THOC2_HUMAN
ID THOC2_HUMAN Reviewed; 1593 AA.
AC Q8NI27; A6NM50; Q5JZ12; Q6IN92; Q9H8I6;
DT 10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=THO complex subunit 2;
DE Short=Tho2;
DE AltName: Full=hTREX120;
GN Name=THOC2; Synonyms=CXorf3;
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 [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 233-1593 (ISOFORM 1), FUNCTION, AND
RP INTERACTION WITH THE TREX COMPLEX.
RX PubMed=11979277; DOI=10.1038/nature746;
RA Straesser K., Masuda S., Mason P., Pfannstiel J., Oppizzi M.,
RA Rodriguez-Navarro S., Rondon A.G., Aguilera A., Struhl K., Reed R.,
RA Hurt E.;
RT "TREX is a conserved complex coupling transcription with messenger RNA
RT export.";
RL Nature 417:304-308(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 559-1277 (ISOFORM 1).
RC TISSUE=Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1266-1593 (ISOFORM 1).
RC TISSUE=Salivary gland;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
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 [7]
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 [8]
RP INTERACTION WITH THOC1.
RX PubMed=15870275; DOI=10.1128/mcb.25.10.4023-4033.2005;
RA Li Y., Wang X., Zhang X., Goodrich D.W.;
RT "Human hHpr1/p84/Thoc1 regulates transcriptional elongation and physically
RT links RNA polymerase II and RNA processing factors.";
RL Mol. Cell. Biol. 25:4023-4033(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-1486, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [11]
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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1385; SER-1393; SER-1417;
RP THR-1443 AND SER-1486, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [13]
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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1385; SER-1393 AND SER-1417,
RP 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 [15]
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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1417 AND SER-1486, 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 [17]
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 [18]
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 [19]
RP INTERACTION WITH POLDIP3 AND ZC3H11A.
RX PubMed=22928037; DOI=10.1371/journal.pone.0043804;
RA Folco E.G., Lee C.S., Dufu K., Yamazaki T., Reed R.;
RT "The proteins PDIP3 and ZC11A associate with the human TREX complex in an
RT ATP-dependent manner and function in mRNA export.";
RL PLoS ONE 7:E43804-E43804(2012).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1385; SER-1390; SER-1393;
RP SER-1417; THR-1443; SER-1450; SER-1486 AND SER-1516, AND IDENTIFICATION BY
RP 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 [21]
RP FUNCTION.
RX PubMed=23222130; DOI=10.1093/nar/gks1188;
RA Chi B., Wang Q., Wu G., Tan M., Wang L., Shi M., Chang X., Cheng H.;
RT "Aly and THO are required for assembly of the human TREX complex and
RT association of TREX components with the spliced mRNA.";
RL Nucleic Acids Res. 41:1294-1306(2013).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1417, AND IDENTIFICATION BY
RP 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 [23]
RP FUNCTION, TISSUE SPECIFICITY, INVOLVEMENT IN XLID12, VARIANTS XLID12
RP PHE-313; PRO-438; THR-800 AND PRO-1012, AND CHARACTERIZATION OF VARIANTS
RP XLID12 PRO-438; THR-800 AND PRO-1012.
RX PubMed=26166480; DOI=10.1016/j.ajhg.2015.05.021;
RA Kumar R., Corbett M.A., van Bon B.W., Woenig J.A., Weir L., Douglas E.,
RA Friend K.L., Gardner A., Shaw M., Jolly L.A., Tan C., Hunter M.F.,
RA Hackett A., Field M., Palmer E.E., Leffler M., Rogers C., Boyle J.,
RA Bienek M., Jensen C., Van Buggenhout G., Van Esch H., Hoffmann K.,
RA Raynaud M., Zhao H., Reed R., Hu H., Haas S.A., Haan E., Kalscheuer V.M.,
RA Gecz J.;
RT "THOC2 Mutations Implicate mRNA-Export Pathway in X-Linked Intellectual
RT Disability.";
RL Am. J. Hum. Genet. 97:302-310(2015).
CC -!- FUNCTION: Required for efficient export of polyadenylated RNA and
CC spliced mRNA. Acts as component of the THO subcomplex of the TREX
CC complex which is thought to couple mRNA transcription, processing and
CC nuclear export, and which specifically associates with spliced mRNA and
CC not 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 THOC2 (and probably the THO complex) is involved in releasing mRNA from
CC nuclear speckle domains. Required for NXF1 localization to the nuclear
CC rim. Plays a role for proper neuronal development.
CC {ECO:0000269|PubMed:11979277, ECO:0000269|PubMed:15833825,
CC ECO:0000269|PubMed:15998806, ECO:0000269|PubMed:17190602,
CC ECO:0000269|PubMed:18974867, ECO:0000269|PubMed:22893130,
CC ECO:0000269|PubMed:23222130, ECO:0000269|PubMed:26166480}.
CC -!- SUBUNIT: Component of the THO complex, which is composed of THOC1,
CC THOC2, THOC3, THOC5, THOC6 and THOC7; together with at least
CC ALYREF/THOC4, DDX39B, SARNP/CIP29 and CHTOP, THO forms the
CC transcription/export (TREX) complex which seems to have a dynamic
CC structure involving ATP-dependent remodeling. Interacts with THOC1,
CC POLDIP3 and ZC3H11A. {ECO:0000269|PubMed:11979277,
CC ECO:0000269|PubMed:15833825, ECO:0000269|PubMed:15870275,
CC ECO:0000269|PubMed:15998806, ECO:0000269|PubMed:22928037}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Nucleus speckle
CC {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8NI27-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8NI27-2; Sequence=VSP_008588;
CC -!- TISSUE SPECIFICITY: Expressed in the hippocampus and the cerebral
CC cortex. {ECO:0000269|PubMed:26166480}.
CC -!- DISEASE: Intellectual developmental disorder, X-linked 12 (XLID12)
CC [MIM:300957]: A form of intellectual disability, a disorder
CC characterized by significantly below average general intellectual
CC functioning associated with impairments in adaptive behavior and
CC manifested during the developmental period. Intellectual deficiency is
CC the only primary symptom of non-syndromic X-linked forms, while
CC syndromic forms present with associated physical, neurological and/or
CC psychiatric manifestations. XLID12 patients manifest variable degrees
CC of intellectual disability. Commonly observed features included speech
CC delay, elevated BMI, short stature, seizure disorders, gait
CC disturbance, and tremors. {ECO:0000269|PubMed:26166480}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the THOC2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM28436.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the N-terminal part.; Evidence={ECO:0000305};
CC Sequence=BAB14630.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL030996; CAI42271.2; -; Genomic_DNA.
DR EMBL; AL023575; CAI42271.2; JOINED; Genomic_DNA.
DR EMBL; Z82901; CAI42271.2; JOINED; Genomic_DNA.
DR EMBL; Z82901; CAI42864.2; -; Genomic_DNA.
DR EMBL; AL023575; CAI42864.2; JOINED; Genomic_DNA.
DR EMBL; AL030996; CAI42864.2; JOINED; Genomic_DNA.
DR EMBL; AL023575; CAO03594.1; -; Genomic_DNA.
DR EMBL; AL030996; CAO03594.1; JOINED; Genomic_DNA.
DR EMBL; Z82901; CAO03594.1; JOINED; Genomic_DNA.
DR EMBL; BC072400; AAH72400.1; -; mRNA.
DR EMBL; AF441770; AAM28436.1; ALT_SEQ; mRNA.
DR EMBL; AK023659; BAB14630.1; ALT_INIT; mRNA.
DR EMBL; BX648654; CAE46196.1; -; mRNA.
DR CCDS; CCDS43988.1; -. [Q8NI27-1]
DR RefSeq; NP_001075019.1; NM_001081550.1. [Q8NI27-1]
DR PDB; 7APK; EM; 3.30 A; B/J/b/j=1-1203.
DR PDBsum; 7APK; -.
DR AlphaFoldDB; Q8NI27; -.
DR SMR; Q8NI27; -.
DR BioGRID; 121436; 156.
DR CORUM; Q8NI27; -.
DR IntAct; Q8NI27; 94.
DR MINT; Q8NI27; -.
DR STRING; 9606.ENSP00000245838; -.
DR GlyGen; Q8NI27; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8NI27; -.
DR MetOSite; Q8NI27; -.
DR PhosphoSitePlus; Q8NI27; -.
DR SwissPalm; Q8NI27; -.
DR BioMuta; THOC2; -.
DR DMDM; 259016155; -.
DR EPD; Q8NI27; -.
DR jPOST; Q8NI27; -.
DR MassIVE; Q8NI27; -.
DR MaxQB; Q8NI27; -.
DR PaxDb; Q8NI27; -.
DR PeptideAtlas; Q8NI27; -.
DR PRIDE; Q8NI27; -.
DR ProteomicsDB; 73816; -. [Q8NI27-1]
DR ProteomicsDB; 73817; -. [Q8NI27-2]
DR Antibodypedia; 51559; 71 antibodies from 15 providers.
DR DNASU; 57187; -.
DR Ensembl; ENST00000245838.13; ENSP00000245838.8; ENSG00000125676.20. [Q8NI27-1]
DR Ensembl; ENST00000355725.8; ENSP00000347959.4; ENSG00000125676.20. [Q8NI27-1]
DR Ensembl; ENST00000618150.4; ENSP00000480478.1; ENSG00000125676.20. [Q8NI27-2]
DR GeneID; 57187; -.
DR KEGG; hsa:57187; -.
DR MANE-Select; ENST00000245838.13; ENSP00000245838.8; NM_001081550.2; NP_001075019.1.
DR UCSC; uc004etu.4; human. [Q8NI27-1]
DR CTD; 57187; -.
DR DisGeNET; 57187; -.
DR GeneCards; THOC2; -.
DR HGNC; HGNC:19073; THOC2.
DR HPA; ENSG00000125676; Low tissue specificity.
DR MalaCards; THOC2; -.
DR MIM; 300395; gene.
DR MIM; 300957; phenotype.
DR neXtProt; NX_Q8NI27; -.
DR OpenTargets; ENSG00000125676; -.
DR Orphanet; 457240; X-linked intellectual disability-short stature-overweight syndrome.
DR PharmGKB; PA128395788; -.
DR VEuPathDB; HostDB:ENSG00000125676; -.
DR eggNOG; KOG1874; Eukaryota.
DR GeneTree; ENSGT00710000106792; -.
DR HOGENOM; CLU_663841_0_0_1; -.
DR InParanoid; Q8NI27; -.
DR PhylomeDB; Q8NI27; -.
DR TreeFam; TF313127; -.
DR PathwayCommons; Q8NI27; -.
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 SignaLink; Q8NI27; -.
DR SIGNOR; Q8NI27; -.
DR BioGRID-ORCS; 57187; 414 hits in 720 CRISPR screens.
DR ChiTaRS; THOC2; human.
DR GeneWiki; THOC2; -.
DR GenomeRNAi; 57187; -.
DR Pharos; Q8NI27; Tbio.
DR PRO; PR:Q8NI27; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q8NI27; protein.
DR Bgee; ENSG00000125676; Expressed in secondary oocyte and 201 other tissues.
DR ExpressionAtlas; Q8NI27; baseline and differential.
DR Genevisible; Q8NI27; HS.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
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:0001824; P:blastocyst development; IEA:Ensembl.
DR GO; GO:0000902; P:cell morphogenesis; IEA:Ensembl.
DR GO; GO:0048699; P:generation of neurons; IMP: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:0010977; P:negative regulation of neuron projection development; IEA:Ensembl.
DR GO; GO:0048666; P:neuron development; IMP:UniProtKB.
DR GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; IDA:UniProtKB.
DR GO; GO:0010468; P:regulation of gene expression; IEA:Ensembl.
DR GO; GO:0010793; P:regulation of mRNA export from nucleus; IEA:Ensembl.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR GO; GO:0017145; P:stem cell division; IEA:Ensembl.
DR GO; GO:0046784; P:viral mRNA export from host cell nucleus; IDA:UniProtKB.
DR InterPro; IPR040007; Tho2.
DR InterPro; IPR021418; THO_THOC2_C.
DR InterPro; IPR021726; THO_THOC2_N.
DR InterPro; IPR032302; THOC2_N.
DR PANTHER; PTHR21597; PTHR21597; 1.
DR Pfam; PF11262; Tho2; 1.
DR Pfam; PF11732; Thoc2; 1.
DR Pfam; PF16134; THOC2_N; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Coiled coil; Disease variant;
KW Intellectual disability; mRNA processing; mRNA splicing; mRNA transport;
KW Nucleus; Phosphoprotein; Reference proteome; RNA-binding; Transport.
FT CHAIN 1..1593
FT /note="THO complex subunit 2"
FT /id="PRO_0000072523"
FT REGION 322..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1184..1593
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 293..339
FT /evidence="ECO:0000255"
FT COILED 896..965
FT /evidence="ECO:0000255"
FT COILED 1464..1491
FT /evidence="ECO:0000255"
FT MOTIF 923..928
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 1202..1220
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1221..1236
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1239..1264
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1265..1381
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1398..1416
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1447..1509
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1518..1585
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1222
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:B1AZI6"
FT MOD_RES 1385
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 1390
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1393
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 1417
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 1443
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1450
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1486
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1516
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..1179
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_008588"
FT VARIANT 313
FT /note="L -> F (in XLID12; dbSNP:rs797045019)"
FT /evidence="ECO:0000269|PubMed:26166480"
FT /id="VAR_075718"
FT VARIANT 438
FT /note="L -> P (in XLID12; reduced amounts of protein;
FT reduced amounts of other THO complex subunits; the mutant
FT protein has a significantly shorter half-life;
FT dbSNP:rs797045018)"
FT /evidence="ECO:0000269|PubMed:26166480"
FT /id="VAR_075719"
FT VARIANT 800
FT /note="I -> T (in XLID12; reduced amounts of mutant
FT protein; reduced amounts of other THO complex subunits; the
FT mutant protein has a significantly shorter half-life;
FT dbSNP:rs797045021)"
FT /evidence="ECO:0000269|PubMed:26166480"
FT /id="VAR_075720"
FT VARIANT 1012
FT /note="S -> P (in XLID12; normal amounts of mutant protein;
FT normal amounts of other THO complex subunits;
FT dbSNP:rs797045020)"
FT /evidence="ECO:0000269|PubMed:26166480"
FT /id="VAR_075721"
FT CONFLICT 807
FT /note="F -> S (in Ref. 4; BAB14630)"
FT /evidence="ECO:0000305"
FT CONFLICT 1276
FT /note="E -> G (in Ref. 5; CAE46196)"
FT /evidence="ECO:0000305"
FT CONFLICT 1356
FT /note="E -> K (in Ref. 5; CAE46196)"
FT /evidence="ECO:0000305"
FT CONFLICT 1426..1429
FT /note="DSLI -> VSIA (in Ref. 5; CAE46196)"
FT /evidence="ECO:0000305"
FT HELIX 169..179
FT /evidence="ECO:0007829|PDB:7APK"
FT HELIX 189..203
FT /evidence="ECO:0007829|PDB:7APK"
FT HELIX 207..220
FT /evidence="ECO:0007829|PDB:7APK"
FT HELIX 225..236
FT /evidence="ECO:0007829|PDB:7APK"
FT HELIX 242..254
FT /evidence="ECO:0007829|PDB:7APK"
FT HELIX 264..273
FT /evidence="ECO:0007829|PDB:7APK"
FT STRAND 276..278
FT /evidence="ECO:0007829|PDB:7APK"
FT HELIX 282..287
FT /evidence="ECO:0007829|PDB:7APK"
FT HELIX 296..306
FT /evidence="ECO:0007829|PDB:7APK"
FT HELIX 344..352
FT /evidence="ECO:0007829|PDB:7APK"
FT HELIX 359..365
FT /evidence="ECO:0007829|PDB:7APK"
FT TURN 370..375
FT /evidence="ECO:0007829|PDB:7APK"
FT HELIX 377..390
FT /evidence="ECO:0007829|PDB:7APK"
FT HELIX 392..397
FT /evidence="ECO:0007829|PDB:7APK"
FT HELIX 425..438
FT /evidence="ECO:0007829|PDB:7APK"
FT HELIX 446..462
FT /evidence="ECO:0007829|PDB:7APK"
FT HELIX 477..496
FT /evidence="ECO:0007829|PDB:7APK"
FT STRAND 498..500
FT /evidence="ECO:0007829|PDB:7APK"
FT HELIX 504..512
FT /evidence="ECO:0007829|PDB:7APK"
FT HELIX 518..525
FT /evidence="ECO:0007829|PDB:7APK"
FT TURN 526..530
FT /evidence="ECO:0007829|PDB:7APK"
FT STRAND 531..535
FT /evidence="ECO:0007829|PDB:7APK"
FT HELIX 536..553
FT /evidence="ECO:0007829|PDB:7APK"
FT HELIX 564..574
FT /evidence="ECO:0007829|PDB:7APK"
FT HELIX 576..589
FT /evidence="ECO:0007829|PDB:7APK"
FT HELIX 594..600
FT /evidence="ECO:0007829|PDB:7APK"
FT HELIX 601..603
FT /evidence="ECO:0007829|PDB:7APK"
FT HELIX 607..619
FT /evidence="ECO:0007829|PDB:7APK"
FT HELIX 637..652
FT /evidence="ECO:0007829|PDB:7APK"
FT HELIX 658..669
FT /evidence="ECO:0007829|PDB:7APK"
FT HELIX 674..686
FT /evidence="ECO:0007829|PDB:7APK"
FT HELIX 697..700
FT /evidence="ECO:0007829|PDB:7APK"
FT HELIX 707..713
FT /evidence="ECO:0007829|PDB:7APK"
FT HELIX 724..732
FT /evidence="ECO:0007829|PDB:7APK"
FT HELIX 741..748
FT /evidence="ECO:0007829|PDB:7APK"
FT HELIX 754..756
FT /evidence="ECO:0007829|PDB:7APK"
FT HELIX 764..785
FT /evidence="ECO:0007829|PDB:7APK"
FT HELIX 857..866
FT /evidence="ECO:0007829|PDB:7APK"
FT HELIX 873..883
FT /evidence="ECO:0007829|PDB:7APK"
FT HELIX 890..892
FT /evidence="ECO:0007829|PDB:7APK"
FT HELIX 897..907
FT /evidence="ECO:0007829|PDB:7APK"
FT HELIX 928..958
FT /evidence="ECO:0007829|PDB:7APK"
FT HELIX 972..987
FT /evidence="ECO:0007829|PDB:7APK"
FT HELIX 992..1004
FT /evidence="ECO:0007829|PDB:7APK"
FT HELIX 1016..1020
FT /evidence="ECO:0007829|PDB:7APK"
FT HELIX 1025..1029
FT /evidence="ECO:0007829|PDB:7APK"
FT HELIX 1035..1053
FT /evidence="ECO:0007829|PDB:7APK"
FT HELIX 1088..1112
FT /evidence="ECO:0007829|PDB:7APK"
FT HELIX 1119..1130
FT /evidence="ECO:0007829|PDB:7APK"
FT HELIX 1138..1153
FT /evidence="ECO:0007829|PDB:7APK"
FT HELIX 1161..1174
FT /evidence="ECO:0007829|PDB:7APK"
SQ SEQUENCE 1593 AA; 182775 MW; A869B3E412CA4356 CRC64;
MAAAAVVVPA EWIKNWEKSG RGEFLHLCRI LSENKSHDSS TYRDFQQALY ELSYHVIKGN
LKHEQASNVL SDISEFREDM PSILADVFCI LDIETNCLEE KSKRDYFTQL VLACLYLVSD
TVLKERLDPE TLESLGLIKQ SQQFNQKSVK IKTKLFYKQQ KFNLLREENE GYAKLIAELG
QDLSGSITSD LILENIKSLI GCFNLDPNRV LDVILEVFEC RPEHDDFFIS LLESYMSMCE
PQTLCHILGF KFKFYQEPNG ETPSSLYRVA AVLLQFNLID LDDLYVHLLP ADNCIMDEHK
REIAEAKQIV RKLTMVVLSS EKMDEREKEK EKEEEKVEKP PDNQKLGLLE ALLKIGDWQH
AQNIMDQMPP YYAASHKLIA LAICKLIHIT IEPLYRRVGV PKGAKGSPVN ALQNKRAPKQ
AESFEDLRRD VFNMFCYLGP HLSHDPILFA KVVRIGKSFM KEFQSDGSKQ EDKEKTEVIL
SCLLSITDQV LLPSLSLMDC NACMSEELWG MFKTFPYQHR YRLYGQWKNE TYNSHPLLVK
VKAQTIDRAK YIMKRLTKEN VKPSGRQIGK LSHSNPTILF DYILSQIQKY DNLITPVVDS
LKYLTSLNYD VLAYCIIEAL ANPEKERMKH DDTTISSWLQ SLASFCGAVF RKYPIDLAGL
LQYVANQLKA GKSFDLLILK EVVQKMAGIE ITEEMTMEQL EAMTGGEQLK AEGGYFGQIR
NTKKSSQRLK DALLDHDLAL PLCLLMAQQR NGVIFQEGGE KHLKLVGKLY DQCHDTLVQF
GGFLASNLST EDYIKRVPSI DVLCNEFHTP HDAAFFLSRP MYAHHISSKY DELKKSEKGS
KQQHKVHKYI TSCEMVMAPV HEAVVSLHVS KVWDDISPQF YATFWSLTMY DLAVPHTSYE
REVNKLKVQM KAIDDNQEMP PNKKKKEKER CTALQDKLLE EEKKQMEHVQ RVLQRLKLEK
DNWLLAKSTK NETITKFLQL CIFPRCIFSA IDAVYCARFV ELVHQQKTPN FSTLLCYDRV
FSDIIYTVAS CTENEASRYG RFLCCMLETV TRWHSDRATY EKECGNYPGF LTILRATGFD
GGNKADQLDY ENFRHVVHKW HYKLTKASVH CLETGEYTHI RNILIVLTKI LPWYPKVLNL
GQALERRVHK ICQEEKEKRP DLYALAMGYS GQLKSRKSYM IPENEFHHKD PPPRNAVASV
QNGPGGGPSS SSIGSASKSD ESSTEETDKS RERSQCGVKA VNKASSTTPK GNSSNGNSGS
NSNKAVKEND KEKGKEKEKE KKEKTPATTP EARVLGKDGK EKPKEERPNK DEKARETKER
TPKSDKEKEK FKKEEKAKDE KFKTTVPNAE SKSTQERERE KEPSRERDIA KEMKSKENVK
GGEKTPVSGS LKSPVPRSDI PEPEREQKRR KIDTHPSPSH SSTVKDSLIE LKESSAKLYI
NHTPPPLSKS KEREMDKKDL DKSRERSRER EKKDEKDRKE RKRDHSNNDR EVPPDLTKRR
KEENGTMGVS KHKSESPCES PYPNEKDKEK NKSKSSGKEK GSDSFKSEKM DKISSGGKKE
SRHDKEKIEK KEKRDSSGGK EEKKHHKSSD KHR
