RRP1B_HUMAN
ID RRP1B_HUMAN Reviewed; 758 AA.
AC Q14684; Q8TBZ4;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 3.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=Ribosomal RNA processing protein 1 homolog B;
DE AltName: Full=RRP1-like protein B;
GN Name=RRP1B; Synonyms=KIAA0179;
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 [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT PRO-436.
RC TISSUE=Bone marrow;
RX PubMed=8724849; DOI=10.1093/dnares/3.1.17;
RA Nagase T., Seki N., Ishikawa K., Tanaka A., Nomura N.;
RT "Prediction of the coding sequences of unidentified human genes. V. The
RT coding sequences of 40 new genes (KIAA0161-KIAA0200) deduced by analysis of
RT cDNA clones from human cell line KG-1.";
RL DNA Res. 3:17-24(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10830953; DOI=10.1038/35012518;
RA Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S.,
RA Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M.,
RA Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A., Menzel U.,
RA Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A.,
RA Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J.,
RA Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K.,
RA Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G.,
RA Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J.,
RA Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S.,
RA Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K.,
RA Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.;
RT "The DNA sequence of human chromosome 21.";
RL Nature 405:311-319(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT PRO-436.
RC TISSUE=Testis;
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 [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=12429849; DOI=10.1091/mbc.e02-05-0271;
RA Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C.,
RA Greco A., Hochstrasser D.F., Diaz J.-J.;
RT "Functional proteomic analysis of human nucleolus.";
RL Mol. Biol. Cell 13:4100-4109(2002).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245, AND IDENTIFICATION BY
RP 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-392 AND SER-513, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245; SER-350; SER-392;
RP SER-394; SER-395; SER-452; SER-458; SER-702; SER-706; SER-732 AND SER-736,
RP AND 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 [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [11]
RP FUNCTION, INTERACTION WITH CBX5; H1-10; NCL; NPM1; PARP1; TRIM28 AND YBX3,
RP AND SUBCELLULAR LOCATION.
RX PubMed=19710015; DOI=10.1074/jbc.m109.023457;
RA Crawford N.P., Yang H., Mattaini K.R., Hunter K.W.;
RT "The metastasis efficiency modifier ribosomal RNA processing 1 homolog B
RT (RRP1B) is a chromatin-associated factor.";
RL J. Biol. Chem. 284:28660-28673(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245; SER-350; SER-732 AND
RP SER-735, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-652, 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 [14]
RP FUNCTION, INTERACTION WITH E2F1, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE,
RP AND INDUCTION.
RX PubMed=20040599; DOI=10.1074/jbc.m109.072074;
RA Paik J.C., Wang B., Liu K., Lue J.K., Lin W.C.;
RT "Regulation of E2F1-induced apoptosis by the nucleolar protein RRP1B.";
RL J. Biol. Chem. 285:6348-6363(2010).
RN [15]
RP FUNCTION, INTERACTION WITH FBL; NOP2; RPL5; RPL27; RRP1; PPP1CB AND PPP1CC,
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF VAL-684 AND PHE-686.
RX PubMed=20926688; DOI=10.1091/mbc.e10-04-0287;
RA Chamousset D., De Wever V., Moorhead G.B., Chen Y., Boisvert F.M.,
RA Lamond A.I., Trinkle-Mulcahy L.;
RT "RRP1B targets PP1 to mammalian cell nucleoli and is associated with pre-
RT 60S ribosomal subunits.";
RL Mol. Biol. Cell 21:4212-4226(2010).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245; SER-350; SER-513;
RP SER-702; SER-706; SER-732 AND SER-735, AND IDENTIFICATION BY MASS
RP 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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245; SER-513; SER-706;
RP THR-728 AND SER-732, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245; SER-392; SER-513;
RP SER-579; SER-706 AND SER-732, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-350, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [21]
RP INTERACTION WITH LUC7L3 AND SRSF1.
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).
RN [22]
RP FUNCTION (MICROBIAL INFECTION), SUBCELLULAR LOCATION, AND INTERACTION WITH
RP INFLUENZA A VIRUS NP; PB1 AND PB2.
RX PubMed=26311876; DOI=10.1128/jvi.01487-15;
RA Su W.C., Hsu S.F., Lee Y.Y., Jeng K.S., Lai M.M.;
RT "A nucleolar protein, ribosomal RNA processing 1 homolog B (RRP1B),
RT enhances the recruitment of cellular mRNA in influenza virus
RT transcription.";
RL J. Virol. 89:11245-11255(2015).
RN [23]
RP VARIANT PRO-436.
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 [24]
RP VARIANT [LARGE SCALE ANALYSIS] PRO-436, AND IDENTIFICATION BY MASS
RP 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).
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 (PubMed:20040599). Likely to play a role
CC in ribosome biogenesis by targeting serine/threonine protein
CC phosphatase PP1 to the nucleolus (PubMed:20926688). Involved in
CC regulation of mRNA splicing (By similarity). Inhibits SIPA1 GTPase
CC activity (By similarity). Involved in regulating expression of
CC extracellular matrix genes (By similarity). Associates with chromatin
CC and may play a role in modulating chromatin structure
CC (PubMed:19710015). {ECO:0000250|UniProtKB:Q91YK2,
CC ECO:0000269|PubMed:19710015, ECO:0000269|PubMed:20040599,
CC ECO:0000269|PubMed:20926688}.
CC -!- FUNCTION: (Microbial infection) Following influenza A virus (IAV)
CC infection, promotes viral mRNA transcription by facilitating the
CC binding of IAV RNA-directed RNA polymerase to capped mRNA.
CC {ECO:0000269|PubMed:26311876}.
CC -!- SUBUNIT: Interacts with the transcriptional activator E2F1
CC (PubMed:20040599). Interacts with serine/threonine-protein phosphatase
CC PP1 subunits PPP1CB and PPP1CC but not with PPP1CA (PubMed:20926688).
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 (PubMed:20926688). Also interacts with nucleolar
CC protein NPM1/B23 (PubMed:20926688, PubMed:19710015). Interacts with
CC splicing factor SRSF1 and with LUC7L3/CROP (PubMed:23604122). Interacts
CC with GTPase activator SIPA1 (By similarity). Interacts with
CC CBX5/HP1alpha, H1-10, NCL, PARP1, TRIM28 and YBX3 (PubMed:19710015).
CC {ECO:0000250|UniProtKB:Q91YK2, ECO:0000269|PubMed:19710015,
CC ECO:0000269|PubMed:20040599, ECO:0000269|PubMed:20926688,
CC ECO:0000269|PubMed:23604122}.
CC -!- SUBUNIT: (Microbial infection) Interacts with influenza A virus
CC nucleoprotein NP and with RNA-directed RNA polymerase subunits PB1 and
CC PB2. {ECO:0000269|PubMed:26311876}.
CC -!- INTERACTION:
CC Q14684; Q01094: E2F1; NbExp=10; IntAct=EBI-372051, EBI-448924;
CC Q14684; P22087: FBL; NbExp=4; IntAct=EBI-372051, EBI-358318;
CC Q14684; P62136: PPP1CA; NbExp=3; IntAct=EBI-372051, EBI-357253;
CC Q14684; P62140: PPP1CB; NbExp=3; IntAct=EBI-372051, EBI-352350;
CC Q14684; P36873: PPP1CC; NbExp=9; IntAct=EBI-372051, EBI-356283;
CC Q14684; P61353: RPL27; NbExp=3; IntAct=EBI-372051, EBI-352760;
CC Q14684; P46777: RPL5; NbExp=2; IntAct=EBI-372051, EBI-358018;
CC Q14684; P56182: RRP1; NbExp=2; IntAct=EBI-372051, EBI-2880285;
CC Q14684; Q07955: SRSF1; NbExp=6; IntAct=EBI-372051, EBI-398920;
CC Q14684-1; P62805: H4C9; NbExp=3; IntAct=EBI-5280110, EBI-302023;
CC Q14684-1; P09874: PARP1; NbExp=4; IntAct=EBI-5280110, EBI-355676;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12429849,
CC ECO:0000269|PubMed:20040599, ECO:0000269|PubMed:20926688,
CC ECO:0000269|PubMed:26311876}. Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:20926688}. Chromosome
CC {ECO:0000269|PubMed:19710015}. Note=Predominantly located in the
CC nucleolus with a small amount found in the nucleoplasm
CC (PubMed:20926688). Associates with the perichromatin region during
CC metaphase and with cytoplasmic foci during telophase before
CC reaccumulation in the nucleolus during G2 (PubMed:20926688). Associates
CC with heterochromatin and euchromatin (PubMed:19710015).
CC {ECO:0000269|PubMed:19710015, ECO:0000269|PubMed:20926688}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:26311876}. Note=(Microbial infection) Following
CC infection by influenza A virus, partially translocates from the
CC nucleolus to the nucleoplasm. {ECO:0000269|PubMed:26311876}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q14684-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q14684-2; Sequence=VSP_007801;
CC -!- DEVELOPMENTAL STAGE: During the cell cycle, expression peaks at the
CC G1/S transition. {ECO:0000269|PubMed:20040599}.
CC -!- INDUCTION: By DNA damage. {ECO:0000269|PubMed:20040599}.
CC -!- PTM: Citrullinated by PADI4. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the RRP1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA11496.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; D80001; BAA11496.1; ALT_INIT; mRNA.
DR EMBL; AP001052; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC028386; AAH28386.1; -; mRNA.
DR CCDS; CCDS33577.1; -. [Q14684-1]
DR RefSeq; NP_055871.1; NM_015056.2. [Q14684-1]
DR AlphaFoldDB; Q14684; -.
DR SMR; Q14684; -.
DR BioGRID; 116708; 268.
DR IntAct; Q14684; 503.
DR MINT; Q14684; -.
DR STRING; 9606.ENSP00000339145; -.
DR GlyConnect; 2857; 1 O-Linked glycan (1 site).
DR GlyGen; Q14684; 6 sites, 1 O-linked glycan (6 sites).
DR iPTMnet; Q14684; -.
DR MetOSite; Q14684; -.
DR PhosphoSitePlus; Q14684; -.
DR SwissPalm; Q14684; -.
DR BioMuta; RRP1B; -.
DR DMDM; 296452976; -.
DR SWISS-2DPAGE; Q14684; -.
DR EPD; Q14684; -.
DR jPOST; Q14684; -.
DR MassIVE; Q14684; -.
DR MaxQB; Q14684; -.
DR PaxDb; Q14684; -.
DR PeptideAtlas; Q14684; -.
DR PRIDE; Q14684; -.
DR ProteomicsDB; 60118; -. [Q14684-1]
DR ProteomicsDB; 60119; -. [Q14684-2]
DR Antibodypedia; 9978; 100 antibodies from 18 providers.
DR DNASU; 23076; -.
DR Ensembl; ENST00000340648.6; ENSP00000339145.4; ENSG00000160208.13. [Q14684-1]
DR GeneID; 23076; -.
DR KEGG; hsa:23076; -.
DR MANE-Select; ENST00000340648.6; ENSP00000339145.4; NM_015056.3; NP_055871.1.
DR UCSC; uc002zdk.4; human. [Q14684-1]
DR CTD; 23076; -.
DR DisGeNET; 23076; -.
DR GeneCards; RRP1B; -.
DR HGNC; HGNC:23818; RRP1B.
DR HPA; ENSG00000160208; Low tissue specificity.
DR MIM; 610654; gene.
DR neXtProt; NX_Q14684; -.
DR OpenTargets; ENSG00000160208; -.
DR PharmGKB; PA162402138; -.
DR VEuPathDB; HostDB:ENSG00000160208; -.
DR eggNOG; KOG3911; Eukaryota.
DR GeneTree; ENSGT00390000011821; -.
DR HOGENOM; CLU_022876_3_0_1; -.
DR InParanoid; Q14684; -.
DR OMA; KEVMDPD; -.
DR OrthoDB; 1337189at2759; -.
DR PhylomeDB; Q14684; -.
DR TreeFam; TF315294; -.
DR PathwayCommons; Q14684; -.
DR SignaLink; Q14684; -.
DR BioGRID-ORCS; 23076; 13 hits in 1081 CRISPR screens.
DR ChiTaRS; RRP1B; human.
DR GeneWiki; RRP1B; -.
DR GenomeRNAi; 23076; -.
DR Pharos; Q14684; Tbio.
DR PRO; PR:Q14684; -.
DR Proteomes; UP000005640; Chromosome 21.
DR RNAct; Q14684; protein.
DR Bgee; ENSG00000160208; Expressed in germinal epithelium of ovary and 202 other tissues.
DR Genevisible; Q14684; HS.
DR GO; GO:0005694; C:chromosome; IDA:HPA.
DR GO; GO:0005829; C:cytosol; HDA:UniProtKB.
DR GO; GO:0000791; C:euchromatin; IEA:Ensembl.
DR GO; GO:0001652; C:granular component; IDA:UniProtKB.
DR GO; GO:0000792; C:heterochromatin; IEA:Ensembl.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
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:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0003713; F:transcription coactivator activity; IMP:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0098586; P:cellular response to virus; IDA:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0034260; P:negative regulation of GTPase activity; ISS:UniProtKB.
DR GO; GO:0043923; P:positive regulation by host of viral transcription; IMP:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IMP:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR GO; GO:0043484; P:regulation of RNA splicing; ISS: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; Alternative splicing; Apoptosis; Chromosome;
KW Citrullination; Host-virus interaction; mRNA processing; mRNA splicing;
KW Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..758
FT /note="Ribosomal RNA processing protein 1 homolog B"
FT /id="PRO_0000050729"
FT REGION 259..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 381..598
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 660..681
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 707..758
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..285
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..397
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 496..512
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 666..681
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 725..742
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 245
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 350
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 392
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163"
FT MOD_RES 394
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 395
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 452
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 458
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 513
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 579
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 652
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 702
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 706
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 712
FT /note="Citrulline"
FT /evidence="ECO:0000250"
FT MOD_RES 728
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 732
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 735
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 736
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VAR_SEQ 51..68
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8724849"
FT /id="VSP_007801"
FT VARIANT 436
FT /note="L -> P (in dbSNP:rs9306160)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:18081427, ECO:0000269|PubMed:8724849,
FT ECO:0007744|PubMed:21269460"
FT /id="VAR_079135"
FT MUTAGEN 684
FT /note="V->A: Abolishes interaction with protein phosphatase
FT PP1 subunits PPP1CB and PPP1CC; when associated with A-
FT 686."
FT /evidence="ECO:0000269|PubMed:20926688"
FT MUTAGEN 686
FT /note="F->A: Abolishes interaction with protein phosphatase
FT PP1 subunits PPP1CB and PPP1CC; when associated with A-
FT 684."
FT /evidence="ECO:0000269|PubMed:20926688"
SQ SEQUENCE 758 AA; 84428 MW; 738117A7062054F2 CRC64;
MAPAMQPAEI QFAQRLASSE KGIRDRAVKK LRQYISVKTQ RETGGFSQEE LLKIWKGLFY
CMWVQDEPLL QEELANTIAQ LVHAVNNSAA QHLFIQTFWQ TMNREWKGID RLRLDKYYML
IRLVLRQSFE VLKRNGWEES RIKVFLDVLM KEVLCPESQS PNGVRFHFID IYLDELSKVG
GKELLADQNL KFIDPFCKIA AKTKDHTLVQ TIARGVFEAI VDQSPFVPEE TMEEQKTKVG
DGDLSAEEIP ENEVSLRRAV SKKKTALGKN HSRKDGLSDE RGRDDCGTFE DTGPLLQFDY
KAVADRLLEM TSRKNTPHFN RKRLSKLIKK FQDLSEGSSI SQLSFAEDIS ADEDDQILSQ
GKHKKKGNKL LEKTNLEKEK GSRVFCVEEE DSESSLQKRR RKKKKKHHLQ PENPGPGGAA
PSLEQNRGRE PEASGLKALK ARVAEPGAEA TSSTGEESGS EHPPAVPMHN KRKRPRKKSP
RAHREMLESA VLPPEDMSQS GPSGSHPQGP RGSPTGGAQL LKRKRKLGVV PVNGSGLSTP
AWPPLQQEGP PTGPAEGANS HTTLPQRRRL QKKKAGPGSL ELCGLPSQKT ASLKKRKKMR
VMSNLVEHNG VLESEAGQPQ ALGSSGTCSS LKKQKLRAES DFVKFDTPFL PKPLFFRRAK
SSTATHPPGP AVQLNKTPSS SKKVTFGLNR NMTAEFKKTD KSILVSPTGP SRVAFDPEQK
PLHGVLKTPT SSPASSPLVA KKPLTTTPRR RPRAMDFF
