ID THO1_HUMAN STANDARD; PRT; 657 AA. AC Q96FV9; Q15219; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE THO complex subunit 1 (Tho1) (Nuclear matrix protein p84). GN THOC1 OR HPR1. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A., SUBCELLULAR LOCATION, AND INTERACTION WITH RB1. RC TISSUE=Lymphocytes; RX MEDLINE=95050936; PubMed=7525595; 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 SEQUENCE FROM N.A. RC TISSUE=Bone marrow; RX MEDLINE=22388257; PubMed=12477932; RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G., RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D., RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K., RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F., RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L., RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E., RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C., RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J., RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H., RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W., RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A., RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G., RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C., RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M., RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E., RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.; RT "Generation and initial analysis of more than 15,000 full-length RT human and mouse cDNA sequences."; RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002). RN [3] RP FUNCTION, AND INTERACTION WITH THE TREX COMPLEX. RX MEDLINE=22010388; PubMed=11979277; 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 RT RNA export."; RL Nature 417:304-308(2002). 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 NFX1/UAP56. Binds to the CC hypophosphorylated form of RB1. CC -!- SUBCELLULAR LOCATION: Nuclear, in multiple discrete foci and CC associated with the nuclear 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; -. DR EMBL; BC010381; AAH10381.1; -. DR PIR; A53545; A53545. DR Genew; HGNC:19070; THOC1. DR MIM; 606930; -. DR InterPro; IPR000488; Death. DR Pfam; PF00531; Death; 1. DR PROSITE; PS50017; DEATH_DOMAIN; 1. KW Transport; mRNA transport; mRNA processing; mRNA splicing; KW Nuclear protein; Matrix protein; DNA-binding; RNA-binding. FT DOMAIN 570 653 Death. FT CONFLICT 130 130 S -> A (in Ref. 1). FT CONFLICT 433 433 M -> T (in Ref. 1). FT CONFLICT 480 480 V -> A (in Ref. 1). FT CONFLICT 487 487 V -> M (in Ref. 1). FT CONFLICT 498 498 R -> K (in Ref. 1). FT CONFLICT 519 519 P -> Q (in Ref. 1). 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 //