Full text data of RRP1B
RRP1B
(KIAA0179)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Ribosomal RNA processing protein 1 homolog B (RRP1-like protein B)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Ribosomal RNA processing protein 1 homolog B (RRP1-like protein B)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00032374
IPI00032374 Conserved hypothetical protein Protein KIAA0179, bone marrow soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a not mentioned n/a found at its expected molecular weight found at molecular weight
IPI00032374 Conserved hypothetical protein Protein KIAA0179, bone marrow soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a not mentioned n/a found at its expected molecular weight found at molecular weight
UniProt
Q14684
ID RRP1B_HUMAN Reviewed; 758 AA.
AC Q14684; Q8TBZ4;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
read moreDT 18-MAY-2010, sequence version 3.
DT 22-JAN-2014, entry version 124.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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.
RT The coding sequences of 40 new genes (KIAA0161-KIAA0200) deduced by
RT analysis of 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.,
RA Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y.,
RA Soeda E., Ohki M., Takagi T., Sakaki Y., Taudien S., Blechschmidt K.,
RA Polley A., Menzel U., Delabar J., Kumpf K., Lehmann R., Patterson D.,
RA Reichwald K., Rump A., Schillhabel M., Schudy A., Zimmermann W.,
RA Rosenthal A., Kudoh J., Shibuya K., Kawasaki K., Asakawa S.,
RA Shintani A., Sasaki T., Nagamine K., Mitsuyama S., Antonarakis S.E.,
RA Minoshima S., Shimizu N., Nordsiek G., Hornischer K., Brandt P.,
RA Scharfe M., Schoen O., Desario A., Reichelt J., Kauer G., Bloecker H.,
RA Ramser J., Beck A., Klages S., Hennig S., Riesselmann L., Dagand E.,
RA Wehrmeyer S., Borzym K., Gardiner K., Nizetic D., Francis F.,
RA 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).
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
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 MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-392 AND SER-513, AND
RP MASS SPECTROMETRY.
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
RT phosphorylation analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245, AND MASS
RP SPECTROMETRY.
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.,
RA Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
RT efficient phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245, AND MASS
RP SPECTROMETRY.
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
RT the 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
RP SER-736, AND MASS SPECTROMETRY.
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.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245; SER-350; SER-732
RP AND SER-735, AND MASS SPECTROMETRY.
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 [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-652, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245; SER-350; SER-513;
RP SER-702; SER-706; SER-732 AND SER-735, AND MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [14]
RP IDENTIFICATION BY MASS 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.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245; SER-513; SER-706;
RP THR-728 AND SER-732, AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [16]
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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- INTERACTION:
CC O15116:LSM1; NbExp=1; IntAct=EBI-372051, EBI-347619;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus.
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 Note=No experimental confirmation available;
CC -!- SIMILARITY: Belongs to the RRP1 family.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA11496.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
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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 RefSeq; NP_055871.1; NM_015056.2.
DR RefSeq; XP_005261151.1; XM_005261094.1.
DR UniGene; Hs.565725; -.
DR ProteinModelPortal; Q14684; -.
DR IntAct; Q14684; 11.
DR MINT; MINT-3029999; -.
DR STRING; 9606.ENSP00000339145; -.
DR PhosphoSite; Q14684; -.
DR DMDM; 296452976; -.
DR SWISS-2DPAGE; Q14684; -.
DR PaxDb; Q14684; -.
DR PRIDE; Q14684; -.
DR Ensembl; ENST00000340648; ENSP00000339145; ENSG00000160208.
DR GeneID; 23076; -.
DR KEGG; hsa:23076; -.
DR UCSC; uc002zdk.3; human.
DR CTD; 23076; -.
DR GeneCards; GC21P045079; -.
DR H-InvDB; HIX0016154; -.
DR HGNC; HGNC:23818; RRP1B.
DR HPA; HPA017893; -.
DR HPA; HPA020324; -.
DR MIM; 610654; gene.
DR neXtProt; NX_Q14684; -.
DR PharmGKB; PA162402138; -.
DR eggNOG; NOG299406; -.
DR HOGENOM; HOG000070179; -.
DR HOVERGEN; HBG098014; -.
DR InParanoid; Q14684; -.
DR KO; K14849; -.
DR OMA; MTAEFKK; -.
DR OrthoDB; EOG718KC8; -.
DR PhylomeDB; Q14684; -.
DR GeneWiki; RRP1B; -.
DR GenomeRNAi; 23076; -.
DR NextBio; 44187; -.
DR PRO; PR:Q14684; -.
DR Bgee; Q14684; -.
DR CleanEx; HS_RRP1B; -.
DR Genevestigator; Q14684; -.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0000791; C:euchromatin; IEA:Ensembl.
DR GO; GO:0000792; C:heterochromatin; IEA:Ensembl.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0030688; C:preribosome, small subunit precursor; IEA:InterPro.
DR GO; GO:0010923; P:negative regulation of phosphatase activity; IDA:UniProtKB.
DR GO; GO:0006364; P:rRNA processing; IEA:InterPro.
DR InterPro; IPR010301; Nop52.
DR PANTHER; PTHR13026; PTHR13026; 1.
DR Pfam; PF05997; Nop52; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Complete proteome; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1 758 Ribosomal RNA processing protein 1
FT homolog B.
FT /FTId=PRO_0000050729.
FT COMPBIAS 402 406 Poly-Lys.
FT MOD_RES 245 245 Phosphoserine.
FT MOD_RES 350 350 Phosphoserine.
FT MOD_RES 392 392 Phosphoserine.
FT MOD_RES 394 394 Phosphoserine.
FT MOD_RES 395 395 Phosphoserine.
FT MOD_RES 452 452 Phosphoserine.
FT MOD_RES 458 458 Phosphoserine.
FT MOD_RES 513 513 Phosphoserine.
FT MOD_RES 652 652 N6-acetyllysine.
FT MOD_RES 702 702 Phosphoserine.
FT MOD_RES 706 706 Phosphoserine.
FT MOD_RES 728 728 Phosphothreonine.
FT MOD_RES 732 732 Phosphoserine.
FT MOD_RES 735 735 Phosphoserine.
FT MOD_RES 736 736 Phosphoserine.
FT VAR_SEQ 51 68 Missing (in isoform 2).
FT /FTId=VSP_007801.
FT CONFLICT 436 436 L -> P (in Ref. 1; BAA11496 and 3;
FT AAH28386).
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
//
ID RRP1B_HUMAN Reviewed; 758 AA.
AC Q14684; Q8TBZ4;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
read moreDT 18-MAY-2010, sequence version 3.
DT 22-JAN-2014, entry version 124.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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.
RT The coding sequences of 40 new genes (KIAA0161-KIAA0200) deduced by
RT analysis of 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.,
RA Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y.,
RA Soeda E., Ohki M., Takagi T., Sakaki Y., Taudien S., Blechschmidt K.,
RA Polley A., Menzel U., Delabar J., Kumpf K., Lehmann R., Patterson D.,
RA Reichwald K., Rump A., Schillhabel M., Schudy A., Zimmermann W.,
RA Rosenthal A., Kudoh J., Shibuya K., Kawasaki K., Asakawa S.,
RA Shintani A., Sasaki T., Nagamine K., Mitsuyama S., Antonarakis S.E.,
RA Minoshima S., Shimizu N., Nordsiek G., Hornischer K., Brandt P.,
RA Scharfe M., Schoen O., Desario A., Reichelt J., Kauer G., Bloecker H.,
RA Ramser J., Beck A., Klages S., Hennig S., Riesselmann L., Dagand E.,
RA Wehrmeyer S., Borzym K., Gardiner K., Nizetic D., Francis F.,
RA 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).
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
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 MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-392 AND SER-513, AND
RP MASS SPECTROMETRY.
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
RT phosphorylation analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245, AND MASS
RP SPECTROMETRY.
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.,
RA Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
RT efficient phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245, AND MASS
RP SPECTROMETRY.
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
RT the 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
RP SER-736, AND MASS SPECTROMETRY.
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.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245; SER-350; SER-732
RP AND SER-735, AND MASS SPECTROMETRY.
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 [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-652, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245; SER-350; SER-513;
RP SER-702; SER-706; SER-732 AND SER-735, AND MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [14]
RP IDENTIFICATION BY MASS 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.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245; SER-513; SER-706;
RP THR-728 AND SER-732, AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [16]
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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- INTERACTION:
CC O15116:LSM1; NbExp=1; IntAct=EBI-372051, EBI-347619;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus.
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 Note=No experimental confirmation available;
CC -!- SIMILARITY: Belongs to the RRP1 family.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA11496.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC -----------------------------------------------------------------------
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CC Distributed under the Creative Commons Attribution-NoDerivs License
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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 RefSeq; NP_055871.1; NM_015056.2.
DR RefSeq; XP_005261151.1; XM_005261094.1.
DR UniGene; Hs.565725; -.
DR ProteinModelPortal; Q14684; -.
DR IntAct; Q14684; 11.
DR MINT; MINT-3029999; -.
DR STRING; 9606.ENSP00000339145; -.
DR PhosphoSite; Q14684; -.
DR DMDM; 296452976; -.
DR SWISS-2DPAGE; Q14684; -.
DR PaxDb; Q14684; -.
DR PRIDE; Q14684; -.
DR Ensembl; ENST00000340648; ENSP00000339145; ENSG00000160208.
DR GeneID; 23076; -.
DR KEGG; hsa:23076; -.
DR UCSC; uc002zdk.3; human.
DR CTD; 23076; -.
DR GeneCards; GC21P045079; -.
DR H-InvDB; HIX0016154; -.
DR HGNC; HGNC:23818; RRP1B.
DR HPA; HPA017893; -.
DR HPA; HPA020324; -.
DR MIM; 610654; gene.
DR neXtProt; NX_Q14684; -.
DR PharmGKB; PA162402138; -.
DR eggNOG; NOG299406; -.
DR HOGENOM; HOG000070179; -.
DR HOVERGEN; HBG098014; -.
DR InParanoid; Q14684; -.
DR KO; K14849; -.
DR OMA; MTAEFKK; -.
DR OrthoDB; EOG718KC8; -.
DR PhylomeDB; Q14684; -.
DR GeneWiki; RRP1B; -.
DR GenomeRNAi; 23076; -.
DR NextBio; 44187; -.
DR PRO; PR:Q14684; -.
DR Bgee; Q14684; -.
DR CleanEx; HS_RRP1B; -.
DR Genevestigator; Q14684; -.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0000791; C:euchromatin; IEA:Ensembl.
DR GO; GO:0000792; C:heterochromatin; IEA:Ensembl.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0030688; C:preribosome, small subunit precursor; IEA:InterPro.
DR GO; GO:0010923; P:negative regulation of phosphatase activity; IDA:UniProtKB.
DR GO; GO:0006364; P:rRNA processing; IEA:InterPro.
DR InterPro; IPR010301; Nop52.
DR PANTHER; PTHR13026; PTHR13026; 1.
DR Pfam; PF05997; Nop52; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Complete proteome; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1 758 Ribosomal RNA processing protein 1
FT homolog B.
FT /FTId=PRO_0000050729.
FT COMPBIAS 402 406 Poly-Lys.
FT MOD_RES 245 245 Phosphoserine.
FT MOD_RES 350 350 Phosphoserine.
FT MOD_RES 392 392 Phosphoserine.
FT MOD_RES 394 394 Phosphoserine.
FT MOD_RES 395 395 Phosphoserine.
FT MOD_RES 452 452 Phosphoserine.
FT MOD_RES 458 458 Phosphoserine.
FT MOD_RES 513 513 Phosphoserine.
FT MOD_RES 652 652 N6-acetyllysine.
FT MOD_RES 702 702 Phosphoserine.
FT MOD_RES 706 706 Phosphoserine.
FT MOD_RES 728 728 Phosphothreonine.
FT MOD_RES 732 732 Phosphoserine.
FT MOD_RES 735 735 Phosphoserine.
FT MOD_RES 736 736 Phosphoserine.
FT VAR_SEQ 51 68 Missing (in isoform 2).
FT /FTId=VSP_007801.
FT CONFLICT 436 436 L -> P (in Ref. 1; BAA11496 and 3;
FT AAH28386).
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
//
MIM
610654
*RECORD*
*FIELD* NO
610654
*FIELD* TI
*610654 RIBOSOMAL RNA-PROCESSING PROTEIN 1, S. CEREVISIAE, HOMOLOG OF, B;
RRP1B
;;KIAA0179 GENE; KIAA0179;;
read moreNNP1-LIKE; NNP1L
*FIELD* TX
DESCRIPTION
RRP1B is a nucleolar protein predicted to be involved in later steps in
60S ribosomal RNA processing (Chamousset et al., 2010).
CLONING
By sequencing clones obtained from a size-fractionated human immature
myeloid cell line cDNA library, Nagase et al. (1996) cloned RRP1B, which
they called KIAA0179. The deduced protein contains 762 amino acids.
Northern blot analysis detected expression in all tissues and cell lines
examined.
By searching an EST database for homologs of NNP1 (610653), Jansen et
al. (1997) identified KIAA0179, which they called NNP1L. The deduced
NNP1L protein contains 762 amino acids. The N-terminal regions of NNP1
and NNP1L share 80% similarity, including the presence of a predicted
nuclear localization signal, but the proteins differ at their C-terminal
ends.
Chamousset et al. (2010) stated that the deduced 758-amino acid RRP1B
protein has an N-terminal NOP52 (RRP1; 610653) homology domain and a
putative C-terminal protein phosphatase-1 (PP1; see 176875)-binding RVxF
motif. Immunofluorescence microscopy of U2OS or HeLa cells revealed that
RRP1B predominantly colocalized with B23 (NPM1; 164040) and pescadillo
(605819), which are markers of the nucleolar granular component. RRP1B
and other granular component proteins diffused with the breakdown of
nucleoli in mitosis and reaccumulated in prenucleolar bodies during late
telophase. Sucrose gradient fractionation confirmed specific association
of RRP1B with nuclear pre-60S. Western blot analysis detected RRP1B at
an apparent molecular mass of about 84 kD.
By immunohistochemical analysis, Paik et al. (2010) found that RRP1B
colocalized with the transcription factor E2F1 (189971) in nucleoli and
punctate nucleoplasmic foci of several human cell lines.
GENE FUNCTION
Using a quantitative proteomics-based approach and immunoprecipitation
analysis, Chamousset et al. (2010) showed that RRP1B interacted with
PP1-beta (PPP1CB; 600590) and PP1-gamma (PPP1CC; 176914) in HeLa and
U2OS cell nucleoli. RRP1B did not interact with PP1-alpha (PPP1CA;
176875), which localized to cytosol. Mutation analysis revealed that the
RVxF motif of RRP1B was required for PP1 binding. Treatment of U2OS or
HeLa cells with RNase disrupted association of RRP1B with nucleoli.
Knockdown of RRP1B did not alter cell growth or proliferation, but it
increased the amount of larger RNA species detected by Northern blot
analysis. Coimmunoprecipitation analysis revealed that RRP1B interacted
with the 60S ribosomal subunit processing complex, including NOL1
(164031) and NOP52.
Using semiquantitative RT-PCR, Paik et al. (2010) found that
overexpression of E2F1, but not other E2F family member, upregulated
expression of RRP1B in several human cell lines. Conversely, knockdown
of E2F1 reduced RRP1B transcription. RRP1B expression peaked at the G1/S
transition in human cell lines and primary foreskin fibroblasts,
consistent with E2F1 expression. Truncation analysis coupled with
reporter gene assays showed that E2F1 bound and activated the RRP1B
promoter at the most proximal E2F site only. RRP1B expression was also
elevated following exposure of human cell lines to several DNA-damaging
agents. Knockdown of RRP1B decreased apoptosis induced by genotoxic
agents or by E2F1 overexpression, but it had no effect on E2F1-regulated
cell proliferation. Knockdown of RRP1B reduced the expression of a
subset of E2F1-dependent apoptotic genes, including caspase-3 (CASP3;
600636), caspase-7 (CASP7; 601761), and APAF1 (602233).
Coimmunoprecipitation, protein pull-down, and chromatin
immunoprecipitation assays showed that regulation of these genes by
RRP1B occurred by direct interaction between RRP1B with E2F1.
GENE STRUCTURE
Jansen et al. (1997) determined that the RRP1B gene contains 14 exons.
MAPPING
By PCR of human-rodent hybrid cell lines, Nagase et al. (1996) mapped
the RRP1B gene to chromosome 21. Jansen et al. (1997) mapped the RRP1B
gene to chromosome 21q22.3, proximal to the cystatin B gene (CSTB;
601145), by genomic sequence analysis. The RRP1B gene also lies 75 kb
proximal to the RRP1 gene.
*FIELD* RF
1. Chamousset, D.; De Wever, V.; Moorhead, G. B.; Chen, Y.; Boisvert,
F.-M.; Lamond, A. I.; Trinkle-Mulcahy, L.: RRP1B targets PP1 to mammalian
cell nucleoli and is associated with pre-60S ribosomal subunits. Molec.
Biol. Cell 21: 4212-4226, 2010.
2. Jansen, E.; Meulemans, S. M. P.; Orlans, I. C. R.; Van de Ven,
W. J. M.: The NNP-1 gene (D21S2056E), which encodes a novel nuclear
protein, maps in close proximity to the cystatin B gene within the
EPM1 and APECED critical region on 21q22.3. Genomics 42: 336-341,
1997.
3. Nagase, T.; Seki, N.; Ishikawa, K.; Tanaka, A.; Nomura, N.: Prediction
of the coding sequences of unidentified human genes. V. The coding
sequences of 40 new genes (KIAA0161-KIAA0200) deduced by analysis
of cDNA clones from human cell line KG-1. DNA Res. 3: 17-24, 1996.
4. Paik, J. C.; Wang, B.; Liu, K.; Lue, J. K.; Lin, W.-C.: Regulation
of E2F1-induced apoptosis by the nucleolar protein RRP1B. J. Biol.
Chem. 285: 6348-6363, 2010.
*FIELD* CN
Patricia A. Hartz - updated: 11/1/2011
Patricia A. Hartz - updated: 9/15/2011
*FIELD* CD
Patricia A. Hartz: 12/15/2006
*FIELD* ED
mgross: 02/08/2012
mgross: 2/8/2012
terry: 11/1/2011
mgross: 9/27/2011
terry: 9/15/2011
mgross: 12/15/2006
*RECORD*
*FIELD* NO
610654
*FIELD* TI
*610654 RIBOSOMAL RNA-PROCESSING PROTEIN 1, S. CEREVISIAE, HOMOLOG OF, B;
RRP1B
;;KIAA0179 GENE; KIAA0179;;
read moreNNP1-LIKE; NNP1L
*FIELD* TX
DESCRIPTION
RRP1B is a nucleolar protein predicted to be involved in later steps in
60S ribosomal RNA processing (Chamousset et al., 2010).
CLONING
By sequencing clones obtained from a size-fractionated human immature
myeloid cell line cDNA library, Nagase et al. (1996) cloned RRP1B, which
they called KIAA0179. The deduced protein contains 762 amino acids.
Northern blot analysis detected expression in all tissues and cell lines
examined.
By searching an EST database for homologs of NNP1 (610653), Jansen et
al. (1997) identified KIAA0179, which they called NNP1L. The deduced
NNP1L protein contains 762 amino acids. The N-terminal regions of NNP1
and NNP1L share 80% similarity, including the presence of a predicted
nuclear localization signal, but the proteins differ at their C-terminal
ends.
Chamousset et al. (2010) stated that the deduced 758-amino acid RRP1B
protein has an N-terminal NOP52 (RRP1; 610653) homology domain and a
putative C-terminal protein phosphatase-1 (PP1; see 176875)-binding RVxF
motif. Immunofluorescence microscopy of U2OS or HeLa cells revealed that
RRP1B predominantly colocalized with B23 (NPM1; 164040) and pescadillo
(605819), which are markers of the nucleolar granular component. RRP1B
and other granular component proteins diffused with the breakdown of
nucleoli in mitosis and reaccumulated in prenucleolar bodies during late
telophase. Sucrose gradient fractionation confirmed specific association
of RRP1B with nuclear pre-60S. Western blot analysis detected RRP1B at
an apparent molecular mass of about 84 kD.
By immunohistochemical analysis, Paik et al. (2010) found that RRP1B
colocalized with the transcription factor E2F1 (189971) in nucleoli and
punctate nucleoplasmic foci of several human cell lines.
GENE FUNCTION
Using a quantitative proteomics-based approach and immunoprecipitation
analysis, Chamousset et al. (2010) showed that RRP1B interacted with
PP1-beta (PPP1CB; 600590) and PP1-gamma (PPP1CC; 176914) in HeLa and
U2OS cell nucleoli. RRP1B did not interact with PP1-alpha (PPP1CA;
176875), which localized to cytosol. Mutation analysis revealed that the
RVxF motif of RRP1B was required for PP1 binding. Treatment of U2OS or
HeLa cells with RNase disrupted association of RRP1B with nucleoli.
Knockdown of RRP1B did not alter cell growth or proliferation, but it
increased the amount of larger RNA species detected by Northern blot
analysis. Coimmunoprecipitation analysis revealed that RRP1B interacted
with the 60S ribosomal subunit processing complex, including NOL1
(164031) and NOP52.
Using semiquantitative RT-PCR, Paik et al. (2010) found that
overexpression of E2F1, but not other E2F family member, upregulated
expression of RRP1B in several human cell lines. Conversely, knockdown
of E2F1 reduced RRP1B transcription. RRP1B expression peaked at the G1/S
transition in human cell lines and primary foreskin fibroblasts,
consistent with E2F1 expression. Truncation analysis coupled with
reporter gene assays showed that E2F1 bound and activated the RRP1B
promoter at the most proximal E2F site only. RRP1B expression was also
elevated following exposure of human cell lines to several DNA-damaging
agents. Knockdown of RRP1B decreased apoptosis induced by genotoxic
agents or by E2F1 overexpression, but it had no effect on E2F1-regulated
cell proliferation. Knockdown of RRP1B reduced the expression of a
subset of E2F1-dependent apoptotic genes, including caspase-3 (CASP3;
600636), caspase-7 (CASP7; 601761), and APAF1 (602233).
Coimmunoprecipitation, protein pull-down, and chromatin
immunoprecipitation assays showed that regulation of these genes by
RRP1B occurred by direct interaction between RRP1B with E2F1.
GENE STRUCTURE
Jansen et al. (1997) determined that the RRP1B gene contains 14 exons.
MAPPING
By PCR of human-rodent hybrid cell lines, Nagase et al. (1996) mapped
the RRP1B gene to chromosome 21. Jansen et al. (1997) mapped the RRP1B
gene to chromosome 21q22.3, proximal to the cystatin B gene (CSTB;
601145), by genomic sequence analysis. The RRP1B gene also lies 75 kb
proximal to the RRP1 gene.
*FIELD* RF
1. Chamousset, D.; De Wever, V.; Moorhead, G. B.; Chen, Y.; Boisvert,
F.-M.; Lamond, A. I.; Trinkle-Mulcahy, L.: RRP1B targets PP1 to mammalian
cell nucleoli and is associated with pre-60S ribosomal subunits. Molec.
Biol. Cell 21: 4212-4226, 2010.
2. Jansen, E.; Meulemans, S. M. P.; Orlans, I. C. R.; Van de Ven,
W. J. M.: The NNP-1 gene (D21S2056E), which encodes a novel nuclear
protein, maps in close proximity to the cystatin B gene within the
EPM1 and APECED critical region on 21q22.3. Genomics 42: 336-341,
1997.
3. Nagase, T.; Seki, N.; Ishikawa, K.; Tanaka, A.; Nomura, N.: Prediction
of the coding sequences of unidentified human genes. V. The coding
sequences of 40 new genes (KIAA0161-KIAA0200) deduced by analysis
of cDNA clones from human cell line KG-1. DNA Res. 3: 17-24, 1996.
4. Paik, J. C.; Wang, B.; Liu, K.; Lue, J. K.; Lin, W.-C.: Regulation
of E2F1-induced apoptosis by the nucleolar protein RRP1B. J. Biol.
Chem. 285: 6348-6363, 2010.
*FIELD* CN
Patricia A. Hartz - updated: 11/1/2011
Patricia A. Hartz - updated: 9/15/2011
*FIELD* CD
Patricia A. Hartz: 12/15/2006
*FIELD* ED
mgross: 02/08/2012
mgross: 2/8/2012
terry: 11/1/2011
mgross: 9/27/2011
terry: 9/15/2011
mgross: 12/15/2006