ID RU1A_HUMAN STANDARD; PRT; 282 AA. AC P09012; DT 01-NOV-1988 (Rel. 09, Created) DT 01-NOV-1988 (Rel. 09, Last sequence update) DT 15-JUL-1998 (Rel. 36, Last annotation update) DE U1 SMALL NUCLEAR RIBONUCLEOPROTEIN A (U1 SNRNP A PROTEIN). GN SNRPA. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Mammalia; OC Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=LIVER; RX MEDLINE; 91340152. RA NELISSEN R.L.H., SILLEKENS P.T.G., BEIJER R.P., RA GEURTS VAN KESSEL A.H.M., VAN VENROOIJ W.J.; RT "Structure, chromosomal localization and evolutionary conservation of RT the gene encoding human U1 snRNP-specific A protein."; RL Gene 102:189-196(1991). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE; 88111575. RA SILLEKENS P.T.G., HABETS W.J., BEIJER R.P., VAN VENROOIJ W.J.; RT "cDNA cloning of the human U1 snRNA-associated A protein: extensive RT homology between U1 and U2 snRNP-specific proteins."; RL EMBO J. 6:3841-3848(1987). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1-95. RX MEDLINE; 91061907. RA NAGAI K., OUBRIDGE C., JESSEN T.-H., LI J., EVANS P.R.; RT "Crystal structure of the RNA-binding domain of the U1 small nuclear RT ribonucleoprotein A."; RL Nature 348:515-520(1990). RN [4] RP X-RAY CRYSTALLOGRAPHY (1.92 ANGSTROMS). RX MEDLINE; 95075454. RA OUBRIDGE C., ITO N., EVANS P.R., TEO C.-H., NAGAI K.; RT "Crystal structure at 1.92-A resolution of the RNA-binding domain of RT the U1A spliceosomal protein complexed with an RNA hairpin."; RL Nature 372:432-438(1994). RN [5] RP STRUCTURE BY NMR OF 11-94. RX MEDLINE; 91172834. RA HOFFMAN D.W., QUERY C.C., GOLDEN B.L., WHITE S.W., KEENE J.D.; RT "RNA-binding domain of the A protein component of the U1 small RT nuclear ribonucleoprotein analyzed by NMR spectroscopy is RT structurally similar to ribosomal proteins."; RL Proc. Natl. Acad. Sci. U.S.A. 88:2495-2499(1991). RN [6] RP STRUCTURE BY NMR OF 1-102. RX MEDLINE; 94349935. RA HOWE P.W.A., NAGAI K., NEUHAUS D., VARANI G.; RT "NMR studies of U1 snRNA recognition by the N-terminal RNP domain of RT the human U1A protein."; RL EMBO J. 13:3873-3881(1994). RN [7] RP STRUCTURE BY NMR OF 2-102. RX MEDLINE; 96186818. RA ALLAIN F.H.-T., GUBSER C.C., HOWE P.W.A., NAGAI K., NEUHAUS D., RA VARANI G.; RT "Specificity of ribonucleoprotein interaction determined by RNA RT folding during complex formulation."; RL Nature 380:646-650(1996). RN [8] RP STRUCTURE BY NMR OF 1-117. RX MEDLINE; 96180024. RA AVIS J.M., ALLAIN F.H.-T., HOWE P.W.A., VARANI G., NAGAI K., RA NEUHAUS D.; RT "Solution structure of the N-terminal RNP domain of U1A protein: the RT role of C-terminal residues in structure stability and RNA binding."; RL J. Mol. Biol. 257:398-411(1996). RN [9] RP STRUCTURE BY NMR OF 1-102. RX MEDLINE; 97459961. RA ALLAIN F.H.-T., HOWE P.W., NEUHAUS D., VARANI G.; RT "Structural basis of the RNA-binding specificity of human U1A RT protein."; RL EMBO J. 16:5764-5772(1997). RN [10] RP STRUCTURE BY NMR OF 195-282. RX MEDLINE; 97410326. RA LU J., HALL K.B.; RT "Tertiary structure of RBD2 and backbone dynamics of RBD1 and RBD2 of RT the human U1A protein determined by NMR spectroscopy."; RL Biochemistry 36:10393-10405(1997). RN [11] RP MUTAGENESIS, AND DETAILED STUDIES OF RNA-BINDING. RX MEDLINE; 92007796. RA JESSEN T.-H., OUBRIDGE C., TEO C.H., PRITCHARD C., NAGAI K.; RT "Identification of molecular contacts between the U1 A small nuclear RT ribonucleoprotein and U1 RNA."; RL EMBO J. 10:3447-3456(1991). CC -!- FUNCTION: BINDS STEM LOOP II OF U1 SNRNA. IT IS THE FIRST SN-RNP CC TO INTERACT WITH PRE-MRNA. THIS INTERACTION IS REQUIRED FOR THE CC SUBSEQUENT BINDING OF U2 SN-RNP AND THE U4/U6/U5 TRI-SN-RNP. CC -!- SUBUNIT: BELONGS TO THE SPLICEOSOME WHERE IT IS ASSOCIATED WITH CC SN-RNP U1. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- SIMILARITY: BELONGS TO THE U1 A/B" FAMILY. CC -!- SIMILARITY: CONTAINS 2 RNA RECOGNITION MOTIFS (RNP). 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 -------------------------------------------------------------------------- DR EMBL; M60784; AAA61245.1; -. DR EMBL; M60779; AAA61245.1; JOINED. DR EMBL; M60780; AAA61245.1; JOINED. DR EMBL; M60781; AAA61245.1; JOINED. DR EMBL; M60782; AAA61245.1; JOINED. DR EMBL; M60783; AAA61245.1; JOINED. DR EMBL; X06347; CAA29653.1; -. DR PIR; JQ1528; JQ1528. DR PDB; 1NRC; 31-JAN-94. DR PDB; 1FHT; 11-JUL-96. DR PDB; 1AUD; 25-FEB-98. DR PDB; 1URN; 08-MAR-96. DR PDB; 2U1A; 26-SEP-97. DR PDB; 3UTR; 03-APR-96. DR MIM; 182285; -. DR PFAM; PF00076; rrm; 2. DR PROSITE; PS00030; RNP_1; 1. KW Nuclear protein; RNA-binding; Ribonucleoprotein; Repeat; KW Spliceosome; 3D-structure. FT DOMAIN 12 17 RNA-BINDING (RNP2) (BY SIMILARITY). FT DOMAIN 52 59 RNA-BINDING (RNP1) (BY SIMILARITY). FT DOMAIN 210 215 RNA-BINDING (RNP2) (BY SIMILARITY). FT DOMAIN 244 251 RNA-BINDING (RNP1) (BY SIMILARITY). FT REPEAT 1 89 FT REPEAT 199 282 FT MUTAGEN 11 11 T->V: ABOLISHES RNA-BINDING. FT MUTAGEN 13 13 Y->F: SUBSTANTIALLY REDUCES RNA-BINDING. FT MUTAGEN 15 15 N->V: ABOLISHES RNA-BINDING. FT MUTAGEN 16 16 N->V: SUBSTANTIALLY REDUCES RNA-BINDING. FT MUTAGEN 52 52 R->Q: ABOLISHES RNA-BINDING. SQ SEQUENCE 282 AA; 31279 MW; 22427816 CRC32; MAVPETRPNH TIYINNLNEK IKKDELKKSL YAIFSQFGQI LDILVSRSLK MRGQAFVIFK EVSSATNALR SMQGFPFYDK PMRIQYAKTD SDIIAKMKGT FVERDRKREK RKPKSQETPA TKKAVQGGGA TPVVGAVQGP VPGMPPMTQA PRIMHHMPGQ PPYMPPPGMI PPPGLAPGQI PPGAMPPQQL MPGQMPPAQP LSENPPNHIL FLTNLPEETN ELMLSMLFNQ FPGFKEVRLV PGRHDIAFVE FDNEVQAGAA RDALQGFKIT QNNAMKISFA KK //