U3IP2_MOUSE
ID U3IP2_MOUSE Reviewed; 475 AA.
AC Q91WM3; Q8CFB7;
DT 24-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=U3 small nucleolar RNA-interacting protein 2;
DE AltName: Full=RRP9 homolog;
DE AltName: Full=U3 small nucleolar ribonucleoprotein-associated 55 kDa protein;
DE Short=U3 snoRNP-associated 55 kDa protein;
DE Short=U3-55K;
GN Name=Rrp9; Synonyms=Rnu3ip2, U3-55k;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=12448766;
RA Urbanek P., Paces J., Kralova J., Dvorak M., Paces V.;
RT "Cloning and expression of PARP-3 (Adprt3) and U3-55k, two genes closely
RT linked on mouse chromosome 9.";
RL Folia Biol. (Praha) 48:182-191(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-470, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50; SER-51; SER-53 AND
RP SER-470, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-470, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50; SER-51; SER-53 AND
RP SER-470, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Liver, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 (pre-rRNA).
CC {ECO:0000250|UniProtKB:O43818}.
CC -!- SUBUNIT: Interacts specifically with the U3 small nucleolar RNA (U3
CC snoRNA). Binds a sub-fragment of the U3 snoRNA surrounding the B/C
CC motif (3UBC). This association with the U3BC RNA is dependent on the
CC binding of a protein called 15.5K to the box B/C motif. The association
CC of the protein with the U3BC RNA was found to be also dependent on a
CC conserved RNA structure that flanks the box B/C motif.
CC {ECO:0000250|UniProtKB:O43818}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:O43818}.
CC -!- DOMAIN: The WD domains are required for nucleolar localization and U3
CC small nucleolar RNAs binding. {ECO:0000250|UniProtKB:O43818}.
CC -!- PTM: Acetylation at Lys-12 and Lys-25 by KAT2B/PCAF under stress
CC impairs pre-rRNA processing. Deacetylation by SIRT7 enhances RRP9-
CC binding to U3 snoRNA, which is a prerequisite for pre-rRNA processing.
CC {ECO:0000250|UniProtKB:O43818}.
CC -!- SIMILARITY: Belongs to the WD repeat RRP9 family. {ECO:0000305}.
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DR EMBL; AF368232; AAN62792.1; -; mRNA.
DR EMBL; AF368234; AAN62794.1; -; Genomic_DNA.
DR EMBL; AK076113; BAC36193.1; -; mRNA.
DR EMBL; BC014703; AAH14703.1; -; mRNA.
DR CCDS; CCDS23481.1; -.
DR RefSeq; NP_663595.1; NM_145620.4.
DR AlphaFoldDB; Q91WM3; -.
DR SMR; Q91WM3; -.
DR BioGRID; 205694; 5.
DR IntAct; Q91WM3; 1.
DR MINT; Q91WM3; -.
DR STRING; 10090.ENSMUSP00000038580; -.
DR iPTMnet; Q91WM3; -.
DR PhosphoSitePlus; Q91WM3; -.
DR EPD; Q91WM3; -.
DR jPOST; Q91WM3; -.
DR MaxQB; Q91WM3; -.
DR PaxDb; Q91WM3; -.
DR PeptideAtlas; Q91WM3; -.
DR PRIDE; Q91WM3; -.
DR ProteomicsDB; 298444; -.
DR Antibodypedia; 14210; 84 antibodies from 21 providers.
DR DNASU; 27966; -.
DR Ensembl; ENSMUST00000047721; ENSMUSP00000038580; ENSMUSG00000041506.
DR GeneID; 27966; -.
DR KEGG; mmu:27966; -.
DR UCSC; uc009rkb.1; mouse.
DR CTD; 9136; -.
DR MGI; MGI:2384313; Rrp9.
DR VEuPathDB; HostDB:ENSMUSG00000041506; -.
DR eggNOG; KOG0299; Eukaryota.
DR GeneTree; ENSGT00940000158328; -.
DR HOGENOM; CLU_014017_1_1_1; -.
DR InParanoid; Q91WM3; -.
DR OMA; RIWKITE; -.
DR OrthoDB; 948159at2759; -.
DR PhylomeDB; Q91WM3; -.
DR TreeFam; TF105828; -.
DR Reactome; R-MMU-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR BioGRID-ORCS; 27966; 27 hits in 77 CRISPR screens.
DR ChiTaRS; Rrp9; mouse.
DR PRO; PR:Q91WM3; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q91WM3; protein.
DR Bgee; ENSMUSG00000041506; Expressed in embryonic brain and 172 other tissues.
DR ExpressionAtlas; Q91WM3; baseline and differential.
DR Genevisible; Q91WM3; MM.
DR GO; GO:0031428; C:box C/D RNP complex; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0032040; C:small-subunit processome; IBA:GO_Central.
DR GO; GO:0030515; F:snoRNA binding; IBA:GO_Central.
DR GO; GO:0034511; F:U3 snoRNA binding; ISS:UniProtKB.
DR GO; GO:0006364; P:rRNA processing; ISS:UniProtKB.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR039241; Rrp9-like.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR19865; PTHR19865; 1.
DR Pfam; PF00400; WD40; 5.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF50978; SSF50978; 1.
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 Acetylation; Isopeptide bond; Methylation; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Ribonucleoprotein; RNA-binding;
KW rRNA processing; Ubl conjugation; WD repeat.
FT CHAIN 1..475
FT /note="U3 small nucleolar RNA-interacting protein 2"
FT /id="PRO_0000051314"
FT REPEAT 144..183
FT /note="WD 1"
FT REPEAT 197..236
FT /note="WD 2"
FT REPEAT 239..278
FT /note="WD 3"
FT REPEAT 281..320
FT /note="WD 4"
FT REPEAT 322..360
FT /note="WD 5"
FT REPEAT 374..413
FT /note="WD 6"
FT REPEAT 419..460
FT /note="WD 7"
FT REGION 1..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 8..40
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 24..64
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 10
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:O43818"
FT MOD_RES 12
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O43818"
FT MOD_RES 25
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O43818"
FT MOD_RES 50
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 51
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 53
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 57
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43818"
FT MOD_RES 470
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT CROSSLNK 113
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O43818"
SQ SEQUENCE 475 AA; 52107 MW; EF7E2B2D9CD68F6B CRC64;
MSTAVATRKR AKPAPGPGAA PVAGKRRRKV DSAADRGKSK GGGKMNEEIS SDSESESLAP
RKTEEEEEEE LEETAQEKKL RLAKLYLEQL RQQEEEKAEA RAFEEDQVAG RLKEDVLEQR
GRLQKSVAKE IQAPAPTDIR VLRGHQLSIT CLVITPDDLA IFSAAKDCTI IKWSVETGRK
LHVIPRAKKG AQGQPAGHSS HVLCMAISSD GKYLASGDRS KLILIWEAQS CQHLYTFTGH
RDAVSGLAFR KGTHQLYSTS HDRSVKVWNA AENSYVETLF GHQDAVAALD ALSRECCVTA
GGRDGTVRVW KIPEESQLVF YGHQGSIDCI HLINEEHMVS GADDGSVALW GLSKKRPLAL
QREAHGLHGE PGLEQPFWVS SVAALLNTDL VATGSHNARV RLWQCGEGFR QLDPLCDIPL
VGFINSLKFS SAGDFLVAGV GQEHRLGRWW RIKEARNSVC IIPLRRLPVS PVAGS
