ID THOC5_HUMAN Reviewed; 683 AA.
AC Q13769; O60839; Q9UPZ5;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 2.
DT 24-JUL-2024, entry version 178.
DE RecName: Full=THO complex subunit 5 homolog;
DE AltName: Full=Functional spliceosome-associated protein 79;
DE Short=fSAP79;
DE AltName: Full=NF2/meningioma region protein pK1.3;
DE AltName: Full=Placental protein 39.2;
DE Short=PP39.2;
DE AltName: Full=hTREX90;
GN Name=THOC5; Synonyms=C22orf19, KIAA0983;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ILE-525 AND ILE-579.
RC TISSUE=Fetus;
RX PubMed=8242058; DOI=10.1093/hmg/2.9.1361;
RA Xie Y.G., Han F.Y., Peyrard M., Ruttledge M.H., Fransson I., deJong P.,
RA Collins J., Dunham I., Nordenskjold M., Dumanski J.P.;
RT "Cloning of a novel, anonymous gene from a megabase-range YAC and cosmid
RT contig in the neurofibromatosis type 2/meningioma region on human
RT chromosome 22q12.";
RL Hum. Mol. Genet. 2:1361-1368(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ILE-525.
RC TISSUE=Brain;
RX PubMed=10231032; DOI=10.1093/dnares/6.1.63;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:63-70(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS ILE-525 AND ILE-579.
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS ILE-525 AND ILE-579.
RC TISSUE=Colon;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 548-650.
RC TISSUE=Placenta;
RA Page N.M., Butlin D.J., Manyonda I., Bicknell A.B., Lowry P.J.;
RT "Differential expression of placental genes.";
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP IDENTIFICATION IN THE TREX COMPLEX, FUNCTION OF THE TREX COMPLEX, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15833825; DOI=10.1158/0008-5472.can-04-3624;
RA Guo S., Hakimi M.A., Baillat D., Chen X., Farber M.J., Klein-Szanto A.J.,
RA Cooch N.S., Godwin A.K., Shiekhattar R.;
RT "Linking transcriptional elongation and messenger RNA export to metastatic
RT breast cancers.";
RL Cancer Res. 65:3011-3016(2005).
RN [8]
RP IDENTIFICATION IN THE THO AND TREX COMPLEX, FUNCTION OF THE TREX COMPLEX,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15998806; DOI=10.1101/gad.1302205;
RA Masuda S., Das R., Cheng H., Hurt E., Dorman N., Reed R.;
RT "Recruitment of the human TREX complex to mRNA during splicing.";
RL Genes Dev. 19:1512-1517(2005).
RN [9]
RP FUNCTION OF THE TREX COMPLEX.
RX PubMed=17190602; DOI=10.1016/j.cell.2006.10.044;
RA Cheng H., Dufu K., Lee C.-S., Hsu J.L., Dias A., Reed R.;
RT "Human mRNA export machinery recruited to the 5' end of mRNA.";
RL Cell 127:1389-1400(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-307; SER-312 AND SER-314, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [11]
RP PHOSPHORYLATION AT TYR-225, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18373705; DOI=10.1111/j.1365-2141.2008.07090.x;
RA Pierce A., Carney L., Hamza H.G., Griffiths J.R., Zhang L., Whetton B.A.,
RA Gonzalez Sanchez M.B., Tamura T., Sternberg D., Whetton A.D.;
RT "THOC5 spliceosome protein: a target for leukaemogenic tyrosine kinases
RT that affects inositol lipid turnover.";
RL Br. J. Haematol. 141:641-650(2008).
RN [12]
RP FUNCTION OF THE TREX COMPLEX.
RX PubMed=18974867; DOI=10.1371/journal.ppat.1000194;
RA Boyne J.R., Colgan K.J., Whitehouse A.;
RT "Recruitment of the complete hTREX complex is required for Kaposi's
RT sarcoma-associated herpesvirus intronless mRNA nuclear export and virus
RT replication.";
RL PLoS Pathog. 4:E1000194-E1000194(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-307; SER-312 AND SER-314, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [15]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH ALYREF/THOC4 AND NXF1.
RX PubMed=19165146; DOI=10.1038/emboj.2009.5;
RA Katahira J., Inoue H., Hurt E., Yoneda Y.;
RT "Adaptor Aly and co-adaptor Thoc5 function in the Tap-p15-mediated nuclear
RT export of HSP70 mRNA.";
RL EMBO J. 28:556-567(2009).
RN [16]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH THOC7.
RX PubMed=19059247; DOI=10.1016/j.febslet.2008.11.024;
RA El Bounkari O., Guria A., Klebba-Faerber S., Claussen M., Pieler T.,
RA Griffiths J.R., Whetton A.D., Koch A., Tamura T.;
RT "Nuclear localization of the pre-mRNA associating protein THOC7 depends
RT upon its direct interaction with Fms tyrosine kinase interacting protein
RT (FMIP).";
RL FEBS Lett. 583:13-18(2009).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-307; SER-312 AND SER-314, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-307; SER-312; SER-314 AND
RP THR-328, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [20]
RP FUNCTION.
RX PubMed=22144908; DOI=10.1371/journal.pgen.1002386;
RA Dominguez-Sanchez M.S., Barroso S., Gomez-Gonzalez B., Luna R.,
RA Aguilera A.;
RT "Genome instability and transcription elongation impairment in human cells
RT depleted of THO/TREX.";
RL PLoS Genet. 7:E1002386-E1002386(2011).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-307; SER-312 AND SER-314, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [22]
RP FUNCTION.
RX PubMed=22893130; DOI=10.1038/ncomms2005;
RA Viphakone N., Hautbergue G.M., Walsh M., Chang C.T., Holland A.,
RA Folco E.G., Reed R., Wilson S.A.;
RT "TREX exposes the RNA-binding domain of Nxf1 to enable mRNA export.";
RL Nat. Commun. 3:1006-1006(2012).
RN [23]
RP ERRATUM OF PUBMED:22893130.
RX DOI=10.1038/ncomms3377;
RA Viphakone N., Hautbergue G.M., Walsh M., Chang C.T., Holland A.,
RA Folco E.G., Reed R., Wilson S.A.;
RL Nat. Commun. 4:2377-2377(2013).
RN [24]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [25]
RP INTERACTION WITH NXF1.
RX PubMed=23299939; DOI=10.1038/emboj.2012.342;
RA Chang C.T., Hautbergue G.M., Walsh M.J., Viphakone N., van Dijk T.B.,
RA Philipsen S., Wilson S.A.;
RT "Chtop is a component of the dynamic TREX mRNA export complex.";
RL EMBO J. 32:473-486(2013).
RN [26]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-312; SER-314 AND THR-328, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [27]
RP PHOSPHORYLATION AT TYR-225 BY SRC, MUTAGENESIS OF TYR-225, AND RNA-BINDING.
RX PubMed=23032722; DOI=10.1038/leu.2012.283;
RA Griaud F., Pierce A., Gonzalez Sanchez M.B., Scott M., Abraham S.A.,
RA Holyoake T.L., Tran D.D., Tamura T., Whetton A.D.;
RT "A pathway from leukemogenic oncogenes and stem cell chemokines to RNA
RT processing via THOC5.";
RL Leukemia 27:932-940(2013).
RN [28]
RP FUNCTION, AND INTERACTION WITH CPSF6.
RX PubMed=23685434; DOI=10.1093/nar/gkt414;
RA Katahira J., Okuzaki D., Inoue H., Yoneda Y., Maehara K., Ohkawa Y.;
RT "Human TREX component Thoc5 affects alternative polyadenylation site choice
RT by recruiting mammalian cleavage factor I.";
RL Nucleic Acids Res. 41:7060-7072(2013).
RN [29]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-307; SER-312; SER-314 AND
RP THR-328, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [30]
RP INTERACTION WITH LUZP4.
RX PubMed=25662211; DOI=10.1093/nar/gkv070;
RA Viphakone N., Cumberbatch M.G., Livingstone M.J., Heath P.R., Dickman M.J.,
RA Catto J.W., Wilson S.A.;
RT "Luzp4 defines a new mRNA export pathway in cancer cells.";
RL Nucleic Acids Res. 43:2353-2366(2015).
RN [31]
RP INTERACTION WITH NCBP3.
RX PubMed=26382858; DOI=10.1038/ncomms9192;
RA Gebhardt A., Habjan M., Benda C., Meiler A., Haas D.A., Hein M.Y., Mann A.,
RA Mann M., Habermann B., Pichlmair A.;
RT "mRNA export through an additional cap-binding complex consisting of NCBP1
RT and NCBP3.";
RL Nat. Commun. 6:8192-8192(2015).
RN [32]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-153, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [33]
RP VARIANTS [LARGE SCALE ANALYSIS] LYS-380 AND SER-499.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Acts as a component of the THO subcomplex of the TREX complex
CC which is thought to couple mRNA transcription, processing and nuclear
CC export, and which specifically associates with spliced mRNA and not
CC with unspliced pre-mRNA. TREX is recruited to spliced mRNAs by a
CC transcription-independent mechanism, binds to mRNA upstream of the
CC exon-junction complex (EJC) and is recruited in a splicing- and cap-
CC dependent manner to a region near the 5' end of the mRNA where it
CC functions in mRNA export to the cytoplasm via the TAP/NFX1 pathway. The
CC TREX complex is essential for the export of Kaposi's sarcoma-associated
CC herpesvirus (KSHV) intronless mRNAs and infectious virus production.
CC THOC5 in conjunction with ALYREF/THOC4 functions in NXF1-NXT1 mediated
CC nuclear export of HSP70 mRNA; both proteins enhance the RNA binding
CC activity of NXF1 and are required for NXF1 localization to the nuclear
CC rim. Involved in transcription elongation and genome stability.
CC Involved in alternative polyadenylation site choice by recruiting CPSF6
CC to 5' region of target genes; probably mediates association of the TREX
CC and CFIm complexes.
CC -!- FUNCTION: Regulates the expression of myeloid transcription factors
CC CEBPA, CEBPB and GAB2 by enhancing the levels of phosphatidylinositol
CC 3,4,5-trisphosphate. May be involved in the differentiation of
CC granulocytes and adipocytes. Essential for hematopoietic primitive cell
CC survival and plays an integral role in monocytic development.
CC -!- SUBUNIT: Interacts with phosphorylated CSF1R (By similarity). Component
CC of the THO complex, which is composed of THOC1, THOC2, THOC3, THOC5,
CC THOC6 and THOC7; together with at least ALYREF/THOC4, DDX39B,
CC SARNP/CIP29 and CHTOP, THO forms the transcription/export (TREX)
CC complex which seems to have a dynamic structure involving ATP-dependent
CC remodeling. Interacts with ALYREF/THOC4, and THOC7. Interacts (via N-
CC terminus) with the NTF2 domain of NXF1. Forms a complex with CEBPB.
CC Interacts with CPSF6; indicative for an association with the cleavage
CC factor Im (CFIm) complex. Interacts with THOC1 (By similarity).
CC Interacts with LUZP4. Interacts with NCBP3 (PubMed:26382858).
CC {ECO:0000250|UniProtKB:Q8BKT7, ECO:0000269|PubMed:15833825,
CC ECO:0000269|PubMed:15998806, ECO:0000269|PubMed:19059247,
CC ECO:0000269|PubMed:19165146, ECO:0000269|PubMed:23299939,
CC ECO:0000269|PubMed:23685434, ECO:0000269|PubMed:25662211,
CC ECO:0000269|PubMed:26382858}.
CC -!- INTERACTION:
CC Q13769; Q03518: TAP1; NbExp=4; IntAct=EBI-5280316, EBI-747259;
CC Q13769; Q96FV9: THOC1; NbExp=10; IntAct=EBI-5280316, EBI-1765605;
CC Q13769; Q6I9Y2: THOC7; NbExp=9; IntAct=EBI-5280316, EBI-716286;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19059247,
CC ECO:0000269|PubMed:19165146}. Cytoplasm {ECO:0000269|PubMed:19059247}.
CC Note=Shuttles between nucleus and cytoplasm.
CC {ECO:0000269|PubMed:19059247}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC -!- PTM: Phosphorylated on tyrosine upon binding to activated CSF1R; which
CC causes a dissociation of the two proteins. Phosphorylation on Ser-5
CC and/or Ser-6 is required for nuclear export. Phosphorylated on Thr-328
CC in insulin-stimulated adipocytes (By similarity). Phosphorylation at
CC Tyr-225 modulates mRNA binding. {ECO:0000250,
CC ECO:0000269|PubMed:18373705, ECO:0000269|PubMed:23032722}.
CC -!- SIMILARITY: Belongs to the THOC5 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA76827.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; L18972; AAC26837.1; -; Genomic_DNA.
DR EMBL; AB023200; BAA76827.2; ALT_INIT; mRNA.
DR EMBL; CR456542; CAG30428.1; -; mRNA.
DR EMBL; AC005529; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC003615; AAH03615.1; -; mRNA.
DR EMBL; AJ006069; CAA06841.1; -; mRNA.
DR CCDS; CCDS13859.1; -.
DR PIR; I39463; I39463.
DR RefSeq; NP_001002877.1; NM_001002877.1.
DR RefSeq; NP_001002878.1; NM_001002878.1.
DR RefSeq; NP_001002879.1; NM_001002879.1.
DR RefSeq; NP_003669.4; NM_003678.4.
DR PDB; 7APK; EM; 3.30 A; E/M/e/m=1-683.
DR PDB; 7ZNK; EM; 3.90 A; E/M/e/m=1-683.
DR PDB; 7ZNL; EM; 3.45 A; E/M/e/m=1-683.
DR PDBsum; 7APK; -.
DR PDBsum; 7ZNK; -.
DR PDBsum; 7ZNL; -.
DR AlphaFoldDB; Q13769; -.
DR EMDB; EMD-11857; -.
DR EMDB; EMD-14804; -.
DR EMDB; EMD-14808; -.
DR SMR; Q13769; -.
DR BioGRID; 114132; 146.
DR ComplexPortal; CPX-2488; TREX transcription-export complex, DX39B variant.
DR ComplexPortal; CPX-7261; TREX transcription-export complex, DX39A variant.
DR CORUM; Q13769; -.
DR IntAct; Q13769; 64.
DR MINT; Q13769; -.
DR STRING; 9606.ENSP00000420306; -.
DR TCDB; 3.A.22.1.2; the transcription-coupled trex/tap nuclear mrna export complex (trex) family.
DR GlyGen; Q13769; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; Q13769; -.
DR MetOSite; Q13769; -.
DR PhosphoSitePlus; Q13769; -.
DR SwissPalm; Q13769; -.
DR BioMuta; THOC5; -.
DR DMDM; 259016156; -.
DR jPOST; Q13769; -.
DR MassIVE; Q13769; -.
DR PaxDb; 9606-ENSP00000420306; -.
DR PeptideAtlas; Q13769; -.
DR ProteomicsDB; 59680; -.
DR Pumba; Q13769; -.
DR Antibodypedia; 24518; 216 antibodies from 34 providers.
DR DNASU; 8563; -.
DR Ensembl; ENST00000397871.5; ENSP00000380969.1; ENSG00000100296.14.
DR Ensembl; ENST00000397872.5; ENSP00000380970.1; ENSG00000100296.14.
DR Ensembl; ENST00000397873.6; ENSP00000380971.2; ENSG00000100296.14.
DR Ensembl; ENST00000490103.6; ENSP00000420306.1; ENSG00000100296.14.
DR GeneID; 8563; -.
DR KEGG; hsa:8563; -.
DR MANE-Select; ENST00000490103.6; ENSP00000420306.1; NM_003678.5; NP_003669.4.
DR UCSC; uc003afr.4; human.
DR AGR; HGNC:19074; -.
DR CTD; 8563; -.
DR DisGeNET; 8563; -.
DR GeneCards; THOC5; -.
DR HGNC; HGNC:19074; THOC5.
DR HPA; ENSG00000100296; Low tissue specificity.
DR MIM; 612733; gene.
DR neXtProt; NX_Q13769; -.
DR OpenTargets; ENSG00000100296; -.
DR PharmGKB; PA38188; -.
DR VEuPathDB; HostDB:ENSG00000100296; -.
DR eggNOG; KOG2216; Eukaryota.
DR GeneTree; ENSGT00390000013777; -.
DR HOGENOM; CLU_023759_1_0_1; -.
DR InParanoid; Q13769; -.
DR OMA; WNGCHTS; -.
DR OrthoDB; 52790at2759; -.
DR PhylomeDB; Q13769; -.
DR TreeFam; TF314812; -.
DR PathwayCommons; Q13769; -.
DR Reactome; R-HSA-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-HSA-72187; mRNA 3'-end processing.
DR Reactome; R-HSA-73856; RNA Polymerase II Transcription Termination.
DR Reactome; R-HSA-9680350; Signaling by CSF1 (M-CSF) in myeloid cells.
DR SignaLink; Q13769; -.
DR SIGNOR; Q13769; -.
DR BioGRID-ORCS; 8563; 780 hits in 1168 CRISPR screens.
DR ChiTaRS; THOC5; human.
DR GeneWiki; THOC5; -.
DR GenomeRNAi; 8563; -.
DR Pharos; Q13769; Tbio.
DR PRO; PR:Q13769; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q13769; Protein.
DR Bgee; ENSG00000100296; Expressed in mucosa of stomach and 197 other cell types or tissues.
DR ExpressionAtlas; Q13769; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000347; C:THO complex; IDA:UniProtKB.
DR GO; GO:0000445; C:THO complex part of transcription export complex; IDA:UniProtKB.
DR GO; GO:0000346; C:transcription export complex; IDA:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0030224; P:monocyte differentiation; IDA:UniProtKB.
DR GO; GO:0006406; P:mRNA export from nucleus; IDA:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0060215; P:primitive hemopoiesis; ISS:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR InterPro; IPR019163; THO_Thoc5.
DR PANTHER; PTHR13375; FMS INTERACTING PROTEIN; 1.
DR PANTHER; PTHR13375:SF3; THO COMPLEX SUBUNIT 5 HOMOLOG; 1.
DR Pfam; PF09766; FmiP_Thoc5; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Differentiation; Isopeptide bond;
KW mRNA processing; mRNA splicing; mRNA transport; Nucleus; Phosphoprotein;
KW Reference proteome; RNA-binding; Transport; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..683
FT /note="THO complex subunit 5 homolog"
FT /id="PRO_0000079577"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2..199
FT /note="Interaction with THOC7"
FT /evidence="ECO:0000269|PubMed:19059247"
FT REGION 2..144
FT /note="Interaction with CSF1R"
FT /evidence="ECO:0000250|UniProtKB:Q8BKT7"
FT REGION 299..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 7..10
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 317..336
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 5
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BKT7"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BKT7"
FT MOD_RES 225
FT /note="Phosphotyrosine; by SRC"
FT /evidence="ECO:0000269|PubMed:18373705,
FT ECO:0000269|PubMed:23032722"
FT MOD_RES 307
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 312
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 314
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 328
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT CROSSLNK 153
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 380
FT /note="T -> K (in a breast cancer sample; somatic mutation;
FT dbSNP:rs1264823745)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035692"
FT VARIANT 475
FT /note="T -> S (in dbSNP:rs8141153)"
FT /id="VAR_037134"
FT VARIANT 499
FT /note="G -> S (in a breast cancer sample; somatic mutation;
FT dbSNP:rs1280359906)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035693"
FT VARIANT 525
FT /note="V -> I (in dbSNP:rs737976)"
FT /evidence="ECO:0000269|PubMed:10231032,
FT ECO:0000269|PubMed:15461802, ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:8242058"
FT /id="VAR_037135"
FT VARIANT 579
FT /note="V -> I (in dbSNP:rs1049534)"
FT /evidence="ECO:0000269|PubMed:15461802,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:8242058"
FT /id="VAR_021410"
FT MUTAGEN 225
FT /note="Y->F: Impairs mRNA binding, enhances CXCL12-
FT dependent cell migration."
FT /evidence="ECO:0000269|PubMed:23032722"
FT HELIX 42..46
FT /evidence="ECO:0007829|PDB:7APK"
FT HELIX 48..54
FT /evidence="ECO:0007829|PDB:7APK"
FT HELIX 56..73
FT /evidence="ECO:0007829|PDB:7APK"
FT HELIX 82..136
FT /evidence="ECO:0007829|PDB:7APK"
FT HELIX 138..147
FT /evidence="ECO:0007829|PDB:7APK"
FT HELIX 162..168
FT /evidence="ECO:0007829|PDB:7APK"
FT HELIX 171..174
FT /evidence="ECO:0007829|PDB:7APK"
FT HELIX 176..178
FT /evidence="ECO:0007829|PDB:7APK"
FT HELIX 183..188
FT /evidence="ECO:0007829|PDB:7APK"
FT HELIX 190..246
FT /evidence="ECO:0007829|PDB:7APK"
FT HELIX 253..261
FT /evidence="ECO:0007829|PDB:7APK"
FT HELIX 266..281
FT /evidence="ECO:0007829|PDB:7APK"
FT STRAND 285..292
FT /evidence="ECO:0007829|PDB:7APK"
FT HELIX 294..298
FT /evidence="ECO:0007829|PDB:7APK"
FT HELIX 334..340
FT /evidence="ECO:0007829|PDB:7APK"
FT STRAND 347..354
FT /evidence="ECO:0007829|PDB:7APK"
FT TURN 355..357
FT /evidence="ECO:0007829|PDB:7APK"
FT STRAND 358..367
FT /evidence="ECO:0007829|PDB:7APK"
FT TURN 368..371
FT /evidence="ECO:0007829|PDB:7APK"
FT STRAND 372..383
FT /evidence="ECO:0007829|PDB:7APK"
FT TURN 389..393
FT /evidence="ECO:0007829|PDB:7APK"
FT STRAND 399..401
FT /evidence="ECO:0007829|PDB:7APK"
FT STRAND 404..406
FT /evidence="ECO:0007829|PDB:7APK"
FT HELIX 416..423
FT /evidence="ECO:0007829|PDB:7APK"
FT HELIX 431..437
FT /evidence="ECO:0007829|PDB:7APK"
FT HELIX 442..448
FT /evidence="ECO:0007829|PDB:7APK"
FT HELIX 465..496
FT /evidence="ECO:0007829|PDB:7APK"
FT TURN 497..499
FT /evidence="ECO:0007829|PDB:7APK"
FT HELIX 507..510
FT /evidence="ECO:0007829|PDB:7APK"
FT STRAND 518..525
FT /evidence="ECO:0007829|PDB:7APK"
FT HELIX 527..531
FT /evidence="ECO:0007829|PDB:7APK"
FT HELIX 537..542
FT /evidence="ECO:0007829|PDB:7APK"
FT STRAND 550..558
FT /evidence="ECO:0007829|PDB:7APK"
FT STRAND 561..569
FT /evidence="ECO:0007829|PDB:7APK"
FT TURN 573..575
FT /evidence="ECO:0007829|PDB:7APK"
FT STRAND 579..588
FT /evidence="ECO:0007829|PDB:7APK"
FT TURN 592..594
FT /evidence="ECO:0007829|PDB:7APK"
FT HELIX 596..606
FT /evidence="ECO:0007829|PDB:7APK"
FT HELIX 609..611
FT /evidence="ECO:0007829|PDB:7APK"
FT STRAND 615..617
FT /evidence="ECO:0007829|PDB:7APK"
FT HELIX 621..638
FT /evidence="ECO:0007829|PDB:7APK"
FT TURN 664..667
FT /evidence="ECO:0007829|PDB:7APK"
FT STRAND 672..674
FT /evidence="ECO:0007829|PDB:7APK"
FT TURN 675..678
FT /evidence="ECO:0007829|PDB:7APK"
FT STRAND 679..681
FT /evidence="ECO:0007829|PDB:7APK"
SQ SEQUENCE 683 AA; 78508 MW; 59550FA548835016 CRC64;
MSSESSKKRK PKVIRSDGAP AEGKRNRSDT EQEGKYYSEE AEVDLRDPGR DYELYKYTCQ
ELQRLMAEIQ DLKSRGGKDV AIEIEERRIQ SCVHFMTLKK LNRLAHIRLK KGRDQTHEAK
QKVDAYHLQL QNLLYEVMHL QKEITKCLEF KSKHEEIDLV SLEEFYKEAP PDISKAEVTM
GDPHQQTLAR LDWELEQRKR LAEKYRECLS NKEKILKEIE VKKEYLSSLQ PRLNSIMQAS
LPVQEYLFMP FDQAHKQYET ARHLPPPLYV LFVQATAYGQ ACDKTLSVAI EGSVDEAKAL
FKPPEDSQDD ESDSDAEEEQ TTKRRRPTLG VQLDDKRKEM LKRHPLSVML DLKCKDDSVL
HLTFYYLMNL NIMTVKAKVT TAMELITPIS AGDLLSPDSV LSCLYPGDHG KKTPNPANQY
QFDKVGILTL SDYVLELGHP YLWVQKLGGL HFPKEQPQQT VIADHSLSAS HMETTMKLLK
TRVQSRLALH KQFASLEHGI VPVTSDCQYL FPAKVVSRLV KWVTVAHEDY MELHFTKDIV
DAGLAGDTNL YYMALIERGT AKLQAAVVLN PGYSSIPPVF QLCLNWKGEK TNSNDDNIRA
MEGEVNVCYK ELCGPWPSHQ LLTNQLQRLC VLLDVYLETE SHDDSVEGPK EFPQEKMCLR
LFRGPSRMKP FKYNHPQGFF SHR
//
