ID U3IP2_HUMAN Reviewed; 475 AA. AC O43818; B2R996; Q8IZ30; DT 10-OCT-2003, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 1. DT 25-JAN-2012, entry version 99. 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, 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]. RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [4] 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 [5] 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 [6] 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 [7] RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE RP SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; 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 [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50; SER-51 AND SER-53, RP AND MASS 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 [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-475, AND MASS RP SPECTROMETRY. RC TISSUE=Cervix carcinoma; 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 [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50; SER-51; SER-53 AND RP SER-57, 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 [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50; SER-51 AND SER-53, RP AND MASS SPECTROMETRY. RC TISSUE=Embryonic kidney; 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 [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50; SER-51; SER-53 AND RP SER-57, 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 [13] 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. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJ001340; CAA04687.1; -; mRNA. DR EMBL; AK313696; BAG36443.1; -; mRNA. DR EMBL; CH471055; EAW65159.1; -; Genomic_DNA. 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; NM_004704.3. DR UniGene; Hs.153768; -. DR ProteinModelPortal; O43818; -. DR SMR; O43818; 136-456. DR IntAct; O43818; 2. 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. 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 HPA; HPA038798; -. DR neXtProt; NX_O43818; -. DR PharmGKB; PA162402176; -. DR eggNOG; prNOG06018; -. DR GeneTree; ENSGT00550000075093; -. DR HOGENOM; HBG713247; -. DR HOVERGEN; HBG079296; -. DR InParanoid; O43818; -. DR OMA; GSHSSCV; -. DR OrthoDB; EOG4XKV6X; -. DR PhylomeDB; O43818; -. 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. DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom. DR InterPro; IPR001680; WD40_repeat. DR InterPro; IPR011046; WD40_repeat-like_dom. DR InterPro; IPR019775; WD40_repeat_CS. DR InterPro; IPR017986; WD40_repeat_dom. DR Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 1. DR KO; K14793; -. DR Pfam; PF00400; WD40; 6. DR PRINTS; PR00320; GPROTEINBRPT. DR SMART; SM00320; WD40; 6. DR SUPFAM; SSF50978; WD40_like; 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 Complete proteome; Direct protein sequencing; Nucleus; Phosphoprotein; KW Polymorphism; Reference proteome; Repeat; Ribonucleoprotein; KW RNA-binding; rRNA processing; 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 //