WDR18_HUMAN
ID WDR18_HUMAN Reviewed; 432 AA.
AC Q9BV38; O60390; Q9BWR2;
DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 2.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=WD repeat-containing protein 18;
GN Name=WDR18;
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 GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT THR-172.
RC TISSUE=Brain, and Lung;
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 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., Buerckstuemmer T.,
RA 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 [4]
RP IDENTIFICATION IN THE PELP1 COMPLEX, AND SUBCELLULAR LOCATION.
RX PubMed=21326211; DOI=10.1038/emboj.2011.33;
RA Finkbeiner E., Haindl M., Muller S.;
RT "The SUMO system controls nucleolar partitioning of a novel mammalian
RT ribosome biogenesis complex.";
RL EMBO J. 30:1067-1078(2011).
RN [5]
RP FUNCTION, AND IDENTIFICATION IN THE 5FMC COMPLEX.
RX PubMed=22872859; DOI=10.1074/mcp.m112.017194;
RA Fanis P., Gillemans N., Aghajanirefah A., Pourfarzad F., Demmers J.,
RA Esteghamat F., Vadlamudi R.K., Grosveld F., Philipsen S., van Dijk T.B.;
RT "Five friends of methylated chromatin target of protein-arginine-
RT methyltransferase[prmt]-1 (chtop), a complex linking arginine methylation
RT to desumoylation.";
RL Mol. Cell. Proteomics 11:1263-1273(2012).
CC -!- FUNCTION: Functions as a component of the Five Friends of Methylated
CC CHTOP (5FMC) complex; the 5FMC complex is recruited to ZNF148 by
CC methylated CHTOP, leading to desumoylation of ZNF148 and subsequent
CC transactivation of ZNF148 target genes (PubMed:22872859). Component of
CC the PELP1 complex involved in the nucleolar steps of 28S rRNA
CC maturation and the subsequent nucleoplasmic transit of the pre-60S
CC ribosomal subunit (PubMed:21326211). May play a role during development
CC (By similarity). {ECO:0000250|UniProtKB:Q68EI0,
CC ECO:0000269|PubMed:21326211, ECO:0000269|PubMed:22872859}.
CC -!- SUBUNIT: Component of the 5FMC complex, at least composed of PELP1,
CC LAS1L, TEX10, WDR18 and SENP3; the complex interacts with methylated
CC CHTOP and ZNF148. Interacts with NOL9. Component of the PELP1 complex,
CC composed of at least PELP1, TEX10 and WDR18. The complex interacts with
CC pre-60S ribosome particles (PubMed:21326211).
CC {ECO:0000269|PubMed:21326211, ECO:0000269|PubMed:22872859}.
CC -!- INTERACTION:
CC Q9BV38; Q8IZL8: PELP1; NbExp=5; IntAct=EBI-727429, EBI-716449;
CC Q9BV38; Q9H4L4: SENP3; NbExp=4; IntAct=EBI-727429, EBI-2880236;
CC Q9BV38; Q9NXF1: TEX10; NbExp=2; IntAct=EBI-727429, EBI-2371062;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:21326211}.
CC Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q4VBE8}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q4VBE8}. Dynein axonemal particle
CC {ECO:0000250|UniProtKB:A0A1L8HX76}. Note=Mainly found in the
CC nucleoplasm, with low levels detected in the cytoplasmic and chromatin
CC fractions. {ECO:0000250|UniProtKB:Q4VBE8}.
CC -!- SIMILARITY: Belongs to the WD repeat IPI3/WDR18 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC12679.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC004528; AAC12679.1; ALT_INIT; Genomic_DNA.
DR EMBL; BC000040; AAH00040.2; -; mRNA.
DR EMBL; BC001648; AAH01648.1; -; mRNA.
DR CCDS; CCDS12051.1; -.
DR RefSeq; NP_077005.2; NM_024100.3.
DR AlphaFoldDB; Q9BV38; -.
DR SMR; Q9BV38; -.
DR BioGRID; 121517; 111.
DR CORUM; Q9BV38; -.
DR IntAct; Q9BV38; 44.
DR MINT; Q9BV38; -.
DR STRING; 9606.ENSP00000476117; -.
DR GlyGen; Q9BV38; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9BV38; -.
DR PhosphoSitePlus; Q9BV38; -.
DR SwissPalm; Q9BV38; -.
DR BioMuta; WDR18; -.
DR DMDM; 143811475; -.
DR EPD; Q9BV38; -.
DR jPOST; Q9BV38; -.
DR MassIVE; Q9BV38; -.
DR MaxQB; Q9BV38; -.
DR PaxDb; Q9BV38; -.
DR PeptideAtlas; Q9BV38; -.
DR PRIDE; Q9BV38; -.
DR ProteomicsDB; 79165; -.
DR TopDownProteomics; Q9BV38; -.
DR Antibodypedia; 22464; 149 antibodies from 27 providers.
DR DNASU; 57418; -.
DR Ensembl; ENST00000585809.6; ENSP00000476117.3; ENSG00000065268.11.
DR GeneID; 57418; -.
DR KEGG; hsa:57418; -.
DR MANE-Select; ENST00000585809.6; ENSP00000476117.3; NM_024100.4; NP_077005.2.
DR UCSC; uc002lqm.2; human.
DR CTD; 57418; -.
DR DisGeNET; 57418; -.
DR GeneCards; WDR18; -.
DR HGNC; HGNC:17956; WDR18.
DR HPA; ENSG00000065268; Low tissue specificity.
DR neXtProt; NX_Q9BV38; -.
DR NIAGADS; ENSG00000065268; -.
DR OpenTargets; ENSG00000065268; -.
DR PharmGKB; PA38269; -.
DR VEuPathDB; HostDB:ENSG00000065268; -.
DR eggNOG; KOG0646; Eukaryota.
DR GeneTree; ENSGT00390000000289; -.
DR InParanoid; Q9BV38; -.
DR OMA; VNARIYT; -.
DR OrthoDB; 747023at2759; -.
DR PhylomeDB; Q9BV38; -.
DR TreeFam; TF313046; -.
DR PathwayCommons; Q9BV38; -.
DR Reactome; R-HSA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR SignaLink; Q9BV38; -.
DR SIGNOR; Q9BV38; -.
DR BioGRID-ORCS; 57418; 729 hits in 1062 CRISPR screens.
DR ChiTaRS; WDR18; human.
DR GenomeRNAi; 57418; -.
DR Pharos; Q9BV38; Tbio.
DR PRO; PR:Q9BV38; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q9BV38; protein.
DR Bgee; ENSG00000065268; Expressed in right hemisphere of cerebellum and 119 other tissues.
DR ExpressionAtlas; Q9BV38; baseline and differential.
DR Genevisible; Q9BV38; HS.
DR GO; GO:0120293; C:dynein axonemal particle; ISS:UniProtKB.
DR GO; GO:0005656; C:nuclear pre-replicative complex; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0097344; C:Rix1 complex; IBA:GO_Central.
DR GO; GO:0006261; P:DNA-templated DNA replication; IBA:GO_Central.
DR GO; GO:0006364; P:rRNA processing; IBA:GO_Central.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
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 InterPro; IPR045227; WDR18/Ipi3/RID3.
DR InterPro; IPR026987; Wdr18_C_dom.
DR PANTHER; PTHR18763; PTHR18763; 1.
DR Pfam; PF00400; WD40; 3.
DR Pfam; PF14077; WD40_alt; 1.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 4.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 2.
DR PROSITE; PS50082; WD_REPEATS_2; 3.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Developmental protein; Nucleus; Reference proteome; Repeat;
KW WD repeat.
FT CHAIN 1..432
FT /note="WD repeat-containing protein 18"
FT /id="PRO_0000051365"
FT REPEAT 36..75
FT /note="WD 1"
FT REPEAT 78..116
FT /note="WD 2"
FT REPEAT 119..158
FT /note="WD 3"
FT REPEAT 170..211
FT /note="WD 4"
FT REPEAT 213..257
FT /note="WD 5"
FT REPEAT 267..306
FT /note="WD 6"
FT VARIANT 172
FT /note="A -> T (in dbSNP:rs2158367)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_031577"
FT VARIANT 213
FT /note="L -> F (in dbSNP:rs35068100)"
FT /id="VAR_031578"
FT VARIANT 264
FT /note="V -> I (in dbSNP:rs11538683)"
FT /id="VAR_031579"
FT CONFLICT 198..199
FT /note="Missing (in Ref. 1; AAC12679)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 432 AA; 47405 MW; 0E00FA0DF124F82C CRC64;
MAAPMEVAVC TDSAAPMWSC IVWELHSGAN LLTYRGGQAG PRGLALLNGE YLLAAQLGKN
YISAWELQRK DQLQQKIMCP GPVTCLTASP NGLYVLAGVA ESIHLWEVST GNLLVILSRH
YQDVSCLQFT GDSSHFISGG KDCLVLVWSL CSVLQADPSR IPAPRHVWSH HALPITDLHC
GFGGPLARVA TSSLDQTVKL WEVSSGELLL SVLFDVSIMA VTMDLAEHHM FCGGSEGSIF
QVDLFTWPGQ RERSFHPEQD AGKVFKGHRN QVTCLSVSTD GSVLLSGSHD ETVRLWDVQS
KQCIRTVALK GPVTNAAILL APVSMLSSDF RPSLPLPHFN KHLLGAEHGD EPRHGGLTLR
LGLHQQGSEP SYLDRTEQLQ AVLCSTMEKS VLGGQDQLRV RVTELEDEVR NLRKINRDLF
DFSTRFITRP AK
