ID U2AF_HUMAN STANDARD; PRT; 475 AA. AC P26368; DT 01-AUG-1992 (Rel. 23, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Splicing factor U2AF 65 kDa subunit (U2 auxiliary factor 65 kDa DE subunit) (U2 snRNP auxiliary factor large subunit) (hU2AF(65)). GN U2AF2 OR U2AF65. 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. RX MEDLINE=92168111; PubMed=1538748; RA Zamore P.D., Patton J.G., Green M.R.; RT "Cloning and domain structure of the mammalian splicing factor U2AF."; RL Nature 355:609-614(1992). RN [2] RP STRUCTURE BY NMR OF 148-237. RX MEDLINE=99380169; PubMed=10449418; RA Ito T., Muto Y., Green M.R., Yokoyama S.; RT "Solution structures of the first and second RNA-binding domains of RT human U2 small nuclear ribonucleoprotein particle auxiliary factor RT (U2AF(65))."; RL EMBO J. 18:4523-4534(1999). CC -!- FUNCTION: Necessary for the splicing of pre-mRNA. Binds to the CC polypyrimidine tract of introns early during spliceosome assembly. CC Required for the export of mRNA out of the nucleus, even if the CC mRNA is encoded by an intron-less gene. CC -!- SUBUNIT: ASSOCIATES WITH A 35 kDa PROTEIN. CC -!- SUBCELLULAR LOCATION: Nuclear. CC -!- SIMILARITY: Contains 3 RNA recognition motif (RRM) domains. CC -!- SIMILARITY: BELONGS TO THE SR FAMILY OF SPLICING FACTORS. 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; X64044; CAA45409.1; -. DR PIR; S20250; S20250. DR PDB; 1U2F; 20-AUG-99. DR PDB; 2U2F; 20-AUG-99. DR PDB; 1JMT; 19-SEP-01. DR GK; P26368; -. DR MIM; 191318; -. DR GO; GO:0008248; F:pre-mRNA splicing factor activity; TAS. DR GO; GO:0006397; P:mRNA processing; TAS. DR InterPro; IPR000504; RNA_rec_mot. DR InterPro; IPR006529; U2AF_lg. DR Pfam; PF00076; rrm; 3. DR SMART; SM00360; RRM; 3. DR TIGRFAMs; TIGR01642; U2AF_lg; 1. DR PROSITE; PS50102; RRM; 3. DR PROSITE; PS00030; RRM_RNP_1; FALSE_NEG. KW Nuclear protein; RNA-binding; mRNA splicing; Repeat; 3D-structure. FT DOMAIN 27 62 ARG/SER-RICH (RS DOMAIN). FT DOMAIN 149 231 RNA-BINDING (RRM) 1. FT DOMAIN 259 337 RNA-BINDING (RRM) 2. FT DOMAIN 385 466 RNA-BINDING (RRM) 3. FT STRAND 150 153 FT TURN 158 159 FT TURN 162 163 FT HELIX 164 173 FT TURN 174 177 FT STRAND 186 188 FT STRAND 191 192 FT TURN 193 196 FT STRAND 197 202 FT TURN 206 210 FT HELIX 211 214 FT STRAND 227 227 FT TURN 229 230 FT STRAND 261 264 FT TURN 265 265 FT HELIX 273 279 FT TURN 280 280 FT STRAND 285 291 FT STRAND 302 307 FT HELIX 311 318 FT TURN 319 319 FT STRAND 331 334 SQ SEQUENCE 475 AA; 53501 MW; 26AD271CD8FC6211 CRC64; MSDFDEFERQ LNENKQERDK ENRHRKRSHS RSRSRDRKRR SRSRDRRNRD QRSASRDRRR RSKPLTRGAK EEHGGLIRSP RHEKKKKVRK YWDVPPPGFE HITPMQYKAM QAAGQIPATA LLPTMTPDGL AVTPTPVPVV GSQMTRQARR LYVGNIPFGI TEEAMMDFFN AQMRLGGLTQ APGNPVLAVQ INQDKNFAFL EFRSVDETTQ AMAFDGIIFQ GQSLKIRRPH DYQPLPGMSE NPSVYVPGVV STVVPDSAHK LFIGGLPNYL NDDQVKELLT SFGPLKAFNL VKDSATGLSK GYAFCEYVDI NVTDQAIAGL NGMQLGDKKL LVQRASVGAK NATLVSPPST INQTPVTLQV PGLMSSQVQM GGHPTEVLCL MNMVLPEELL DDEEYEEIVE DVRDECSKYG LVKSIEIPRP VDGVEVPGCG KIFVEFTSVF DCQKAMQGLT GRKFANRVVV TKYCDPDSYH RRDFW //