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RU2A_MOUSE
ID   RU2A_MOUSE              Reviewed;         255 AA.
AC   P57784; Q3U7R8; Q8K2W4; Q91YW1; Q9JKQ3;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   23-MAY-2003, sequence version 2.
DT   03-AUG-2022, entry version 166.
DE   RecName: Full=U2 small nuclear ribonucleoprotein A';
DE            Short=U2 snRNP A';
GN   Name=Snrpa1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=12036604; DOI=10.1016/s0165-2478(02)00064-0;
RA   Antica M., Kusic B., Hranilovic D., Dietz A.B., Vuk-Pavlovic S.;
RT   "Cloning the cDNA for murine U2 snRNP-A' gene and its differential
RT   expression in lymphocyte development.";
RL   Immunol. Lett. 82:217-223(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Bone marrow, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [6]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-172, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA   Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA   Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT   "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT   pathways.";
RL   Mol. Cell 50:919-930(2013).
CC   -!- FUNCTION: Involved in pre-mRNA splicing as component of the
CC       spliceosome. Associated with sn-RNP U2, where it contributes to the
CC       binding of stem loop IV of U2 snRNA. {ECO:0000250|UniProtKB:P09661}.
CC   -!- SUBUNIT: Identified in the spliceosome B complex. Identified in the
CC       spliceosome C complex. Found in a pre-mRNA splicing complex with SFRS4,
CC       SFRS5, SNRNP70, SNRPA1, SRRM1 and SRRM2. Found in a pre-mRNA exonic
CC       splicing enhancer (ESE) complex with SNRNP70, SNRPA1, SRRM1 and TRA2B.
CC       Contributes to the binding of stem loop IV of U2 snRNA with SNRPB2.
CC       {ECO:0000250|UniProtKB:P09661}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P09661}.
CC   -!- SIMILARITY: Belongs to the U2 small nuclear ribonucleoprotein A family.
CC       {ECO:0000305}.
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DR   EMBL; AF230356; AAF35392.1; -; mRNA.
DR   EMBL; BC013777; AAH13777.1; -; mRNA.
DR   EMBL; BC029642; AAH29642.1; -; mRNA.
DR   EMBL; AK088438; BAC40353.1; -; mRNA.
DR   EMBL; AK151800; BAE30700.1; -; mRNA.
DR   EMBL; AK152546; BAE31301.1; -; mRNA.
DR   EMBL; AK153502; BAE32048.1; -; mRNA.
DR   CCDS; CCDS21342.1; -.
DR   RefSeq; NP_067311.4; NM_021336.4.
DR   AlphaFoldDB; P57784; -.
DR   SMR; P57784; -.
DR   BioGRID; 213157; 20.
DR   IntAct; P57784; 11.
DR   MINT; P57784; -.
DR   STRING; 10090.ENSMUSP00000117947; -.
DR   iPTMnet; P57784; -.
DR   PhosphoSitePlus; P57784; -.
DR   EPD; P57784; -.
DR   MaxQB; P57784; -.
DR   PaxDb; P57784; -.
DR   PeptideAtlas; P57784; -.
DR   PRIDE; P57784; -.
DR   ProteomicsDB; 260872; -.
DR   Antibodypedia; 29301; 116 antibodies from 25 providers.
DR   DNASU; 68981; -.
DR   Ensembl; ENSMUST00000153609; ENSMUSP00000117947; ENSMUSG00000030512.
DR   GeneID; 68981; -.
DR   KEGG; mmu:68981; -.
DR   UCSC; uc009hgy.2; mouse.
DR   CTD; 6627; -.
DR   MGI; MGI:1916231; Snrpa1.
DR   VEuPathDB; HostDB:ENSMUSG00000030512; -.
DR   eggNOG; KOG1644; Eukaryota.
DR   GeneTree; ENSGT00940000153289; -.
DR   HOGENOM; CLU_061027_0_1_1; -.
DR   InParanoid; P57784; -.
DR   OMA; PNYREYM; -.
DR   OrthoDB; 1447031at2759; -.
DR   PhylomeDB; P57784; -.
DR   TreeFam; TF313776; -.
DR   Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
DR   BioGRID-ORCS; 68981; 27 hits in 77 CRISPR screens.
DR   ChiTaRS; Snrpa1; mouse.
DR   PRO; PR:P57784; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   RNAct; P57784; protein.
DR   Bgee; ENSMUSG00000030512; Expressed in respiratory primordium and 274 other tissues.
DR   ExpressionAtlas; P57784; baseline and differential.
DR   Genevisible; P57784; MM.
DR   GO; GO:0071013; C:catalytic step 2 spliceosome; ISO:MGI.
DR   GO; GO:0016604; C:nuclear body; ISO:MGI.
DR   GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0005681; C:spliceosomal complex; ISO:MGI.
DR   GO; GO:0005686; C:U2 snRNP; IBA:GO_Central.
DR   GO; GO:0071007; C:U2-type catalytic step 2 spliceosome; ISS:UniProtKB.
DR   GO; GO:0071005; C:U2-type precatalytic spliceosome; ISO:MGI.
DR   GO; GO:0030620; F:U2 snRNA binding; IBA:GO_Central.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; ISS:UniProtKB.
DR   GO; GO:0007283; P:spermatogenesis; ISO:MGI.
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   Acetylation; Isopeptide bond; Leucine-rich repeat; mRNA processing;
KW   mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW   Ribonucleoprotein; RNA-binding; Spliceosome; Ubl conjugation.
FT   CHAIN           1..255
FT                   /note="U2 small nuclear ribonucleoprotein A'"
FT                   /id="PRO_0000074175"
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          179..199
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:23806337"
FT   MOD_RES         178
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P09661"
FT   MOD_RES         197
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P09661"
FT   MOD_RES         236
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P09661"
FT   MOD_RES         255
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P09661"
FT   CROSSLNK        172
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P09661"
FT   CROSSLNK        221
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P09661"
FT   CONFLICT        63
FT                   /note="L -> S (in Ref. 3; AAH13777)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        172..173
FT                   /note="KD -> N (in Ref. 1; AAF35392)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   255 AA;  28357 MW;  D5847A07883A734D CRC64;
     MVKLTAELIE QAAQYTNAVR DRELDLRGYK IPVIENLGAT LDQFDAIDFS DNEIRKLDGF
     PLLRRLKTLL VNNNRICRIG EGLDQALPCL TELILTNNSL VELGDLDPLA SLKSLTYLSI
     LRNPVTNKKH YRLYVIYKVP QVRVLDFQKV KLKERQEAEK MFKGKRGAQL AKDIARRSKT
     FNPGAGLPTD KKKGGPSAGD VEAIKNAIAN ASTLAEVERL KGLLQSGQIP GRERRSGPSD
     EGEEEIEDDT VTNGS
 
 
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