ID THOC1_HUMAN Reviewed; 657 AA. AC Q96FV9; Q15219; DT 10-OCT-2003, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 14-APR-2009, entry version 67. DE RecName: Full=THO complex subunit 1; DE Short=Tho1; DE AltName: Full=Nuclear matrix protein p84; GN Name=THOC1; Synonyms=HPR1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND INTERACTION WITH RP RB1. RC TISSUE=Lymphocyte; RX MEDLINE=95050936; PubMed=7525595; DOI=10.1083/jcb.127.3.609; RA Durfee T., Mancini M.A., Jones D., Elledge S.J., Lee W.H.; RT "The amino-terminal region of the retinoblastoma gene product binds a RT novel nuclear matrix protein that co-localizes to centers for RNA RT processing."; RL J. Cell Biol. 127:609-622(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Bone marrow; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP FUNCTION, AND INTERACTION WITH THE TREX COMPLEX. RX MEDLINE=22010388; 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-560, AND MASS RP SPECTROMETRY. RC TISSUE=Epithelium; RX PubMed=15302935; DOI=10.1073/pnas.0404720101; RA Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., RA Li J., Cohn M.A., Cantley L.C., Gygi S.P.; RT "Large-scale characterization of HeLa cell nuclear phosphoproteins."; RL Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004). RN [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-560, AND MASS RP SPECTROMETRY. RC TISSUE=Epithelium; 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., RA Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in RT signaling networks."; RL Cell 127:635-648(2006). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND MASS RP SPECTROMETRY. RX PubMed=18220336; DOI=10.1021/pr0705441; RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., RA Yates J.R. III; RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for RT efficient phosphoproteomic analysis."; RL J. Proteome Res. 7:1346-1351(2008). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND MASS RP SPECTROMETRY. 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 [8] RP IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY. RA Colinge J., Superti-Furga G., Bennett K.L.; RL Submitted (OCT-2008) to UniProtKB. RN [9] RP STRUCTURE BY NMR OF 561-657. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of the death domain of nuclear matrix protein RT p84."; RL Submitted (JUL-2005) to the PDB data bank. CC -!- FUNCTION: The THO/TREX complex is recruited to transcribed genes CC and travels with the RNA polymerase during elongation. It may CC physically link proteins that function in transcription and in RNA CC export. CC -!- SUBUNIT: Part of the heteromultimeric THO/TREX complex containing CC THOC1, THOC2, THOC3, THOC4 and UAP56. Binds to the CC hypophosphorylated form of RB1. CC -!- SUBCELLULAR LOCATION: Nucleus speckle. Nucleus, nucleoplasm. CC Nucleus matrix. CC -!- SIMILARITY: Contains 1 death domain. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; L36529; AAA53571.1; -; mRNA. DR EMBL; BC010381; AAH10381.1; -; mRNA. DR IPI; IPI00305374; -. DR PIR; A53545; A53545. DR RefSeq; NP_005122.2; -. DR UniGene; Hs.712543; -. DR PDB; 1WXP; NMR; -; A=561-657. DR PDBsum; 1WXP; -. DR PhosphoSite; Q96FV9; -. DR PRIDE; Q96FV9; -. DR Ensembl; ENSG00000079134; Homo sapiens. DR GeneID; 9984; -. DR KEGG; hsa:9984; -. DR GeneCards; GC18M000204; -. DR H-InvDB; HIX0014291; -. DR HGNC; HGNC:19070; THOC1. DR MIM; 606930; gene. DR PharmGKB; PA134887435; -. DR HOGENOM; Q96FV9; -. DR HOVERGEN; Q96FV9; -. DR NextBio; 37696; -. DR Bgee; Q96FV9; -. DR CleanEx; HS_THOC1; -. DR GermOnline; ENSG00000079134; Homo sapiens. DR GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell. DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0005515; F:protein binding; IEA:InterPro. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW. DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW. DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW. DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW. DR GO; GO:0007165; P:signal transduction; IEA:InterPro. DR InterPro; IPR000488; Death. DR InterPro; IPR011029; DEATH_like. DR Gene3D; G3DSA:1.10.533.10; DEATH_like; 1. DR Pfam; PF00531; Death; 1. DR SMART; SM00005; DEATH; 1. DR PROSITE; PS50017; DEATH_DOMAIN; 1. PE 1: Evidence at protein level; KW 3D-structure; DNA-binding; mRNA processing; mRNA splicing; KW mRNA transport; Nucleus; Phosphoprotein; RNA-binding; Transport. FT CHAIN 1 657 THO complex subunit 1. FT /FTId=PRO_0000072520. FT DOMAIN 570 653 Death. FT MOD_RES 2 2 Phosphoserine. FT MOD_RES 560 560 Phosphoserine. FT CONFLICT 130 130 S -> A (in Ref. 1; AAA53571). FT CONFLICT 433 433 M -> T (in Ref. 1; AAA53571). FT CONFLICT 480 480 V -> A (in Ref. 1; AAA53571). FT CONFLICT 487 487 V -> M (in Ref. 1; AAA53571). FT CONFLICT 498 498 R -> K (in Ref. 1; AAA53571). FT CONFLICT 519 519 P -> Q (in Ref. 1; AAA53571). FT STRAND 565 567 FT HELIX 571 581 FT TURN 582 584 FT HELIX 585 588 FT TURN 589 593 FT HELIX 596 605 FT HELIX 609 624 FT HELIX 625 627 FT HELIX 630 639 FT HELIX 643 650 SQ SEQUENCE 657 AA; 75666 MW; DB7980BD0F252DAB CRC64; MSPTPPLFSL PEARTRFTKS TREALNNKNI KPLLSTFSQV PGSENEKKCT LDQAFRGILE EEIINHSSCE NVLAIISLAI GGVTEGICTA STPFVLLGDV LDCLPLDQCD TIFTFVEKNV ATWKSNTFYS AGKNYLLRMC NDLLRRLSKS QNTVFCGRIQ LFLARLFPLS EKSGLNLQSQ FNLENVTVFN TNEQESTLGQ KHTEDREEGM DVEEGEMGDE EAPTTCSIPI DYNLYRKFWS LQDYFRNPVQ CYEKISWKTF LKYSEEVLAV FKSYKLDDTQ ASRKKMEELK TGGEHVYFAK FLTSEKLMDL QLSDSNFRRH ILLQYLILFQ YLKGQVKFKS SNYVLTDEQS LWIEDTTKSV YQLLSENPPD GERFSKMVEH ILNTEENWNS WKNEGCPSFV KERTSDTKPT RIIRKRTAPE DFLGKGPTKK ILMGNEELTR LWNLCPDNME ACKSETREHM PTLEEFFEEA IEQADPENMV ENEYKAVNNS NYGWRALRLL ARRSPHFFQP TNQQFKSLPE YLENMVIKLA KELPPPSEEI KTGEDEDEED NDALLKENES PDVRRDKPVT GEQIEVFANK LGEQWKILAP YLEMKDSEIR QIECDSEDMK MRAKQLLVAW QDQEGVHATP ENLINALNKS GLSDLAESLT NDNETNS //