UniProt Accession

 THOC2_HUMAN; Q8NI27; A6NM50; Q5JZ12; Q6IN92; Q9H8I6 

Genbank Protein ID

 AL030996; AL023575; Z82901; Z82901; AL023575; AL030996; AL023575; AL030996; Z82901; BC072400; AF441770; AK023659; BX648654 

Genbank Nucleotide ID

 CAI42271.2; CAI42271.2; CAI42271.2; CAI42864.2; CAI42864.2; CAI42864.2; CAO03594.1; CAO03594.1; CAO03594.1; AAH72400.1; AAM28436.1; BAB14630.1; CAE46196.1 

Protein Name

 THO complex subunit 2 

Protein Synonyms/Alias

 Tho2; hTREX120 

Gene Name

 THOC2 

Gene Synonyms/Alias

 CXorf3 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
14	VVPAEWIKNWEKSGR	ubiquitination	[1]
18	EWIKNWEKSGRGEFL	ubiquitination	[1]
139	LESLGLIKQSQQFNQ	ubiquitination	[1, 2, 3]
147	QSQQFNQKSVKIKTK	ubiquitination	[1]
158	IKTKLFYKQQKFNLL	ubiquitination	[1]
307	KREIAEAKQIVRKLT	ubiquitination	[1, 4]
345	EKPPDNQKLGLLEAL	ubiquitination	[5, 6]
415	PVNALQNKRAPKQAE	ubiquitination	[1]
457	AKVVRIGKSFMKEFQ	ubiquitination	[1]
528	YRLYGQWKNETYNSH	ubiquitination	[1]
562	RLTKENVKPSGRQIG	ubiquitination	[7]
730	KKSSQRLKDALLDHD	ubiquitination	[1]
761	IFQEGGEKHLKLVGK	ubiquitination	[1]
829	YAHHISSKYDELKKS	acetylation	[8]
928	PNKKKKEKERCTALQ	acetylation	[9]
937	RCTALQDKLLEEEKK	ubiquitination	[1]
960	LQRLKLEKDNWLLAK	ubiquitination	[1]
967	KDNWLLAKSTKNETI	ubiquitination	[1]
1007	VELVHQQKTPNFSTL	ubiquitination	[1]
1062	SDRATYEKECGNYPG	ubiquitination	[1]
1084	TGFDGGNKADQLDYE	ubiquitination	[1, 3]
1136	KILPWYPKVLNLGQA	ubiquitination	[1]

Reference

 [1] 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]
 [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] 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]
 [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] 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]
 [6] 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]
 [7] 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]
 [8] 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]
 [9] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786] 

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. 

Sequence Annotation

 MOTIF 923 928 Nuclear localization signal (Potential).
 MOD_RES 1385 1385 Phosphothreonine.
 MOD_RES 1393 1393 Phosphoserine.
 MOD_RES 1417 1417 Phosphoserine.
 MOD_RES 1443 1443 Phosphothreonine.
 MOD_RES 1486 1486 Phosphoserine.  

Keyword

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

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 1593 AA 

Protein Sequence

Gene Ontology

 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. 

Interpro

 IPR021418; THO_THOC2_C.
 IPR021726; THO_THOC2_N. 

Pfam

 PF11262; Tho2
 PF11732; Thoc2 

SMART

  

PROSITE

  

PRINTS