BRX1_HUMAN
ID BRX1_HUMAN Reviewed; 353 AA.
AC Q8TDN6; A8K0P5; Q3ZTT4; Q8N453; Q96DH1;
DT 09-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 09-MAY-2003, sequence version 2.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Ribosome biogenesis protein BRX1 homolog;
DE AltName: Full=Brix domain-containing protein 2;
GN Name=BRIX1; Synonyms=BRIX, BXDC2;
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=11843177; DOI=10.1515/bc.2001.199;
RA Kaser A., Bogengruber E., Hallegger M., Doppler E., Lepperdinger G.,
RA Jantsch M., Breitenbach M., Kreil G.;
RT "Brix from Xenopus laevis and brx1p from yeast define a new family of
RT proteins involved in the biogenesis of large ribosomal subunits.";
RL Biol. Chem. 382:1637-1647(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=16533400; DOI=10.1186/1471-2164-7-48;
RA Kemmer D., Podowski R.M., Arenillas D., Lim J., Hodges E., Roth P.,
RA Sonnhammer E.L.L., Hoeoeg C., Wasserman W.W.;
RT "NovelFam3000 -- uncharacterized human protein domains conserved across
RT model organisms.";
RL BMC Genomics 7:48-48(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cervix;
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [7]
RP IDENTIFICATION BY 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 [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-276, 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 [9]
RP IDENTIFICATION BY 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 [10]
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-261, AND IDENTIFICATION BY
RP 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 [12]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-322, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [13]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-160; LYS-314 AND LYS-322, 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).
CC -!- FUNCTION: Required for biogenesis of the 60S ribosomal subunit.
CC -!- INTERACTION:
CC Q8TDN6; Q99848: EBNA1BP2; NbExp=4; IntAct=EBI-1052326, EBI-1048111;
CC Q8TDN6; Q00839: HNRNPU; NbExp=2; IntAct=EBI-1052326, EBI-351126;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus.
CC -!- SIMILARITY: Belongs to the BRX1 family. {ECO:0000305}.
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DR EMBL; AF347667; AAL83818.1; -; mRNA.
DR EMBL; AY364244; AAQ76803.1; -; mRNA.
DR EMBL; AK289610; BAF82299.1; -; mRNA.
DR EMBL; CH471119; EAW55909.1; -; Genomic_DNA.
DR EMBL; BC001546; AAH01546.2; -; mRNA.
DR EMBL; BC036741; AAH36741.1; -; mRNA.
DR CCDS; CCDS34143.1; -.
DR RefSeq; NP_060791.3; NM_018321.3.
DR AlphaFoldDB; Q8TDN6; -.
DR SMR; Q8TDN6; -.
DR BioGRID; 120586; 268.
DR CORUM; Q8TDN6; -.
DR IntAct; Q8TDN6; 87.
DR MINT; Q8TDN6; -.
DR STRING; 9606.ENSP00000338862; -.
DR iPTMnet; Q8TDN6; -.
DR MetOSite; Q8TDN6; -.
DR PhosphoSitePlus; Q8TDN6; -.
DR SwissPalm; Q8TDN6; -.
DR BioMuta; BRIX1; -.
DR DMDM; 30580352; -.
DR EPD; Q8TDN6; -.
DR jPOST; Q8TDN6; -.
DR MassIVE; Q8TDN6; -.
DR MaxQB; Q8TDN6; -.
DR PaxDb; Q8TDN6; -.
DR PeptideAtlas; Q8TDN6; -.
DR PRIDE; Q8TDN6; -.
DR ProteomicsDB; 74313; -.
DR Antibodypedia; 10048; 203 antibodies from 25 providers.
DR DNASU; 55299; -.
DR Ensembl; ENST00000336767.6; ENSP00000338862.5; ENSG00000113460.13.
DR GeneID; 55299; -.
DR KEGG; hsa:55299; -.
DR MANE-Select; ENST00000336767.6; ENSP00000338862.5; NM_018321.4; NP_060791.3.
DR UCSC; uc003jja.4; human.
DR CTD; 55299; -.
DR GeneCards; BRIX1; -.
DR HGNC; HGNC:24170; BRIX1.
DR HPA; ENSG00000113460; Low tissue specificity.
DR MIM; 618466; gene.
DR neXtProt; NX_Q8TDN6; -.
DR OpenTargets; ENSG00000113460; -.
DR PharmGKB; PA165660166; -.
DR VEuPathDB; HostDB:ENSG00000113460; -.
DR eggNOG; KOG2971; Eukaryota.
DR GeneTree; ENSGT00390000014467; -.
DR HOGENOM; CLU_048373_2_0_1; -.
DR InParanoid; Q8TDN6; -.
DR OMA; GPTVKMH; -.
DR OrthoDB; 973436at2759; -.
DR PhylomeDB; Q8TDN6; -.
DR TreeFam; TF105766; -.
DR PathwayCommons; Q8TDN6; -.
DR SignaLink; Q8TDN6; -.
DR BioGRID-ORCS; 55299; 718 hits in 1080 CRISPR screens.
DR ChiTaRS; BRIX1; human.
DR GeneWiki; BXDC2; -.
DR GenomeRNAi; 55299; -.
DR Pharos; Q8TDN6; Tbio.
DR PRO; PR:Q8TDN6; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q8TDN6; protein.
DR Bgee; ENSG00000113460; Expressed in calcaneal tendon and 117 other tissues.
DR Genevisible; Q8TDN6; HS.
DR GO; GO:0005694; C:chromosome; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
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_0000120230"
FT DOMAIN 60..249
FT /note="Brix"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00034"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..46
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 261
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 276
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT CROSSLNK 160
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 314
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 322
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT CONFLICT 11..27
FT /note="GFAVQAKKPKRNEIDAE -> RLCSSGEEAKKKRNRCG (in Ref. 1;
FT AAL83818)"
FT /evidence="ECO:0000305"
FT CONFLICT 34
FT /note="A -> V (in Ref. 1; AAL83818)"
FT /evidence="ECO:0000305"
FT CONFLICT 286
FT /note="V -> VP (in Ref. 1; AAL83818)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 353 AA; 41401 MW; F05597673A13B7CC CRC64;
MAATKRKRRG GFAVQAKKPK RNEIDAEPPA KRHATAEEVE EEERDRIPGP VCKGKWKNKE
RILIFSSRGI NFRTRHLMQD LRMLMPHSKA DTKMDRKDKL FVINEVCEMK NCNKCIYFEA
KKKQDLYMWL SNSPHGPSAK FLVQNIHTLA ELKMTGNCLK GSRPLLSFDP AFDELPHYAL
LKELLIQIFS TPRYHPKSQP FVDHVFTFTI LDNRIWFRNF QIIEEDAALV EIGPRFVLNL
IKIFQGSFGG PTLYENPHYQ SPNMHRRVIR SITAAKYREK QQVKDVQKLR KKEPKTLLPH
DPTADVFVTP AEEKPIEIQW VKPEPKVDLK ARKKRIYKRQ RKMKQRMDSG KTK
