ID SNRPA_HUMAN Reviewed; 282 AA. AC P09012; DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 27-MAR-2024, entry version 250. DE RecName: Full=U1 small nuclear ribonucleoprotein A; DE Short=U1 snRNP A; DE Short=U1-A; DE Short=U1A; GN Name=SNRPA; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC TISSUE=Liver; RX PubMed=1831431; DOI=10.1016/0378-1119(91)90077-o; RA Nelissen R.L.H., Sillekens P.T.G., Beijer R.P., Geurts van Kessel A.H.M., RA van Venrooij W.J.; RT "Structure, chromosomal localization and evolutionary conservation of the RT gene encoding human U1 snRNP-specific A protein."; RL Gene 102:189-196(1991). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=2962859; DOI=10.1002/j.1460-2075.1987.tb02721.x; 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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Lung, and Lymph; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP PROTEIN SEQUENCE OF 2-19, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RC TISSUE=B-cell lymphoma; RA Bienvenut W.V.; RL Submitted (JAN-2004) to UniProtKB. RN [5] RP FUNCTION IN COUPLED SPLICING, FUNCTION IN POLYADENYLATION PROCESS, RP INTERACTION WITH SFPQ, AND IDENTIFICATION IN A SNRNP-FREE COMPLEX WITH RP SFPQ. RX PubMed=9848648; DOI=10.1017/s1355838298981183; RA Lutz C.S., Cooke C., O'Connor J.P., Kobayashi R., Alwine J.C.; RT "The snRNP-free U1A (SF-A) complex(es): identification of the largest RT subunit as PSF, the polypyrimidine-tract binding protein-associated RT splicing factor."; RL RNA 4:1493-1499(1998). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-131, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [7] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [8] RP RNA-BINDING. RX PubMed=19561594; DOI=10.1038/nbt.1550; RA Ray D., Kazan H., Chan E.T., Pena Castillo L., Chaudhry S., Talukder S., RA Blencowe B.J., Morris Q., Hughes T.R.; RT "Rapid and systematic analysis of the RNA recognition specificities of RNA- RT binding proteins."; RL Nat. Biotechnol. 27:667-670(2009). RN [9] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-60, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-131, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-131, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [14] RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-152, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Colon carcinoma; RX PubMed=24129315; DOI=10.1074/mcp.o113.027870; RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M., RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V., RA Bedford M.T., Comb M.J.; RT "Immunoaffinity enrichment and mass spectrometry analysis of protein RT methylation."; RL Mol. Cell. Proteomics 13:372-387(2014). RN [15] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1-95. RX PubMed=2147232; DOI=10.1038/348515a0; 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 [16] RP X-RAY CRYSTALLOGRAPHY (1.92 ANGSTROMS). RX PubMed=7984237; DOI=10.1038/372432a0; 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 the RT U1A spliceosomal protein complexed with an RNA hairpin."; RL Nature 372:432-438(1994). RN [17] RP STRUCTURE BY NMR OF 11-94. RX PubMed=1826055; DOI=10.1073/pnas.88.6.2495; 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 nuclear RT ribonucleoprotein analyzed by NMR spectroscopy is structurally similar to RT ribosomal proteins."; RL Proc. Natl. Acad. Sci. U.S.A. 88:2495-2499(1991). RN [18] RP STRUCTURE BY NMR OF 1-102. RX PubMed=8070414; DOI=10.1002/j.1460-2075.1994.tb06698.x; 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 the RT human U1A protein."; RL EMBO J. 13:3873-3881(1994). RN [19] RP STRUCTURE BY NMR OF 1-102. RX PubMed=8602269; DOI=10.1038/380646a0; RA Allain F.H.-T., Gubser C.C., Howe P.W.A., Nagai K., Neuhaus D., Varani G.; RT "Specificity of ribonucleoprotein interaction determined by RNA folding RT during complex formulation."; RL Nature 380:646-650(1996). RN [20] RP STRUCTURE BY NMR OF 1-117. RX PubMed=8609632; DOI=10.1006/jmbi.1996.0171; RA Avis J.M., Allain F.H.-T., Howe P.W.A., Varani G., Nagai K., Neuhaus D.; RT "Solution structure of the N-terminal RNP domain of U1A protein: the role RT of C-terminal residues in structure stability and RNA binding."; RL J. Mol. Biol. 257:398-411(1996). RN [21] RP STRUCTURE BY NMR OF 1-102. RX PubMed=9312034; DOI=10.1093/emboj/16.18.5764; RA Allain F.H.-T., Howe P.W., Neuhaus D., Varani G.; RT "Structural basis of the RNA-binding specificity of human U1A protein."; RL EMBO J. 16:5764-5772(1997). RN [22] RP STRUCTURE BY NMR OF 195-282. RX PubMed=9265619; DOI=10.1021/bi9709811; RA Lu J., Hall K.B.; RT "Tertiary structure of RBD2 and backbone dynamics of RBD1 and RBD2 of the RT human U1A protein determined by NMR spectroscopy."; RL Biochemistry 36:10393-10405(1997). RN [23] RP MUTAGENESIS, AND DETAILED STUDIES OF RNA-BINDING. RX PubMed=1833186; DOI=10.1002/j.1460-2075.1991.tb04909.x; 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: Component of the spliceosomal U1 snRNP, which is essential CC for recognition of the pre-mRNA 5' splice-site and the subsequent CC assembly of the spliceosome. U1 snRNP is the first snRNP to interact CC with pre-mRNA. This interaction is required for the subsequent binding CC of U2 snRNP and the U4/U6/U5 tri-snRNP. SNRPA binds stem loop II of U1 CC snRNA. In a snRNP-free form (SF-A) may be involved in coupled pre-mRNA CC splicing and polyadenylation process. May bind preferentially to the CC 5'-UGCAC-3' motif on RNAs. {ECO:0000269|PubMed:9848648}. CC -!- SUBUNIT: U1 snRNP is composed of the 7 core Sm proteins SNRPB, SNRPD1, CC SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric CC protein ring on the Sm site of the small nuclear RNA to form the core CC snRNP, and at least three U1 snRNP-specific proteins SNRNP70/U1-70K, CC SNRPA/U1-A and SNRPC/U1-C. Interacts with SFPQ; component of a snRNP- CC free complex with SFPQ. {ECO:0000269|PubMed:9848648}. CC -!- INTERACTION: CC P09012; Q9Y3Y2-3: CHTOP; NbExp=3; IntAct=EBI-607085, EBI-11984237; CC P09012; Q14011: CIRBP; NbExp=4; IntAct=EBI-607085, EBI-538850; CC P09012; Q96EP5: DAZAP1; NbExp=3; IntAct=EBI-607085, EBI-2133162; CC P09012; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-607085, EBI-742054; CC P09012; Q13838: DDX39B; NbExp=3; IntAct=EBI-607085, EBI-348622; CC P09012; Q16206-2: ENOX2; NbExp=3; IntAct=EBI-607085, EBI-10179508; CC P09012; Q96AE4-2: FUBP1; NbExp=3; IntAct=EBI-607085, EBI-12121668; CC P09012; Q06547: GABPB1; NbExp=3; IntAct=EBI-607085, EBI-618165; CC P09012; O75420: GIGYF1; NbExp=3; IntAct=EBI-607085, EBI-947774; CC P09012; P61978: HNRNPK; NbExp=4; IntAct=EBI-607085, EBI-304185; CC P09012; P61978-2: HNRNPK; NbExp=3; IntAct=EBI-607085, EBI-7060731; CC P09012; Q96PV6: LENG8; NbExp=8; IntAct=EBI-607085, EBI-739546; CC P09012; Q969G2: LHX4; NbExp=3; IntAct=EBI-607085, EBI-2865388; CC P09012; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-607085, EBI-739832; CC P09012; Q5VZF2-2: MBNL2; NbExp=3; IntAct=EBI-607085, EBI-13307411; CC P09012; Q8N6R0: METTL13; NbExp=3; IntAct=EBI-607085, EBI-1053295; CC P09012; Q9P015: MRPL15; NbExp=3; IntAct=EBI-607085, EBI-2371967; CC P09012; Q5JR59: MTUS2; NbExp=3; IntAct=EBI-607085, EBI-742948; CC P09012; Q9BU61: NDUFAF3; NbExp=6; IntAct=EBI-607085, EBI-2114801; CC P09012; Q9BU61-2: NDUFAF3; NbExp=3; IntAct=EBI-607085, EBI-10298649; CC P09012; P32243-2: OTX2; NbExp=3; IntAct=EBI-607085, EBI-9087860; CC P09012; Q15365: PCBP1; NbExp=9; IntAct=EBI-607085, EBI-946095; CC P09012; Q15366: PCBP2; NbExp=3; IntAct=EBI-607085, EBI-945799; CC P09012; P57721-2: PCBP3; NbExp=5; IntAct=EBI-607085, EBI-11983983; CC P09012; P26599: PTBP1; NbExp=7; IntAct=EBI-607085, EBI-350540; CC P09012; Q9UKA9-2: PTBP2; NbExp=3; IntAct=EBI-607085, EBI-12255608; CC P09012; Q96PU8: QKI; NbExp=3; IntAct=EBI-607085, EBI-945792; CC P09012; Q86YV0: RASAL3; NbExp=3; IntAct=EBI-607085, EBI-3437896; CC P09012; P57052: RBM11; NbExp=3; IntAct=EBI-607085, EBI-741332; CC P09012; P98179: RBM3; NbExp=8; IntAct=EBI-607085, EBI-2949699; CC P09012; Q9BQ04: RBM4B; NbExp=3; IntAct=EBI-607085, EBI-715531; CC P09012; P38159: RBMX; NbExp=3; IntAct=EBI-607085, EBI-743526; CC P09012; P0DJD3-2: RBMY1A1; NbExp=4; IntAct=EBI-607085, EBI-11994018; CC P09012; Q15415: RBMY1J; NbExp=3; IntAct=EBI-607085, EBI-8642021; CC P09012; Q6ZRY4: RBPMS2; NbExp=6; IntAct=EBI-607085, EBI-11987469; CC P09012; O00560: SDCBP; NbExp=3; IntAct=EBI-607085, EBI-727004; CC P09012; P23246: SFPQ; NbExp=4; IntAct=EBI-607085, EBI-355453; CC P09012; P09012: SNRPA; NbExp=8; IntAct=EBI-607085, EBI-607085; CC P09012; P09661: SNRPA1; NbExp=9; IntAct=EBI-607085, EBI-876439; CC P09012; P31483: TIA1; NbExp=4; IntAct=EBI-607085, EBI-1387216; CC P09012; Q01085-2: TIAL1; NbExp=3; IntAct=EBI-607085, EBI-11064654; CC P09012; Q08117-2: TLE5; NbExp=3; IntAct=EBI-607085, EBI-11741437; CC P09012; Q8WVP5: TNFAIP8L1; NbExp=3; IntAct=EBI-607085, EBI-752102; CC P09012; P14373: TRIM27; NbExp=6; IntAct=EBI-607085, EBI-719493; CC P09012; Q9BQ61: TRIR; NbExp=10; IntAct=EBI-607085, EBI-744881; CC P09012; P26368: U2AF2; NbExp=5; IntAct=EBI-607085, EBI-742339; CC P09012; P26368-2: U2AF2; NbExp=6; IntAct=EBI-607085, EBI-11097439; CC P09012; Q8WW36: ZCCHC13; NbExp=3; IntAct=EBI-607085, EBI-954111; CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- SIMILARITY: Belongs to the RRM U1 A/B'' family. {ECO:0000305}. 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; M60784; AAA61245.1; -; Genomic_DNA. DR EMBL; M60779; AAA61245.1; JOINED; Genomic_DNA. DR EMBL; M60780; AAA61245.1; JOINED; Genomic_DNA. DR EMBL; M60781; AAA61245.1; JOINED; Genomic_DNA. DR EMBL; M60782; AAA61245.1; JOINED; Genomic_DNA. DR EMBL; M60783; AAA61245.1; JOINED; Genomic_DNA. DR EMBL; X06347; CAA29653.1; -; mRNA. DR EMBL; BC000405; AAH00405.1; -; mRNA. DR EMBL; BC008290; AAH08290.1; -; mRNA. DR CCDS; CCDS12565.1; -. DR PIR; JQ1528; JQ1528. DR RefSeq; NP_004587.1; NM_004596.4. DR PDB; 1AUD; NMR; -; A=2-102. DR PDB; 1DRZ; X-ray; 2.30 A; A=2-98. DR PDB; 1DZ5; NMR; -; A/B=2-102. DR PDB; 1FHT; NMR; -; A=2-117. DR PDB; 1M5K; X-ray; 2.40 A; C/F=1-100. DR PDB; 1M5O; X-ray; 2.20 A; C/F=1-100. DR PDB; 1M5P; X-ray; 2.60 A; C/F=1-100. DR PDB; 1M5V; X-ray; 2.40 A; C/F=1-100. DR PDB; 1NU4; X-ray; 1.80 A; A/B=2-98. DR PDB; 1OIA; X-ray; 2.40 A; A/B=1-95. DR PDB; 1SJ3; X-ray; 2.20 A; P=1-100. DR PDB; 1SJ4; X-ray; 2.70 A; P=1-100. DR PDB; 1SJF; X-ray; 2.75 A; A=1-100. DR PDB; 1U6B; X-ray; 3.10 A; A=1-98. DR PDB; 1URN; X-ray; 1.92 A; A/B/C=2-98. DR PDB; 1VBX; X-ray; 2.70 A; A=1-100. DR PDB; 1VBY; X-ray; 2.90 A; A=1-100. DR PDB; 1VBZ; X-ray; 2.80 A; A=1-100. DR PDB; 1VC0; X-ray; 2.50 A; A=1-100. DR PDB; 1VC5; X-ray; 3.40 A; A=1-100. DR PDB; 1VC6; X-ray; 2.80 A; A=1-100. DR PDB; 1ZZN; X-ray; 3.37 A; A=1-98. DR PDB; 2A3J; NMR; -; A=3-80. DR PDB; 2NZ4; X-ray; 2.50 A; A/B/C/D=5-98. DR PDB; 2OIH; X-ray; 2.40 A; A=2-100. DR PDB; 2OJ3; X-ray; 2.90 A; A=2-100. DR PDB; 2U1A; NMR; -; A=195-282. DR PDB; 3BO2; X-ray; 3.31 A; A=4-98. DR PDB; 3BO3; X-ray; 3.40 A; A=4-98. DR PDB; 3BO4; X-ray; 3.33 A; A=4-98. DR PDB; 3CUL; X-ray; 2.80 A; A/B=1-96. DR PDB; 3CUN; X-ray; 3.00 A; A/B=1-98. DR PDB; 3EGZ; X-ray; 2.20 A; A=1-98. DR PDB; 3G8S; X-ray; 3.10 A; A/B/C/D=1-98. DR PDB; 3G8T; X-ray; 3.00 A; A/B/C/D=1-98. DR PDB; 3G96; X-ray; 3.01 A; A/B/C/D=1-98. DR PDB; 3G9C; X-ray; 2.90 A; A/B/C/D=1-98. DR PDB; 3HHN; X-ray; 2.99 A; B/D=2-98. DR PDB; 3IIN; X-ray; 4.18 A; A=4-98. DR PDB; 3IRW; X-ray; 2.70 A; P=1-98. DR PDB; 3IWN; X-ray; 3.20 A; C/D=6-96. DR PDB; 3K0J; X-ray; 3.10 A; A/B/C/D=2-97. DR PDB; 3L3C; X-ray; 2.85 A; A/B/C/D=7-96. DR PDB; 3MUM; X-ray; 2.90 A; P=1-98. DR PDB; 3MUR; X-ray; 3.00 A; P=1-98. DR PDB; 3MUT; X-ray; 3.00 A; P=1-98. DR PDB; 3MUV; X-ray; 3.20 A; P=1-98. DR PDB; 3MXH; X-ray; 2.30 A; P=1-98. DR PDB; 3P49; X-ray; 3.55 A; B=1-98. DR PDB; 3PGW; X-ray; 4.40 A; A/P=1-282. DR PDB; 3R1H; X-ray; 3.15 A; A/D=1-98. DR PDB; 3R1L; X-ray; 3.12 A; A/D=1-98. DR PDB; 3UCU; X-ray; 2.80 A; P=1-98. DR PDB; 3UCZ; X-ray; 2.80 A; P=1-98. DR PDB; 3UD3; X-ray; 3.10 A; P=1-98. DR PDB; 3UD4; X-ray; 2.70 A; P=1-98. DR PDB; 4C4W; X-ray; 2.95 A; A/B/E/F=1-102. DR PDB; 4PR6; X-ray; 2.30 A; A=4-96. DR PDB; 4PRF; X-ray; 2.40 A; A=1-100. DR PDB; 4W90; X-ray; 3.12 A; B=6-96. DR PDB; 4W92; X-ray; 3.21 A; B=6-96. DR PDB; 4YB1; X-ray; 2.08 A; P=7-97. DR PDB; 5DDO; X-ray; 3.10 A; C/G=2-98. DR PDB; 5DDP; X-ray; 2.30 A; C/D=2-98. DR PDB; 5DDQ; X-ray; 2.40 A; C/D=2-98. DR PDB; 5DDR; X-ray; 2.60 A; C/D=2-98. DR PDB; 5FJ4; X-ray; 2.95 A; A/B/E/F=1-102. DR PDB; 6LAS; X-ray; 2.71 A; C/D/E=6-96. DR PDB; 6LAU; X-ray; 3.11 A; C/D/E=6-96. DR PDB; 6LAX; X-ray; 2.70 A; C/D/E=6-96. DR PDB; 6LAZ; X-ray; 2.76 A; C/D/E=6-96. DR PDB; 6QX9; EM; 3.28 A; 1A=1-282. DR PDB; 6SQN; X-ray; 2.05 A; A/B/C=2-98. DR PDB; 6SQQ; X-ray; 2.37 A; AAA/BBB/CCC=1-98. DR PDB; 6SQT; X-ray; 1.84 A; AAA/BBB/CCC=1-98. DR PDB; 6SQV; X-ray; 2.45 A; AAA/BBB/CCC/DDD=1-97. DR PDB; 6SR7; X-ray; 1.86 A; AAA/BBB/CCC/DDD=1-98. DR PDB; 6XH0; X-ray; 3.10 A; A=6-90. DR PDB; 6XH1; X-ray; 2.60 A; A=6-90. DR PDB; 6XH2; X-ray; 1.71 A; A=2-93. DR PDB; 6XH3; X-ray; 2.35 A; A=6-93. DR PDB; 7AEP; NMR; -; A=157-282. DR PDB; 7B0Y; EM; 3.60 A; c=1-282. DR PDB; 7D7V; X-ray; 2.80 A; C=5-96. DR PDB; 7DLZ; X-ray; 3.00 A; A/B/C/D=1-102. DR PDB; 7DWH; X-ray; 3.10 A; A/B/C/D=1-102. DR PDB; 7LHX; X-ray; 2.20 A; A=1-98. DR PDB; 7QR3; X-ray; 2.18 A; A/B=7-97. DR PDB; 7QR4; X-ray; 2.83 A; A=7-97. DR PDB; 7VPX; EM; 3.00 A; M=1-282. DR PDB; 8GXB; X-ray; 2.15 A; C/D/E/F/G=2-98. DR PDB; 8GXC; X-ray; 2.50 A; C/D/E/F/G=2-98. DR PDBsum; 1AUD; -. DR PDBsum; 1DRZ; -. DR PDBsum; 1DZ5; -. DR PDBsum; 1FHT; -. DR PDBsum; 1M5K; -. DR PDBsum; 1M5O; -. DR PDBsum; 1M5P; -. DR PDBsum; 1M5V; -. DR PDBsum; 1NU4; -. DR PDBsum; 1OIA; -. DR PDBsum; 1SJ3; -. DR PDBsum; 1SJ4; -. DR PDBsum; 1SJF; -. DR PDBsum; 1U6B; -. DR PDBsum; 1URN; -. DR PDBsum; 1VBX; -. DR PDBsum; 1VBY; -. DR PDBsum; 1VBZ; -. DR PDBsum; 1VC0; -. DR PDBsum; 1VC5; -. DR PDBsum; 1VC6; -. DR PDBsum; 1ZZN; -. DR PDBsum; 2A3J; -. DR PDBsum; 2NZ4; -. DR PDBsum; 2OIH; -. DR PDBsum; 2OJ3; -. DR PDBsum; 2U1A; -. DR PDBsum; 3BO2; -. DR PDBsum; 3BO3; -. DR PDBsum; 3BO4; -. DR PDBsum; 3CUL; -. DR PDBsum; 3CUN; -. DR PDBsum; 3EGZ; -. DR PDBsum; 3G8S; -. DR PDBsum; 3G8T; -. DR PDBsum; 3G96; -. DR PDBsum; 3G9C; -. DR PDBsum; 3HHN; -. DR PDBsum; 3IIN; -. DR PDBsum; 3IRW; -. DR PDBsum; 3IWN; -. DR PDBsum; 3K0J; -. DR PDBsum; 3L3C; -. DR PDBsum; 3MUM; -. DR PDBsum; 3MUR; -. DR PDBsum; 3MUT; -. DR PDBsum; 3MUV; -. DR PDBsum; 3MXH; -. DR PDBsum; 3P49; -. DR PDBsum; 3PGW; -. DR PDBsum; 3R1H; -. DR PDBsum; 3R1L; -. DR PDBsum; 3UCU; -. DR PDBsum; 3UCZ; -. DR PDBsum; 3UD3; -. DR PDBsum; 3UD4; -. DR PDBsum; 4C4W; -. DR PDBsum; 4PR6; -. DR PDBsum; 4PRF; -. DR PDBsum; 4W90; -. DR PDBsum; 4W92; -. DR PDBsum; 4YB1; -. DR PDBsum; 5DDO; -. DR PDBsum; 5DDP; -. DR PDBsum; 5DDQ; -. DR PDBsum; 5DDR; -. DR PDBsum; 5FJ4; -. DR PDBsum; 6LAS; -. DR PDBsum; 6LAU; -. DR PDBsum; 6LAX; -. DR PDBsum; 6LAZ; -. DR PDBsum; 6QX9; -. DR PDBsum; 6SQN; -. DR PDBsum; 6SQQ; -. DR PDBsum; 6SQT; -. DR PDBsum; 6SQV; -. DR PDBsum; 6SR7; -. DR PDBsum; 6XH0; -. DR PDBsum; 6XH1; -. DR PDBsum; 6XH2; -. DR PDBsum; 6XH3; -. DR PDBsum; 7AEP; -. DR PDBsum; 7B0Y; -. DR PDBsum; 7D7V; -. DR PDBsum; 7DLZ; -. DR PDBsum; 7DWH; -. DR PDBsum; 7LHX; -. DR PDBsum; 7QR3; -. DR PDBsum; 7QR4; -. DR PDBsum; 7VPX; -. DR PDBsum; 8GXB; -. DR PDBsum; 8GXC; -. DR AlphaFoldDB; P09012; -. DR EMDB; EMD-11972; -. DR EMDB; EMD-32074; -. DR EMDB; EMD-4665; -. DR SMR; P09012; -. DR BioGRID; 112510; 497. DR ComplexPortal; CPX-2391; U4/U6.U5 small nuclear ribonucleoprotein complex. DR ComplexPortal; CPX-2392; U1 small nuclear ribonucleoprotein complex. DR CORUM; P09012; -. DR DIP; DIP-29407N; -. DR IntAct; P09012; 108. DR MINT; P09012; -. DR STRING; 9606.ENSP00000243563; -. DR DrugBank; DB02175; Malonic acid. DR GlyCosmos; P09012; 1 site, 1 glycan. DR GlyGen; P09012; 2 sites, 1 O-linked glycan (2 sites). DR iPTMnet; P09012; -. DR MetOSite; P09012; -. DR PhosphoSitePlus; P09012; -. DR BioMuta; SNRPA; -. DR DMDM; 134092; -. DR EPD; P09012; -. DR jPOST; P09012; -. DR MassIVE; P09012; -. DR MaxQB; P09012; -. DR PaxDb; 9606-ENSP00000243563; -. DR PeptideAtlas; P09012; -. DR ProteomicsDB; 52184; -. DR Pumba; P09012; -. DR TopDownProteomics; P09012; -. DR Antibodypedia; 3308; 366 antibodies from 31 providers. DR DNASU; 6626; -. DR Ensembl; ENST00000243563.8; ENSP00000243563.2; ENSG00000077312.9. DR GeneID; 6626; -. DR KEGG; hsa:6626; -. DR MANE-Select; ENST00000243563.8; ENSP00000243563.2; NM_004596.5; NP_004587.1. DR UCSC; uc002ooz.4; human. DR AGR; HGNC:11151; -. DR CTD; 6626; -. DR DisGeNET; 6626; -. DR GeneCards; SNRPA; -. DR HGNC; HGNC:11151; SNRPA. DR HPA; ENSG00000077312; Low tissue specificity. DR MIM; 182285; gene. DR neXtProt; NX_P09012; -. DR OpenTargets; ENSG00000077312; -. DR PharmGKB; PA35993; -. DR VEuPathDB; HostDB:ENSG00000077312; -. DR eggNOG; KOG4206; Eukaryota. DR GeneTree; ENSGT00390000007046; -. DR HOGENOM; CLU_041869_1_3_1; -. DR InParanoid; P09012; -. DR OMA; VRMIPTK; -. DR OrthoDB; 227381at2759; -. DR PhylomeDB; P09012; -. DR TreeFam; TF313834; -. DR PathwayCommons; P09012; -. DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway. DR SignaLink; P09012; -. DR SIGNOR; P09012; -. DR BioGRID-ORCS; 6626; 242 hits in 1170 CRISPR screens. DR ChiTaRS; SNRPA; human. DR EvolutionaryTrace; P09012; -. DR GeneWiki; Small_nuclear_ribonucleoprotein_polypeptide_A; -. DR GenomeRNAi; 6626; -. DR Pharos; P09012; Tbio. DR PRO; PR:P09012; -. DR Proteomes; UP000005640; Chromosome 19. DR RNAct; P09012; Protein. DR Bgee; ENSG00000077312; Expressed in ganglionic eminence and 201 other cell types or tissues. DR ExpressionAtlas; P09012; baseline and differential. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; NAS:ComplexPortal. DR GO; GO:0005681; C:spliceosomal complex; IDA:HGNC-UCL. DR GO; GO:0005685; C:U1 snRNP; IDA:UniProtKB. DR GO; GO:0046540; C:U4/U6 x U5 tri-snRNP complex; IPI:ComplexPortal. DR GO; GO:0003677; F:DNA binding; EXP:DisProt. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB. DR GO; GO:0030619; F:U1 snRNA binding; IDA:UniProtKB. DR GO; GO:1990446; F:U1 snRNP binding; IEA:Ensembl. DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central. DR CDD; cd12477; RRM1_U1A; 1. DR CDD; cd12480; RRM2_U1A; 1. DR DisProt; DP01857; -. DR Gene3D; 3.30.70.330; -; 2. DR IDEAL; IID00018; -. DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf. DR InterPro; IPR035979; RBD_domain_sf. DR InterPro; IPR000504; RRM_dom. DR InterPro; IPR034407; U1A_RRM1. DR InterPro; IPR034409; U1A_RRM2. DR PANTHER; PTHR10501:SF85; U1 SMALL NUCLEAR RIBONUCLEOPROTEIN A; 1. DR PANTHER; PTHR10501; U1 SMALL NUCLEAR RIBONUCLEOPROTEIN A/U2 SMALL NUCLEAR RIBONUCLEOPROTEIN B; 1. DR Pfam; PF00076; RRM_1; 2. DR SMART; SM00360; RRM; 2. DR SUPFAM; SSF54928; RNA-binding domain, RBD; 1. DR PROSITE; PS50102; RRM; 2. DR Genevisible; P09012; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Direct protein sequencing; Methylation; KW mRNA processing; mRNA splicing; Nucleus; Phosphoprotein; KW Reference proteome; Repeat; Ribonucleoprotein; RNA-binding; Spliceosome. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|Ref.4, ECO:0007744|PubMed:19413330" FT CHAIN 2..282 FT /note="U1 small nuclear ribonucleoprotein A" FT /id="PRO_0000081887" FT DOMAIN 10..89 FT /note="RRM 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176" FT DOMAIN 208..282 FT /note="RRM 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176" FT REGION 100..132 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 100..118 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000269|Ref.4, ECO:0007744|PubMed:19413330" FT MOD_RES 60 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 131 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163" FT MOD_RES 152 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MUTAGEN 11 FT /note="T->V: Abolishes RNA binding." FT /evidence="ECO:0000269|PubMed:1833186" FT MUTAGEN 13 FT /note="Y->F: Substantially reduces RNA binding." FT /evidence="ECO:0000269|PubMed:1833186" FT MUTAGEN 15 FT /note="N->V: Abolishes RNA binding." FT /evidence="ECO:0000269|PubMed:1833186" FT MUTAGEN 16 FT /note="N->V: Substantially reduces RNA binding." FT /evidence="ECO:0000269|PubMed:1833186" FT MUTAGEN 52 FT /note="R->Q: Abolishes RNA binding." FT /evidence="ECO:0000269|PubMed:1833186" FT STRAND 10..16 FT /evidence="ECO:0007829|PDB:6XH2" FT STRAND 19..21 FT /evidence="ECO:0007829|PDB:3CUL" FT HELIX 23..34 FT /evidence="ECO:0007829|PDB:6XH2" FT HELIX 35..37 FT /evidence="ECO:0007829|PDB:6XH2" FT STRAND 40..44 FT /evidence="ECO:0007829|PDB:6XH2" FT HELIX 47..51 FT /evidence="ECO:0007829|PDB:1NU4" FT STRAND 55..61 FT /evidence="ECO:0007829|PDB:6XH2" FT HELIX 62..72 FT /evidence="ECO:0007829|PDB:6XH2" FT STRAND 76..81 FT /evidence="ECO:0007829|PDB:6XH3" FT STRAND 83..86 FT /evidence="ECO:0007829|PDB:6XH2" FT HELIX 93..96 FT /evidence="ECO:0007829|PDB:1NU4" FT TURN 97..99 FT /evidence="ECO:0007829|PDB:7DLZ" FT STRAND 201..203 FT /evidence="ECO:0007829|PDB:7AEP" FT STRAND 208..213 FT /evidence="ECO:0007829|PDB:2U1A" FT HELIX 221..229 FT /evidence="ECO:0007829|PDB:2U1A" FT STRAND 234..238 FT /evidence="ECO:0007829|PDB:2U1A" FT STRAND 246..253 FT /evidence="ECO:0007829|PDB:2U1A" FT HELIX 254..263 FT /evidence="ECO:0007829|PDB:2U1A" FT TURN 264..266 FT /evidence="ECO:0007829|PDB:2U1A" FT HELIX 269..271 FT /evidence="ECO:0007829|PDB:2U1A" FT STRAND 273..279 FT /evidence="ECO:0007829|PDB:7AEP" SQ SEQUENCE 282 AA; 31280 MW; 9426E83EE5A22894 CRC64; 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 //