RU2A_HUMAN
ID RU2A_HUMAN Reviewed; 255 AA.
AC P09661; B2R5I6; Q8TBD2;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-MAY-2003, sequence version 2.
DT 03-AUG-2022, entry version 213.
DE RecName: Full=U2 small nuclear ribonucleoprotein A';
DE Short=U2 snRNP A' {ECO:0000303|PubMed:2928112, ECO:0000303|PubMed:9716128};
GN Name=SNRPA1;
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 [MRNA].
RX PubMed=2928112; DOI=10.1093/nar/17.5.1893;
RA Sillekens P.T.G., Beijer R.P., Habets W.J., van Venrooij W.J.;
RT "Molecular cloning of the cDNA for the human U2 snRNA-specific A'
RT protein.";
RL Nucleic Acids Res. 17:1893-1906(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skeletal muscle;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Muscle, and Urinary bladder;
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 [5]
RP PROTEIN SEQUENCE OF 2-20; 114-122; 133-143 AND 222-232, CLEAVAGE OF
RP INITIATOR METHIONINE, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Colon carcinoma;
RA Bienvenut W.V., Heiserich L., Gottlieb E.;
RL Submitted (MAR-2008) to UniProtKB.
RN [6]
RP IDENTIFICATION IN A MRNA SPLICING COMPLEX WITH SFRS4; SFRS5; SNRNP70; SRRM1
RP AND SRRM2.
RX PubMed=9531537; DOI=10.1101/gad.12.7.996;
RA Blencowe B.J., Issner R., Nickerson J.A., Sharp P.A.;
RT "A coactivator of pre-mRNA splicing.";
RL Genes Dev. 12:996-1009(1998).
RN [7]
RP IDENTIFICATION IN A MRNA EXONIC SPLICING ENHANCER (ESE) COMPLEX WITH
RP SNRNP70; SRRM1 AND TRA2B.
RX PubMed=10339552; DOI=10.1073/pnas.96.11.6125;
RA Eldridge A.G., Li Y., Sharp P.A., Blencowe B.J.;
RT "The SRm160/300 splicing coactivator is required for exon-enhancer
RT function.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:6125-6130(1999).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SPLICEOSOMAL C
RP COMPLEX, FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=11991638; DOI=10.1017/s1355838202021088;
RA Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.;
RT "Purification and characterization of native spliceosomes suitable for
RT three-dimensional structural analysis.";
RL RNA 8:426-439(2002).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178, 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-172, 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197, 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 [14]
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 [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197; SER-236 AND SER-255, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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 [17]
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 [18]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-172 AND LYS-221, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.38 ANGSTROMS) OF 1-176 IN COMPLEX WITH SNRPB2 AND
RP U2 SMALL NUCLEAR RNA, SUBUNIT, AND FUNCTION.
RX PubMed=9716128; DOI=10.1038/29234;
RA Price S.R., Evans P.R., Nagai K.;
RT "Crystal structure of the spliceosomal U2B'-U2A' protein complex bound to a
RT fragment of U2 small nuclear RNA.";
RL Nature 394:645-650(1998).
RN [20]
RP FUNCTION, SUBUNIT, AND MUTAGENESIS OF TYR-15; ARG-27; THR-68; ASN-72;
RP ASN-73; GLU-92 AND GLN-148.
RX PubMed=27035939; DOI=10.1073/pnas.1513682113;
RA Wu H., Sun L., Wen Y., Liu Y., Yu J., Mao F., Wang Y., Tong C., Guo X.,
RA Hu Z., Sha J., Liu M., Xia L.;
RT "Major spliceosome defects cause male infertility and are associated with
RT nonobstructive azoospermia in humans.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:4134-4139(2016).
RN [21] {ECO:0007744|PDB:5XJC}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.60 ANGSTROMS), FUNCTION, SUBUNIT, AND
RP SUBCELLULAR LOCATION.
RX PubMed=28502770; DOI=10.1016/j.cell.2017.04.033;
RA Zhang X., Yan C., Hang J., Finci L.I., Lei J., Shi Y.;
RT "An Atomic Structure of the Human Spliceosome.";
RL Cell 169:918-929(2017).
RN [22] {ECO:0007744|PDB:5O9Z}
RP STRUCTURE BY ELECTRON MICROSCOPY (4.50 ANGSTROMS), FUNCTION, IDENTIFICATION
RP BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=28781166; DOI=10.1016/j.cell.2017.07.011;
RA Bertram K., Agafonov D.E., Dybkov O., Haselbach D., Leelaram M.N.,
RA Will C.L., Urlaub H., Kastner B., Luhrmann R., Stark H.;
RT "Cryo-EM Structure of a Pre-catalytic Human Spliceosome Primed for
RT Activation.";
RL Cell 170:701-713(2017).
RN [23] {ECO:0007744|PDB:5MQF}
RP STRUCTURE BY ELECTRON MICROSCOPY (5.90 ANGSTROMS), FUNCTION, SUBUNIT,
RP SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=28076346; DOI=10.1038/nature21079;
RA Bertram K., Agafonov D.E., Liu W.T., Dybkov O., Will C.L., Hartmuth K.,
RA Urlaub H., Kastner B., Stark H., Luhrmann R.;
RT "Cryo-EM structure of a human spliceosome activated for step 2 of
RT splicing.";
RL Nature 542:318-323(2017).
CC -!- FUNCTION: Involved in pre-mRNA splicing as component of the spliceosome
CC (PubMed:11991638, PubMed:28502770, PubMed:28781166, PubMed:28076346,
CC PubMed:27035939). Associated with sn-RNP U2, where it contributes to
CC the binding of stem loop IV of U2 snRNA (PubMed:9716128,
CC PubMed:27035939). {ECO:0000269|PubMed:11991638,
CC ECO:0000269|PubMed:27035939, ECO:0000269|PubMed:28076346,
CC ECO:0000269|PubMed:28502770, ECO:0000269|PubMed:28781166,
CC ECO:0000269|PubMed:9716128}.
CC -!- SUBUNIT: Identified in the spliceosome B complex (PubMed:28781166).
CC Identified in the spliceosome C complex (PubMed:11991638,
CC PubMed:28502770, PubMed:28076346). Found in a pre-mRNA splicing complex
CC with SFRS4, SFRS5, SNRNP70, SNRPA1, SRRM1 and SRRM2 (PubMed:9531537).
CC Found in a pre-mRNA exonic splicing enhancer (ESE) complex with
CC SNRNP70, SNRPA1, SRRM1 and TRA2B (PubMed:10339552). Contributes to the
CC binding of stem loop IV of U2 snRNA with SNRPB2 (PubMed:9716128,
CC PubMed:27035939). {ECO:0000269|PubMed:10339552,
CC ECO:0000269|PubMed:11991638, ECO:0000269|PubMed:27035939,
CC ECO:0000269|PubMed:28076346, ECO:0000269|PubMed:28502770,
CC ECO:0000269|PubMed:28781166, ECO:0000269|PubMed:9531537,
CC ECO:0000269|PubMed:9716128}.
CC -!- INTERACTION:
CC P09661; Q13422-7: IKZF1; NbExp=3; IntAct=EBI-876439, EBI-11522367;
CC P09661; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-876439, EBI-79165;
CC P09661; Q15428: SF3A2; NbExp=2; IntAct=EBI-876439, EBI-2462271;
CC P09661; P09012: SNRPA; NbExp=9; IntAct=EBI-876439, EBI-607085;
CC P09661; P08579: SNRPB2; NbExp=4; IntAct=EBI-876439, EBI-1053651;
CC P09661; Q9HCS7: XAB2; NbExp=2; IntAct=EBI-876439, EBI-295232;
CC P09661; Q8N5A5-2: ZGPAT; NbExp=3; IntAct=EBI-876439, EBI-10183064;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11991638,
CC ECO:0000269|PubMed:28076346, ECO:0000269|PubMed:28502770,
CC ECO:0000269|PubMed:28781166}.
CC -!- SIMILARITY: Belongs to the U2 small nuclear ribonucleoprotein A family.
CC {ECO:0000305}.
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DR EMBL; X13482; CAA31838.1; -; mRNA.
DR EMBL; AK312200; BAG35133.1; -; mRNA.
DR EMBL; CH471101; EAX02300.1; -; Genomic_DNA.
DR EMBL; BC022816; AAH22816.1; -; mRNA.
DR EMBL; BC071717; AAH71717.1; -; mRNA.
DR CCDS; CCDS10391.1; -.
DR PIR; S03616; S03616.
DR RefSeq; NP_003081.2; NM_003090.3.
DR PDB; 1A9N; X-ray; 2.38 A; A/C=1-176.
DR PDB; 5MQF; EM; 5.90 A; W=1-255.
DR PDB; 5O9Z; EM; 4.50 A; z=1-255.
DR PDB; 5XJC; EM; 3.60 A; o=1-255.
DR PDB; 5YZG; EM; 4.10 A; o=1-255.
DR PDB; 5Z56; EM; 5.10 A; o=1-255.
DR PDB; 5Z57; EM; 6.50 A; o=1-255.
DR PDB; 5Z58; EM; 4.90 A; o=1-255.
DR PDB; 6AH0; EM; 5.70 A; o=1-255.
DR PDB; 6AHD; EM; 3.80 A; o=1-255.
DR PDB; 6FF7; EM; 4.50 A; W=1-255.
DR PDB; 6ICZ; EM; 3.00 A; o=1-255.
DR PDB; 6ID0; EM; 2.90 A; o=1-255.
DR PDB; 6ID1; EM; 2.86 A; o=1-255.
DR PDB; 6QDV; EM; 3.30 A; W=2-162.
DR PDB; 6QX9; EM; 3.28 A; 2A=1-255.
DR PDB; 6Y53; EM; 7.10 A; a=1-255.
DR PDB; 6Y5Q; EM; 7.10 A; a=1-255.
DR PDB; 7A5P; EM; 5.00 A; W=1-255.
DR PDB; 7ABG; EM; 7.80 A; W=1-255.
DR PDB; 7ABI; EM; 8.00 A; W=1-255.
DR PDBsum; 1A9N; -.
DR PDBsum; 5MQF; -.
DR PDBsum; 5O9Z; -.
DR PDBsum; 5XJC; -.
DR PDBsum; 5YZG; -.
DR PDBsum; 5Z56; -.
DR PDBsum; 5Z57; -.
DR PDBsum; 5Z58; -.
DR PDBsum; 6AH0; -.
DR PDBsum; 6AHD; -.
DR PDBsum; 6FF7; -.
DR PDBsum; 6ICZ; -.
DR PDBsum; 6ID0; -.
DR PDBsum; 6ID1; -.
DR PDBsum; 6QDV; -.
DR PDBsum; 6QX9; -.
DR PDBsum; 6Y53; -.
DR PDBsum; 6Y5Q; -.
DR PDBsum; 7A5P; -.
DR PDBsum; 7ABG; -.
DR PDBsum; 7ABI; -.
DR AlphaFoldDB; P09661; -.
DR SMR; P09661; -.
DR BioGRID; 112511; 248.
DR ComplexPortal; CPX-2539; U2 small nuclear ribonucleoprotein complex.
DR CORUM; P09661; -.
DR DIP; DIP-625N; -.
DR IntAct; P09661; 91.
DR MINT; P09661; -.
DR STRING; 9606.ENSP00000254193; -.
DR GlyGen; P09661; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P09661; -.
DR MetOSite; P09661; -.
DR PhosphoSitePlus; P09661; -.
DR SwissPalm; P09661; -.
DR BioMuta; SNRPA1; -.
DR DMDM; 31077165; -.
DR EPD; P09661; -.
DR jPOST; P09661; -.
DR MassIVE; P09661; -.
DR MaxQB; P09661; -.
DR PaxDb; P09661; -.
DR PeptideAtlas; P09661; -.
DR PRIDE; P09661; -.
DR ProteomicsDB; 52261; -.
DR Antibodypedia; 29301; 116 antibodies from 25 providers.
DR DNASU; 6627; -.
DR Ensembl; ENST00000254193.11; ENSP00000254193.6; ENSG00000131876.18.
DR GeneID; 6627; -.
DR KEGG; hsa:6627; -.
DR MANE-Select; ENST00000254193.11; ENSP00000254193.6; NM_003090.4; NP_003081.2.
DR UCSC; uc002bww.4; human.
DR CTD; 6627; -.
DR DisGeNET; 6627; -.
DR GeneCards; SNRPA1; -.
DR HGNC; HGNC:11152; SNRPA1.
DR HPA; ENSG00000131876; Low tissue specificity.
DR MIM; 603521; gene.
DR neXtProt; NX_P09661; -.
DR OpenTargets; ENSG00000131876; -.
DR PharmGKB; PA35994; -.
DR VEuPathDB; HostDB:ENSG00000131876; -.
DR eggNOG; KOG1644; Eukaryota.
DR GeneTree; ENSGT00940000153289; -.
DR HOGENOM; CLU_061027_0_1_1; -.
DR OMA; PNYREYM; -.
DR OrthoDB; 1447031at2759; -.
DR PhylomeDB; P09661; -.
DR TreeFam; TF313776; -.
DR PathwayCommons; P09661; -.
DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-HSA-8950505; Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation.
DR SignaLink; P09661; -.
DR BioGRID-ORCS; 6627; 784 hits in 1013 CRISPR screens.
DR ChiTaRS; SNRPA1; human.
DR EvolutionaryTrace; P09661; -.
DR GeneWiki; SNRPA1; -.
DR GenomeRNAi; 6627; -.
DR Pharos; P09661; Tbio.
DR PRO; PR:P09661; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; P09661; protein.
DR Bgee; ENSG00000131876; Expressed in left testis and 94 other tissues.
DR ExpressionAtlas; P09661; baseline and differential.
DR Genevisible; P09661; HS.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0030532; C:small nuclear ribonucleoprotein complex; TAS:ProtInc.
DR GO; GO:0005681; C:spliceosomal complex; IDA:HGNC-UCL.
DR GO; GO:0005686; C:U2 snRNP; IBA:GO_Central.
DR GO; GO:0071007; C:U2-type catalytic step 2 spliceosome; IDA:UniProtKB.
DR GO; GO:0071005; C:U2-type precatalytic spliceosome; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0030620; F:U2 snRNA binding; IBA:GO_Central.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IDA:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; TAS:ProtInc.
DR GO; GO:0007283; P:spermatogenesis; IGI:UniProtKB.
DR GO; GO:1903241; P:U2-type prespliceosome assembly; IC:ComplexPortal.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR044640; RU2A.
DR InterPro; IPR003603; U2A'_phosphoprotein32A_C.
DR PANTHER; PTHR10552; PTHR10552; 1.
DR SMART; SM00446; LRRcap; 1.
DR PROSITE; PS51450; LRR; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing; Isopeptide bond;
KW Leucine-rich repeat; mRNA processing; mRNA splicing; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Ribonucleoprotein; RNA-binding;
KW Spliceosome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.5"
FT CHAIN 2..255
FT /note="U2 small nuclear ribonucleoprotein A'"
FT /id="PRO_0000074173"
FT REPEAT 20..41
FT /note="LRR 1"
FT REPEAT 43..64
FT /note="LRR 2"
FT REPEAT 65..86
FT /note="LRR 3"
FT REPEAT 89..110
FT /note="LRR 4"
FT DOMAIN 123..161
FT /note="LRRCT"
FT REGION 174..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 222..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 172
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 178
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 197
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19369195,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 236
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 255
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 172
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 221
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT MUTAGEN 15
FT /note="Y->D: Results in defective spliceosome assembly."
FT /evidence="ECO:0000269|PubMed:27035939"
FT MUTAGEN 27
FT /note="R->Q: No change in spliceosome assembly."
FT /evidence="ECO:0000269|PubMed:27035939"
FT MUTAGEN 68
FT /note="T->K: No change in spliceosome assembly."
FT /evidence="ECO:0000269|PubMed:27035939"
FT MUTAGEN 72
FT /note="N->K: No change in spliceosome assembly."
FT /evidence="ECO:0000269|PubMed:27035939"
FT MUTAGEN 73
FT /note="N->K: No change in spliceosome assembly."
FT /evidence="ECO:0000269|PubMed:27035939"
FT MUTAGEN 92
FT /note="E->V: Results in defective spliceosome assembly."
FT /evidence="ECO:0000269|PubMed:27035939"
FT MUTAGEN 148
FT /note="Q->R: Results in defective spliceosome assembly."
FT /evidence="ECO:0000269|PubMed:27035939"
FT CONFLICT 193
FT /note="K -> R (in Ref. 1; CAA31838)"
FT /evidence="ECO:0000305"
FT HELIX 6..10
FT /evidence="ECO:0007829|PDB:1A9N"
FT STRAND 14..16
FT /evidence="ECO:0007829|PDB:1A9N"
FT STRAND 22..25
FT /evidence="ECO:0007829|PDB:1A9N"
FT HELIX 37..40
FT /evidence="ECO:0007829|PDB:1A9N"
FT STRAND 45..48
FT /evidence="ECO:0007829|PDB:1A9N"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:1A9N"
FT HELIX 83..86
FT /evidence="ECO:0007829|PDB:1A9N"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:1A9N"
FT HELIX 103..111
FT /evidence="ECO:0007829|PDB:1A9N"
FT STRAND 117..119
FT /evidence="ECO:0007829|PDB:1A9N"
FT HELIX 124..127
FT /evidence="ECO:0007829|PDB:1A9N"
FT HELIX 131..138
FT /evidence="ECO:0007829|PDB:1A9N"
FT STRAND 143..145
FT /evidence="ECO:0007829|PDB:1A9N"
FT HELIX 152..160
FT /evidence="ECO:0007829|PDB:1A9N"
FT HELIX 165..172
FT /evidence="ECO:0007829|PDB:1A9N"
SQ SEQUENCE 255 AA; 28416 MW; 25902F07992B7209 CRC64;
MVKLTAELIE QAAQYTNAVR DRELDLRGYK IPVIENLGAT LDQFDAIDFS DNEIRKLDGF
PLLRRLKTLL VNNNRICRIG EGLDQALPCL TELILTNNSL VELGDLDPLA SLKSLTYLSI
LRNPVTNKKH YRLYVIYKVP QVRVLDFQKV KLKERQEAEK MFKGKRGAQL AKDIARRSKT
FNPGAGLPTD KKKGGPSPGD VEAIKNAIAN ASTLAEVERL KGLLQSGQIP GRERRSGPTD
DGEEEMEEDT VTNGS
