CPLM-000159

Genbank Nucleotide ID

THO complex subunit 4

Protein Synonyms/Alias

Tho4; Ally of AML-1 and LEF-1; Aly/REF export factor; REF1-I; RNA and export factor-binding protein 1; Transcriptional coactivator Aly/REF

Aly; Ref1; Refbp1; THOC4

Mus musculus (Mouse)

Position	Peptide	Type	References
80	PAPYSRPKQLPDKWQ	acetylation	[1]
85	RPKQLPDKWQHDLFD	acetylation	[1, 2]
85	RPKQLPDKWQHDLFD	ubiquitination	[3]
163	ADALKAMKQYNGVPL	acetylation	[4]
163	ADALKAMKQYNGVPL	ubiquitination	[3]
233	RGTGRNSKQQLSAEE	acetylation	[4, 5]
233	RGTGRNSKQQLSAEE	ubiquitination	[3]

[1] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
[2] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
[3] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
[4] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405]
[5] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
PLoS One. 2012;7(12):e50545. [PMID: 23236377]

Functional Description

Component of the THO subcomplex of the TREX complex. The TREX complex specifically associates with spliced mRNA and not with unspliced pre-mRNA. It is recruited to spliced mRNAs by a transcription-independent mechanism. Binds to mRNA upstream of the exon-junction complex (EJC) and is recruited in a splicing- and cap-dependent manner to a region near the 5' end of the mRNA where it functions in mRNA export. The recruitment occurs via an interaction between ALYREF/THOC4 and the cap-binding protein NCBP1. DDX39B functions as a bridge between ALYREF/THOC4 and the THO complex (By similarity).

DOMAIN 105 182 RRM.
MOD_RES 2 2 N-acetylalanine (By similarity).
MOD_RES 8 8 Phosphoserine (By similarity).
MOD_RES 50 50 Omega-N-methylated arginine (By
MOD_RES 93 93 Phosphoserine (By similarity).
MOD_RES 203 203 Dimethylated arginine; alternate (By
MOD_RES 203 203 Omega-N-methylated arginine; alternate
MOD_RES 218 218 Omega-N-methylarginine.
MOD_RES 237 237 Phosphoserine.

3D-structure; Acetylation; Alternative splicing; Chaperone; Complete proteome; Cytoplasm; Methylation; mRNA processing; mRNA splicing; mRNA transport; Nucleus; Phosphoprotein; Reference proteome; RNA-binding; Spliceosome; Transport.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
GO:0005634; C:nucleus; TAS:MGI.
GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
GO:0000166; F:nucleotide binding; IEA:InterPro.
GO:0003723; F:RNA binding; IDA:MGI.
GO:0003697; F:single-stranded DNA binding; IDA:MGI.
GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.

IPR025715; FoP_duplication.
IPR012677; Nucleotide-bd_a/b_plait.
IPR000504; RRM_dom.

PF13865; FoP_duplication
PF00076; RRM_1