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Entry: P09661
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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   29-SEP-2021, entry version 210.
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   SMR; P09661; -.
DR   BioGRID; 112511; 205.
DR   CORUM; P09661; -.
DR   DIP; DIP-625N; -.
DR   IntAct; P09661; 89.
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; 111 antibodies.
DR   DNASU; 6627; -.
DR   Ensembl; ENST00000254193; ENSP00000254193; ENSG00000131876.
DR   GeneID; 6627; -.
DR   KEGG; hsa:6627; -.
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   BioGRID-ORCS; 6627; 777 hits in 956 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 small intestine Peyer's patch and 116 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   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
//
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