ID DMWD_HUMAN Reviewed; 674 AA. AC Q09019; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 25-NOV-2008, sequence version 3. DT 24-JAN-2024, entry version 181. DE RecName: Full=Dystrophia myotonica WD repeat-containing protein; DE AltName: Full=Dystrophia myotonica-containing WD repeat motif protein; DE AltName: Full=Protein 59; DE AltName: Full=Protein DMR-N9; GN Name=DMWD {ECO:0000312|HGNC:HGNC:2936}; Synonyms=DM9; 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 [MRNA] OF 123-674. RC TISSUE=Brain; RX PubMed=7905855; DOI=10.1016/s0888-7543(05)80372-6; RA Shaw D.J., McCurrach M., Rundle S.A., Harley H.G., Crow S.R., Sohn R., RA Thirion J.-P., Hamshere M.G., Buckler A.J., Harper P.S., Housman D.E., RA Brook J.D.; RT "Genomic organization and transcriptional units at the myotonic dystrophy RT locus."; RL Genomics 18:673-679(1993). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 660-674. RX PubMed=8499920; DOI=10.1093/hmg/2.3.299; RA Mahadevan M.S., Amemiya C., Jansen G., Sabourin L., Baird S., Neville C.E., RA Wormskamp N., Segers B., Batzer M., Lamerdin J., de Jong P.J., Wieringa B., RA Korneluk R.G.; RT "Structure and genomic sequence of the myotonic dystrophy (DM kinase) RT gene."; RL Hum. Mol. Genet. 2:299-304(1993). RN [4] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-495, AND IDENTIFICATION BY RP 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 [6] RP 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 [7] RP FUNCTION, SUBUNIT, INTERACTION WITH USP12 AND USP46, SUBCELLULAR LOCATION, RP AND MUTAGENESIS OF PHE-326 AND TRP-370. RX PubMed=33844468; DOI=10.1111/febs.15875; RA Olazabal-Herrero A., Bilbao-Arribas M., Carlevaris O., Sendino M., RA Varela-Martinez E., Jugo B.M., Berra E., Rodriguez J.A.; RT "The dystrophia myotonica WD repeat-containing protein DMWD and WDR20 RT differentially regulate USP12 deubiquitinase."; RL FEBS J. 288:5943-5963(2021). CC -!- FUNCTION: Regulator of the deubiquitinating USP12/DMWD/WDR48 complex CC (PubMed:33844468). Functions as a cofactor that promotes USP12 CC enzymatic activity (PubMed:33844468). {ECO:0000269|PubMed:33844468}. CC -!- SUBUNIT: Component of the USP12/DMWD/WDR48 deubiquitinating complex CC (PubMed:33844468). Interacts with USP12; promotes its enzymatic CC activity (PubMed:33844468). Interacts with USP46 (PubMed:33844468). CC {ECO:0000269|PubMed:33844468}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:33844468}. Nucleus CC {ECO:0000269|PubMed:33844468}. Perikaryon CC {ECO:0000250|UniProtKB:Q08274}. Cell projection, dendrite CC {ECO:0000250|UniProtKB:Q08274}. Note=Localizes mainly to the cytoplasm CC however shuttles between the cytoplasm and nucleus (PubMed:33844468). CC In neurons, shows punctate expression throughout the cell body, nucleus CC and dendrites. Not detected in axons. {ECO:0000250|UniProtKB:Q08274, CC ECO:0000269|PubMed:33844468}. 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; AC011530; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; L19267; AAA35767.1; -; mRNA. DR EMBL; L08835; AAC14447.1; -; Genomic_DNA. DR CCDS; CCDS33054.1; -. DR PIR; A49364; A49364. DR RefSeq; NP_004934.1; NM_004943.1. DR AlphaFoldDB; Q09019; -. DR SMR; Q09019; -. DR BioGRID; 108102; 86. DR IntAct; Q09019; 59. DR MINT; Q09019; -. DR STRING; 9606.ENSP00000270223; -. DR GlyGen; Q09019; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q09019; -. DR PhosphoSitePlus; Q09019; -. DR BioMuta; DMWD; -. DR DMDM; 215274169; -. DR EPD; Q09019; -. DR jPOST; Q09019; -. DR MassIVE; Q09019; -. DR MaxQB; Q09019; -. DR PaxDb; 9606-ENSP00000270223; -. DR PeptideAtlas; Q09019; -. DR ProteomicsDB; 58711; -. DR Pumba; Q09019; -. DR Antibodypedia; 31398; 161 antibodies from 21 providers. DR DNASU; 1762; -. DR Ensembl; ENST00000270223.7; ENSP00000270223.5; ENSG00000185800.12. DR GeneID; 1762; -. DR KEGG; hsa:1762; -. DR MANE-Select; ENST00000270223.7; ENSP00000270223.5; NM_004943.2; NP_004934.1. DR UCSC; uc002pdj.2; human. DR AGR; HGNC:2936; -. DR CTD; 1762; -. DR DisGeNET; 1762; -. DR GeneCards; DMWD; -. DR HGNC; HGNC:2936; DMWD. DR HPA; ENSG00000185800; Low tissue specificity. DR MIM; 609857; gene. DR neXtProt; NX_Q09019; -. DR OpenTargets; ENSG00000185800; -. DR PharmGKB; PA27390; -. DR VEuPathDB; HostDB:ENSG00000185800; -. DR eggNOG; KOG2394; Eukaryota. DR GeneTree; ENSGT00390000007686; -. DR InParanoid; Q09019; -. DR OMA; AVEGHHH; -. DR OrthoDB; 1513505at2759; -. DR PhylomeDB; Q09019; -. DR TreeFam; TF314961; -. DR PathwayCommons; Q09019; -. DR SignaLink; Q09019; -. DR BioGRID-ORCS; 1762; 15 hits in 1154 CRISPR screens. DR GeneWiki; DMWD_(gene); -. DR GenomeRNAi; 1762; -. DR Pharos; Q09019; Tbio. DR PRO; PR:Q09019; -. DR Proteomes; UP000005640; Chromosome 19. DR RNAct; Q09019; Protein. DR Bgee; ENSG00000185800; Expressed in apex of heart and 159 other cell types or tissues. DR ExpressionAtlas; Q09019; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell. DR GO; GO:0035800; F:deubiquitinase activator activity; IDA:UniProtKB. DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1. DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf. DR InterPro; IPR036322; WD40_repeat_dom_sf. DR InterPro; IPR001680; WD40_rpt. DR PANTHER; PTHR14107:SF15; DYSTROPHIA MYOTONICA WD REPEAT-CONTAINING PROTEIN; 1. DR PANTHER; PTHR14107; WD REPEAT PROTEIN; 1. DR Pfam; PF00400; WD40; 2. DR SMART; SM00320; WD40; 4. DR SUPFAM; SSF50978; WD40 repeat-like; 1. DR PROSITE; PS50082; WD_REPEATS_2; 1. DR PROSITE; PS50294; WD_REPEATS_REGION; 1. DR Genevisible; Q09019; HS. PE 1: Evidence at protein level; KW Acetylation; Cell projection; Cytoplasm; Methylation; Nucleus; KW Phosphoprotein; Reference proteome; Repeat; WD repeat. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:22814378" FT CHAIN 2..674 FT /note="Dystrophia myotonica WD repeat-containing protein" FT /id="PRO_0000050956" FT REPEAT 211..251 FT /note="WD 1" FT /evidence="ECO:0000255" FT REPEAT 282..321 FT /note="WD 2" FT /evidence="ECO:0000255" FT REPEAT 324..363 FT /note="WD 3" FT /evidence="ECO:0000255" FT REPEAT 366..409 FT /note="WD 4" FT /evidence="ECO:0000255" FT REPEAT 413..453 FT /note="WD 5" FT /evidence="ECO:0000255" FT REPEAT 601..638 FT /note="WD 6" FT /evidence="ECO:0000255" FT REGION 31..92 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 103..122 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 384..419 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 456..516 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 532..573 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 637..674 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 51..89 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 532..546 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 641..674 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0007744|PubMed:22814378" FT MOD_RES 495 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 551 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0000250|UniProtKB:Q08274" FT MUTAGEN 326 FT /note="F->A: Impairs binding to USP12." FT /evidence="ECO:0000269|PubMed:33844468" FT MUTAGEN 370 FT /note="W->A: Impairs binding to USP12." FT /evidence="ECO:0000269|PubMed:33844468" FT CONFLICT 306 FT /note="G -> A (in Ref. 2; AAA35767)" FT /evidence="ECO:0000305" FT CONFLICT 378 FT /note="P -> SL (in Ref. 2; AAA35767)" FT /evidence="ECO:0000305" FT CONFLICT 629 FT /note="A -> P (in Ref. 2; AAA35767)" FT /evidence="ECO:0000305" SQ SEQUENCE 674 AA; 70438 MW; DC93F6930915E928 CRC64; MAAGGAEGGS GPGAAMGDCA EIKSQFRTRE GFYKLLPGDG AARRSGPASA QTPVPPQPPQ PPPGPASASG PGAAGPASSP PPAGPGPGPA LPAVRLSLVR LGEPDSAGAG EPPATPAGLG SGGDRVCFNL GRELYFYPGC CRRGSQRSID LNKPIDKRIY KGTQPTCHDF NQFTAATETI SLLVGFSAGQ VQYLDLIKKD TSKLFNEERL IDKTKVTYLK WLPESESLFL ASHASGHLYL YNVSHPCASA PPQYSLLKQG EGFSVYAAKS KAPRNPLAKW AVGEGPLNEF AFSPDGRHLA CVSQDGCLRV FHFDSMLLRG LMKSYFGGLL CVCWSPDGRY VVTGGEDDLV TVWSFTEGRV VARGHGHKSW VNAVAFDPYT TRAEEAATAA GADGERSGEE EEEEPEAAGT GSAGGAPLSP LPKAGSITYR FGSAGQDTQF CLWDLTEDVL YPHPPLARTR TLPGTPGTTP PAASSSRGGE PGPGPLPRSL SRSNSLPHPA GGGKAGGPGV AAEPGTPFSI GRFATLTLQE RRDRGAEKEH KRYHSLGNIS RGGSGGSGSG GEKPSGPVPR SRLDPAKVLG TALCPRIHEV PLLEPLVCKK IAQERLTVLL FLEDCIITAC QEGLICTWAR PGKAFTDEET EAQTGEGSWP RSPSKSVVEG ISSQPGNSPS GTVV //