zinc finger protein 2 homolog isoform X1 [Salmo trutta]
C2H2-type zinc finger protein( domain architecture ID 11589988)
Cys2His2 (C2H2)-type zinc finger protein may be involved in transcriptional regulation
List of domain hits
Name | Accession | Description | Interval | E-value | |||||||
TIN2_N | cd11657 | N-terminal domain of TRF-interacting nuclear factor 2; shelterin complex protein of telomeres; ... |
34-212 | 6.69e-85 | |||||||
N-terminal domain of TRF-interacting nuclear factor 2; shelterin complex protein of telomeres; TIN2 is one of the six proteins of shelterin complex, which acts to protect telomeres from DNA damage repair machinery. TIN2 binds directly to TRF1 and TRF2 and stabilizes TRF2 complex-telomere binding by tethering it to the TRF1 complex. TIN2 binding to TRF2 is primarily via the TRF binding motif (TBM) region and the N-terminus, while the far C-terminal region has lower affinity. The TIN2 TBM, but not the N-terminal region, is involved in TIN2 binding to TRF1. Truncation of the TIN2 N-terminus in mouse results in telomere elongation, suggesting a negative regulatory function of this region. Three shelterin components (TRF1, TRF2, POT1) bind DNA and 3 components (TIN2, RAP1, TPP1) are recruited by these DNA binding factors. TRF1 activity at telomeres is regulated in part by selective ubiquitination and degradation. Ubiquitination of TRF1 is mediated by Fbx4, which binds TRF1 in the TRFH domain, via a small GTPase module. When bound to telomeres, TIN2 acts to protect TRF1 from SCF-Fbx4 mediated ubiquitination. F-box proteins act in substrate recognition as part of Skp1-Cul1-Rbx1-F- box (SCF) protein complexes. Tankyrase-mediated ADP-ribosylation releases TRF1 from telomeres, rendering them susceptible to ubiquitination and degradation, promoting telomere elongation. TIN2 also binds PIP1, which recruits POT1 to telomeres. : Pssm-ID: 240667 Cd Length: 188 Bit Score: 265.70 E-value: 6.69e-85
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COG5048 | COG5048 | FOG: Zn-finger [General function prediction only]; |
298-636 | 9.58e-15 | |||||||
FOG: Zn-finger [General function prediction only]; : Pssm-ID: 227381 [Multi-domain] Cd Length: 467 Bit Score: 77.43 E-value: 9.58e-15
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zf-H2C2_2 | pfam13465 | Zinc-finger double domain; |
669-694 | 2.85e-03 | |||||||
Zinc-finger double domain; : Pssm-ID: 463886 [Multi-domain] Cd Length: 26 Bit Score: 35.81 E-value: 2.85e-03
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zf-H2C2_2 | pfam13465 | Zinc-finger double domain; |
641-666 | 5.51e-03 | |||||||
Zinc-finger double domain; : Pssm-ID: 463886 [Multi-domain] Cd Length: 26 Bit Score: 34.65 E-value: 5.51e-03
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Name | Accession | Description | Interval | E-value | |||||||
TIN2_N | cd11657 | N-terminal domain of TRF-interacting nuclear factor 2; shelterin complex protein of telomeres; ... |
34-212 | 6.69e-85 | |||||||
N-terminal domain of TRF-interacting nuclear factor 2; shelterin complex protein of telomeres; TIN2 is one of the six proteins of shelterin complex, which acts to protect telomeres from DNA damage repair machinery. TIN2 binds directly to TRF1 and TRF2 and stabilizes TRF2 complex-telomere binding by tethering it to the TRF1 complex. TIN2 binding to TRF2 is primarily via the TRF binding motif (TBM) region and the N-terminus, while the far C-terminal region has lower affinity. The TIN2 TBM, but not the N-terminal region, is involved in TIN2 binding to TRF1. Truncation of the TIN2 N-terminus in mouse results in telomere elongation, suggesting a negative regulatory function of this region. Three shelterin components (TRF1, TRF2, POT1) bind DNA and 3 components (TIN2, RAP1, TPP1) are recruited by these DNA binding factors. TRF1 activity at telomeres is regulated in part by selective ubiquitination and degradation. Ubiquitination of TRF1 is mediated by Fbx4, which binds TRF1 in the TRFH domain, via a small GTPase module. When bound to telomeres, TIN2 acts to protect TRF1 from SCF-Fbx4 mediated ubiquitination. F-box proteins act in substrate recognition as part of Skp1-Cul1-Rbx1-F- box (SCF) protein complexes. Tankyrase-mediated ADP-ribosylation releases TRF1 from telomeres, rendering them susceptible to ubiquitination and degradation, promoting telomere elongation. TIN2 also binds PIP1, which recruits POT1 to telomeres. Pssm-ID: 240667 Cd Length: 188 Bit Score: 265.70 E-value: 6.69e-85
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TINF2_N | pfam14973 | TERF1-interacting nuclear factor 2 N-terminus; This is the N-terminus of TERF1-interacting ... |
38-182 | 3.37e-61 | |||||||
TERF1-interacting nuclear factor 2 N-terminus; This is the N-terminus of TERF1-interacting nuclear factor 2. It is required for the formation of the shelterin complex. The shelterin complex is involved in the protection and maintenance of telomeres. Pssm-ID: 464415 Cd Length: 148 Bit Score: 201.74 E-value: 3.37e-61
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COG5048 | COG5048 | FOG: Zn-finger [General function prediction only]; |
298-636 | 9.58e-15 | |||||||
FOG: Zn-finger [General function prediction only]; Pssm-ID: 227381 [Multi-domain] Cd Length: 467 Bit Score: 77.43 E-value: 9.58e-15
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zf-H2C2_2 | pfam13465 | Zinc-finger double domain; |
445-470 | 2.57e-04 | |||||||
Zinc-finger double domain; Pssm-ID: 463886 [Multi-domain] Cd Length: 26 Bit Score: 38.51 E-value: 2.57e-04
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zf-H2C2_2 | pfam13465 | Zinc-finger double domain; |
669-694 | 2.85e-03 | |||||||
Zinc-finger double domain; Pssm-ID: 463886 [Multi-domain] Cd Length: 26 Bit Score: 35.81 E-value: 2.85e-03
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zf-H2C2_2 | pfam13465 | Zinc-finger double domain; |
641-666 | 5.51e-03 | |||||||
Zinc-finger double domain; Pssm-ID: 463886 [Multi-domain] Cd Length: 26 Bit Score: 34.65 E-value: 5.51e-03
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Name | Accession | Description | Interval | E-value | |||||||
TIN2_N | cd11657 | N-terminal domain of TRF-interacting nuclear factor 2; shelterin complex protein of telomeres; ... |
34-212 | 6.69e-85 | |||||||
N-terminal domain of TRF-interacting nuclear factor 2; shelterin complex protein of telomeres; TIN2 is one of the six proteins of shelterin complex, which acts to protect telomeres from DNA damage repair machinery. TIN2 binds directly to TRF1 and TRF2 and stabilizes TRF2 complex-telomere binding by tethering it to the TRF1 complex. TIN2 binding to TRF2 is primarily via the TRF binding motif (TBM) region and the N-terminus, while the far C-terminal region has lower affinity. The TIN2 TBM, but not the N-terminal region, is involved in TIN2 binding to TRF1. Truncation of the TIN2 N-terminus in mouse results in telomere elongation, suggesting a negative regulatory function of this region. Three shelterin components (TRF1, TRF2, POT1) bind DNA and 3 components (TIN2, RAP1, TPP1) are recruited by these DNA binding factors. TRF1 activity at telomeres is regulated in part by selective ubiquitination and degradation. Ubiquitination of TRF1 is mediated by Fbx4, which binds TRF1 in the TRFH domain, via a small GTPase module. When bound to telomeres, TIN2 acts to protect TRF1 from SCF-Fbx4 mediated ubiquitination. F-box proteins act in substrate recognition as part of Skp1-Cul1-Rbx1-F- box (SCF) protein complexes. Tankyrase-mediated ADP-ribosylation releases TRF1 from telomeres, rendering them susceptible to ubiquitination and degradation, promoting telomere elongation. TIN2 also binds PIP1, which recruits POT1 to telomeres. Pssm-ID: 240667 Cd Length: 188 Bit Score: 265.70 E-value: 6.69e-85
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TINF2_N | pfam14973 | TERF1-interacting nuclear factor 2 N-terminus; This is the N-terminus of TERF1-interacting ... |
38-182 | 3.37e-61 | |||||||
TERF1-interacting nuclear factor 2 N-terminus; This is the N-terminus of TERF1-interacting nuclear factor 2. It is required for the formation of the shelterin complex. The shelterin complex is involved in the protection and maintenance of telomeres. Pssm-ID: 464415 Cd Length: 148 Bit Score: 201.74 E-value: 3.37e-61
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COG5048 | COG5048 | FOG: Zn-finger [General function prediction only]; |
298-636 | 9.58e-15 | |||||||
FOG: Zn-finger [General function prediction only]; Pssm-ID: 227381 [Multi-domain] Cd Length: 467 Bit Score: 77.43 E-value: 9.58e-15
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COG5048 | COG5048 | FOG: Zn-finger [General function prediction only]; |
230-582 | 5.96e-10 | |||||||
FOG: Zn-finger [General function prediction only]; Pssm-ID: 227381 [Multi-domain] Cd Length: 467 Bit Score: 62.02 E-value: 5.96e-10
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COG5048 | COG5048 | FOG: Zn-finger [General function prediction only]; |
476-627 | 2.93e-05 | |||||||
FOG: Zn-finger [General function prediction only]; Pssm-ID: 227381 [Multi-domain] Cd Length: 467 Bit Score: 47.00 E-value: 2.93e-05
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COG5048 | COG5048 | FOG: Zn-finger [General function prediction only]; |
378-708 | 1.26e-04 | |||||||
FOG: Zn-finger [General function prediction only]; Pssm-ID: 227381 [Multi-domain] Cd Length: 467 Bit Score: 45.07 E-value: 1.26e-04
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zf-H2C2_2 | pfam13465 | Zinc-finger double domain; |
445-470 | 2.57e-04 | |||||||
Zinc-finger double domain; Pssm-ID: 463886 [Multi-domain] Cd Length: 26 Bit Score: 38.51 E-value: 2.57e-04
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zf-H2C2_2 | pfam13465 | Zinc-finger double domain; |
315-337 | 3.04e-04 | |||||||
Zinc-finger double domain; Pssm-ID: 463886 [Multi-domain] Cd Length: 26 Bit Score: 38.51 E-value: 3.04e-04
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zf-H2C2_2 | pfam13465 | Zinc-finger double domain; |
474-498 | 3.74e-04 | |||||||
Zinc-finger double domain; Pssm-ID: 463886 [Multi-domain] Cd Length: 26 Bit Score: 38.12 E-value: 3.74e-04
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zf-H2C2_2 | pfam13465 | Zinc-finger double domain; |
340-365 | 8.86e-04 | |||||||
Zinc-finger double domain; Pssm-ID: 463886 [Multi-domain] Cd Length: 26 Bit Score: 36.97 E-value: 8.86e-04
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zf-C2H2 | pfam00096 | Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ... |
298-320 | 1.44e-03 | |||||||
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter. Pssm-ID: 395048 [Multi-domain] Cd Length: 23 Bit Score: 36.51 E-value: 1.44e-03
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zf-H2C2_2 | pfam13465 | Zinc-finger double domain; |
669-694 | 2.85e-03 | |||||||
Zinc-finger double domain; Pssm-ID: 463886 [Multi-domain] Cd Length: 26 Bit Score: 35.81 E-value: 2.85e-03
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zf-C2H2 | pfam00096 | Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ... |
326-348 | 2.89e-03 | |||||||
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter. Pssm-ID: 395048 [Multi-domain] Cd Length: 23 Bit Score: 35.74 E-value: 2.89e-03
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zf-H2C2_2 | pfam13465 | Zinc-finger double domain; |
641-666 | 5.51e-03 | |||||||
Zinc-finger double domain; Pssm-ID: 463886 [Multi-domain] Cd Length: 26 Bit Score: 34.65 E-value: 5.51e-03
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zf-H2C2_2 | pfam13465 | Zinc-finger double domain; |
613-638 | 6.32e-03 | |||||||
Zinc-finger double domain; Pssm-ID: 463886 [Multi-domain] Cd Length: 26 Bit Score: 34.65 E-value: 6.32e-03
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Blast search parameters | ||||
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