ID THOC1_HUMAN STANDARD; PRT; 657 AA. AC Q96FV9; Q15219; DT 10-OCT-2003, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 16-MAY-2006, entry version 35. DE THO complex subunit 1 (Tho1) (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 MEDLINE=22388257; PubMed=12477932; DOI=10.1073/pnas.242603899; 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 human RT 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; 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 AT SER-560. 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). 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: Nucleus; nucleoplasm; nuclear speckle. CC Nucleus; nucleoplasm; 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; -; mRNA. DR EMBL; BC010381; AAH10381.1; -; mRNA. DR PIR; A53545; A53545. DR UniGene; Hs.1540; -. DR PDB; 1WXP; NMR; A=561-657. DR Ensembl; ENSG00000079134; Homo sapiens. DR H-InvDB; HIX0014291; -. DR HGNC; HGNC:19070; THOC1. DR MIM; 606930; gene. DR GO; GO:0005634; C:nucleus; TAS. DR GO; GO:0006396; P:RNA processing; TAS. DR InterPro; IPR000488; Death. DR InterPro; IPR011029; DEATH_like. DR Pfam; PF00531; Death; 1. DR SMART; SM00005; DEATH; 1. DR PROSITE; PS50017; DEATH_DOMAIN; 1. KW 3D-structure; DNA-binding; mRNA processing; mRNA splicing; KW mRNA transport; Nuclear protein; Phosphorylation; RNA-binding; KW Transport. FT CHAIN 1 657 THO complex subunit 1. FT /FTId=PRO_0000072520. FT DOMAIN 570 653 Death. FT MOD_RES 560 560 Phosphoserine. 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). 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 STRAND 607 608 FT HELIX 609 627 FT HELIX 630 639 FT TURN 640 641 FT HELIX 643 650 FT STRAND 654 655 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 //