ID   U3IP2_HUMAN             Reviewed;         475 AA.
AC   O43818; Q8IZ30;
DT   10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-NOV-2009, entry version 82.
DE   RecName: Full=U3 small nucleolar RNA-interacting protein 2;
DE   AltName: Full=U3 small nucleolar ribonucleoprotein-associated 55 kDa protein;
DE            Short=U3 snoRNP-associated 55 kDa protein;
DE            Short=U3-55K;
DE   AltName: Full=RRP9 homolog;
GN   Name=RRP9; Synonyms=RNU3IP2, U355K;
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 [MRNA], AND PROTEIN SEQUENCE OF 102-113 AND
RP   267-273.
RC   TISSUE=Teratocarcinoma;
RX   MEDLINE=98078705; PubMed=9418896;
RA   Pluk H., Soffner J., Luehrmann R., van Venrooij W.J.;
RT   "cDNA cloning and characterization of the human U3 small nucleolar
RT   ribonucleoprotein complex-associated 55-kilodalton protein.";
RL   Mol. Cell. Biol. 18:488-498(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain, and Skin;
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   [3]
RP   INTERACTION WITH U3 SNRNA.
RX   MEDLINE=20440388; PubMed=10982864; DOI=10.1093/nar/28.18.3462;
RA   Lukowiak A.A., Granneman S., Mattox S.A., Speckmann W.A., Jones K.,
RA   Pluk H., van Venrooij W.J., Terns R.M., Terns M.P.;
RT   "Interaction of the U3-55k protein with U3 snoRNA is mediated by the
RT   box B/C motif of U3 and the WD repeats of U3-55k.";
RL   Nucleic Acids Res. 28:3462-3471(2000).
RN   [4]
RP   INTERACTION WITH U3 SNRNA.
RX   MEDLINE=22359099; PubMed=12381732; DOI=10.1074/jbc.M206631200;
RA   Granneman S., Pruijn G.J.M., Horstman W., van Venrooij W.J.,
RA   Luehrmann R., Watkins N.J.;
RT   "The hU3-55K protein requires 15.5K binding to the box B/C motif as
RT   well as flanking RNA elements for its association with the U3 small
RT   nucleolar RNA in Vitro.";
RL   J. Biol. Chem. 277:48490-48500(2002).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE
RP   SCALE ANALYSIS].
RX   MEDLINE=22317277; 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   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50; SER-51 AND SER-53,
RP   AND MASS SPECTROMETRY.
RC   TISSUE=Epithelium;
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   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-475, AND MASS
RP   SPECTROMETRY.
RX   PubMed=19007248; DOI=10.1021/ac801708p;
RA   Wang B., Malik R., Nigg E.A., Korner R.;
RT   "Evaluation of the low-specificity protease elastase for large-scale
RT   phosphoproteome analysis.";
RL   Anal. Chem. 80:9526-9533(2008).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50; SER-51; SER-53 AND
RP   SER-57, AND MASS SPECTROMETRY.
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   [9]
RP   VARIANTS [LARGE SCALE ANALYSIS] GLY-8 AND GLU-342.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
RA   Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA   Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA   Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA   Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal
RT   cancers.";
RL   Science 314:268-274(2006).
CC   -!- FUNCTION: Component of a nucleolar small nuclear ribonucleoprotein
CC       particle (snoRNP) thought to participate in the processing and
CC       modification of pre-ribosomal RNA.
CC   -!- SUBUNIT: Interacts specifically with the U3 small nucleolar RNA
CC       (U3 snoRNA). Binds a sub-fragment of the U3 snoRNA surrounding the
CC       B/C motif (3UBC). This association with the U3BC RNA is dependent
CC       on the binding of a protein called 15.5K to the box B/C motif. The
CC       association of the protein with the U3BC RNA was found to be also
CC       dependent on a conserved RNA structure that flanks the box B/C
CC       motif.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus.
CC   -!- DOMAIN: The WD domains are required for nucleolar localization and
CC       U3 small nucleolar RNAs binding.
CC   -!- SIMILARITY: Belongs to the WD repeat RRP9 family.
CC   -!- SIMILARITY: Contains 7 WD repeats.
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DR   EMBL; AJ001340; CAA04687.1; -; mRNA.
DR   EMBL; BC001113; AAH01113.1; -; mRNA.
DR   EMBL; BC009879; AAH09879.1; -; mRNA.
DR   EMBL; BC010048; AAH10048.1; -; mRNA.
DR   EMBL; BC023662; AAH23662.2; -; mRNA.
DR   IPI; IPI00217862; -.
DR   RefSeq; NP_004695.1; -.
DR   UniGene; Hs.153768; -.
DR   HSSP; P16649; 1ERJ.
DR   IntAct; O43818; 1.
DR   STRING; O43818; -.
DR   PhosphoSite; O43818; -.
DR   SWISS-2DPAGE; O43818; -.
DR   DOSAC-COBS-2DPAGE; O43818; -.
DR   PeptideAtlas; O43818; -.
DR   PRIDE; O43818; -.
DR   Ensembl; ENST00000232888; ENSP00000232888; ENSG00000114767; Homo sapiens.
DR   GeneID; 9136; -.
DR   KEGG; hsa:9136; -.
DR   UCSC; uc003dbw.1; human.
DR   CTD; 9136; -.
DR   GeneCards; GC03M051943; -.
DR   H-InvDB; HIX0003335; -.
DR   HGNC; HGNC:16829; RRP9.
DR   HOGENOM; O43818; -.
DR   HOVERGEN; O43818; -.
DR   OMA; WEAQSCQ; -.
DR   NextBio; 34259; -.
DR   ArrayExpress; O43818; -.
DR   Bgee; O43818; -.
DR   CleanEx; HS_RRP9; -.
DR   Genevestigator; O43818; -.
DR   GermOnline; ENSG00000114767; Homo sapiens.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0030532; C:small nuclear ribonucleoprotein complex; TAS:ProtInc.
DR   GO; GO:0005732; C:small nucleolar ribonucleoprotein complex; TAS:ProtInc.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006364; P:rRNA processing; TAS:ProtInc.
DR   InterPro; IPR020472; G-protein_beta_WD-40_rep_reg.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR019782; WD40_repeat_2.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR017986; WD40_repeat_dom.
DR   InterPro; IPR019781; WD40_repeat_sg.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 1.
DR   Pfam; PF00400; WD40; 5.
DR   PRINTS; PR00320; GPROTEINBRPT.
DR   ProDom; PD000018; WD40; 1.
DR   SMART; SM00320; WD40; 6.
DR   PROSITE; PS00678; WD_REPEATS_1; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 5.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Direct protein sequencing; Nucleus; Phosphoprotein;
KW   Polymorphism; Repeat; Ribonucleoprotein; RNA-binding; rRNA processing;
KW   WD repeat.
FT   CHAIN         1    475       U3 small nucleolar RNA-interacting
FT                                protein 2.
FT                                /FTId=PRO_0000051313.
FT   REPEAT      144    183       WD 1.
FT   REPEAT      197    236       WD 2.
FT   REPEAT      239    278       WD 3.
FT   REPEAT      281    320       WD 4.
FT   REPEAT      322    360       WD 5.
FT   REPEAT      374    413       WD 6.
FT   REPEAT      419    460       WD 7.
FT   MOTIF         8     40       Nuclear localization signal (Potential).
FT   COMPBIAS     47    105       Glu-rich.
FT   MOD_RES      50     50       Phosphoserine.
FT   MOD_RES      51     51       Phosphoserine.
FT   MOD_RES      53     53       Phosphoserine.
FT   MOD_RES      57     57       Phosphoserine.
FT   MOD_RES     475    475       Phosphoserine.
FT   VARIANT       8      8       R -> G (in a breast cancer sample;
FT                                somatic mutation).
FT                                /FTId=VAR_035887.
FT   VARIANT     342    342       A -> E (in a breast cancer sample;
FT                                somatic mutation).
FT                                /FTId=VAR_035888.
SQ   SEQUENCE   475 AA;  51841 MW;  3CD19F66EA75B627 CRC64;
     MSATAAARKR GKPASGAGAG AGAGKRRRKA DSAGDRGKSK GGGKMNEEIS SDSESESLAP
     RKPEEEEEEE LEETAQEKKL RLAKLYLEQL RQQEEEKAEA RAFEEDQVAG RLKEDVLEQR
     GRLQKLVAKE IQAPASADIR VLRGHQLSIT CLVVTPDDSA IFSAAKDCSI IKWSVESGRK
     LHVIPRAKKG AEGKPPGHSS HVLCMAISSD GKYLASGDRS KLILIWEAQS CQHLYTFTGH
     RDAVSGLAFR RGTHQLYSTS HDRSVKVWNV AENSYVETLF GHQDAVAALD ALSRECCVTA
     GGRDGTVRVW KIPEESQLVF YGHQGSIDCI HLINEEHMVS GADDGSVALW GLSKKRPLAL
     QREAHGLRGE PGLEQPFWIS SVAALLNTDL VATGSHSSCV RLWQCGEGFR QLDLLCDIPL
     VGFINSLKFS SSGDFLVAGV GQEHRLGRWW RIKEARNSVC IIPLRRVPVP PAAGS
//