BYST_MOUSE
ID BYST_MOUSE Reviewed; 436 AA.
AC O54825; Q3THF4; Q3UPY9; Q8VD68;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 3.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Bystin;
GN Name=Bysl;
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 [LARGE SCALE MRNA].
RC STRAIN=BALB/cJ, and C57BL/6J;
RC TISSUE=Embryo, Embryonic spinal cord, and Lung;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Salivary gland;
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 151-436.
RA Suzuki N., Fukuda M.N.;
RT "Characterization of mouse bystin.";
RL Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17055491; DOI=10.1016/j.febslet.2006.09.072;
RA Aoki R., Suzuki N., Paria B.C., Sugihara K., Akama T.O., Raab G.,
RA Miyoshi M., Nadano D., Fukuda M.N.;
RT "The Bysl gene product, bystin, is essential for survival of mouse
RT embryos.";
RL FEBS Lett. 580:6062-6068(2006).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=17242206; DOI=10.1128/mcb.01908-06;
RA Adachi K., Soeta-Saneyoshi C., Sagara H., Iwakura Y.;
RT "Crucial role of Bysl in mammalian preimplantation development as an
RT integral factor for 40S ribosome biogenesis.";
RL Mol. Cell. Biol. 27:2202-2214(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-97, AND IDENTIFICATION BY
RP 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-97, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-97, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-97, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas, Spleen,
RC 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).
CC -!- FUNCTION: Required for processing of 20S pre-rRNA precursor and
CC biogenesis of 40S ribosomal subunits. {ECO:0000269|PubMed:17055491,
CC ECO:0000269|PubMed:17242206}.
CC -!- SUBUNIT: Binds trophinin, tastin and cytokeratins. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17242206}. Nucleus,
CC nucleolus {ECO:0000269|PubMed:17242206}. Note=Associated with 40S
CC ribosomal subunits.
CC -!- TISSUE SPECIFICITY: High levels in preimplantation embryos, bone
CC marrow, brain, testis and ovary. {ECO:0000269|PubMed:17242206}.
CC -!- DEVELOPMENTAL STAGE: High levels of maternal transcript in unfertilized
CC eggs. High levels up to blastocyst stage.
CC {ECO:0000269|PubMed:17242206}.
CC -!- DISRUPTION PHENOTYPE: Mice show embryonic lethality around stage 6.5
CC dpc shortly after implantation. Mice lacking maternal Bysl transcript
CC upon injection of siRNA into fertilized eggs are arrested at the 16-
CC cell stage, fail to induce trophectoderm, and show altered morphology
CC of developing nucleoli. Embryonic stem cells lacking Bysl show
CC accumulation of pre-20S rRNA precursors and a reduction of 40S
CC ribosomal subunits in the cytoplasm. {ECO:0000269|PubMed:17055491}.
CC -!- SIMILARITY: Belongs to the bystin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH17530.3; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB31619.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC38736.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK019239; BAB31619.2; ALT_INIT; mRNA.
DR EMBL; AK083033; BAC38736.1; ALT_INIT; mRNA.
DR EMBL; AK143027; BAE25255.1; -; mRNA.
DR EMBL; AK168301; BAE40242.1; -; mRNA.
DR EMBL; BC017530; AAH17530.3; ALT_INIT; mRNA.
DR EMBL; AF007802; AAB94491.1; -; mRNA.
DR CCDS; CCDS50132.1; -.
DR RefSeq; NP_058555.3; NM_016859.3.
DR AlphaFoldDB; O54825; -.
DR SMR; O54825; -.
DR BioGRID; 207308; 4.
DR IntAct; O54825; 2.
DR STRING; 10090.ENSMUSP00000024783; -.
DR iPTMnet; O54825; -.
DR PhosphoSitePlus; O54825; -.
DR EPD; O54825; -.
DR jPOST; O54825; -.
DR MaxQB; O54825; -.
DR PaxDb; O54825; -.
DR PeptideAtlas; O54825; -.
DR PRIDE; O54825; -.
DR ProteomicsDB; 265394; -.
DR Antibodypedia; 30110; 82 antibodies from 17 providers.
DR DNASU; 53414; -.
DR Ensembl; ENSMUST00000024783; ENSMUSP00000024783; ENSMUSG00000023988.
DR GeneID; 53414; -.
DR KEGG; mmu:53414; -.
DR UCSC; uc008cvq.2; mouse.
DR CTD; 705; -.
DR MGI; MGI:1858419; Bysl.
DR VEuPathDB; HostDB:ENSMUSG00000023988; -.
DR eggNOG; KOG3871; Eukaryota.
DR GeneTree; ENSGT00390000007241; -.
DR HOGENOM; CLU_029727_0_0_1; -.
DR InParanoid; O54825; -.
DR OMA; AGGQEKH; -.
DR OrthoDB; 1193442at2759; -.
DR PhylomeDB; O54825; -.
DR TreeFam; TF312968; -.
DR Reactome; R-MMU-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR BioGRID-ORCS; 53414; 27 hits in 73 CRISPR screens.
DR ChiTaRS; Bysl; mouse.
DR PRO; PR:O54825; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; O54825; protein.
DR Bgee; ENSMUSG00000023988; Expressed in otic placode and 259 other tissues.
DR Genevisible; O54825; MM.
DR GO; GO:0045177; C:apical part of cell; IDA:MGI.
DR GO; GO:0042995; C:cell projection; ISO:MGI.
DR GO; GO:0005694; C:chromosome; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005881; C:cytoplasmic microtubule; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0030688; C:preribosome, small subunit precursor; IBA:GO_Central.
DR GO; GO:0030515; F:snoRNA binding; IBA:GO_Central.
DR GO; GO:0001825; P:blastocyst formation; IMP:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:MGI.
DR GO; GO:0006364; P:rRNA processing; IBA:GO_Central.
DR GO; GO:0072089; P:stem cell proliferation; IMP:MGI.
DR GO; GO:0001829; P:trophectodermal cell differentiation; IMP:MGI.
DR InterPro; IPR007955; Bystin.
DR PANTHER; PTHR12821; PTHR12821; 1.
DR Pfam; PF05291; Bystin; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Methylation; Nucleus; Phosphoprotein; Reference proteome;
KW Ribosome biogenesis.
FT CHAIN 1..436
FT /note="Bystin"
FT /id="PRO_0000186115"
FT REGION 1..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..52
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..83
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 40
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q13895"
FT MOD_RES 54
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13895"
FT MOD_RES 97
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 155
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q13895"
FT MOD_RES 166
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13895"
FT MOD_RES 413
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13895"
FT CONFLICT 284
FT /note="A -> V (in Ref. 1; BAE40242)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 436 AA; 49784 MW; EFA148BED2072B72 CRC64;
MPKFKVTRGA SNREKHAPLA EQILAGNAVR AGTREKRRGR EVEEEEEYVG PRLSRRILQQ
ARQQQEELET DHGAGDRSAP PRERATRLGP GLPQDGSDEE DEEWPTLEKA AKMAGVDHQA
EVIVDPEDER AIEMFMNKNP PVRRTLADII MEKLTEKQTE VETVMSEVSG FPMPQLDPRV
LEVYRGVREV LCKYRSGKLP KAFKVIPALS NWEQILYVTE PEAWTAAAMY QATRIFASNL
KERMAQRFYN LVLLPRVRDD IAEYKRLNFH LYMALKKALF KPGAWFKGIL IPLCESGTCT
LREAIIVGSI ITKCSIPVLH SSAAMLKIAE MEYSGANSIF LRLLLDKKYA LPYRVLDALV
FHFLAFRTEK RQLPVLWHQC LLTLAQRYKA DLATEQKEAL LELLRLQPHP QLSPEIRREL
QSAVPRDVED GGVTME
