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 15-DEC-1998 (REL. 37, LAST ANNOTATION UPDATE) DE SPLICING FACTOR U2AF 65 KD SUBUNIT (U2 AUXILIARY FACTOR 65 KD DE SUBUNIT) (U2 SNRNP AUXILIARY FACTOR LARGE SUBUNIT). GN U2AF2 OR U2AF65. OS HOMO SAPIENS (HUMAN). OC EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; MAMMALIA; EUTHERIA; OC PRIMATES; CATARRHINI; HOMINIDAE; HOMO. RN [1] RP SEQUENCE FROM N.A. RX MEDLINE; 92168111. 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). CC -!- FUNCTION: NECESSARY FOR THE SPLICING OF PRE-MRNA. BINDS TO THE CC POLYPYRIMIDINE TRACT OF INTRONS EARLY DURING SPLICEOSOME ASSEMBLY. CC -!- SUBUNIT: ASSOCIATES WITH A 35 KD PROTEIN. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- SIMILARITY: CONTAINS 3 RNA RECOGNITION MOTIFS (RNP). CC -!- SIMILARITY: BELONGS TO THE SR FAMILY OF SPLICING FACTORS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- 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; G37545; -. DR PIR; S20250; S20250. DR PIR; S26095; S26095. DR MIM; 191318; -. DR PROSITE; PS00030; RNP_1; FALSE_NEG. DR PFAM; PF00076; rrm; 3. DR HSSP; P19339; 2SXL. KW NUCLEAR PROTEIN; RNA-BINDING; MRNA SPLICING; REPEAT. FT DOMAIN 27 62 ARG/SER-RICH (RS DOMAIN). FT DOMAIN 64 182 INVOLVED IN BINDING U2AF-35. FT DOMAIN 151 156 RNA-BINDING (RNP2) (BY SIMILARITY). FT DOMAIN 195 202 RNA-BINDING (RNP1) (BY SIMILARITY). FT DOMAIN 260 265 RNA-BINDING (RNP2) (BY SIMILARITY). FT DOMAIN 300 307 RNA-BINDING (RNP1) (BY SIMILARITY). FT DOMAIN 377 382 RNA-BINDING (RNP2) (BY SIMILARITY). FT DOMAIN 429 436 RNA-BINDING (RNP1) (BY SIMILARITY). SQ SEQUENCE 475 AA; 53501 MW; 83BC0A52 CRC32; 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 //