retinoblastoma-like protein 2 isoform X4 [Trachypithecus francoisi]
List of domain hits
Name | Accession | Description | Interval | E-value | ||||
CYCLIN_RBL2 | cd20606 | cyclin box found in retinoblastoma-like protein 2 (RBL2) and similar proteins; RBL2, also ... |
757-946 | 4.15e-134 | ||||
cyclin box found in retinoblastoma-like protein 2 (RBL2) and similar proteins; RBL2, also called 130 kDa retinoblastoma-associated protein (p130), retinoblastoma-related protein 2 (RBR-2), or pRb2, is a key regulator of entry into cell division. It is directly involved in heterochromatin formation by maintaining overall chromatin structure, especially that of constitutive heterochromatin by stabilizing histone methylation. RBL2 recruits and targets histone methyltransferases KMT5B and KMT5C, leading to epigenetic transcriptional repression. It controls histone H4 'Lys-20' trimethylation. It probably acts as a transcription repressor by recruiting chromatin-modifying enzymes to promoters. It may also act as a tumor suppressor. RBL2 contains one cyclin box. The cyclin box is a protein binding domain. : Pssm-ID: 410309 Cd Length: 189 Bit Score: 402.74 E-value: 4.15e-134
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RB_A | pfam01858 | Retinoblastoma-associated protein A domain; This domain has the cyclin fold as predicted. |
339-531 | 4.28e-99 | ||||
Retinoblastoma-associated protein A domain; This domain has the cyclin fold as predicted. : Pssm-ID: 460364 Cd Length: 195 Bit Score: 310.67 E-value: 4.28e-99
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DUF3452 | pfam11934 | Domain of unknown function (DUF3452); This presumed domain is functionally uncharacterized. ... |
26-161 | 1.05e-58 | ||||
Domain of unknown function (DUF3452); This presumed domain is functionally uncharacterized. This domain is found in bacteria and eukaryotes. This domain is typically between 124 to 150 amino acids in length. This domain is found associated with pfam01858, pfam01857. This domain has a single completely conserved residue W that may be functionally important. : Pssm-ID: 463402 Cd Length: 134 Bit Score: 197.43 E-value: 1.05e-58
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SP1-4_N super family | cl41773 | N-terminal domain of transcription factor Specificity Proteins (SP) 1-4; Specificity Proteins ... |
592-732 | 7.42e-07 | ||||
N-terminal domain of transcription factor Specificity Proteins (SP) 1-4; Specificity Proteins (SPs) are transcription factors that are involved in many cellular processes, including cell differentiation, cell growth, apoptosis, immune responses, response to DNA damage, and chromatin remodeling. There are many SPs in vertebrates (9 SPs in humans and mice, 7 SPs in chicken, and 11 SPs in teleost fish), but arthropods only have 3 SPs. SPs belong to a family of proteins, called the SP/Kruppel or Krueppel-like Factor (KLF) family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. SP factors preferentially bind GC boxes, while KLFs bind CACCC boxes. Another characteristic hallmark of SP factors is the presence of the Buttonhead (BTD) box CXCPXC, just N-terminal to the zinc fingers. The function of the BTD box is unknown, but it is thought to play an important physiological role. Another feature of most SP factors is the presence of a conserved amino acid stretch, the so-called SP box, located close to the N-terminus. SP factors may be separated into three groups based on their domain architecture and the similarity of their N-terminal transactivation domains: SP1-4, SP5, and SP6-9. The transactivation domains between the three groups are not homologous to one another. SP1-4 have similar N-terminal transactivation domains characterized by glutamine-rich regions, which, in most cases, have adjacent serine/threonine-rich regions. This model represents the N-terminal domain of SP1-4. The actual alignment was detected with superfamily member cd22553: Pssm-ID: 425404 [Multi-domain] Cd Length: 384 Bit Score: 52.72 E-value: 7.42e-07
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Name | Accession | Description | Interval | E-value | ||||
CYCLIN_RBL2 | cd20606 | cyclin box found in retinoblastoma-like protein 2 (RBL2) and similar proteins; RBL2, also ... |
757-946 | 4.15e-134 | ||||
cyclin box found in retinoblastoma-like protein 2 (RBL2) and similar proteins; RBL2, also called 130 kDa retinoblastoma-associated protein (p130), retinoblastoma-related protein 2 (RBR-2), or pRb2, is a key regulator of entry into cell division. It is directly involved in heterochromatin formation by maintaining overall chromatin structure, especially that of constitutive heterochromatin by stabilizing histone methylation. RBL2 recruits and targets histone methyltransferases KMT5B and KMT5C, leading to epigenetic transcriptional repression. It controls histone H4 'Lys-20' trimethylation. It probably acts as a transcription repressor by recruiting chromatin-modifying enzymes to promoters. It may also act as a tumor suppressor. RBL2 contains one cyclin box. The cyclin box is a protein binding domain. Pssm-ID: 410309 Cd Length: 189 Bit Score: 402.74 E-value: 4.15e-134
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RB_A | pfam01858 | Retinoblastoma-associated protein A domain; This domain has the cyclin fold as predicted. |
339-531 | 4.28e-99 | ||||
Retinoblastoma-associated protein A domain; This domain has the cyclin fold as predicted. Pssm-ID: 460364 Cd Length: 195 Bit Score: 310.67 E-value: 4.28e-99
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RB_B | pfam01857 | Retinoblastoma-associated protein B domain; The crystal structure of the Rb pocket bound to a ... |
757-940 | 6.62e-73 | ||||
Retinoblastoma-associated protein B domain; The crystal structure of the Rb pocket bound to a nine-residue E7 peptide containing the LxCxE motif, shared by other Rb-binding viral and cellular proteins, shows that the LxCxE peptide binds a highly conserved groove on the B domain. The B domain has a cyclin fold. Pssm-ID: 460363 Cd Length: 131 Bit Score: 237.08 E-value: 6.62e-73
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DUF3452 | pfam11934 | Domain of unknown function (DUF3452); This presumed domain is functionally uncharacterized. ... |
26-161 | 1.05e-58 | ||||
Domain of unknown function (DUF3452); This presumed domain is functionally uncharacterized. This domain is found in bacteria and eukaryotes. This domain is typically between 124 to 150 amino acids in length. This domain is found associated with pfam01858, pfam01857. This domain has a single completely conserved residue W that may be functionally important. Pssm-ID: 463402 Cd Length: 134 Bit Score: 197.43 E-value: 1.05e-58
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SP1-4_arthropods_N | cd22553 | N-terminal domain of transcription factor Specificity Protein (SP) 1-4 from arthropods; ... |
592-732 | 7.42e-07 | ||||
N-terminal domain of transcription factor Specificity Protein (SP) 1-4 from arthropods; Specificity Proteins (SPs) are transcription factors that are involved in many cellular processes, including cell differentiation, cell growth, apoptosis, immune responses, response to DNA damage, and chromatin remodeling. There are many SPs in vertebrates (9 SPs in humans and mice, 7 SPs in the chicken, and 11 SPs in teleost fish), but arthropods only have 3 SPs. One SP is clade SP1-4, which is expressed ubiquitously throughout development. SP1-4 belongs to a family of proteins, called the SP/Kruppel or Krueppel-like Factor (KLF) family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. SP factors preferentially bind GC boxes, while KLFs bind CACCC boxes. Another characteristic hallmark of SP factors is the presence of the Buttonhead (BTD) box CXCPXC, just N-terminal to the zinc fingers. The function of the BTD box is unknown, but it is thought to play an important physiological role. Another feature of most SP factors is the presence of a conserved amino acid stretch, the so-called SP box, located close to the N-terminus. This model represents the N-terminal domain of SP1-4 from arthropods. Pssm-ID: 411778 [Multi-domain] Cd Length: 384 Bit Score: 52.72 E-value: 7.42e-07
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CYCLIN | smart00385 | domain present in cyclins, TFIIB and Retinoblastoma; A helical domain present in cyclins and ... |
771-854 | 1.12e-04 | ||||
domain present in cyclins, TFIIB and Retinoblastoma; A helical domain present in cyclins and TFIIB (twice) and Retinoblastoma (once). A protein recognition domain functioning in cell-cycle and transcription control. Pssm-ID: 214641 [Multi-domain] Cd Length: 83 Bit Score: 41.81 E-value: 1.12e-04
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Name | Accession | Description | Interval | E-value | ||||
CYCLIN_RBL2 | cd20606 | cyclin box found in retinoblastoma-like protein 2 (RBL2) and similar proteins; RBL2, also ... |
757-946 | 4.15e-134 | ||||
cyclin box found in retinoblastoma-like protein 2 (RBL2) and similar proteins; RBL2, also called 130 kDa retinoblastoma-associated protein (p130), retinoblastoma-related protein 2 (RBR-2), or pRb2, is a key regulator of entry into cell division. It is directly involved in heterochromatin formation by maintaining overall chromatin structure, especially that of constitutive heterochromatin by stabilizing histone methylation. RBL2 recruits and targets histone methyltransferases KMT5B and KMT5C, leading to epigenetic transcriptional repression. It controls histone H4 'Lys-20' trimethylation. It probably acts as a transcription repressor by recruiting chromatin-modifying enzymes to promoters. It may also act as a tumor suppressor. RBL2 contains one cyclin box. The cyclin box is a protein binding domain. Pssm-ID: 410309 Cd Length: 189 Bit Score: 402.74 E-value: 4.15e-134
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RB_A | pfam01858 | Retinoblastoma-associated protein A domain; This domain has the cyclin fold as predicted. |
339-531 | 4.28e-99 | ||||
Retinoblastoma-associated protein A domain; This domain has the cyclin fold as predicted. Pssm-ID: 460364 Cd Length: 195 Bit Score: 310.67 E-value: 4.28e-99
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RB_B | pfam01857 | Retinoblastoma-associated protein B domain; The crystal structure of the Rb pocket bound to a ... |
757-940 | 6.62e-73 | ||||
Retinoblastoma-associated protein B domain; The crystal structure of the Rb pocket bound to a nine-residue E7 peptide containing the LxCxE motif, shared by other Rb-binding viral and cellular proteins, shows that the LxCxE peptide binds a highly conserved groove on the B domain. The B domain has a cyclin fold. Pssm-ID: 460363 Cd Length: 131 Bit Score: 237.08 E-value: 6.62e-73
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CYCLIN_RBL1 | cd20605 | cyclin box found in retinoblastoma-like protein 1 (RBL1) and similar proteins; RBL1, also ... |
751-946 | 2.86e-66 | ||||
cyclin box found in retinoblastoma-like protein 1 (RBL1) and similar proteins; RBL1, also called 107 kDa retinoblastoma-associated protein (p107), retinoblastoma-related protein 1 (RBR-1), or pRb1, is a key regulator of entry into cell division. It is directly involved in heterochromatin formation by maintaining overall chromatin structure, especially that of constitutive heterochromatin by stabilizing histone methylation. RBL1 recruits and targets histone methyltransferases KMT5B and KMT5C, leading to epigenetic transcriptional repression. It controls histone H4 'Lys-20' trimethylation. RBL1 probably acts as a transcription repressor by recruiting chromatin-modifying enzymes to promoters. It may also act as a tumor suppressor. RBL1 contains one cyclin box. The cyclin box is a protein binding domain. Pssm-ID: 410308 Cd Length: 130 Bit Score: 218.60 E-value: 2.86e-66
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CYCLIN_RBL | cd20600 | cyclin box found in retinoblastoma-like protein (RBL) subfamily; The RBL subfamily includes ... |
757-946 | 3.81e-66 | ||||
cyclin box found in retinoblastoma-like protein (RBL) subfamily; The RBL subfamily includes two retinoblastoma-like proteins, RBL1 and RBL2. They are key regulators of entry into cell division and are directly involved in heterochromatin formation by maintaining overall chromatin structure. RBL1 and RBL2 recruit and target histone methyltransferases KMT5B and KMT5C, leading to epigenetic transcriptional repression. They control histone H4 'Lys-20' trimethylation and probably act as transcription repressors by recruiting chromatin-modifying enzymes to promoters. They may also act as tumor suppressors. Members of this family contain one cyclin box. The cyclin box is a protein binding domain. Pssm-ID: 410303 Cd Length: 112 Bit Score: 217.66 E-value: 3.81e-66
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DUF3452 | pfam11934 | Domain of unknown function (DUF3452); This presumed domain is functionally uncharacterized. ... |
26-161 | 1.05e-58 | ||||
Domain of unknown function (DUF3452); This presumed domain is functionally uncharacterized. This domain is found in bacteria and eukaryotes. This domain is typically between 124 to 150 amino acids in length. This domain is found associated with pfam01858, pfam01857. This domain has a single completely conserved residue W that may be functionally important. Pssm-ID: 463402 Cd Length: 134 Bit Score: 197.43 E-value: 1.05e-58
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CYCLIN_RB-like | cd20548 | cyclin box found in retinoblastoma-associated protein (RB) family; The RB family includes ... |
758-935 | 7.35e-37 | ||||
cyclin box found in retinoblastoma-associated protein (RB) family; The RB family includes retinoblastoma-associated protein (RB), and two retinoblastoma-like proteins, RBL1 and RBL2. RB, also called p105-Rb, pRb, or pp110, is a key regulator of entry into cell division, and also acts as a tumor suppressor. It promotes G0-G1 transition when phosphorylated by CDK3/cyclin-C. It also acts as a transcription repressor of E2F1 target genes. RB is directly involved in heterochromatin formation by maintaining overall chromatin structure. It recruits and targets histone methyltransferases SUV39H1, KMT5B and KMT5C, leading to epigenetic transcriptional repression. RBL1 and RBL2 are also key regulators of entry into cell division. RBL1 and RBL2 recruit and target histone methyltransferases KMT5B and KMT5C, leading to epigenetic transcriptional repression. They control histone H4 'Lys-20' trimethylation and probably act as transcription repressors by recruiting chromatin-modifying enzymes to promoters. They may also act as tumor suppressors. Members of this family contain one cyclin box. The cyclin box is a protein binding domain. Pssm-ID: 410251 Cd Length: 122 Bit Score: 134.74 E-value: 7.35e-37
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CYCLIN_RB | cd20599 | cyclin box found in retinoblastoma-associated protein (RB) and similar proteins; RB, also ... |
757-859 | 2.00e-36 | ||||
cyclin box found in retinoblastoma-associated protein (RB) and similar proteins; RB, also called p105-Rb, pRb, or pp110, is a key regulator of entry into cell division and also acts as a tumor suppressor. It promotes G0-G1 transition when phosphorylated by CDK3/cyclin-C. It also acts as a transcription repressor of E2F1 target genes. RB is directly involved in heterochromatin formation by maintaining overall chromatin structure, especially that of constitutive heterochromatin by stabilizing histone methylation. It recruits and targets histone methyltransferases SUV39H1, KMT5B and KMT5C, leading to epigenetic transcriptional repression. It controls histone H4 'Lys-20' trimethylation. RB contains one cyclin box. The cyclin box is a protein binding domain. Pssm-ID: 410302 Cd Length: 126 Bit Score: 133.57 E-value: 2.00e-36
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CYCLIN_AtRBR_like | cd20601 | cyclin box found in Arabidopsis thaliana retinoblastoma-related protein 1 (AtRBR1) and similar ... |
758-944 | 5.42e-26 | ||||
cyclin box found in Arabidopsis thaliana retinoblastoma-related protein 1 (AtRBR1) and similar proteins; AtRBR1 is a key regulator of entry into cell division. It acts as a transcription repressor of E2F target genes, whose activity is required for progress from the G1 to the S phase of the cell cycle. AtRBR1 plays a central role in the mechanism controlling meristem cell differentiation, cell fate establishment and cell fate maintenance during organogenesis and gametogenesis. AtRBR1 contains one cyclin box. The cyclin box is a protein binding domain. Pssm-ID: 410304 Cd Length: 129 Bit Score: 104.01 E-value: 5.42e-26
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SP1-4_arthropods_N | cd22553 | N-terminal domain of transcription factor Specificity Protein (SP) 1-4 from arthropods; ... |
592-732 | 7.42e-07 | ||||
N-terminal domain of transcription factor Specificity Protein (SP) 1-4 from arthropods; Specificity Proteins (SPs) are transcription factors that are involved in many cellular processes, including cell differentiation, cell growth, apoptosis, immune responses, response to DNA damage, and chromatin remodeling. There are many SPs in vertebrates (9 SPs in humans and mice, 7 SPs in the chicken, and 11 SPs in teleost fish), but arthropods only have 3 SPs. One SP is clade SP1-4, which is expressed ubiquitously throughout development. SP1-4 belongs to a family of proteins, called the SP/Kruppel or Krueppel-like Factor (KLF) family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. SP factors preferentially bind GC boxes, while KLFs bind CACCC boxes. Another characteristic hallmark of SP factors is the presence of the Buttonhead (BTD) box CXCPXC, just N-terminal to the zinc fingers. The function of the BTD box is unknown, but it is thought to play an important physiological role. Another feature of most SP factors is the presence of a conserved amino acid stretch, the so-called SP box, located close to the N-terminus. This model represents the N-terminal domain of SP1-4 from arthropods. Pssm-ID: 411778 [Multi-domain] Cd Length: 384 Bit Score: 52.72 E-value: 7.42e-07
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CYCLIN | smart00385 | domain present in cyclins, TFIIB and Retinoblastoma; A helical domain present in cyclins and ... |
771-854 | 1.12e-04 | ||||
domain present in cyclins, TFIIB and Retinoblastoma; A helical domain present in cyclins and TFIIB (twice) and Retinoblastoma (once). A protein recognition domain functioning in cell-cycle and transcription control. Pssm-ID: 214641 [Multi-domain] Cd Length: 83 Bit Score: 41.81 E-value: 1.12e-04
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Blast search parameters | ||||
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