length: 210 Bit Score: 355.18 E-value: 6.25e-125
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zf-MYND | pfam01753 | MYND finger; |
47-85 | 4.12e-14 | |||||
MYND finger; Pssm-ID: 460312 Cd Length: 39 Bit Score: 65.13 E-value: 4.12e-14
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SET | COG2940 | SET domain-containing protein (function unknown) [General function prediction only]; |
184-271 | 9.80e-10 | |||||
SET domain-containing protein (function unknown) [General function prediction only]; Pssm-ID: 442183 [Multi-domain] Cd Length: 134 Bit Score: 55.74 E-value: 9.80e-10
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SET | pfam00856 | SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be ... |
205-241 | 1.25e-08 | |||||
SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be protein-protein interaction domains. It has been demonstrated that SET domains mediate interactions with a family of proteins that display similarity with dual-specificity phosphatases (dsPTPases). A subset of SET domains have been called PR domains. These domains are divergent in sequence from other SET domains, but also appear to mediate protein-protein interaction. The SET domain consists of two regions known as SET-N and SET-C. SET-C forms an unusual and conserved knot-like structure of probably functional importance. Additionally to SET-N and SET-C, an insert region (SET-I) and flanking regions of high structural variability form part of the overall structure. Pssm-ID: 459965 [Multi-domain] Cd Length: 115 Bit Score: 52.14 E-value: 1.25e-08
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SET | smart00317 | SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on ... |
160-246 | 1.27e-08 | |||||
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on outlier plant homologues Pssm-ID: 214614 [Multi-domain] Cd Length: 124 Bit Score: 52.34 E-value: 1.27e-08
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Name | Accession | Description | Interval | E-value | ||||||
SET_SMYD1 | cd10526 | SET domain (including post-SET domain) found in SET and MYND domain-containing protein 1 ... |
3-269 | 6.25e-125 | ||||||
SET domain (including post-SET domain) found in SET and MYND domain-containing protein 1 (SMYD1) and similar proteins; SMYD1 (EC 2.1.1.43), also termed BOP, is a heart and muscle specific SET-MYND domain containing protein, which functions as a histone methyltransferase and regulates downstream gene transcription. It methylates histone H3 at 'Lys-4' (H3K4me), seems able to perform both mono-, di-, and trimethylation. SMYD1 plays a critical role in cardiomyocyte differentiation, cardiac morphogenesis and myofibril organization, as well as in the regulation of endothelial cells (ECs). It is expressed in vascular endothelial cells, it has beenshown that knockdown of SMYD1 in endothelial cells impairs EC migration and tube formation. Pssm-ID: 380924 [Multi-domain] Cd Length: 210 Bit Score: 355.18 E-value: 6.25e-125
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SET_SMYD1_2_3-like | cd19167 | SET domain (including post-SET domain) found in SET and MYND domain-containing proteins, SMYD1, ... |
3-268 | 3.25e-78 | ||||||
SET domain (including post-SET domain) found in SET and MYND domain-containing proteins, SMYD1, SMYD2, SMYD3 and similar proteins; The family includes SET and MYND domain-containing proteins, SMYD1, SMYD2 and SMYD3. SMYD1 (EC 2.1.1.43; also termed BOP) is a heart and muscle specific SET-MYND domain containing protein, which functions as a histone methyltransferase and regulates downstream gene transcription. It methylates histone H3 at 'Lys-4' (H3K4me), seems able to perform both mono-, di-, and trimethylation. SMYD2 (also termed HSKM-B, or lysine N-methyltransferase 3C (KMT3C)) functions as a histone methyltransferase that methylates both histones and non-histone proteins, including p53/TP53 and RB1. It specifically methylates histone H3 'Lys-4' (H3K4me) and dimethylates histone H3 'Lys-36' (H3K36me2). SMYD3 (also termed zinc finger MYND domain-containing protein 1) functions as a histone methyltransferase that specifically methylates 'Lys-4' of histone H3, inducing di- and tri-methylation, but not monomethylation. It also methylates 'Lys-5' of histone H4. SMYD3 plays an important role in transcriptional activation as a member of an RNA polymerase complex. Pssm-ID: 380944 [Multi-domain] Cd Length: 205 Bit Score: 236.55 E-value: 3.25e-78
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SET_SMYD3 | cd19203 | SET domain (including post-SET domain) found in SET and MYND domain-containing protein 3 ... |
2-269 | 4.87e-51 | ||||||
SET domain (including post-SET domain) found in SET and MYND domain-containing protein 3 (SMYD3) and similar proteins; SMYD3 (also termed zinc finger MYND domain-containing protein 1) functions as a histone methyltransferase that specifically methylates 'Lys-4' of histone H3, inducing di- and tri-methylation, but not monomethylation. It also methylates 'Lys-5' of histone H4. SMYD3 plays an important role in transcriptional activation as a member of an RNA polymerase complex. It is overexpressed in colorectal, breast, prostate, and hepatocellular tumors, and has been implicated as an oncogene in human malignancies. Methylation of MEKK2 by SMYD3 is important for regulation of the MEK/ERK pathway, suggesting the possibility of selectively targeting SMYD3 in RAS-driven cancers. Pssm-ID: 380980 [Multi-domain] Cd Length: 210 Bit Score: 167.16 E-value: 4.87e-51
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SET_SMYD2 | cd19202 | SET domain (including post-SET domain) found in SET and MYND domain-containing protein 2 ... |
2-268 | 2.65e-37 | ||||||
SET domain (including post-SET domain) found in SET and MYND domain-containing protein 2 (SMYD2) and similar proteins; SMYD2 (also termed HSKM-B, lysine N-methyltransferase 3C (KMT3C)) functions as a histone methyltransferase that methylates both histones and non-histone proteins, including p53/TP53 and RB1. It specifically methylates histone H3 'Lys-4' (H3K4me) and dimethylates histone H3 'Lys-36' (H3K36me2). It plays a role in myofilament organization in both skeletal and cardiac muscles via Hsp90 methylation. SMYD2 overexpression is associated with tumor cell proliferation and a worse outcome in human papillomavirus-unrelated nonmultiple head and neck carcinomas. It regulates leukemia cell growth such that diminished SMYD2 expression upregulates SET7/9, thereby possibly shifting leukemia cells from growth to quiescence state associated with resistance to DNA damage associated with Acute Myeloid Leukemia (AML). Pssm-ID: 380979 [Multi-domain] Cd Length: 206 Bit Score: 131.87 E-value: 2.65e-37
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SET_SMYD | cd20071 | SET domain (including SET domain and post-SET domain) found in SET and MYND domain-containing ... |
182-268 | 2.14e-28 | ||||||
SET domain (including SET domain and post-SET domain) found in SET and MYND domain-containing protein, and similar proteins; The family includes SET and MYND domain-containing proteins, SMYD1-SYMD5. SMYD1 (EC 2.1.1.43; also termed BOP) is a heart and muscle specific SET-MYND domain containing protein, which functions as a histone methyltransferase and regulates downstream gene transcription. It methylates histone H3 at 'Lys-4' (H3K4me), seems able to perform both mono-, di-, and trimethylation. SMYD2 (also termed HSKM-B, or lysine N-methyltransferase 3C (KMT3C)) functions as a histone methyltransferase that methylates both histones and non-histone proteins, including p53/TP53 and RB1. It specifically methylates histone H3 'Lys-4' (H3K4me) and dimethylates histone H3 'Lys-36' (H3K36me2). SMYD3 (also termed zinc finger MYND domain-containing protein 1) functions as a histone methyltransferase that specifically methylates 'Lys-4' of histone H3, inducing di- and tri-methylation, but not monomethylation. It also methylates 'Lys-5' of histone H4. SMYD3 plays an important role in transcriptional activation as a member of an RNA polymerase complex. SMYD4 functions as a potential tumor suppressor that plays a critical role in breast carcinogenesis at least partly through inhibiting the expression of PDGFR-alpha. SMYD5 (also termed protein NN8-4AG, or retinoic acid-induced protein 15) functions as histone lysine methyltransferase that mediates H4K20me3 at heterochromatin regions. Pssm-ID: 380997 [Multi-domain] Cd Length: 122 Bit Score: 105.92 E-value: 2.14e-28
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SET_SMYD4 | cd10536 | SET domain (including iSET domain and post-SET domain) found in SET and MYND domain-containing ... |
2-268 | 5.17e-23 | ||||||
SET domain (including iSET domain and post-SET domain) found in SET and MYND domain-containing protein 4 (SMYD4) and similar proteins; SMYD4 functions as a potential tumor suppressor that plays a critical role in breast carcinogenesis at least partly through inhibiting the expression of PDGFR-alpha. In zebrafish, SMYD4 is ubiquitously expressed in early embryos and becomes enriched in the developing heart; mutants show a strong defect in cardiomyocyte proliferation, which lead to a severe cardiac malformation. Pssm-ID: 380934 [Multi-domain] Cd Length: 218 Bit Score: 94.29 E-value: 5.17e-23
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zf-MYND | pfam01753 | MYND finger; |
47-85 | 4.12e-14 | ||||||
MYND finger; Pssm-ID: 460312 Cd Length: 39 Bit Score: 65.13 E-value: 4.12e-14
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SET_SMYD5 | cd10521 | SET domain (including iSET domain and post-SET domain) found in SET and MYND domain-containing ... |
3-268 | 3.05e-13 | ||||||
SET domain (including iSET domain and post-SET domain) found in SET and MYND domain-containing protein 5 (SMYD5) and similar proteins; SMYD5 (also termed protein NN8-4AG, or retinoic acid-induced protein 15) functions as histone lysine methyltransferase that mediates H4K20me3 at heterochromatin regions. It plays an important role in chromosome integrity by regulating heterochromatin and repressing endogenous repetitive DNA elements during differentiation. In zebrafish embryogenesis, it plays pivotal roles in both primitive and definitive hematopoiesis. Pssm-ID: 380919 [Multi-domain] Cd Length: 282 Bit Score: 68.49 E-value: 3.05e-13
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SET | COG2940 | SET domain-containing protein (function unknown) [General function prediction only]; |
184-271 | 9.80e-10 | ||||||
SET domain-containing protein (function unknown) [General function prediction only]; Pssm-ID: 442183 [Multi-domain] Cd Length: 134 Bit Score: 55.74 E-value: 9.80e-10
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SET_Suv4-20-like | cd10524 | SET domain (including post-SET domain) found in Drosophila melanogaster suppressor of ... |
205-269 | 8.49e-09 | ||||||
SET domain (including post-SET domain) found in Drosophila melanogaster suppressor of variegation 4-20 (Suv4-20) and similar proteins; Suv4-20 (also termed Su(var)4-20) is a histone-lysine N-methyltransferase that specifically trimethylates 'Lys-20' of histone H4. It acts as a dominant suppressor of position-effect variegation. The family also includes Suv4-20 homologs, lysine N-methyltransferase 5B (KMT5B) and lysine N-methyltransferase 5C (KMT5C). Both KMT5B (also termed lysine-specific methyltransferase 5B, or suppressor of variegation 4-20 homolog 1, or Su(var)4-20 homolog 1, or Suv4-20h1) and KMT5C (also termed lysine-specific methyltransferase 5C, or suppressor of variegation 4-20 homolog 2, or Su(var)4-20 homolog 2, or Suv4-20h2) are histone methyltransferases that specifically trimethylate 'Lys-20' of histone H4 (H4K20me3). They play central roles in the establishment of constitutive heterochromatin in pericentric heterochromatin regions. Pssm-ID: 380922 [Multi-domain] Cd Length: 141 Bit Score: 53.44 E-value: 8.49e-09
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SET | pfam00856 | SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be ... |
205-241 | 1.25e-08 | ||||||
SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be protein-protein interaction domains. It has been demonstrated that SET domains mediate interactions with a family of proteins that display similarity with dual-specificity phosphatases (dsPTPases). A subset of SET domains have been called PR domains. These domains are divergent in sequence from other SET domains, but also appear to mediate protein-protein interaction. The SET domain consists of two regions known as SET-N and SET-C. SET-C forms an unusual and conserved knot-like structure of probably functional importance. Additionally to SET-N and SET-C, an insert region (SET-I) and flanking regions of high structural variability form part of the overall structure. Pssm-ID: 459965 [Multi-domain] Cd Length: 115 Bit Score: 52.14 E-value: 1.25e-08
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SET | smart00317 | SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on ... |
160-246 | 1.27e-08 | ||||||
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on outlier plant homologues Pssm-ID: 214614 [Multi-domain] Cd Length: 124 Bit Score: 52.34 E-value: 1.27e-08
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SET_LSMT | cd10527 | SET domain found in Rubisco large subunit methyltransferase (LSMT) and similar proteins; ... |
3-241 | 2.25e-06 | ||||||
SET domain found in Rubisco large subunit methyltransferase (LSMT) and similar proteins; Rubisco LSMT is a non-histone protein methyl transferase responsible for the trimethylation of lysine14 in the large subunit of Rubisco (ribulose-1,5-bisphosphate carboxylase/oxygenase). The family also includes SET domain-containing proteins, SETD3, SETD4 and SETD6, which belong to methyltransferase class VII that represents classical non-histone SET domain methyltransferases. Members in this family contain a SET domain and a C-terminal RubisCO LSMT substrate-binding (Rubis-subs-bind) domain. Pssm-ID: 380925 [Multi-domain] Cd Length: 236 Bit Score: 47.83 E-value: 2.25e-06
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SET | cd08161 | SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain superfamily; The Su(var)3-9, ... |
206-241 | 1.24e-05 | ||||||
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain superfamily; The Su(var)3-9, Enhancer-of-zeste, Trithorax (SET) domain superfamily corresponds to SET domain-containing lysine methyltransferases, which catalyze site and state-specific methylation of lysine residues in histones that are fundamental in epigenetic regulation of gene activation and silencing in eukaryotic organisms. SET domains appear to be protein-protein interaction domains. It has been demonstrated that SET domains mediate interactions with a family of proteins that display similarity with dual-specificity phosphatases (dsPTPases). A subset of SET domains has been called PR domains. These domains are divergent in sequence from other SET domains, but also appear to mediate protein-protein interaction. The SET domain consists of two regions known as N-SET and C-SET. C-SET forms an unusual and conserved knot-like structure of probable functional importance. In addition to N-SET and C-SET, an insert region (I-SET) and flanking regions of high structural variability form part of the overall structure. Some family members contain a pre-SET domain, which is found in a number of histone methyltransferases (HMTase), and a post-SET domain, which harbors a zinc-binding site. Pssm-ID: 380914 [Multi-domain] Cd Length: 72 Bit Score: 42.62 E-value: 1.24e-05
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SET_ASH1L | cd19174 | SET domain (including post-SET domain) found in ASH1-like protein (ASH1L) and similar proteins; ... |
205-272 | 6.76e-05 | ||||||
SET domain (including post-SET domain) found in ASH1-like protein (ASH1L) and similar proteins; ASH1L (EC 2.1.1.43; also termed absent small and homeotic disks protein 1 homolog, KMT2H, or lysine N-methyltransferase 2H) acts as histone-lysine N-methyltransferase that specifically methylates 'Lys-36' of histone H3 (H3K36me). It plays important roles in development; heterozygous mutation of ASH1L is associated with severe intellectual disability (ID) and multiple congenital anomaly (MCA). Pssm-ID: 380951 [Multi-domain] Cd Length: 141 Bit Score: 41.89 E-value: 6.76e-05
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SET_SpSet7-like | cd10540 | SET domain found in Schizossacharomyces pombe Set7 and similar proteins; Schizosaccharomyces ... |
184-241 | 1.09e-04 | ||||||
SET domain found in Schizossacharomyces pombe Set7 and similar proteins; Schizosaccharomyces pombe Set7 is a novel histone-lysine N-methyltransferase. The family also includes a viral histone H3 lysine 27 methyltransferase from Paramecium bursaria Chlorella virus 1 (PBCV-1). Pssm-ID: 380938 Cd Length: 112 Bit Score: 40.70 E-value: 1.09e-04
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SET_KMT5C | cd19185 | SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 5C (KMT5C) ... |
205-241 | 1.74e-04 | ||||||
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 5C (KMT5C) and similar proteins; KMT5C (also termed lysine N-methyltransferase 5C, lysine-specific methyltransferase 5C, suppressor of variegation 4-20 homolog 2, Su(var)4-20 homolog 2 or Suv4-20h2) is a histone methyltransferase that specifically trimethylates 'Lys-20' of histone H4 (H4K20me3). It plays a central role in the establishment of constitutive heterochromatin in pericentric heterochromatin regions. Pssm-ID: 380962 Cd Length: 142 Bit Score: 40.79 E-value: 1.74e-04
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SET_SETD1-like | cd10518 | SET domain (including post-SET domain) found in SET domain-containing proteins (SETD1A/SETD1B), ... |
205-241 | 3.48e-03 | ||||||
SET domain (including post-SET domain) found in SET domain-containing proteins (SETD1A/SETD1B), histone-lysine N-methyltransferases (KMT2A/KMT2B/KMT2C/KMT2D) and similar proteins; This family includes SET domain-containing protein 1A (SETD1A), 1B (SETD1B), as well as histone-lysine N-methyltransferase 2A (KMT2A), 2B (KMT2B), 2C (KMT2C), 2D (KMT2D). These proteins are histone-lysine N-methyltransferases (EC 2.1.1.43) that specifically methylate 'Lys-4' of histone H3 (H3K4me). Pssm-ID: 380916 Cd Length: 150 Bit Score: 37.19 E-value: 3.48e-03
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SET_KMT2A_2B | cd19170 | SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2A (KMT2A), ... |
206-241 | 3.70e-03 | ||||||
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2A (KMT2A), 2B (KMT2B) and similar proteins; This family includes KMT2A and KMT2B. Both KMT2A (also termed ALL-1 or CXXC7 or MLL or MLL1 or TRX1 or HRX) and KMT2B (also termed MLL4 or TRX2) act as histone methyltransferases that methylate 'Lys-4' of histone H3 (H3K4me). Pssm-ID: 380947 [Multi-domain] Cd Length: 152 Bit Score: 37.37 E-value: 3.70e-03
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SET_LegAS4-like | cd10522 | SET domain found in Legionella pneumophila type IV secretion system effector LegAS4 and ... |
202-241 | 5.42e-03 | ||||||
SET domain found in Legionella pneumophila type IV secretion system effector LegAS4 and similar proteins; LegAS4 is a type IV secretion system effector of Legionella pneumophila. It contains a SET domain that is involved in the modification of Lys4 of histone H3 (H3K4) in the nucleolus of the host cell, thereby enhancing heterochromatic rDNA transcription. It also contains an ankyrin repeat domain of unknown function at its C-terminal region. Pssm-ID: 380920 [Multi-domain] Cd Length: 122 Bit Score: 36.17 E-value: 5.42e-03
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Blast search parameters | ||||
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