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Conserved domains on  [gi|148704309|gb|EDL36256|]
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Terf1 (TRF1)-interacting nuclear factor 2, isoform CRA_a, partial [Mus musculus]

Protein Classification

TIN2_N domain-containing protein( domain architecture ID 11237162)

TIN2_N domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TINF2_N pfam14973
TERF1-interacting nuclear factor 2 N-terminus; This is the N-terminus of TERF1-interacting ...
 81-220 1.03e-58

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: 183.25  E-value: 1.03e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148704309   81 WLVVRRRRVEHFPKVVEFLQSLRAAAPGLVCYRHHERLCMSLKAKVVVELILQARPwdQVLNALKHHFP-----AESRTT 155
Cdd:pfam14973   1 WQVVQQRDVEHYGKVEEFVSLVTEAVPGLLSYRHHAQLIMGLRAKLILELCRGERP--QDLKAIQSHLDrlgptVSPKAT 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148704309  156 KE-DRKLLEARENFCLLVKHLSEDP---PSSLQE-LEQDYGESFLVAMEKLLFEYLCQLEKALPPVRAQE 220
Cdd:pfam14973  79 KQdDVKVEEAQENFLQLVQSLLEDPverEHFFQEvFPVEYGPKFDAALEKLVWEFLSRLEQLLPVPDLQQ 148
 
Name Accession Description Interval E-value
TINF2_N pfam14973
TERF1-interacting nuclear factor 2 N-terminus; This is the N-terminus of TERF1-interacting ...
 81-220 1.03e-58

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: 183.25  E-value: 1.03e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148704309   81 WLVVRRRRVEHFPKVVEFLQSLRAAAPGLVCYRHHERLCMSLKAKVVVELILQARPwdQVLNALKHHFP-----AESRTT 155
Cdd:pfam14973   1 WQVVQQRDVEHYGKVEEFVSLVTEAVPGLLSYRHHAQLIMGLRAKLILELCRGERP--QDLKAIQSHLDrlgptVSPKAT 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148704309  156 KE-DRKLLEARENFCLLVKHLSEDP---PSSLQE-LEQDYGESFLVAMEKLLFEYLCQLEKALPPVRAQE 220
Cdd:pfam14973  79 KQdDVKVEEAQENFLQLVQSLLEDPverEHFFQEvFPVEYGPKFDAALEKLVWEFLSRLEQLLPVPDLQQ 148
TIN2_N cd11657
N-terminal domain of TRF-interacting nuclear factor 2; shelterin complex protein of telomeres; ...
 70-231 1.07e-46

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: 153.99  E-value: 1.07e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148704309  70 PASLRFAAAASWLVVRRRRVEHFPKVVEFLQSLRAAAPGLVCYRHHERLCMSLKAKVVVELILqaRPWDQVLNALKHHFP 149
Cdd:cd11657    1 VPPLRLVSAAMWQVVQRRDVKHYGKVEEFVSLVTETVPELLTFRQRAKLILGLRARVILELCR--NEKAADLAALNPHLP 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148704309 150 -----AESRTTKEDRKLLEARENFCLLVKHLSEDPPSS----LQELEQDYGESFLVAMEKLLFEYLCQLEKALPPVRAQE 220
Cdd:cd11657   79 rllppYPNKCQREDALMEEPQLNFLQLVQSLLKDPEERehffQEVFPVEYGEEFDQALEKLLWEFLSRLEKLLPVPDLKQ 158

                        170
                 ....*....|.
gi 148704309 221 LQDALSWSQPG 231
Cdd:cd11657  159 TVSWLSTSPSV 169
 
Name Accession Description Interval E-value
TINF2_N pfam14973
TERF1-interacting nuclear factor 2 N-terminus; This is the N-terminus of TERF1-interacting ...
 81-220 1.03e-58

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: 183.25  E-value: 1.03e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148704309   81 WLVVRRRRVEHFPKVVEFLQSLRAAAPGLVCYRHHERLCMSLKAKVVVELILQARPwdQVLNALKHHFP-----AESRTT 155
Cdd:pfam14973   1 WQVVQQRDVEHYGKVEEFVSLVTEAVPGLLSYRHHAQLIMGLRAKLILELCRGERP--QDLKAIQSHLDrlgptVSPKAT 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148704309  156 KE-DRKLLEARENFCLLVKHLSEDP---PSSLQE-LEQDYGESFLVAMEKLLFEYLCQLEKALPPVRAQE 220
Cdd:pfam14973  79 KQdDVKVEEAQENFLQLVQSLLEDPverEHFFQEvFPVEYGPKFDAALEKLVWEFLSRLEQLLPVPDLQQ 148
TIN2_N cd11657
N-terminal domain of TRF-interacting nuclear factor 2; shelterin complex protein of telomeres; ...
 70-231 1.07e-46

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: 153.99  E-value: 1.07e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148704309  70 PASLRFAAAASWLVVRRRRVEHFPKVVEFLQSLRAAAPGLVCYRHHERLCMSLKAKVVVELILqaRPWDQVLNALKHHFP 149
Cdd:cd11657    1 VPPLRLVSAAMWQVVQRRDVKHYGKVEEFVSLVTETVPELLTFRQRAKLILGLRARVILELCR--NEKAADLAALNPHLP 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148704309 150 -----AESRTTKEDRKLLEARENFCLLVKHLSEDPPSS----LQELEQDYGESFLVAMEKLLFEYLCQLEKALPPVRAQE 220
Cdd:cd11657   79 rllppYPNKCQREDALMEEPQLNFLQLVQSLLKDPEERehffQEVFPVEYGEEFDQALEKLLWEFLSRLEKLLPVPDLKQ 158

                        170
                 ....*....|.
gi 148704309 221 LQDALSWSQPG 231
Cdd:cd11657  159 TVSWLSTSPSV 169
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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