UTP18_HUMAN
ID UTP18_HUMAN Reviewed; 556 AA.
AC Q9Y5J1; Q9H4N6;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 3.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=U3 small nucleolar RNA-associated protein 18 homolog;
DE AltName: Full=WD repeat-containing protein 50;
GN Name=UTP18; Synonyms=WDR50; ORFNames=CDABP0061, CGI-48;
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].
RX PubMed=10810093; DOI=10.1101/gr.10.5.703;
RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
RT "Identification of novel human genes evolutionarily conserved in
RT Caenorhabditis elegans by comparative proteomics.";
RL Genome Res. 10:703-713(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 162-556.
RC TISSUE=Leukemia;
RA Zhou J., Yu W., Tang H., Mei G., Tsang Y.T.M., Bouck J., Gibbs R.A.,
RA Margolin J.F.;
RT "Pediatric leukemia cDNA sequencing project.";
RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
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-121 AND SER-124, AND
RP IDENTIFICATION BY 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-121 AND SER-124, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=T-cell;
RX PubMed=19367720; DOI=10.1021/pr800500r;
RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
RT "Phosphorylation analysis of primary human T lymphocytes using sequential
RT IMAC and titanium oxide enrichment.";
RL J. Proteome Res. 7:5167-5176(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-204; SER-205; SER-206 AND
RP SER-210, 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-121 AND SER-124, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by enrichment
RT and fractionation of phosphopeptides with strong anion exchange
RT chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [9]
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-206 AND SER-210, AND
RP 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-121; SER-124 AND SER-210, AND
RP IDENTIFICATION BY MASS 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-121; SER-124; THR-204;
RP SER-206 AND SER-210, 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-121; SER-124; SER-210 AND
RP THR-221, AND IDENTIFICATION BY MASS SPECTROMETRY [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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-121; SER-124; THR-204 AND
RP SER-210, AND IDENTIFICATION BY 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 [15]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-84; LYS-183; LYS-201 AND LYS-517,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- FUNCTION: Involved in nucleolar processing of pre-18S ribosomal RNA.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12429849}.
CC -!- SIMILARITY: Belongs to the WD repeat UTP18 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD34043.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAG01999.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF151806; AAD34043.1; ALT_FRAME; mRNA.
DR EMBL; BC025276; AAH25276.2; -; mRNA.
DR EMBL; AY007138; AAG01999.1; ALT_INIT; mRNA.
DR CCDS; CCDS42362.1; -.
DR RefSeq; NP_057085.2; NM_016001.2.
DR PDB; 7MQ8; EM; 3.60 A; LS=1-556.
DR PDB; 7MQ9; EM; 3.87 A; LS=1-556.
DR PDB; 7MQA; EM; 2.70 A; LS=1-556.
DR PDBsum; 7MQ8; -.
DR PDBsum; 7MQ9; -.
DR PDBsum; 7MQA; -.
DR AlphaFoldDB; Q9Y5J1; -.
DR SMR; Q9Y5J1; -.
DR BioGRID; 119285; 150.
DR IntAct; Q9Y5J1; 36.
DR MINT; Q9Y5J1; -.
DR STRING; 9606.ENSP00000225298; -.
DR GlyGen; Q9Y5J1; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9Y5J1; -.
DR PhosphoSitePlus; Q9Y5J1; -.
DR BioMuta; UTP18; -.
DR DMDM; 73920973; -.
DR SWISS-2DPAGE; Q9Y5J1; -.
DR EPD; Q9Y5J1; -.
DR jPOST; Q9Y5J1; -.
DR MassIVE; Q9Y5J1; -.
DR MaxQB; Q9Y5J1; -.
DR PaxDb; Q9Y5J1; -.
DR PeptideAtlas; Q9Y5J1; -.
DR PRIDE; Q9Y5J1; -.
DR ProteomicsDB; 86417; -.
DR Antibodypedia; 30799; 75 antibodies from 19 providers.
DR DNASU; 51096; -.
DR Ensembl; ENST00000225298.12; ENSP00000225298.7; ENSG00000011260.14.
DR GeneID; 51096; -.
DR KEGG; hsa:51096; -.
DR MANE-Select; ENST00000225298.12; ENSP00000225298.7; NM_016001.3; NP_057085.2.
DR UCSC; uc002its.4; human.
DR CTD; 51096; -.
DR DisGeNET; 51096; -.
DR GeneCards; UTP18; -.
DR HGNC; HGNC:24274; UTP18.
DR HPA; ENSG00000011260; Low tissue specificity.
DR MIM; 612816; gene.
DR neXtProt; NX_Q9Y5J1; -.
DR OpenTargets; ENSG00000011260; -.
DR PharmGKB; PA134984104; -.
DR VEuPathDB; HostDB:ENSG00000011260; -.
DR eggNOG; KOG2055; Eukaryota.
DR GeneTree; ENSGT00440000033919; -.
DR HOGENOM; CLU_011055_3_1_1; -.
DR InParanoid; Q9Y5J1; -.
DR OMA; QFHPTST; -.
DR OrthoDB; 462558at2759; -.
DR PhylomeDB; Q9Y5J1; -.
DR TreeFam; TF313426; -.
DR PathwayCommons; Q9Y5J1; -.
DR Reactome; R-HSA-6790901; rRNA modification in the nucleus and cytosol.
DR Reactome; R-HSA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR SignaLink; Q9Y5J1; -.
DR BioGRID-ORCS; 51096; 640 hits in 1091 CRISPR screens.
DR ChiTaRS; UTP18; human.
DR GeneWiki; UTP18; -.
DR GenomeRNAi; 51096; -.
DR Pharos; Q9Y5J1; Tdark.
DR PRO; PR:Q9Y5J1; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q9Y5J1; protein.
DR Bgee; ENSG00000011260; Expressed in right testis and 203 other tissues.
DR ExpressionAtlas; Q9Y5J1; baseline and differential.
DR Genevisible; Q9Y5J1; HS.
DR GO; GO:0031965; C:nuclear membrane; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0034388; C:Pwp2p-containing subcomplex of 90S preribosome; IBA:GO_Central.
DR GO; GO:0032040; C:small-subunit processome; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR045161; Utp18.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR18359; PTHR18359; 1.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; rRNA processing; Ubl conjugation; WD repeat.
FT CHAIN 1..556
FT /note="U3 small nucleolar RNA-associated protein 18
FT homolog"
FT /id="PRO_0000051405"
FT REPEAT 249..288
FT /note="WD 1"
FT REPEAT 293..333
FT /note="WD 2"
FT REPEAT 339..380
FT /note="WD 3"
FT REPEAT 381..419
FT /note="WD 4"
FT REPEAT 421..462
FT /note="WD 5"
FT REPEAT 471..512
FT /note="WD 6"
FT REGION 1..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 111..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 193..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..127
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 121
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:19367720,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 124
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:19367720,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 204
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569"
FT MOD_RES 205
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 206
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692"
FT MOD_RES 210
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 ECO:0007744|PubMed:24275569"
FT MOD_RES 221
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 84
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 183
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 201
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 517
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CONFLICT 543..556
FT /note="GKALMYRLHHYSDF -> ARP (in Ref. 1; AAD34043)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 556 AA; 62004 MW; 800139F974F4EDF6 CRC64;
MPPERRRRMK LDRRTGAKPK RKPGMRPDWK AGAGPGGPPQ KPAPSSQRKP PARPSAAAAA
IAVAAAEEER RLRQRNRLRL EEDKPAVERC LEELVFGDVE NDEDALLRRL RGPRVQEHED
SGDSEVENEA KGNFPPQKKP VWVDEEDEDE EMVDMMNNRF RKDMMKNASE SKLSKDNLKK
RLKEEFQHAM GGVPAWAETT KRKTSSDDES EEDEDDLLQR TGNFISTSTS LPRGILKMKN
CQHANAERPT VARISSVQFH PGAQIVMVAG LDNAVSLFQV DGKTNPKIQS IYLERFPIFK
ACFSANGEEV LATSTHSKVL YVYDMLAGKL IPVHQVRGLK EKIVRSFEVS PDGSFLLING
IAGYLHLLAM KTKELIGSMK INGRVAASTF SSDSKKVYAS SGDGEVYVWD VNSRKCLNRF
VDEGSLYGLS IATSRNGQYV ACGSNCGVVN IYNQDSCLQE TNPKPIKAIM NLVTGVTSLT
FNPTTEILAI ASEKMKEAVR LVHLPSCTVF SNFPVIKNKN ISHVHTMDFS PRSGYFALGN
EKGKALMYRL HHYSDF
