WDR4_HUMAN
ID WDR4_HUMAN Reviewed; 412 AA.
AC P57081; A8KA58; B2RCA3; B4DNQ7; D3DSK3; Q9BVM5; Q9HCR3;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 11-FEB-2002, sequence version 2.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=tRNA (guanine-N(7)-)-methyltransferase non-catalytic subunit WDR4 {ECO:0000255|HAMAP-Rule:MF_03056};
DE AltName: Full=Protein Wuho homolog {ECO:0000303|PubMed:26751069};
DE Short=hWH {ECO:0000303|PubMed:26751069};
DE AltName: Full=WD repeat-containing protein 4 {ECO:0000255|HAMAP-Rule:MF_03056};
GN Name=WDR4 {ECO:0000255|HAMAP-Rule:MF_03056, ECO:0000312|HGNC:HGNC:12756};
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 [GENOMIC DNA / MRNA] (ISOFORM 1).
RX PubMed=10950928; DOI=10.1006/geno.2000.6258;
RA Michaud J., Kudoh J., Berry A., Bonne-Tamir B., Lalioti M.D., Rossier C.,
RA Shibuya K., Kawasaki K., Asakawa S., Minoshima S., Shimizu N.,
RA Antonarakis S.E., Scott H.S.;
RT "Isolation and characterization of a human chromosome 21q22.3 gene (WDR4)
RT and its mouse homologue that code for a WD-repeat protein.";
RL Genomics 68:71-79(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), AND VARIANTS
RP ASN-71 AND SER-266.
RC TISSUE=Lung, and Trachea;
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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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].
RX PubMed=10830953; DOI=10.1038/35012518;
RA Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S.,
RA Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M.,
RA Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A., Menzel U.,
RA Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A.,
RA Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J.,
RA Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K.,
RA Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G.,
RA Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J.,
RA Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S.,
RA Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K.,
RA Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.;
RT "The DNA sequence of human chromosome 21.";
RL Nature 405:311-319(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ASN-71.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANT
RP SER-266.
RC TISSUE=Lung, and Uterus;
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 PROTEIN SEQUENCE OF 2-17 AND 105-116, CLEAVAGE OF INITIATOR METHIONINE,
RP ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Ovarian carcinoma;
RA Bienvenut W.V.;
RL Submitted (JAN-2010) to UniProtKB.
RN [7]
RP FUNCTION, PATHWAY, AND INTERACTION WITH METTL1.
RX PubMed=12403464; DOI=10.1017/s1355838202024019;
RA Alexandrov A., Martzen M.R., Phizicky E.M.;
RT "Two proteins that form a complex are required for 7-methylguanosine
RT modification of yeast tRNA.";
RL RNA 8:1253-1266(2002).
RN [8]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH METTL1.
RX PubMed=15861136; DOI=10.1038/sj.emboj.7600648;
RA Cartlidge R.A., Knebel A., Peggie M., Alexandrov A., Phizicky E.M.,
RA Cohen P.;
RT "The tRNA methylase METTL1 is phosphorylated and inactivated by PKB and RSK
RT in vitro and in cells.";
RL EMBO J. 24:1696-1705(2005).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-411, AND IDENTIFICATION BY
RP 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 [10]
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 [11]
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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-391, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE 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-391, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH METTL1 AND FEN1.
RX PubMed=26751069; DOI=10.1371/journal.pbio.1002349;
RA Cheng I.C., Chen B.C., Shuai H.H., Chien F.C., Chen P., Hsieh T.S.;
RT "Wuho is a new member in maintaining genome stability through its
RT interaction with flap endonuclease 1.";
RL PLoS Biol. 14:E1002349-E1002349(2016).
RN [15]
RP INVOLVEMENT IN GAMOS6.
RX PubMed=30079490; DOI=10.1002/ajmg.a.40489;
RA Braun D.A., Shril S., Sinha A., Schneider R., Tan W., Ashraf S., Hermle T.,
RA Jobst-Schwan T., Widmeier E., Majmundar A.J., Daga A., Warejko J.K.,
RA Nakayama M., Schapiro D., Chen J., Airik M., Rao J., Schmidt J.M.,
RA Hoogstraten C.A., Hugo H., Meena J., Lek M., Laricchia K.M., Bagga A.,
RA Hildebrandt F.;
RT "Mutations in WDR4 as a new cause of Galloway-Mowat syndrome.";
RL Am. J. Med. Genet. A 176:2460-2465(2018).
RN [16]
RP FUNCTION, AND PATHWAY.
RX PubMed=31031084; DOI=10.1016/j.molcel.2019.03.036;
RA Zhang L.S., Liu C., Ma H., Dai Q., Sun H.L., Luo G., Zhang Z., Zhang L.,
RA Hu L., Dong X., He C.;
RT "Transcriptome-wide mapping of internal N7-methylguanosine methylome in
RT mammalian mRNA.";
RL Mol. Cell 0:0-0(2019).
RN [17]
RP FUNCTION.
RX PubMed=31031083; DOI=10.1016/j.molcel.2019.03.040;
RA Pandolfini L., Barbieri I., Bannister A.J., Hendrick A., Andrews B.,
RA Webster N., Murat P., Mach P., Brandi R., Robson S.C., Migliori V.,
RA Alendar A., d'Onofrio M., Balasubramanian S., Kouzarides T.;
RT "METTL1 promotes let-7 microRNA processing via m7G methylation.";
RL Mol. Cell 0:0-0(2019).
RN [18]
RP VARIANT MIGSB LEU-170.
RX PubMed=26416026; DOI=10.1186/s13059-015-0779-x;
RA Shaheen R., Abdel-Salam G.M., Guy M.P., Alomar R., Abdel-Hamid M.S.,
RA Afifi H.H., Ismail S.I., Emam B.A., Phizicky E.M., Alkuraya F.S.;
RT "Mutation in WDR4 impairs tRNA m(7)G46 methylation and causes a distinct
RT form of microcephalic primordial dwarfism.";
RL Genome Biol. 16:RESEARCH210.1-RESEARCH210.11(2015).
RN [19]
RP VARIANT GAMOS6 ALA-164.
RX PubMed=29597095; DOI=10.1016/j.ejmg.2018.03.007;
RA Chen X., Gao Y., Yang L., Wu B., Dong X., Liu B., Lu Y., Zhou W., Wang H.;
RT "Speech and language delay in a patient with WDR4 mutations.";
RL Eur. J. Med. Genet. 61:468-472(2018).
RN [20]
RP VARIANT GAMOS6 GLN-170.
RX PubMed=28617965; DOI=10.1111/cge.13074;
RA Trimouille A., Lasseaux E., Barat P., Deiller C., Drunat S., Rooryck C.,
RA Arveiler B., Lacombe D.;
RT "Further delineation of the phenotype caused by biallelic variants in the
RT WDR4 gene.";
RL Clin. Genet. 93:374-377(2018).
CC -!- FUNCTION: Non-catalytic component of a methyltransferase complex
CC required for the formation of N(7)-methylguanine in a subset of RNA
CC species, such as tRNAs, mRNAs and microRNAs (miRNAs) (PubMed:12403464,
CC PubMed:31031084, PubMed:31031083). In the methyltransferase complex, it
CC is required to stabilize and induce conformational changes of the
CC catalytic subunit (PubMed:12403464). Required for the formation of
CC N(7)-methylguanine at position 46 (m7G46) in tRNA (PubMed:12403464,
CC PubMed:31031084). Also required for the formation of N(7)-methylguanine
CC at internal sites in a subset of mRNAs (PubMed:31031084). Also required
CC for methylation of a specific subset of miRNAs, such as let-7
CC (PubMed:31031083). Independently of METTL1, also plays a role in genome
CC stability: localizes at the DNA replication site and regulates
CC endonucleolytic activities of FEN1 (PubMed:26751069).
CC {ECO:0000269|PubMed:12403464, ECO:0000269|PubMed:26751069,
CC ECO:0000269|PubMed:31031083, ECO:0000269|PubMed:31031084}.
CC -!- PATHWAY: tRNA modification; N(7)-methylguanine-tRNA biosynthesis.
CC {ECO:0000269|PubMed:12403464, ECO:0000269|PubMed:31031084}.
CC -!- SUBUNIT: Forms a heterodimer with the catalytic subunit METTL1
CC (PubMed:12403464, PubMed:26751069). Interacts with FEN1; the
CC interaction is direct (PubMed:26751069). {ECO:0000269|PubMed:12403464,
CC ECO:0000269|PubMed:26751069}.
CC -!- INTERACTION:
CC P57081; Q9NWS6: FAM118A; NbExp=7; IntAct=EBI-750427, EBI-8638992;
CC P57081; P39748: FEN1; NbExp=8; IntAct=EBI-750427, EBI-707816;
CC P57081; Q9UBP6: METTL1; NbExp=13; IntAct=EBI-750427, EBI-750415;
CC P57081; P53611: RABGGTB; NbExp=6; IntAct=EBI-750427, EBI-536715;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15861136,
CC ECO:0000269|PubMed:26751069}. Chromosome {ECO:0000269|PubMed:26751069}.
CC Note=Localizes at the site of nascent DNA synthesis.
CC {ECO:0000269|PubMed:26751069}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P57081-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P57081-2; Sequence=VSP_036936;
CC Name=3;
CC IsoId=P57081-3; Sequence=VSP_036935;
CC -!- DISEASE: Galloway-Mowat syndrome 6 (GAMOS6) [MIM:618347]: A form of
CC Galloway-Mowat syndrome, a severe renal-neurological disease
CC characterized by early-onset nephrotic syndrome associated with
CC microcephaly, central nervous system abnormalities, developmental
CC delays, and a propensity for seizures. Brain anomalies include gyration
CC defects ranging from lissencephaly to pachygyria and polymicrogyria,
CC and cerebellar hypoplasia. Most patients show facial dysmorphism
CC characterized by a small, narrow forehead, large/floppy ears, deep-set
CC eyes, hypertelorism and micrognathia. Additional variable features are
CC visual impairment and arachnodactyly. Most patients die in early
CC childhood. GAMOS6 is an autosomal recessive form with onset in infancy
CC or early childhood. Affected individuals manifest microcephaly, global
CC developmental delay, variable degrees of intellectual disability, and
CC growth deficiency. Renal impairment may be age-dependent or may not be
CC present. {ECO:0000269|PubMed:28617965, ECO:0000269|PubMed:29597095,
CC ECO:0000269|PubMed:30079490}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Microcephaly, growth deficiency, seizures, and brain
CC malformations (MIGSB) [MIM:618346]: An autosomal recessive disorder
CC characterized by intrauterine growth retardation, postnatal growth
CC deficiency, microcephaly, facial dysmorphism, early-onset seizures,
CC brain malformations such as partial agenesis of the corpus callosum and
CC simplified gyration, and poor or absent psychomotor development.
CC {ECO:0000269|PubMed:26416026}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the WD repeat TRM82 family. {ECO:0000255|HAMAP-
CC Rule:MF_03056}.
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DR EMBL; AJ243912; CAB93144.1; -; mRNA.
DR EMBL; AJ243913; CAB93145.1; -; mRNA.
DR EMBL; AK056343; BAG51684.1; -; mRNA.
DR EMBL; AK292923; BAF85612.1; -; mRNA.
DR EMBL; AK298015; BAG60319.1; -; mRNA.
DR EMBL; AK315008; BAG37500.1; -; mRNA.
DR EMBL; AB039887; BAB13726.1; -; Genomic_DNA.
DR EMBL; AP001629; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471079; EAX09528.1; -; Genomic_DNA.
DR EMBL; CH471079; EAX09529.1; -; Genomic_DNA.
DR EMBL; BC001074; AAH01074.1; -; mRNA.
DR EMBL; BC006341; AAH06341.1; -; mRNA.
DR CCDS; CCDS13691.1; -. [P57081-1]
DR RefSeq; NP_001247403.1; NM_001260474.1. [P57081-2]
DR RefSeq; NP_001247404.1; NM_001260475.1. [P57081-3]
DR RefSeq; NP_001247405.1; NM_001260476.1. [P57081-3]
DR RefSeq; NP_001247406.1; NM_001260477.1. [P57081-3]
DR RefSeq; NP_061139.2; NM_018669.5. [P57081-1]
DR RefSeq; NP_387510.1; NM_033661.4. [P57081-1]
DR AlphaFoldDB; P57081; -.
DR SMR; P57081; -.
DR BioGRID; 116001; 66.
DR DIP; DIP-61919N; -.
DR IntAct; P57081; 16.
DR STRING; 9606.ENSP00000381266; -.
DR iPTMnet; P57081; -.
DR PhosphoSitePlus; P57081; -.
DR BioMuta; WDR4; -.
DR DMDM; 20141943; -.
DR EPD; P57081; -.
DR jPOST; P57081; -.
DR MassIVE; P57081; -.
DR MaxQB; P57081; -.
DR PaxDb; P57081; -.
DR PeptideAtlas; P57081; -.
DR PRIDE; P57081; -.
DR ProteomicsDB; 56991; -. [P57081-1]
DR ProteomicsDB; 56992; -. [P57081-2]
DR ProteomicsDB; 56993; -. [P57081-3]
DR Antibodypedia; 9776; 215 antibodies from 25 providers.
DR DNASU; 10785; -.
DR Ensembl; ENST00000330317.6; ENSP00000328671.2; ENSG00000160193.12. [P57081-1]
DR Ensembl; ENST00000398208.3; ENSP00000381266.2; ENSG00000160193.12. [P57081-1]
DR GeneID; 10785; -.
DR KEGG; hsa:10785; -.
DR MANE-Select; ENST00000398208.3; ENSP00000381266.2; NM_018669.6; NP_061139.2.
DR UCSC; uc002zci.5; human. [P57081-1]
DR CTD; 10785; -.
DR DisGeNET; 10785; -.
DR GeneCards; WDR4; -.
DR HGNC; HGNC:12756; WDR4.
DR HPA; ENSG00000160193; Low tissue specificity.
DR MalaCards; WDR4; -.
DR MIM; 605924; gene.
DR MIM; 618346; phenotype.
DR MIM; 618347; phenotype.
DR neXtProt; NX_P57081; -.
DR OpenTargets; ENSG00000160193; -.
DR Orphanet; 2065; Galloway-Mowat syndrome.
DR PharmGKB; PA37360; -.
DR VEuPathDB; HostDB:ENSG00000160193; -.
DR eggNOG; KOG3914; Eukaryota.
DR GeneTree; ENSGT00390000012174; -.
DR HOGENOM; CLU_054270_1_0_1; -.
DR InParanoid; P57081; -.
DR OMA; IFVVPDH; -.
DR OrthoDB; 937275at2759; -.
DR PhylomeDB; P57081; -.
DR TreeFam; TF105877; -.
DR PathwayCommons; P57081; -.
DR Reactome; R-HSA-6782315; tRNA modification in the nucleus and cytosol.
DR SignaLink; P57081; -.
DR UniPathway; UPA00989; -.
DR BioGRID-ORCS; 10785; 215 hits in 1084 CRISPR screens.
DR ChiTaRS; WDR4; human.
DR GeneWiki; WDR4; -.
DR GenomeRNAi; 10785; -.
DR Pharos; P57081; Tbio.
DR PRO; PR:P57081; -.
DR Proteomes; UP000005640; Chromosome 21.
DR RNAct; P57081; protein.
DR Bgee; ENSG00000160193; Expressed in gingival epithelium and 131 other tissues.
DR Genevisible; P57081; HS.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0043527; C:tRNA methyltransferase complex; IDA:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEA:UniProtKB-KW.
DR GO; GO:0106004; P:tRNA (guanine-N7)-methylation; IEA:GOC.
DR GO; GO:0006400; P:tRNA modification; IDA:UniProtKB.
DR Gene3D; 2.130.10.10; -; 1.
DR HAMAP; MF_03056; TRM82; 1.
DR InterPro; IPR028884; Trm82.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR16288; PTHR16288; 1.
DR Pfam; PF00400; WD40; 1.
DR SMART; SM00320; WD40; 4.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Chromosome; Direct protein sequencing;
KW Disease variant; DNA damage; Epilepsy; Intellectual disability; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; tRNA processing; WD repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.6"
FT CHAIN 2..412
FT /note="tRNA (guanine-N(7)-)-methyltransferase non-catalytic
FT subunit WDR4"
FT /id="PRO_0000051348"
FT REPEAT 3..40
FT /note="WD 1"
FT REPEAT 50..90
FT /note="WD 2"
FT REPEAT 94..131
FT /note="WD 3"
FT REPEAT 137..174
FT /note="WD 4"
FT REPEAT 180..218
FT /note="WD 5"
FT REPEAT 230..273
FT /note="WD 6"
FT REPEAT 319..373
FT /note="WD 7"
FT REGION 377..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 377..404
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.6"
FT MOD_RES 391
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 411
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VAR_SEQ 1..146
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_036935"
FT VAR_SEQ 243
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_036936"
FT VARIANT 71
FT /note="K -> N (in dbSNP:rs2248490)"
FT /evidence="ECO:0000269|PubMed:14702039, ECO:0000269|Ref.4"
FT /id="VAR_020120"
FT VARIANT 164
FT /note="D -> A (in GAMOS6; unknown pathological
FT significance; dbSNP:rs1555976610)"
FT /evidence="ECO:0000269|PubMed:29597095"
FT /id="VAR_081828"
FT VARIANT 170
FT /note="R -> L (in MIGSB)"
FT /evidence="ECO:0000269|PubMed:26416026"
FT /id="VAR_081829"
FT VARIANT 170
FT /note="R -> Q (in GAMOS6; dbSNP:rs1292041526)"
FT /evidence="ECO:0000269|PubMed:28617965"
FT /id="VAR_081830"
FT VARIANT 266
FT /note="P -> S (in dbSNP:rs15736)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_033121"
FT VARIANT 390
FT /note="R -> Q (in dbSNP:rs6586250)"
FT /id="VAR_033122"
FT CONFLICT 141
FT /note="E -> K (in Ref. 1; CAB93144/CAB93145)"
FT /evidence="ECO:0000305"
FT CONFLICT 149
FT /note="L -> V (in Ref. 1; CAB93144/CAB93145)"
FT /evidence="ECO:0000305"
FT CONFLICT 236
FT /note="V -> A (in Ref. 2; BAG37500)"
FT /evidence="ECO:0000305"
FT CONFLICT 318
FT /note="R -> K (in Ref. 2; BAG60319)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 412 AA; 45490 MW; 394B11A2AFB1CADB CRC64;
MAGSVGLALC GQTLVVRGGS RFLATSIASS DDDSLFIYDC SAAEKKSQEN KGEDAPLDQG
SGAILASTFS KSGSYFALTD DSKRLILFRT KPWQCLSVRT VARRCTALTF IASEEKVLVA
DKSGDVYSFS VLEPHGCGRL ELGHLSMLLD VAVSPDDRFI LTADRDEKIR VSWAAAPHSI
ESFCLGHTEF VSRISVVPTQ PGLLLSSSGD GTLRLWEYRS GRQLHCCHLA SLQELVDPQA
PQKFAASRIA FWCQENCVAL LCDGTPVVYI FQLDARRQQL VYRQQLAFQH QVWDVAFEET
QGLWVLQDCQ EAPLVLYRPV GDQWQSVPES TVLKKVSGVL RGNWAMLEGS AGADASFSSL
YKATFDNVTS YLKKKEERLQ QQLEKKQRRR SPPPGPDGHA KKMRPGEATL SC
