AAR2_YEAST
ID AAR2_YEAST Reviewed; 355 AA.
AC P32357; D6VPS8;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=A1 cistron-splicing factor AAR2;
GN Name=AAR2; OrderedLocusNames=YBL074C; ORFNames=YBL06.06, YBL0611;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=1922071; DOI=10.1128/mcb.11.11.5693-5700.1991;
RA Nakazawa N., Harashima S., Oshima Y.;
RT "AAR2, a gene for splicing pre-mRNA of the MATa1 cistron in cell type
RT control of Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 11:5693-5700(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7992509; DOI=10.1002/yea.320100811;
RA Logghe M., Molemans F., Fiers W., Contreras R.;
RT "The two genes encoding yeast ribosomal protein S8 reside on different
RT chromosomes, and are closely linked to the hsp70 stress protein genes SSA3
RT and SSA4.";
RL Yeast 10:1093-1100(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 77-355.
RX PubMed=2188113; DOI=10.1128/mcb.10.6.3262-3267.1990;
RA Boorstein W.R., Craig E.A.;
RT "Transcriptional regulation of SSA3, an HSP70 gene from Saccharomyces
RT cerevisiae.";
RL Mol. Cell. Biol. 10:3262-3267(1990).
RN [6]
RP FUNCTION, AND SUBUNIT.
RX PubMed=11720285;
RA Gottschalk A., Kastner B., Luhrmann R., Fabrizio P.;
RT "The yeast U5 snRNP coisolated with the U1 snRNP has an unexpected protein
RT composition and includes the splicing factor Aar2p.";
RL RNA 7:1554-1565(2001).
RN [7]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), INTERACTION WITH PRP8,
RP PHOSPHORYLATION AT SER-253; THR-274; TYR-328; SER-331 AND THR-345,
RP IDENTIFICATION BY MASS SPECTROMETRY, AND MUTAGENESIS OF SER-253.
RX PubMed=21764848; DOI=10.1101/gad.635911;
RA Weber G., Cristao V.F., de Lima Alves F., Santos K.F., Holton N.,
RA Rappsilber J., Beggs J.D., Wahl M.C.;
RT "Mechanism for Aar2p function as a U5 snRNP assembly factor.";
RL Genes Dev. 25:1601-1612(2011).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH PRP8, AND INTERACTION
RP WITH PRP8.
RX PubMed=23354046; DOI=10.1038/nature11843;
RA Galej W.P., Oubridge C., Newman A.J., Nagai K.;
RT "Crystal structure of Prp8 reveals active site cavity of the spliceosome.";
RL Nature 493:638-643(2013).
CC -!- FUNCTION: Component of the U5 snRNP complex that is required for
CC spliceosome assembly and for pre-mRNA splicing. Involved in splicing
CC pre-mRNA of the A1 cistron and other genes that are important for cell
CC growth. {ECO:0000269|PubMed:11720285, ECO:0000269|PubMed:1922071}.
CC -!- SUBUNIT: Heterodimer (Probable). Interacts with PRP8 (via RNase H
CC homology domain and MPN domain), competing with BRR2 for the same
CC binding site. Component of a U5 snRNP complex that contains at least
CC the U5 snRNA, PRP8, SNU114, AAR2, SMB1, SMD1, SMD2, SMD3, SME1, SMX2
CC and SMX3, but is not a component of the U4/U6-U5 tri-snRNP complex.
CC {ECO:0000269|PubMed:11720285, ECO:0000269|PubMed:21764848,
CC ECO:0000269|PubMed:23354046, ECO:0000305}.
CC -!- INTERACTION:
CC P32357; P33334: PRP8; NbExp=11; IntAct=EBI-340, EBI-465;
CC P32357; P36048: SNU114; NbExp=3; IntAct=EBI-340, EBI-243;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=This protein lacks a
CC nuclear localization signal, it may interact in the cytoplasm with a
CC component of spliceosomes via the leucine-zipper and then be
CC transported into the nucleus.
CC -!- PTM: Phosphorylated on serine and tyrosine residues.
CC {ECO:0000269|PubMed:21764848}.
CC -!- MISCELLANEOUS: Present with 7330 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the AAR2 family. {ECO:0000305}.
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DR EMBL; D90455; BAA14421.1; -; Genomic_DNA.
DR EMBL; Z26879; CAA81524.1; -; Genomic_DNA.
DR EMBL; Z35835; CAA84894.1; -; Genomic_DNA.
DR EMBL; M36115; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BK006936; DAA07048.1; -; Genomic_DNA.
DR PIR; S18510; S18510.
DR RefSeq; NP_009479.1; NM_001178314.1.
DR PDB; 3SBS; X-ray; 2.10 A; A=1-355.
DR PDB; 3SBT; X-ray; 1.80 A; B=1-355.
DR PDB; 3ZEF; X-ray; 3.10 A; A/D=1-355.
DR PDB; 4I43; X-ray; 2.00 A; A=1-355.
DR PDB; 4ILG; X-ray; 2.10 A; A=1-355.
DR PDB; 4ILH; X-ray; 1.85 A; B=1-331.
DR PDB; 4ILI; X-ray; 3.20 A; A/B=1-318.
DR PDB; 5QY1; X-ray; 1.72 A; B=1-152, B=171-317.
DR PDB; 5QY2; X-ray; 1.36 A; B=1-152, B=171-317.
DR PDB; 5QY3; X-ray; 1.58 A; B=1-152, B=171-317.
DR PDB; 5QY4; X-ray; 1.57 A; B=1-152, B=171-317.
DR PDB; 5QY5; X-ray; 1.51 A; B=1-152, B=171-317.
DR PDB; 5QY6; X-ray; 1.51 A; B=1-152, B=171-317.
DR PDB; 5QY7; X-ray; 1.67 A; B=1-152, B=171-317.
DR PDB; 5QY8; X-ray; 1.59 A; B=1-152, B=171-317.
DR PDB; 5QY9; X-ray; 1.40 A; B=1-152, B=171-317.
DR PDB; 5QYA; X-ray; 1.55 A; B=1-152, B=171-317.
DR PDB; 5QYB; X-ray; 2.10 A; B=1-152, B=171-317.
DR PDB; 5QYC; X-ray; 1.70 A; B=1-152, B=171-317.
DR PDB; 5QYD; X-ray; 1.67 A; B=1-152, B=171-317.
DR PDB; 5QYE; X-ray; 1.51 A; B=1-152, B=171-317.
DR PDB; 5QYF; X-ray; 1.49 A; B=1-152, B=171-317.
DR PDB; 5QYG; X-ray; 1.67 A; B=1-152, B=171-317.
DR PDB; 5QYH; X-ray; 1.47 A; B=1-152, B=171-317.
DR PDB; 5QYI; X-ray; 1.58 A; B=1-152, B=171-317.
DR PDB; 5QYJ; X-ray; 1.51 A; B=1-152, B=171-317.
DR PDB; 5QYK; X-ray; 1.63 A; B=1-152, B=171-317.
DR PDB; 5QYL; X-ray; 1.56 A; B=1-152, B=171-317.
DR PDB; 5QYM; X-ray; 1.47 A; B=1-152, B=171-317.
DR PDB; 5QYN; X-ray; 1.65 A; B=1-152, B=171-317.
DR PDB; 5QYO; X-ray; 1.58 A; B=1-152, B=171-317.
DR PDB; 5QYP; X-ray; 1.61 A; B=1-152, B=171-317.
DR PDB; 5QYQ; X-ray; 1.67 A; B=1-152, B=171-317.
DR PDB; 5QYR; X-ray; 1.54 A; B=1-152, B=171-317.
DR PDB; 5QYS; X-ray; 1.52 A; B=1-152, B=171-317.
DR PDB; 5QYT; X-ray; 1.52 A; B=1-152, B=171-317.
DR PDB; 5QYU; X-ray; 1.51 A; B=1-152, B=171-317.
DR PDB; 5QYV; X-ray; 1.59 A; B=1-152, B=171-317.
DR PDB; 5QYW; X-ray; 1.63 A; B=1-152, B=171-317.
DR PDB; 5QYX; X-ray; 1.60 A; B=1-152, B=171-317.
DR PDB; 5QYY; X-ray; 1.71 A; B=1-152, B=171-317.
DR PDB; 5QYZ; X-ray; 1.37 A; B=1-152, B=171-317.
DR PDB; 5QZ0; X-ray; 1.57 A; B=1-152, B=171-317.
DR PDB; 5QZ1; X-ray; 1.58 A; B=1-152, B=171-317.
DR PDB; 5QZ2; X-ray; 1.54 A; B=1-152, B=171-317.
DR PDB; 5QZ3; X-ray; 1.53 A; B=1-152, B=171-317.
DR PDB; 5QZ4; X-ray; 1.75 A; B=1-152, B=171-317.
DR PDB; 5QZ5; X-ray; 1.51 A; B=1-152, B=171-317.
DR PDB; 5QZ6; X-ray; 1.32 A; B=1-152, B=171-317.
DR PDB; 5QZ7; X-ray; 1.48 A; B=1-152, B=171-317.
DR PDB; 5QZ8; X-ray; 1.62 A; B=1-152, B=171-317.
DR PDB; 5QZ9; X-ray; 1.43 A; B=1-152, B=171-317.
DR PDB; 5QZA; X-ray; 1.51 A; B=1-152, B=171-317.
DR PDB; 5QZB; X-ray; 1.69 A; B=1-152, B=171-317.
DR PDB; 5QZC; X-ray; 1.72 A; B=1-152, B=171-317.
DR PDB; 5QZD; X-ray; 1.59 A; B=1-152, B=171-317.
DR PDB; 5QZE; X-ray; 1.55 A; B=1-152, B=171-317.
DR PDB; 5QZF; X-ray; 1.68 A; B=1-152, B=171-317.
DR PDB; 5QZG; X-ray; 1.55 A; B=1-152, B=171-317.
DR PDB; 5QZH; X-ray; 1.77 A; B=1-152, B=171-317.
DR PDB; 5QZI; X-ray; 1.51 A; B=1-152, B=171-317.
DR PDB; 5QZJ; X-ray; 1.51 A; B=1-152, B=171-317.
DR PDB; 5QZK; X-ray; 1.73 A; B=1-152, B=171-317.
DR PDB; 5QZL; X-ray; 1.54 A; B=1-152, B=171-317.
DR PDB; 5QZM; X-ray; 1.66 A; B=1-152, B=171-317.
DR PDB; 5QZN; X-ray; 1.44 A; B=1-152, B=171-317.
DR PDB; 5QZO; X-ray; 1.39 A; B=1-152, B=171-317.
DR PDB; 5QZP; X-ray; 1.50 A; B=1-152, B=171-317.
DR PDB; 5QZQ; X-ray; 2.11 A; B=1-152, B=171-317.
DR PDB; 5QZR; X-ray; 1.59 A; B=1-152, B=171-317.
DR PDB; 5QZS; X-ray; 1.58 A; B=1-152, B=171-317.
DR PDB; 5QZT; X-ray; 1.53 A; B=1-152, B=171-317.
DR PDB; 5QZU; X-ray; 1.54 A; B=1-152, B=171-317.
DR PDB; 5QZV; X-ray; 2.11 A; B=1-152, B=171-317.
DR PDB; 5QZW; X-ray; 1.36 A; B=1-152, B=171-317.
DR PDB; 5QZX; X-ray; 1.55 A; B=1-152, B=171-317.
DR PDB; 5QZY; X-ray; 1.66 A; B=1-152, B=171-317.
DR PDB; 5QZZ; X-ray; 1.59 A; B=1-152, B=171-317.
DR PDB; 5R00; X-ray; 1.72 A; B=1-152, B=171-317.
DR PDB; 5R01; X-ray; 1.72 A; B=1-152, B=171-317.
DR PDB; 5R02; X-ray; 1.66 A; B=1-152, B=171-317.
DR PDB; 5R03; X-ray; 1.51 A; B=1-152, B=171-317.
DR PDB; 5R04; X-ray; 1.34 A; B=1-152, B=171-317.
DR PDB; 5R05; X-ray; 1.57 A; B=1-152, B=171-317.
DR PDB; 5R06; X-ray; 1.67 A; B=1-152, B=171-317.
DR PDB; 5R07; X-ray; 1.71 A; B=1-152, B=171-317.
DR PDB; 5R08; X-ray; 1.70 A; B=1-317.
DR PDB; 5R09; X-ray; 1.56 A; B=1-317.
DR PDB; 5R0A; X-ray; 1.54 A; B=1-317.
DR PDB; 5R0B; X-ray; 1.82 A; B=1-317.
DR PDB; 5R0C; X-ray; 1.60 A; B=1-317.
DR PDB; 5R0D; X-ray; 1.27 A; B=1-317.
DR PDB; 5R0E; X-ray; 1.59 A; B=1-317.
DR PDB; 5R0F; X-ray; 1.97 A; B=1-317.
DR PDB; 5R0G; X-ray; 1.73 A; B=1-317.
DR PDB; 5R0H; X-ray; 1.57 A; B=1-317.
DR PDB; 5R0I; X-ray; 1.86 A; B=1-317.
DR PDB; 5R0J; X-ray; 1.81 A; B=1-317.
DR PDB; 5R0K; X-ray; 1.80 A; B=1-317.
DR PDB; 5R0L; X-ray; 1.70 A; B=1-317.
DR PDB; 5R0M; X-ray; 1.70 A; B=1-317.
DR PDB; 5R0N; X-ray; 1.78 A; B=1-317.
DR PDB; 5R0O; X-ray; 1.86 A; B=1-317.
DR PDB; 5R0P; X-ray; 1.73 A; B=1-317.
DR PDB; 5R0Q; X-ray; 1.91 A; B=1-317.
DR PDB; 5R0R; X-ray; 1.73 A; B=1-317.
DR PDB; 5R0S; X-ray; 1.81 A; B=1-317.
DR PDB; 5R0T; X-ray; 1.96 A; B=1-317.
DR PDB; 5R0U; X-ray; 1.86 A; B=1-317.
DR PDB; 5R0V; X-ray; 1.81 A; B=1-317.
DR PDB; 5R0W; X-ray; 1.86 A; B=1-317.
DR PDB; 5R0X; X-ray; 1.84 A; B=1-317.
DR PDB; 5R0Y; X-ray; 1.75 A; B=1-317.
DR PDB; 5R0Z; X-ray; 1.86 A; B=1-317.
DR PDB; 5R10; X-ray; 1.70 A; B=1-317.
DR PDB; 5R11; X-ray; 1.82 A; B=1-317.
DR PDB; 5R12; X-ray; 1.70 A; B=1-317.
DR PDB; 5R13; X-ray; 1.87 A; B=1-317.
DR PDB; 5R14; X-ray; 1.74 A; B=1-317.
DR PDB; 5R15; X-ray; 1.79 A; B=1-317.
DR PDB; 5R16; X-ray; 1.84 A; B=1-317.
DR PDB; 5R17; X-ray; 1.87 A; B=1-317.
DR PDB; 5R18; X-ray; 1.79 A; B=1-317.
DR PDB; 5R19; X-ray; 1.70 A; B=1-317.
DR PDB; 5R1A; X-ray; 1.73 A; B=1-317.
DR PDB; 5R1B; X-ray; 1.89 A; B=1-317.
DR PDB; 5R1C; X-ray; 1.91 A; B=1-317.
DR PDB; 5R1D; X-ray; 1.82 A; B=1-317.
DR PDB; 5R1E; X-ray; 1.70 A; B=1-317.
DR PDB; 5R1F; X-ray; 1.80 A; B=1-317.
DR PDB; 5R1G; X-ray; 1.81 A; B=1-317.
DR PDB; 5R1H; X-ray; 2.06 A; B=1-317.
DR PDB; 5R1I; X-ray; 2.01 A; B=1-317.
DR PDB; 5R1J; X-ray; 1.96 A; B=1-317.
DR PDB; 5R1K; X-ray; 1.99 A; B=1-317.
DR PDB; 5R1L; X-ray; 1.94 A; B=1-317.
DR PDB; 5R1M; X-ray; 1.90 A; B=1-317.
DR PDB; 5R1N; X-ray; 1.94 A; B=1-317.
DR PDB; 5R1O; X-ray; 1.90 A; B=1-317.
DR PDB; 5R1P; X-ray; 1.95 A; B=1-317.
DR PDB; 5R1Q; X-ray; 1.86 A; B=1-317.
DR PDB; 5R1S; X-ray; 2.05 A; B=1-317.
DR PDBsum; 3SBS; -.
DR PDBsum; 3SBT; -.
DR PDBsum; 3ZEF; -.
DR PDBsum; 4I43; -.
DR PDBsum; 4ILG; -.
DR PDBsum; 4ILH; -.
DR PDBsum; 4ILI; -.
DR PDBsum; 5QY1; -.
DR PDBsum; 5QY2; -.
DR PDBsum; 5QY3; -.
DR PDBsum; 5QY4; -.
DR PDBsum; 5QY5; -.
DR PDBsum; 5QY6; -.
DR PDBsum; 5QY7; -.
DR PDBsum; 5QY8; -.
DR PDBsum; 5QY9; -.
DR PDBsum; 5QYA; -.
DR PDBsum; 5QYB; -.
DR PDBsum; 5QYC; -.
DR PDBsum; 5QYD; -.
DR PDBsum; 5QYE; -.
DR PDBsum; 5QYF; -.
DR PDBsum; 5QYG; -.
DR PDBsum; 5QYH; -.
DR PDBsum; 5QYI; -.
DR PDBsum; 5QYJ; -.
DR PDBsum; 5QYK; -.
DR PDBsum; 5QYL; -.
DR PDBsum; 5QYM; -.
DR PDBsum; 5QYN; -.
DR PDBsum; 5QYO; -.
DR PDBsum; 5QYP; -.
DR PDBsum; 5QYQ; -.
DR PDBsum; 5QYR; -.
DR PDBsum; 5QYS; -.
DR PDBsum; 5QYT; -.
DR PDBsum; 5QYU; -.
DR PDBsum; 5QYV; -.
DR PDBsum; 5QYW; -.
DR PDBsum; 5QYX; -.
DR PDBsum; 5QYY; -.
DR PDBsum; 5QYZ; -.
DR PDBsum; 5QZ0; -.
DR PDBsum; 5QZ1; -.
DR PDBsum; 5QZ2; -.
DR PDBsum; 5QZ3; -.
DR PDBsum; 5QZ4; -.
DR PDBsum; 5QZ5; -.
DR PDBsum; 5QZ6; -.
DR PDBsum; 5QZ7; -.
DR PDBsum; 5QZ8; -.
DR PDBsum; 5QZ9; -.
DR PDBsum; 5QZA; -.
DR PDBsum; 5QZB; -.
DR PDBsum; 5QZC; -.
DR PDBsum; 5QZD; -.
DR PDBsum; 5QZE; -.
DR PDBsum; 5QZF; -.
DR PDBsum; 5QZG; -.
DR PDBsum; 5QZH; -.
DR PDBsum; 5QZI; -.
DR PDBsum; 5QZJ; -.
DR PDBsum; 5QZK; -.
DR PDBsum; 5QZL; -.
DR PDBsum; 5QZM; -.
DR PDBsum; 5QZN; -.
DR PDBsum; 5QZO; -.
DR PDBsum; 5QZP; -.
DR PDBsum; 5QZQ; -.
DR PDBsum; 5QZR; -.
DR PDBsum; 5QZS; -.
DR PDBsum; 5QZT; -.
DR PDBsum; 5QZU; -.
DR PDBsum; 5QZV; -.
DR PDBsum; 5QZW; -.
DR PDBsum; 5QZX; -.
DR PDBsum; 5QZY; -.
DR PDBsum; 5QZZ; -.
DR PDBsum; 5R00; -.
DR PDBsum; 5R01; -.
DR PDBsum; 5R02; -.
DR PDBsum; 5R03; -.
DR PDBsum; 5R04; -.
DR PDBsum; 5R05; -.
DR PDBsum; 5R06; -.
DR PDBsum; 5R07; -.
DR PDBsum; 5R08; -.
DR PDBsum; 5R09; -.
DR PDBsum; 5R0A; -.
DR PDBsum; 5R0B; -.
DR PDBsum; 5R0C; -.
DR PDBsum; 5R0D; -.
DR PDBsum; 5R0E; -.
DR PDBsum; 5R0F; -.
DR PDBsum; 5R0G; -.
DR PDBsum; 5R0H; -.
DR PDBsum; 5R0I; -.
DR PDBsum; 5R0J; -.
DR PDBsum; 5R0K; -.
DR PDBsum; 5R0L; -.
DR PDBsum; 5R0M; -.
DR PDBsum; 5R0N; -.
DR PDBsum; 5R0O; -.
DR PDBsum; 5R0P; -.
DR PDBsum; 5R0Q; -.
DR PDBsum; 5R0R; -.
DR PDBsum; 5R0S; -.
DR PDBsum; 5R0T; -.
DR PDBsum; 5R0U; -.
DR PDBsum; 5R0V; -.
DR PDBsum; 5R0W; -.
DR PDBsum; 5R0X; -.
DR PDBsum; 5R0Y; -.
DR PDBsum; 5R0Z; -.
DR PDBsum; 5R10; -.
DR PDBsum; 5R11; -.
DR PDBsum; 5R12; -.
DR PDBsum; 5R13; -.
DR PDBsum; 5R14; -.
DR PDBsum; 5R15; -.
DR PDBsum; 5R16; -.
DR PDBsum; 5R17; -.
DR PDBsum; 5R18; -.
DR PDBsum; 5R19; -.
DR PDBsum; 5R1A; -.
DR PDBsum; 5R1B; -.
DR PDBsum; 5R1C; -.
DR PDBsum; 5R1D; -.
DR PDBsum; 5R1E; -.
DR PDBsum; 5R1F; -.
DR PDBsum; 5R1G; -.
DR PDBsum; 5R1H; -.
DR PDBsum; 5R1I; -.
DR PDBsum; 5R1J; -.
DR PDBsum; 5R1K; -.
DR PDBsum; 5R1L; -.
DR PDBsum; 5R1M; -.
DR PDBsum; 5R1N; -.
DR PDBsum; 5R1O; -.
DR PDBsum; 5R1P; -.
DR PDBsum; 5R1Q; -.
DR PDBsum; 5R1S; -.
DR AlphaFoldDB; P32357; -.
DR SMR; P32357; -.
DR BioGRID; 32628; 313.
DR ComplexPortal; CPX-30; U5 small nuclear ribonucleoprotein complex, AAR2 variant.
DR DIP; DIP-6642N; -.
DR IntAct; P32357; 8.
DR MINT; P32357; -.
DR STRING; 4932.YBL074C; -.
DR iPTMnet; P32357; -.
DR MaxQB; P32357; -.
DR PaxDb; P32357; -.
DR PRIDE; P32357; -.
DR EnsemblFungi; YBL074C_mRNA; YBL074C; YBL074C.
DR GeneID; 852205; -.
DR KEGG; sce:YBL074C; -.
DR SGD; S000000170; AAR2.
DR VEuPathDB; FungiDB:YBL074C; -.
DR eggNOG; KOG3937; Eukaryota.
DR GeneTree; ENSGT00390000007796; -.
DR HOGENOM; CLU_858447_0_0_1; -.
DR InParanoid; P32357; -.
DR OMA; GSSLQWH; -.
DR BioCyc; YEAST:G3O-28966-MON; -.
DR PRO; PR:P32357; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P32357; protein.
DR GO; GO:0005737; C:cytoplasm; IC:ComplexPortal.
DR GO; GO:0005682; C:U5 snRNP; IDA:SGD.
DR GO; GO:0000387; P:spliceosomal snRNP assembly; IC:ComplexPortal.
DR GO; GO:0000244; P:spliceosomal tri-snRNP complex assembly; IMP:SGD.
DR CDD; cd13778; Aar2_C; 1.
DR CDD; cd13777; Aar2_N; 1.
DR DisProt; DP02721; -.
DR Gene3D; 1.25.40.550; -; 1.
DR Gene3D; 2.60.34.20; -; 1.
DR InterPro; IPR007946; AAR2.
DR InterPro; IPR033648; AAR2_C.
DR InterPro; IPR038514; AAR2_C_sf.
DR InterPro; IPR033647; Aar2_N.
DR InterPro; IPR038516; AAR2_N_sf.
DR PANTHER; PTHR12689; PTHR12689; 1.
DR Pfam; PF05282; AAR2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; mRNA processing; mRNA splicing; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..355
FT /note="A1 cistron-splicing factor AAR2"
FT /id="PRO_0000209705"
FT REGION 261..282
FT /note="Leucine-zipper"
FT REGION 331..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 253
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:21764848"
FT MOD_RES 274
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:21764848"
FT MOD_RES 328
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:21764848"
FT MOD_RES 331
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:21764848"
FT MOD_RES 345
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:21764848"
FT MUTAGEN 253
FT /note="S->A: No effect on interaction with PRP8."
FT /evidence="ECO:0000269|PubMed:21764848"
FT MUTAGEN 253
FT /note="S->D,E: Disrupts interaction with PRP8."
FT /evidence="ECO:0000269|PubMed:21764848"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:5R0D"
FT STRAND 13..17
FT /evidence="ECO:0007829|PDB:5R0D"
FT STRAND 20..24
FT /evidence="ECO:0007829|PDB:5R0D"
FT STRAND 32..36
FT /evidence="ECO:0007829|PDB:5R0D"
FT STRAND 38..40
FT /evidence="ECO:0007829|PDB:3SBS"
FT STRAND 42..48
FT /evidence="ECO:0007829|PDB:5R0D"
FT STRAND 51..60
FT /evidence="ECO:0007829|PDB:5R0D"
FT HELIX 62..64
FT /evidence="ECO:0007829|PDB:5R0D"
FT STRAND 67..72
FT /evidence="ECO:0007829|PDB:5R0D"
FT TURN 73..76
FT /evidence="ECO:0007829|PDB:5R0D"
FT STRAND 77..82
FT /evidence="ECO:0007829|PDB:5R0D"
FT HELIX 86..98
FT /evidence="ECO:0007829|PDB:5R0D"
FT STRAND 102..104
FT /evidence="ECO:0007829|PDB:5R0D"
FT HELIX 113..118
FT /evidence="ECO:0007829|PDB:5R0D"
FT HELIX 123..129
FT /evidence="ECO:0007829|PDB:5R0D"
FT STRAND 136..141
FT /evidence="ECO:0007829|PDB:5R0D"
FT HELIX 147..151
FT /evidence="ECO:0007829|PDB:5R0D"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:4ILI"
FT HELIX 172..174
FT /evidence="ECO:0007829|PDB:5R0D"
FT STRAND 183..185
FT /evidence="ECO:0007829|PDB:5R0D"
FT TURN 186..188
FT /evidence="ECO:0007829|PDB:5R0D"
FT HELIX 194..199
FT /evidence="ECO:0007829|PDB:5R0D"
FT HELIX 202..206
FT /evidence="ECO:0007829|PDB:5R0D"
FT HELIX 207..214
FT /evidence="ECO:0007829|PDB:5R0D"
FT HELIX 217..234
FT /evidence="ECO:0007829|PDB:5R0D"
FT HELIX 237..251
FT /evidence="ECO:0007829|PDB:5R0D"
FT HELIX 258..274
FT /evidence="ECO:0007829|PDB:5R0D"
FT HELIX 277..279
FT /evidence="ECO:0007829|PDB:5R0D"
FT HELIX 280..283
FT /evidence="ECO:0007829|PDB:5R0D"
FT HELIX 286..294
FT /evidence="ECO:0007829|PDB:5R0D"
FT TURN 297..300
FT /evidence="ECO:0007829|PDB:5R0D"
FT HELIX 303..312
FT /evidence="ECO:0007829|PDB:5R0D"
FT TURN 314..316
FT /evidence="ECO:0007829|PDB:5R0D"
FT STRAND 345..353
FT /evidence="ECO:0007829|PDB:4I43"
SQ SEQUENCE 355 AA; 41688 MW; 1F030D821D974131 CRC64;
MNTVPFTSAP IEVTIGIDQY SFNVKENQPF HGIKDIPIGH VHVIHFQHAD NSSMRYGYWF
DCRMGNFYIQ YDPKDGLYKM MEERDGAKFE NIVHNFKERQ MMVSYPKIDE DDTWYNLTEF
VQMDKIRKIV RKDENQFSYV DSSMTTVQEN ELLKSSLQKA GSKMEAKNED DPAHSLNYTV
INFKSREAIR PGHEMEDFLD KSYYLNTVML QGIFKNSSNY FGELQFAFLN AMFFGNYGSS
LQWHAMIELI CSSATVPKHM LDKLDEILYY QIKTLPEQYS DILLNERVWN ICLYSSFQKN
SLHNTEKIME NKYPELLGKD NEDDALIYGI SDEERDDEDD EHNPTIVGGL YYQRP
