CPLM-014926

Genbank Nucleotide ID

THO complex subunit 7 homolog

Protein Synonyms/Alias

Functional spliceosome-associated protein 24; fSAP24; Ngg1-interacting factor 3-like protein 1-binding protein 1; NIF3L1-binding protein 1; hTREX30

Homo sapiens (Human)

Position	Peptide	Type	References
32	RRINLLVKSFIKWCN	ubiquitination	[1, 2]
36	LLVKSFIKWCNSGSQ	acetylation	[3, 4]
36	LLVKSFIKWCNSGSQ	ubiquitination	[2, 4, 5]
83	REMENYEKIYKEIEC	ubiquitination	[4]
86	ENYEKIYKEIECSIA	acetylation	[4]
86	ENYEKIYKEIECSIA	ubiquitination	[4, 5]
98	SIAGAHEKIAECKKQ	ubiquitination	[5]
110	KKQILQAKRIRKNRQ	ubiquitination	[5]
114	LQAKRIRKNRQEYDA	ubiquitination	[5]
144	KELEALGKELEHLSH	ubiquitination	[5]
153	LEHLSHIKESVEDKL	ubiquitination	[5]
159	IKESVEDKLELRRKQ	ubiquitination	[4, 5]

[1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
[2] Global identification of modular cullin-RING ligase substrates.
Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
[3] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
[4] Integrated proteomic analysis of post-translational modifications by serial enrichment.
Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
[5] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]

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. The TREX complex is essential for the export of Kaposi's sarcoma-associated herpesvirus (KSHV) intronless mRNAs and infectious virus production. The recruitment of the TREX complex to the intronless viral mRNA occurs via an interaction between KSHV ORF57 protein and ALYREF/THOC4.

REGION 50 137 Interaction with THOC5.
REGION 105 204 Interaction with NIF3L1.
MOD_RES 2 2 N-acetylglycine.
MOD_RES 36 36 N6-acetyllysine.

Acetylation; Coiled coil; Complete proteome; Cytoplasm; mRNA processing; mRNA splicing; mRNA transport; Nucleus; Reference proteome; RNA-binding; Transport.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005737; C:cytoplasm; IDA:HPA.
GO:0000445; C:THO complex part of transcription export complex; IDA:UniProtKB.
GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
GO:0046784; P:intronless viral mRNA export from host nucleus; IDA:UniProtKB.
GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.

IPR018018; THOC7.
IPR008501; THOC7/Mft1.