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
Fms-interacting protein/Thoc5; This entry carries part of the crucial 144 N-terminal residues ...
103-463
9.83e-165
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: 476.80 E-value: 9.83e-165
Fms-interacting protein/Thoc5; This entry carries part of the crucial 144 N-terminal residues ...
103-463
9.83e-165
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: 476.80 E-value: 9.83e-165
Fms-interacting protein/Thoc5; This entry carries part of the crucial 144 N-terminal residues ...
103-463
9.83e-165
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: 476.80 E-value: 9.83e-165
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.
of the residues that compose this conserved feature have been mapped to the query sequence.
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