ID   RRP1B_MOUSE             Reviewed;         724 AA.
AC   Q91YK2; B0V2W7;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 2.
DT   24-JAN-2024, entry version 137.
DE   RecName: Full=Ribosomal RNA processing protein 1 homolog B;
DE   AltName: Full=RRP1-like protein B;
GN   Name=Rrp1b;
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 GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
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   FUNCTION, AND INTERACTION WITH SIPA1.
RX   PubMed=18081427; DOI=10.1371/journal.pgen.0030214;
RA   Crawford N.P., Qian X., Ziogas A., Papageorge A.G., Boersma B.J.,
RA   Walker R.C., Lukes L., Rowe W.L., Zhang J., Ambs S., Lowy D.R.,
RA   Anton-Culver H., Hunter K.W.;
RT   "Rrp1b, a new candidate susceptibility gene for breast cancer progression
RT   and metastasis.";
RL   PLoS Genet. 3:E214-E214(2007).
RN   [4]
RP   CITRULLINATION AT ARG-678.
RX   PubMed=24463520; DOI=10.1038/nature12942;
RA   Christophorou M.A., Castelo-Branco G., Halley-Stott R.P., Oliveira C.S.,
RA   Loos R., Radzisheuskaya A., Mowen K.A., Bertone P., Silva J.C.,
RA   Zernicka-Goetz M., Nielsen M.L., Gurdon J.B., Kouzarides T.;
RT   "Citrullination regulates pluripotency and histone H1 binding to
RT   chromatin.";
RL   Nature 507:104-108(2014).
RN   [5]
RP   FUNCTION.
RX   PubMed=23604122; DOI=10.1038/onc.2013.133;
RG   NISC Comparative Sequencing Program;
RA   Lee M., Dworkin A.M., Gildea D., Trivedi N.S., Moorhead G.B.,
RA   Crawford N.P.;
RT   "RRP1B is a metastasis modifier that regulates the expression of
RT   alternative mRNA isoforms through interactions with SRSF1.";
RL   Oncogene 33:1818-1827(2014).
CC   -!- FUNCTION: Positively regulates DNA damage-induced apoptosis by acting
CC       as a transcriptional coactivator of proapoptotic target genes of the
CC       transcriptional activator E2F1 (By similarity). Likely to play a role
CC       in ribosome biogenesis by targeting serine/threonine protein
CC       phosphatase PP1 to the nucleolus (By similarity). Involved in
CC       regulation of mRNA splicing (PubMed:23604122). Inhibits SIPA1 GTPase
CC       activity (PubMed:18081427). Involved in regulating expression of
CC       extracellular matrix genes (PubMed:18081427). Associates with chromatin
CC       and may play a role in modulating chromatin structure (By similarity).
CC       {ECO:0000250|UniProtKB:Q14684, ECO:0000269|PubMed:18081427,
CC       ECO:0000269|PubMed:23604122}.
CC   -!- SUBUNIT: Interacts with the transcriptional activator E2F1 (By
CC       similarity). Interacts with serine/threonine-protein phosphatase PP1
CC       subunits PPP1CB and PPP1CC but not with PPP1CA (By similarity).
CC       Interacts with 60S ribosomal proteins RPL5 and RPL27, ribosomal
CC       processing protein RRP1/NNP1 and other nucleolar proteins including
CC       NOP2/NOL1 and FBL (By similarity). Also interacts with nucleolar
CC       protein NPM1/B23 (By similarity). Interacts with splicing factor SRSF1
CC       and LUC7L3/CROP (By similarity). Interacts with GTPase activator SIPA1
CC       (PubMed:18081427). Interacts with H1-10, NCL, PARP1, TRIM28 and YBX3
CC       (By similarity). {ECO:0000250|UniProtKB:Q14684,
CC       ECO:0000269|PubMed:18081427}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC       {ECO:0000250|UniProtKB:Q14684}. Nucleus, nucleoplasm
CC       {ECO:0000250|UniProtKB:Q14684}. Chromosome
CC       {ECO:0000250|UniProtKB:Q14684}. Note=Predominantly located in the
CC       nucleolus with a small amount found in the nucleoplasm. Associates with
CC       the perichromatin region during metaphase and with cytoplasmic foci
CC       during telophase before reaccumulation in the nucleolus during G2.
CC       Associates with heterochromatin and euchromatin.
CC       {ECO:0000250|UniProtKB:Q14684}.
CC   -!- PTM: Citrullinated by PADI4. {ECO:0000269|PubMed:24463520}.
CC   -!- SIMILARITY: Belongs to the RRP1 family. {ECO:0000305}.
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DR   EMBL; CT033797; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC016569; AAH16569.1; -; mRNA.
DR   CCDS; CCDS28613.1; -.
DR   RefSeq; NP_082520.2; NM_028244.2.
DR   AlphaFoldDB; Q91YK2; -.
DR   SMR; Q91YK2; -.
DR   BioGRID; 215383; 46.
DR   STRING; 10090.ENSMUSP00000080085; -.
DR   iPTMnet; Q91YK2; -.
DR   PhosphoSitePlus; Q91YK2; -.
DR   SwissPalm; Q91YK2; -.
DR   EPD; Q91YK2; -.
DR   jPOST; Q91YK2; -.
DR   MaxQB; Q91YK2; -.
DR   PaxDb; 10090-ENSMUSP00000080085; -.
DR   PeptideAtlas; Q91YK2; -.
DR   ProteomicsDB; 260842; -.
DR   Pumba; Q91YK2; -.
DR   Antibodypedia; 9978; 126 antibodies from 18 providers.
DR   Ensembl; ENSMUST00000081339.13; ENSMUSP00000080085.7; ENSMUSG00000058392.14.
DR   GeneID; 72462; -.
DR   KEGG; mmu:72462; -.
DR   UCSC; uc008bvt.2; mouse.
DR   AGR; MGI:1919712; -.
DR   CTD; 23076; -.
DR   MGI; MGI:1919712; Rrp1b.
DR   VEuPathDB; HostDB:ENSMUSG00000058392; -.
DR   eggNOG; KOG3911; Eukaryota.
DR   GeneTree; ENSGT00390000011821; -.
DR   HOGENOM; CLU_022876_3_0_1; -.
DR   InParanoid; Q91YK2; -.
DR   OMA; QYLSVKT; -.
DR   OrthoDB; 231685at2759; -.
DR   PhylomeDB; Q91YK2; -.
DR   TreeFam; TF315294; -.
DR   BioGRID-ORCS; 72462; 3 hits in 80 CRISPR screens.
DR   ChiTaRS; Rrp1b; mouse.
DR   PRO; PR:Q91YK2; -.
DR   Proteomes; UP000000589; Chromosome 17.
DR   RNAct; Q91YK2; Protein.
DR   Bgee; ENSMUSG00000058392; Expressed in embryonic post-anal tail and 271 other cell types or tissues.
DR   ExpressionAtlas; Q91YK2; baseline and differential.
DR   GO; GO:0005694; C:chromosome; ISO:MGI.
DR   GO; GO:0000791; C:euchromatin; IDA:MGI.
DR   GO; GO:0001652; C:granular component; ISS:UniProtKB.
DR   GO; GO:0000792; C:heterochromatin; IDA:MGI.
DR   GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0030688; C:preribosome, small subunit precursor; IEA:InterPro.
DR   GO; GO:0003713; F:transcription coactivator activity; ISS:UniProtKB.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0098586; P:cellular response to virus; ISO:MGI.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0034260; P:negative regulation of GTPase activity; IMP:UniProtKB.
DR   GO; GO:0043923; P:positive regulation by host of viral transcription; ISO:MGI.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR   GO; GO:0043484; P:regulation of RNA splicing; IMP:UniProtKB.
DR   GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR   GO; GO:0006364; P:rRNA processing; IEA:InterPro.
DR   InterPro; IPR010301; RRP1.
DR   PANTHER; PTHR13026; NNP-1 PROTEIN NOVEL NUCLEAR PROTEIN 1 NOP52; 1.
DR   PANTHER; PTHR13026:SF2; RIBOSOMAL RNA PROCESSING PROTEIN 1 HOMOLOG B; 1.
DR   Pfam; PF05997; Nop52; 1.
DR   Genevisible; Q91YK2; MM.
PE   1: Evidence at protein level;
KW   Acetylation; Activator; Apoptosis; Chromosome; Citrullination;
KW   mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW   Reference proteome; Transcription; Transcription regulation.
FT   CHAIN           1..724
FT                   /note="Ribosomal RNA processing protein 1 homolog B"
FT                   /id="PRO_0000340116"
FT   REGION          331..576
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          625..649
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          687..724
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        353..374
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        409..444
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        446..463
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        470..498
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        516..534
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        542..560
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        627..649
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        691..708
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         336
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14684"
FT   MOD_RES         370
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14684"
FT   MOD_RES         432
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14684"
FT   MOD_RES         438
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14684"
FT   MOD_RES         494
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14684"
FT   MOD_RES         618
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14684"
FT   MOD_RES         668
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14684"
FT   MOD_RES         672
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14684"
FT   MOD_RES         678
FT                   /note="Citrulline"
FT                   /evidence="ECO:0000269|PubMed:24463520"
FT   MOD_RES         694
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14684"
FT   MOD_RES         698
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14684"
FT   MOD_RES         701
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14684"
FT   CONFLICT        209
FT                   /note="V -> A (in Ref. 2; AAH16569)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        229
FT                   /note="Q -> E (in Ref. 2; AAH16569)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   724 AA;  80582 MW;  4DEFC78AADBA38F1 CRC64;
     MALAMQSSEF QFAQRLASSE KGVRDRAVRK LRQYLSARTQ SDTGSFSQEE LLKIWKGLFY
     CMWVQDEPLL QEELANIISQ LIHVVNSLEA QYLFIQTFWQ TMNREWQGID KLQLDKYYML
     IRLVLRQSFE VLKRNAWEES QITLFLDILM KEILSPESQS PNGVRTHLID VYLEELTTVG
     GAELLADQNL KLIDPFCRIA AKTKDHTLVQ TVARGVFEVI VDQSACVPQE SVEERKTKED
     GSGFPTKALA CRKAVSGKKA ALDECLRDGV IGSRERDICA ALKDSGSPLQ FDYKAVADRL
     LEIANSKSTP PFNRKRLCRL VRKFQDLCEG NGAPLSSAED NGQRRHKRKR KKLLESEKGD
     TVSPAAEEDS GGHIHKKKRK KRKRSHFQPD TQNLDAVAVP KVPDSESEPD TAQRQAPCGQ
     ACVTEPTAEA VSSIGENSSK PTPVMPIHNK RKRPRKKKLR AHKEICKSTT LPQEDMSKND
     AVSGHSQSSA AHISSSEGVQ AQKRKRKLGA LPDSSSDLPV QKSGTPTSPV EGKDGQTTLP
     RCKRSQKKTA SSTLDPCDPS SQKPAISKKK KKTMKLMSNG VLESNPGQIQ ALGSNRTLKK
     PLKTEDDFVK FDTRFLPKPL FFRKAKNSSA TRPQGPAGQL NKTPSSSKKV TFGLNRNMTA
     EFKKTDKSIL VSPTGLSRVA FNPEQRPLHG VLKTATSSPA STPLSPMRLP ATTPKRRPRA
     ADFF
//