ID   BRX1_PONAB              Reviewed;         353 AA.
AC   Q5RAN2;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 59.
DE   RecName: Full=Ribosome biogenesis protein BRX1 homolog;
DE   AltName: Full=Brix domain-containing protein 2;
GN   Name=BRIX1; Synonyms=BRIX, BXDC2;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; CR858983; CAH91178.1; -; mRNA.
DR   RefSeq; NP_001125690.1; NM_001132218.1.
DR   AlphaFoldDB; Q5RAN2; -.
DR   SMR; Q5RAN2; -.
DR   STRING; 9601.ENSPPYP00000017190; -.
DR   GeneID; 100172612; -.
DR   KEGG; pon:100172612; -.
DR   CTD; 55299; -.
DR   eggNOG; KOG2971; Eukaryota.
DR   InParanoid; Q5RAN2; -.
DR   OrthoDB; 973436at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0019843; F:rRNA binding; IEA:InterPro.
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   2: Evidence at transcript 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_0000269724"
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: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"
SQ   SEQUENCE   353 AA;  41370 MW;  4C5CAC05A9D3A47B CRC64;
     MAATKRKRRG GFAVQAKKPK RNEKDAEPPA KRHATAEEVE EEERDRIPGP VCKGKWKNKE
     RILIFSSRGI NFRTRHLMQD LRMLMPHSKA DTKMDRKDKL FVINEVCEMK NCNKCIYFEA
     KKKQDLYMWL SNSPHGPSAK FLVQNIHTLA ELKMTGNCLK GSRPLLSFDP AFDELPHYAL
     LKELLIQILS TPRYHPKSQP FVDHVFTFTI LDNRIWFRNF QIIEEDAALV EIGPRFVLNL
     IKIFQGSFGG PTLYENPHYQ SPNMHRRVTR SITAAKYREK QQVKDVQKLR KKEPKTLLPH
     DPTADVFVTP AEEKPIEIQW VKPEPKVDLK ARKKRIYKRQ RKMKQRMDSG KTK