RRP1B_MOUSE
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 03-AUG-2022, entry version 130.
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; Q91YK2; -.
DR PeptideAtlas; Q91YK2; -.
DR PRIDE; Q91YK2; -.
DR ProteomicsDB; 260842; -.
DR Antibodypedia; 9978; 100 antibodies from 18 providers.
DR Ensembl; ENSMUST00000081339; ENSMUSP00000080085; ENSMUSG00000058392.
DR GeneID; 72462; -.
DR KEGG; mmu:72462; -.
DR UCSC; uc008bvt.2; mouse.
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; KEVMDPD; -.
DR OrthoDB; 1337189at2759; -.
DR PhylomeDB; Q91YK2; -.
DR TreeFam; TF315294; -.
DR BioGRID-ORCS; 72462; 3 hits in 75 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 268 other tissues.
DR ExpressionAtlas; Q91YK2; baseline and differential.
DR Genevisible; Q91YK2; MM.
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:0030687; C:preribosome, large subunit precursor; IBA:GO_Central.
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; IBA:GO_Central.
DR InterPro; IPR010301; RRP1-like.
DR PANTHER; PTHR13026; PTHR13026; 1.
DR Pfam; PF05997; Nop52; 1.
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
