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Conserved domains on  [gi|1276317594|ref|NP_001344801|]
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activating signal cointegrator 1 isoform 1 [Mus musculus]

Protein Classification

activating signal cointegrator 1( domain architecture ID 10533281)

activating signal cointegrator 1 (ASC-1) acts as transcription coactivator which associates with nuclear receptors, transcriptional coactivators including EP300, CREBBP and NCOA1, and basal transcription factors like TBP and TFIIA to facilitate nuclear receptors-mediated transcription

Gene Symbol:  TRIP4
Gene Ontology:  GO:0008270|GO:0003713|GO:0099053
PubMed:  16322048|12665246

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ASCH_ASC-1_like cd06554
ASC-1 homology domain, ASC-1-like subfamily. The ASCH domain, a small beta-barrel domain found ...
 434-547 5.94e-55

ASC-1 homology domain, ASC-1-like subfamily. The ASCH domain, a small beta-barrel domain found in all three kingdoms of life, resembles the RNA-binding PUA domain and may also interact with RNA. ASCH has been proposed to function as an RNA-binding domain during coactivation, RNA-processing and the regulation of prokaryotic translation. The domain has been named after the ASC-1 protein, the activating signal cointegrator 1 or thyroid hormone receptor interactor protein 4 (TRIP4). ASC-1 is conserved in many eukaryotes and has been suggested to participate in a protein complex that interacts with RNA. It has been shown that ASC-1 mediates the interaction between various transciption factors and the basal transcriptional machinery.


:

Pssm-ID: 119346  Cd Length: 113  Bit Score: 181.38  E-value: 5.94e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317594 434 GWCLSMHQPWASLLVRGIKRVEGRSWYTPHRGRLWIAATGKRPSPQEVSELQATYRLLRGKDVEFPNDYPSGCLLGCVDL 513
Cdd:cd06554     1 MKALSIHQPWASLIVRGIKRIEGRSWATNYRGRLWIHASAKLPTKLDIEEVEEFYRILYKLDIELPTGYPTGCLLGCVDV 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1276317594 514 IDCLSQKQFQEQFPDISQEsDSSFVFICKNPQEM 547
Cdd:cd06554    81 VDCLTQEEYREQYPWGKSE-ESPYAWVLANPRPL 113
zf-C2HC5 pfam06221
Putative zinc finger motif, C2HC5-type; This zinc finger appears to be common in activating ...
 168-216 1.20e-13

Putative zinc finger motif, C2HC5-type; This zinc finger appears to be common in activating signal cointegrator 1/thyroid receptor interacting protein 4.


:

Pssm-ID: 428833  Cd Length: 54  Bit Score: 65.37  E-value: 1.20e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1276317594 168 RHPCDCLGQKHKLIN---NCLVCGRIVCEQEG-SGPCLFCGS-LVCTNEEQDIL 216
Cdd:pfam06221   1 RRKCNCQARRHPLFEaapNCLNCGKIICAKEGlHGPCSFCGSpLLSPEERQELI 54
 
Name Accession Description Interval E-value
ASCH_ASC-1_like cd06554
ASC-1 homology domain, ASC-1-like subfamily. The ASCH domain, a small beta-barrel domain found ...
 434-547 5.94e-55

ASC-1 homology domain, ASC-1-like subfamily. The ASCH domain, a small beta-barrel domain found in all three kingdoms of life, resembles the RNA-binding PUA domain and may also interact with RNA. ASCH has been proposed to function as an RNA-binding domain during coactivation, RNA-processing and the regulation of prokaryotic translation. The domain has been named after the ASC-1 protein, the activating signal cointegrator 1 or thyroid hormone receptor interactor protein 4 (TRIP4). ASC-1 is conserved in many eukaryotes and has been suggested to participate in a protein complex that interacts with RNA. It has been shown that ASC-1 mediates the interaction between various transciption factors and the basal transcriptional machinery.


Pssm-ID: 119346  Cd Length: 113  Bit Score: 181.38  E-value: 5.94e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317594 434 GWCLSMHQPWASLLVRGIKRVEGRSWYTPHRGRLWIAATGKRPSPQEVSELQATYRLLRGKDVEFPNDYPSGCLLGCVDL 513
Cdd:cd06554     1 MKALSIHQPWASLIVRGIKRIEGRSWATNYRGRLWIHASAKLPTKLDIEEVEEFYRILYKLDIELPTGYPTGCLLGCVDV 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1276317594 514 IDCLSQKQFQEQFPDISQEsDSSFVFICKNPQEM 547
Cdd:cd06554    81 VDCLTQEEYREQYPWGKSE-ESPYAWVLANPRPL 113
zf-C2HC5 pfam06221
Putative zinc finger motif, C2HC5-type; This zinc finger appears to be common in activating ...
 168-216 1.20e-13

Putative zinc finger motif, C2HC5-type; This zinc finger appears to be common in activating signal cointegrator 1/thyroid receptor interacting protein 4.


Pssm-ID: 428833  Cd Length: 54  Bit Score: 65.37  E-value: 1.20e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1276317594 168 RHPCDCLGQKHKLIN---NCLVCGRIVCEQEG-SGPCLFCGS-LVCTNEEQDIL 216
Cdd:pfam06221   1 RRKCNCQARRHPLFEaapNCLNCGKIICAKEGlHGPCSFCGSpLLSPEERQELI 54
ASCH pfam04266
ASCH domain; The ASCH domain adopts a beta-barrel fold similar to the pfam01472 domain. It is ...
 437-474 1.59e-08

ASCH domain; The ASCH domain adopts a beta-barrel fold similar to the pfam01472 domain. It is thought to function as an RNA-binding domain during coactivation, RNA-processing and possibly during prokaryotic translation regulation.


Pssm-ID: 398105  Cd Length: 102  Bit Score: 52.38  E-value: 1.59e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1276317594 437 LSMHQPWASLLVRGIKRVEGRSWYTPHR--GRLWIAATGK 474
Cdd:pfam04266   1 LSFGQEYADLILSGKKTAEIRVWDEPLPvvGDLLILLDST 40
ASCH smart01022
The ASCH domain adopts a beta-barrel fold similar to that of the PUA domain; It is thought to ...
 437-531 1.17e-06

The ASCH domain adopts a beta-barrel fold similar to that of the PUA domain; It is thought to function as an RNA-binding domain during coactivation, RNA-processing and possibly during prokaryotic translation regulation.


Pssm-ID: 214979  Cd Length: 99  Bit Score: 46.95  E-value: 1.17e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317594  437 LSMHQPWASLLVRGIKRVEGRSWYTPH--RGRLWIAATGKRPSPQEVSELQATYRLLRGKDVEFpndypsGCLLGCVDLi 514
Cdd:smart01022   1 LSFKDELADLILSGKKTATIRLENEPLpkVGDLLIVLDGEGKPVCVIEVTSVEIIPFKDVTAEH------AYLEGEGSL- 73

                           90
                   ....*....|....*..
gi 1276317594  515 DCLsQKQFQEQFPDISQ 531
Cdd:smart01022  74 EEW-RKVHKEFYPEDME 89
 
Name Accession Description Interval E-value
ASCH_ASC-1_like cd06554
ASC-1 homology domain, ASC-1-like subfamily. The ASCH domain, a small beta-barrel domain found ...
 434-547 5.94e-55

ASC-1 homology domain, ASC-1-like subfamily. The ASCH domain, a small beta-barrel domain found in all three kingdoms of life, resembles the RNA-binding PUA domain and may also interact with RNA. ASCH has been proposed to function as an RNA-binding domain during coactivation, RNA-processing and the regulation of prokaryotic translation. The domain has been named after the ASC-1 protein, the activating signal cointegrator 1 or thyroid hormone receptor interactor protein 4 (TRIP4). ASC-1 is conserved in many eukaryotes and has been suggested to participate in a protein complex that interacts with RNA. It has been shown that ASC-1 mediates the interaction between various transciption factors and the basal transcriptional machinery.


Pssm-ID: 119346  Cd Length: 113  Bit Score: 181.38  E-value: 5.94e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317594 434 GWCLSMHQPWASLLVRGIKRVEGRSWYTPHRGRLWIAATGKRPSPQEVSELQATYRLLRGKDVEFPNDYPSGCLLGCVDL 513
Cdd:cd06554     1 MKALSIHQPWASLIVRGIKRIEGRSWATNYRGRLWIHASAKLPTKLDIEEVEEFYRILYKLDIELPTGYPTGCLLGCVDV 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1276317594 514 IDCLSQKQFQEQFPDISQEsDSSFVFICKNPQEM 547
Cdd:cd06554    81 VDCLTQEEYREQYPWGKSE-ESPYAWVLANPRPL 113
zf-C2HC5 pfam06221
Putative zinc finger motif, C2HC5-type; This zinc finger appears to be common in activating ...
 168-216 1.20e-13

Putative zinc finger motif, C2HC5-type; This zinc finger appears to be common in activating signal cointegrator 1/thyroid receptor interacting protein 4.


Pssm-ID: 428833  Cd Length: 54  Bit Score: 65.37  E-value: 1.20e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1276317594 168 RHPCDCLGQKHKLIN---NCLVCGRIVCEQEG-SGPCLFCGS-LVCTNEEQDIL 216
Cdd:pfam06221   1 RRKCNCQARRHPLFEaapNCLNCGKIICAKEGlHGPCSFCGSpLLSPEERQELI 54
ASCH pfam04266
ASCH domain; The ASCH domain adopts a beta-barrel fold similar to the pfam01472 domain. It is ...
 437-474 1.59e-08

ASCH domain; The ASCH domain adopts a beta-barrel fold similar to the pfam01472 domain. It is thought to function as an RNA-binding domain during coactivation, RNA-processing and possibly during prokaryotic translation regulation.


Pssm-ID: 398105  Cd Length: 102  Bit Score: 52.38  E-value: 1.59e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1276317594 437 LSMHQPWASLLVRGIKRVEGRSWYTPHR--GRLWIAATGK 474
Cdd:pfam04266   1 LSFGQEYADLILSGKKTAEIRVWDEPLPvvGDLLILLDST 40
ASCH smart01022
The ASCH domain adopts a beta-barrel fold similar to that of the PUA domain; It is thought to ...
 437-531 1.17e-06

The ASCH domain adopts a beta-barrel fold similar to that of the PUA domain; It is thought to function as an RNA-binding domain during coactivation, RNA-processing and possibly during prokaryotic translation regulation.


Pssm-ID: 214979  Cd Length: 99  Bit Score: 46.95  E-value: 1.17e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317594  437 LSMHQPWASLLVRGIKRVEGRSWYTPH--RGRLWIAATGKRPSPQEVSELQATYRLLRGKDVEFpndypsGCLLGCVDLi 514
Cdd:smart01022   1 LSFKDELADLILSGKKTATIRLENEPLpkVGDLLIVLDGEGKPVCVIEVTSVEIIPFKDVTAEH------AYLEGEGSL- 73

                           90
                   ....*....|....*..
gi 1276317594  515 DCLsQKQFQEQFPDISQ 531
Cdd:smart01022  74 EEW-RKVHKEFYPEDME 89
 
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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