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 27-MAR-2024, entry version 204. 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 PDB; 7T0Y; X-ray; 1.80 A; B/D=682-727. DR PDBsum; 7T0Y; -. DR AlphaFoldDB; Q14684; -. DR SMR; Q14684; -. DR BioGRID; 116708; 325. DR IntAct; Q14684; 511. DR MINT; Q14684; -. DR STRING; 9606.ENSP00000339145; -. DR GlyConnect; 2857; 1 O-GlcNAc glycan (1 site). DR GlyCosmos; Q14684; 6 sites, 1 glycan. DR GlyGen; Q14684; 9 sites, 1 O-linked glycan (9 sites). DR iPTMnet; Q14684; -. DR MetOSite; Q14684; -. DR PhosphoSitePlus; Q14684; -. DR SwissPalm; Q14684; -. DR BioMuta; RRP1B; -. DR DMDM; 296452976; -. DR EPD; Q14684; -. DR jPOST; Q14684; -. DR MassIVE; Q14684; -. DR MaxQB; Q14684; -. DR PaxDb; 9606-ENSP00000339145; -. DR PeptideAtlas; Q14684; -. DR ProteomicsDB; 60118; -. [Q14684-1] DR ProteomicsDB; 60119; -. [Q14684-2] DR Pumba; Q14684; -. DR Antibodypedia; 9978; 126 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 AGR; HGNC:23818; -. 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; QYLSVKT; -. DR OrthoDB; 231685at2759; -. DR PhylomeDB; Q14684; -. DR TreeFam; TF315294; -. DR PathwayCommons; Q14684; -. DR SignaLink; Q14684; -. DR BioGRID-ORCS; 23076; 14 hits in 1159 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 204 other cell types or tissues. 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:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; HDA:UniProtKB. 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; 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 SWISS-2DPAGE; Q14684; -. DR Genevisible; Q14684; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Activator; Alternative splicing; Apoptosis; KW Chromosome; Citrullination; Host-virus interaction; mRNA processing; KW mRNA splicing; 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 FT A-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 FT A-684." FT /evidence="ECO:0000269|PubMed:20926688" FT HELIX 688..690 FT /evidence="ECO:0007829|PDB:7T0Y" FT STRAND 692..696 FT /evidence="ECO:0007829|PDB:7T0Y" FT HELIX 702..705 FT /evidence="ECO:0007829|PDB:7T0Y" 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 //