WDR12_MOUSE
ID WDR12_MOUSE Reviewed; 423 AA.
AC Q9JJA4; Q9CST3; Q9JKF5;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Ribosome biogenesis protein WDR12 {ECO:0000255|HAMAP-Rule:MF_03029};
DE AltName: Full=WD repeat-containing protein 12 {ECO:0000255|HAMAP-Rule:MF_03029};
GN Name=Wdr12; ORFNames=MNCb-5414;
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 [MRNA].
RC TISSUE=Thymocyte, and Thymus;
RX PubMed=11827460; DOI=10.1006/geno.2001.6682;
RA Nal B., Mohr E., Da Silva M.I., Tagett R., Navarro C., Carroll P.,
RA Depetris D., Verthuy C., Jordan B.R., Ferrier P.;
RT "Wdr12, a mouse gene encoding a novel WD-repeat protein with a notchless-
RT like amino-terminal domain.";
RL Genomics 79:77-86(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J X 129/SvJ; TISSUE=Embryo;
RA Matsumoto S.;
RT "Mouse homologue of Saccharomyces cervisiae YTM1.";
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Osada N., Kusuda J., Tanuma R., Ito A., Hirata M., Sugano S., Hashimoto K.;
RT "Isolation of full-length cDNA clones from mouse brain cDNA library made by
RT oligo-capping method.";
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo, Pancreas, and Testis;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and Mammary gland;
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, 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 the PeBoW complex, which is required for
CC maturation of 28S and 5.8S ribosomal RNAs and formation of the 60S
CC ribosome. {ECO:0000255|HAMAP-Rule:MF_03029}.
CC -!- SUBUNIT: Component of the PeBoW complex, composed of BOP1, PES1 and
CC WDR12. The complex is held together by BOP1, which interacts with PES1
CC via its N-terminal domain and with WDR12 via a high-affinity
CC interaction between the seven-bladed beta-propeller domains of the 2
CC proteins. The PeBoW complex associates with the 66S pre-ribosome.
CC Interacts (via UBL domain) with MDN1 (via VWFA/MIDAS domain).
CC {ECO:0000255|HAMAP-Rule:MF_03029}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000255|HAMAP-
CC Rule:MF_03029}. Nucleus, nucleoplasm {ECO:0000255|HAMAP-Rule:MF_03029}.
CC -!- SIMILARITY: Belongs to the WD repeat WDR12/YTM1 family.
CC {ECO:0000255|HAMAP-Rule:MF_03029}.
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DR EMBL; AY059431; AAL29680.1; -; mRNA.
DR EMBL; AY059432; AAL29681.1; -; mRNA.
DR EMBL; AF239765; AAF44683.1; -; mRNA.
DR EMBL; AB041608; BAA95091.1; -; mRNA.
DR EMBL; AK007500; BAB25072.1; -; mRNA.
DR EMBL; AK012022; BAB27979.3; -; mRNA.
DR EMBL; AK016611; BAB30336.1; -; mRNA.
DR EMBL; AK031436; BAC27402.1; -; mRNA.
DR EMBL; BC004748; AAH04748.1; -; mRNA.
DR EMBL; BC052386; AAH52386.1; -; mRNA.
DR CCDS; CCDS14988.1; -.
DR RefSeq; NP_001185989.1; NM_001199060.1.
DR RefSeq; NP_001185990.1; NM_001199061.1.
DR RefSeq; NP_067287.1; NM_021312.5.
DR RefSeq; XP_011236865.1; XM_011238563.2.
DR RefSeq; XP_017177350.1; XM_017321861.1.
DR AlphaFoldDB; Q9JJA4; -.
DR SMR; Q9JJA4; -.
DR BioGRID; 208312; 27.
DR CORUM; Q9JJA4; -.
DR STRING; 10090.ENSMUSP00000027173; -.
DR iPTMnet; Q9JJA4; -.
DR PhosphoSitePlus; Q9JJA4; -.
DR EPD; Q9JJA4; -.
DR MaxQB; Q9JJA4; -.
DR PaxDb; Q9JJA4; -.
DR PRIDE; Q9JJA4; -.
DR ProteomicsDB; 297635; -.
DR Antibodypedia; 19949; 160 antibodies from 25 providers.
DR DNASU; 57750; -.
DR Ensembl; ENSMUST00000027173; ENSMUSP00000027173; ENSMUSG00000026019.
DR Ensembl; ENSMUST00000117438; ENSMUSP00000113494; ENSMUSG00000026019.
DR Ensembl; ENSMUST00000122038; ENSMUSP00000113148; ENSMUSG00000026019.
DR GeneID; 57750; -.
DR KEGG; mmu:57750; -.
DR UCSC; uc007bee.2; mouse.
DR CTD; 55759; -.
DR MGI; MGI:1927241; Wdr12.
DR VEuPathDB; HostDB:ENSMUSG00000026019; -.
DR eggNOG; KOG0313; Eukaryota.
DR GeneTree; ENSGT00930000150950; -.
DR HOGENOM; CLU_000288_57_0_1; -.
DR InParanoid; Q9JJA4; -.
DR OMA; VDCTRTK; -.
DR OrthoDB; 1540178at2759; -.
DR PhylomeDB; Q9JJA4; -.
DR TreeFam; TF313023; -.
DR Reactome; R-MMU-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR BioGRID-ORCS; 57750; 25 hits in 75 CRISPR screens.
DR ChiTaRS; Wdr12; mouse.
DR PRO; PR:Q9JJA4; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q9JJA4; protein.
DR Bgee; ENSMUSG00000026019; Expressed in spermatid and 242 other tissues.
DR ExpressionAtlas; Q9JJA4; baseline and differential.
DR Genevisible; Q9JJA4; MM.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0070545; C:PeBoW complex; ISS:UniProtKB.
DR GO; GO:0030687; C:preribosome, large subunit precursor; ISS:UniProtKB.
DR GO; GO:0043021; F:ribonucleoprotein complex binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000466; P:maturation of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); ISS:UniProtKB.
DR GO; GO:0000463; P:maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); ISS:UniProtKB.
DR GO; GO:0007219; P:Notch signaling pathway; IPI:MGI.
DR GO; GO:0051726; P:regulation of cell cycle; ISS:UniProtKB.
DR Gene3D; 2.130.10.10; -; 1.
DR HAMAP; MF_03029; WDR12; 1.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR012972; NLE.
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; IPR028599; WDR12/Ytm1.
DR Pfam; PF08154; NLE; 1.
DR Pfam; PF00400; WD40; 6.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 2.
DR PROSITE; PS50082; WD_REPEATS_2; 5.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Acetylation; Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Ribosome biogenesis; rRNA processing; Ubl conjugation; WD repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9GZL7"
FT CHAIN 2..423
FT /note="Ribosome biogenesis protein WDR12"
FT /id="PRO_0000051359"
FT REPEAT 99..137
FT /note="WD 1"
FT REPEAT 138..180
FT /note="WD 2"
FT REPEAT 187..226
FT /note="WD 3"
FT REPEAT 255..293
FT /note="WD 4"
FT REPEAT 295..334
FT /note="WD 5"
FT REPEAT 340..380
FT /note="WD 6"
FT REPEAT 384..422
FT /note="WD 7"
FT REGION 4..87
FT /note="Ubiquitin-like (UBL) domain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03029"
FT REGION 98..423
FT /note="Sufficient for nucleolar localization"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9GZL7"
FT MOD_RES 415
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9GZL7"
FT CROSSLNK 239
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0000250|UniProtKB:Q9GZL7"
FT CONFLICT 99
FT /note="F -> S (in Ref. 2; AAF44683)"
FT /evidence="ECO:0000305"
FT CONFLICT 418
FT /note="T -> A (in Ref. 1; AAL29680/AAL29681)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 423 AA; 47347 MW; DF57952520373667 CRC64;
MAQLQARFYS ENKKYAVDDV PFSIPAAAEV ADLSNIINKL LETKNELHKH VEFDFLIKGQ
FLRVPLVKHM ELENISSEEV VELEYVEKYT APQPEQCMFH DDWISSIEGA EEWILSGSYD
KTSRIWSLEG KSIMTIVGHT DVVKDVAWVK KDSLSCLLLT ASMDQTVLLW EWNVEKNKVK
ALHCCRGHAG SVDAIAVDSS GAKFCSGSWD KMLKIWSTVP TDEEDEMEEA TNRPRKKQKT
EQLGLTRTPL VTLSGHTEAI SSVLWSDAEE ICSASWDHTI RVWDVESGGL KSTLTGNKVF
NCISYSPLCK RLASGSTDRH IRLWDPRTKD GSLVSLSLTS HTGWVTSVKW SPTHEQQLIS
GSLDNIVKLW DTRSCKAPLY DLAAHEDKVL SVDWTDTGLL LSGGADNKLY SYSYSPTTSH
VGA
