CPLM-019355

Genbank Nucleotide ID

THO complex subunit 3

Protein Synonyms/Alias

Tho3; TEX1 homolog; hTREX45

Homo sapiens (Human)

Position	Peptide	Type	References
77	LASGSFDKTASVFLL	ubiquitination	[1, 2, 3, 4, 5]
86	ASVFLLEKDRLVKEN	ubiquitination	[2, 3, 4, 6]
91	LEKDRLVKENNYRGH	ubiquitination	[2, 3]
133	IWDVRTTKCIATVNT	ubiquitination	[3]
171	VVTFIDAKTHRSKAE	ubiquitination	[1, 5, 7]
176	DAKTHRSKAEEQFKF	ubiquitination	[2]
332	ACDDKDGKYDSSREA	ubiquitination	[6]
343	SREAGTVKLFGLPND	ubiquitination	[2, 3, 4, 6]

[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] Systematic and quantitative assessment of the ubiquitin-modified proteome.
Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
[3] 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]
[4] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
[5] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
Chen Z, Zhou Y, Song J, Zhang Z.
Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
[6] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
[7] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]

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.

REPEAT 53 94 WD 1.
REPEAT 97 137 WD 2.
REPEAT 139 178 WD 3.
REPEAT 180 221 WD 4.
REPEAT 222 261 WD 5.
REPEAT 264 303 WD 6.

Complete proteome; mRNA processing; mRNA splicing; mRNA transport; Nucleus; Reference proteome; Repeat; RNA-binding; Transport; WD repeat.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0000346; C: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.

IPR020472; G-protein_beta_WD-40_rep.
IPR011659; PD40.
IPR015943; WD40/YVTN_repeat-like_dom.
IPR001680; WD40_repeat.
IPR017986; WD40_repeat_dom.

PF07676; PD40
PF00400; WD40

PS00678; WD_REPEATS_1
PS50082; WD_REPEATS_2
PS50294; WD_REPEATS_REGION

PR00320; GPROTEINBRPT.