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 25-JAN-2012, entry version 124. DE RecName: Full=U2 small nuclear ribonucleoprotein A'; DE Short=U2 snRNP A'; GN Name=SNRPA1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=89183600; 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., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA 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., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., 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., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA 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 RT project: 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 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; RP SRRM1 AND SRRM2. RX PubMed=9531537; 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 MEDLINE=99272658; 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, AND IDENTIFICATION IN THE RP SPLICEOSOMAL C COMPLEX. 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-197, AND MASS RP SPECTROMETRY. RC TISSUE=Cervix carcinoma; RX PubMed=16964243; DOI=10.1038/nbt1240; RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; RT "A probability-based approach for high-throughput protein RT phosphorylation analysis and site localization."; RL Nat. Biotechnol. 24:1285-1292(2006). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197, AND MASS RP SPECTROMETRY. 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 [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178 AND SER-197, AND RP MASS SPECTROMETRY. 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 [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197, AND MASS RP SPECTROMETRY. 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 [13] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-172, AND MASS SPECTROMETRY. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., 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 [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., RA Buerckstuemmer T., 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 X-RAY CRYSTALLOGRAPHY (2.38 ANGSTROMS) OF 1-176. RX MEDLINE=98379985; 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 RT to a fragment of U2 small nuclear RNA."; RL Nature 394:645-650(1998). CC -!- FUNCTION: This protein is associated with sn-RNP U2. It helps the CC A' protein to bind stem loop IV of U2 snRNA. CC -!- SUBUNIT: Identified in the spliceosome C complex. Found in a pre- CC mRNA splicing complex with SFRS4, SFRS5, SNRNP70, SNRPA1, SRRM1 CC and SRRM2. Found in a pre-mRNA exonic splicing enhancer (ESE) CC complex with SNRNP70, SNRPA1, SRRM1 and TRA2B. CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- SIMILARITY: Belongs to the U2 small nuclear ribonucleoprotein A CC family. CC -!- SIMILARITY: Contains 4 LRR (leucine-rich) repeats. CC -!- SIMILARITY: Contains 1 LRRCT domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- 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 IPI; IPI00297477; -. DR PIR; S03616; S03616. DR RefSeq; NP_003081.2; NM_003090.2. DR UniGene; Hs.528763; -. DR PDB; 1A9N; X-ray; 2.38 A; A/C=1-176. DR PDBsum; 1A9N; -. DR ProteinModelPortal; P09661; -. DR SMR; P09661; 2-175. DR DIP; DIP-625N; -. DR IntAct; P09661; 7. DR MINT; MINT-3007227; -. DR STRING; P09661; -. DR PhosphoSite; P09661; -. DR DMDM; 31077165; -. DR PeptideAtlas; P09661; -. DR PRIDE; P09661; -. DR Ensembl; ENST00000254193; ENSP00000254193; ENSG00000131876. DR GeneID; 6627; -. DR KEGG; hsa:6627; -. DR UCSC; uc002bww.1; human. DR CTD; 6627; -. DR GeneCards; GC15M101821; -. DR H-InvDB; HIX0012630; -. DR H-InvDB; HIX0203213; -. DR HGNC; HGNC:11152; SNRPA1. DR MIM; 603521; gene. DR neXtProt; NX_P09661; -. DR PharmGKB; PA35994; -. DR eggNOG; prNOG10427; -. DR HOGENOM; HBG747960; -. DR HOVERGEN; HBG007330; -. DR InParanoid; P09661; -. DR OMA; NNNRILR; -. DR OrthoDB; EOG4BG8WS; -. DR PhylomeDB; P09661; -. DR Reactome; REACT_1675; mRNA Processing. DR Reactome; REACT_71; Gene Expression. DR NextBio; 25813; -. DR ArrayExpress; P09661; -. DR Bgee; P09661; -. DR CleanEx; HS_SNRPA1; -. DR Genevestigator; P09661; -. DR GermOnline; ENSG00000131876; Homo sapiens. DR GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0005686; C:U2 snRNP; TAS:ProtInc. DR GO; GO:0005515; F:protein binding; IPI:HGNC. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW. DR GO; GO:0000398; P:nuclear mRNA splicing, via spliceosome; IC:UniProtKB. DR InterPro; IPR001611; Leu-rich_rpt. DR InterPro; IPR003603; U2A'_phosphoprotein32A_C. DR KO; K11092; -. DR SMART; SM00446; LRRcap; 1. DR PROSITE; PS51450; LRR; 4. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Complete proteome; KW Direct protein sequencing; Leucine-rich repeat; mRNA processing; KW mRNA splicing; Nucleus; Phosphoprotein; Polymorphism; KW Reference proteome; Repeat; Ribonucleoprotein; RNA-binding; KW Spliceosome. FT INIT_MET 1 1 Removed. FT CHAIN 2 255 U2 small nuclear ribonucleoprotein A'. FT /FTId=PRO_0000074173. FT REPEAT 20 41 LRR 1. FT REPEAT 43 64 LRR 2. FT REPEAT 65 86 LRR 3. FT REPEAT 89 110 LRR 4. FT DOMAIN 123 161 LRRCT. FT MOD_RES 172 172 N6-acetyllysine. FT MOD_RES 178 178 Phosphoserine. FT MOD_RES 197 197 Phosphoserine. FT VARIANT 234 234 R -> H (in dbSNP:rs1050843). FT /FTId=VAR_052030. FT CONFLICT 193 193 K -> R (in Ref. 1; CAA31838). FT HELIX 6 10 FT STRAND 14 16 FT STRAND 22 25 FT HELIX 37 40 FT STRAND 45 48 FT STRAND 68 70 FT HELIX 83 86 FT STRAND 92 94 FT HELIX 103 111 FT STRAND 117 119 FT HELIX 124 127 FT HELIX 131 138 FT STRAND 143 145 FT HELIX 152 160 FT HELIX 165 172 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 //