SNRPA_HUMAN
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 03-AUG-2022, entry version 241.
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}.
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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 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 AlphaFoldDB; P09012; -.
DR SMR; P09012; -.
DR BioGRID; 112510; 246.
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; 104.
DR MINT; P09012; -.
DR STRING; 9606.ENSP00000243563; -.
DR DrugBank; DB02175; Malonic acid.
DR GlyGen; P09012; 1 site, 1 O-linked glycan (1 site).
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; P09012; -.
DR PeptideAtlas; P09012; -.
DR PRIDE; P09012; -.
DR ProteomicsDB; 52184; -.
DR TopDownProteomics; P09012; -.
DR Antibodypedia; 3308; 327 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 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; NQTIYVN; -.
DR OrthoDB; 1608132at2759; -.
DR PhylomeDB; P09012; -.
DR TreeFam; TF313834; -.
DR PathwayCommons; P09012; -.
DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR SignaLink; P09012; -.
DR BioGRID-ORCS; 6626; 239 hits in 1090 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 199 other tissues.
DR ExpressionAtlas; P09012; baseline and differential.
DR Genevisible; P09012; HS.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IC: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: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 GO; GO:1900363; P:regulation of mRNA polyadenylation; IEA:Ensembl.
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 Pfam; PF00076; RRM_1; 2.
DR SMART; SM00360; RRM; 2.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 2.
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
