THO complex subunit 5 homolog isoform X3 [Homo sapiens]
THO complex subunit 5( domain architecture ID 582274)
THO complex subunit 5 is a component of the THO subcomplex of the TREX complex which is thought to couple mRNA transcription, processing and nuclear export, and which specifically associates with spliced mRNA and not with unspliced pre-mRNA
List of domain hits
Name | Accession | Description | Interval | E-value | |||
FmiP_Thoc5 super family | cl24222 | Fms-interacting protein/Thoc5; This entry carries part of the crucial 144 N-terminal residues ... |
1-113 | 1.74e-45 | |||
Fms-interacting protein/Thoc5; This entry carries part of the crucial 144 N-terminal residues of the FmiP (Fms interacting protein). A member of the THO (suppressors of the transcriptional defects of hpr1delta by overexpression) complex which is a subcomplex of the transcription/export (TREX) complex. It is essential for the binding of the protein to the cytoplasmic domain of activated Fms-molecules in M-CSF induced haematopoietic differentiation of macrophages. Fmip is also known as THOC5 (THO complex subunit 5) a 683 amino acids long protein which contains a nuclear localization sequence (NLS), a leucine zipper and a PEST like sequence (aa. 303-319) that carries three ataxia-telangiectasia mutated (ATM) kinase specific phosphorylation sites. The C-terminus contains a THOC1 binding site. The level of FMIP/Thoc5 expression might form a threshold that determines whether cells differentiate into macrophages or into granulocytes. The actual alignment was detected with superfamily member pfam09766: Pssm-ID: 462889 Cd Length: 347 Bit Score: 158.24 E-value: 1.74e-45
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Name | Accession | Description | Interval | E-value | |||
FmiP_Thoc5 | pfam09766 | Fms-interacting protein/Thoc5; This entry carries part of the crucial 144 N-terminal residues ... |
1-113 | 1.74e-45 | |||
Fms-interacting protein/Thoc5; This entry carries part of the crucial 144 N-terminal residues of the FmiP (Fms interacting protein). A member of the THO (suppressors of the transcriptional defects of hpr1delta by overexpression) complex which is a subcomplex of the transcription/export (TREX) complex. It is essential for the binding of the protein to the cytoplasmic domain of activated Fms-molecules in M-CSF induced haematopoietic differentiation of macrophages. Fmip is also known as THOC5 (THO complex subunit 5) a 683 amino acids long protein which contains a nuclear localization sequence (NLS), a leucine zipper and a PEST like sequence (aa. 303-319) that carries three ataxia-telangiectasia mutated (ATM) kinase specific phosphorylation sites. The C-terminus contains a THOC1 binding site. The level of FMIP/Thoc5 expression might form a threshold that determines whether cells differentiate into macrophages or into granulocytes. Pssm-ID: 462889 Cd Length: 347 Bit Score: 158.24 E-value: 1.74e-45
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Name | Accession | Description | Interval | E-value | |||
FmiP_Thoc5 | pfam09766 | Fms-interacting protein/Thoc5; This entry carries part of the crucial 144 N-terminal residues ... |
1-113 | 1.74e-45 | |||
Fms-interacting protein/Thoc5; This entry carries part of the crucial 144 N-terminal residues of the FmiP (Fms interacting protein). A member of the THO (suppressors of the transcriptional defects of hpr1delta by overexpression) complex which is a subcomplex of the transcription/export (TREX) complex. It is essential for the binding of the protein to the cytoplasmic domain of activated Fms-molecules in M-CSF induced haematopoietic differentiation of macrophages. Fmip is also known as THOC5 (THO complex subunit 5) a 683 amino acids long protein which contains a nuclear localization sequence (NLS), a leucine zipper and a PEST like sequence (aa. 303-319) that carries three ataxia-telangiectasia mutated (ATM) kinase specific phosphorylation sites. The C-terminus contains a THOC1 binding site. The level of FMIP/Thoc5 expression might form a threshold that determines whether cells differentiate into macrophages or into granulocytes. Pssm-ID: 462889 Cd Length: 347 Bit Score: 158.24 E-value: 1.74e-45
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Blast search parameters | ||||
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