BRX1_MOUSE
ID BRX1_MOUSE Reviewed; 353 AA.
AC Q9DCA5; Q3THD3; Q91YS6;
DT 09-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Ribosome biogenesis protein BRX1 homolog;
DE AltName: Full=Brix domain-containing protein 2;
GN Name=Brix1; Synonyms=Brix, Bxdc2;
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=C57BL/6J, and DBA/2J; TISSUE=Brain;
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].
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
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 biogenesis of the 60S ribosomal subunit.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the BRX1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH14832.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB22497.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK002985; BAB22497.1; ALT_INIT; mRNA.
DR EMBL; AK168325; BAE40264.1; -; mRNA.
DR EMBL; BC014832; AAH14832.1; ALT_INIT; mRNA.
DR CCDS; CCDS37042.1; -.
DR RefSeq; NP_080672.3; NM_026396.3.
DR AlphaFoldDB; Q9DCA5; -.
DR SMR; Q9DCA5; -.
DR BioGRID; 212465; 4.
DR IntAct; Q9DCA5; 1.
DR STRING; 10090.ENSMUSP00000022855; -.
DR iPTMnet; Q9DCA5; -.
DR PhosphoSitePlus; Q9DCA5; -.
DR EPD; Q9DCA5; -.
DR MaxQB; Q9DCA5; -.
DR PaxDb; Q9DCA5; -.
DR PeptideAtlas; Q9DCA5; -.
DR PRIDE; Q9DCA5; -.
DR ProteomicsDB; 265245; -.
DR Antibodypedia; 10048; 203 antibodies from 25 providers.
DR DNASU; 67832; -.
DR Ensembl; ENSMUST00000022855; ENSMUSP00000022855; ENSMUSG00000022247.
DR GeneID; 67832; -.
DR KEGG; mmu:67832; -.
DR UCSC; uc007vgg.1; mouse.
DR CTD; 55299; -.
DR MGI; MGI:1915082; Brix1.
DR VEuPathDB; HostDB:ENSMUSG00000022247; -.
DR eggNOG; KOG2971; Eukaryota.
DR GeneTree; ENSGT00390000014467; -.
DR HOGENOM; CLU_048373_2_0_1; -.
DR InParanoid; Q9DCA5; -.
DR OMA; GPTVKMH; -.
DR OrthoDB; 973436at2759; -.
DR PhylomeDB; Q9DCA5; -.
DR TreeFam; TF105766; -.
DR BioGRID-ORCS; 67832; 27 hits in 76 CRISPR screens.
DR ChiTaRS; Brix1; mouse.
DR PRO; PR:Q9DCA5; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q9DCA5; protein.
DR Bgee; ENSMUSG00000022247; Expressed in animal zygote and 264 other tissues.
DR ExpressionAtlas; Q9DCA5; baseline and differential.
DR Genevisible; Q9DCA5; MM.
DR GO; GO:0005694; C:chromosome; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0019843; F:rRNA binding; IEA:InterPro.
DR GO; GO:0000027; P:ribosomal large subunit assembly; IBA:GO_Central.
DR GO; GO:0006364; P:rRNA processing; IEA:InterPro.
DR InterPro; IPR007109; Brix.
DR InterPro; IPR026532; BRX1.
DR PANTHER; PTHR13634; PTHR13634; 1.
DR Pfam; PF04427; Brix; 1.
DR SMART; SM00879; Brix; 1.
DR PROSITE; PS50833; BRIX; 1.
PE 1: Evidence at protein level;
KW Acetylation; Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW Ribosome biogenesis; Ubl conjugation.
FT CHAIN 1..353
FT /note="Ribosome biogenesis protein BRX1 homolog"
FT /id="PRO_0000120231"
FT DOMAIN 60..249
FT /note="Brix"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00034"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 334..353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..27
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..50
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 261
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TDN6"
FT MOD_RES 276
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8TDN6"
FT CROSSLNK 160
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8TDN6"
FT CROSSLNK 314
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8TDN6"
FT CROSSLNK 322
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8TDN6"
FT CONFLICT 195
FT /note="H -> N (in Ref. 1; BAE40264)"
FT /evidence="ECO:0000305"
FT CONFLICT 242
FT /note="K -> E (in Ref. 1; BAB22497)"
FT /evidence="ECO:0000305"
FT CONFLICT 265
FT /note="H -> Q (in Ref. 1; BAB22497)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 353 AA; 41241 MW; 6087F4F9C340692F CRC64;
MAATKRKRRG GLEVQAKKPK RSSKDAGQPA KQADVAKEAE EENRDRIPGP VCKGKWKNKE
RILIFSSRGI NFRTRHLMQD LRMLMPHSKA DTKMDRKDKL FVINEVCEMK NCNKCIYFEA
KKKQDLYMWL SNSPHGPSAK FLVQNIHTLA ELKMTGNCLK GSRPLLSFDP AFDDLPHYAL
LKEFLIQIFS TPRYHPKSQP FVDHVFTFTI LDNRIWFRNF QIIEEDAALV EIGPRFVLNL
IKIFQGSFGG PTLYENPHYQ SPNMHRRVIR SITAAKYRER QQVKDVQKLR KKEPKTILPH
DPTADVFVIP AEEKPVEIQW VKPEPKVDLK ARKRRIYKRH RKLQQKMSRG SAK
