ID MEP50_HUMAN Reviewed; 342 AA. AC Q9BQA1; B3KMW6; B4DP38; Q3LID2; Q53FU2; Q6JZZ5; Q96GK4; Q9BWY3; DT 20-JUN-2003, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 02-JUN-2021, entry version 182. DE RecName: Full=Methylosome protein 50; DE Short=MEP-50; DE AltName: Full=Androgen receptor cofactor p44; DE AltName: Full=WD repeat-containing protein 77; DE AltName: Full=p44/Mep50; GN Name=WDR77; Synonyms=MEP50, WD45; ORFNames=HKMT1069, Nbla10071; 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 [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 4-15; 38-52; RP 122-145; 151-164 AND 192-198, FUNCTION, INTERACTION WITH PRMT5; SNRPB; RP SNRPD2; SNRPD3 AND SNRPE, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=11756452; DOI=10.1074/jbc.m109984200; RA Friesen W.J., Wyce A., Paushkin S., Abel L., Rappsilber J., Mann M., RA Dreyfuss G.; RT "A novel WD repeat protein component of the methylosome binds Sm RT proteins."; RL J. Biol. Chem. 277:8243-8247(2002). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 3-15, TISSUE RP SPECIFICITY, AND INTERACTION WITH AR AND NKX3-1. RX PubMed=12972618; DOI=10.1128/mcb.23.19.7019-7029.2003; RA Hosohata K., Li P., Hosohata Y., Qin J., Roeder R.G., Wang Z.; RT "Purification and identification of a novel complex which is involved in RT androgen receptor-dependent transcription."; RL Mol. Cell. Biol. 23:7019-7029(2003). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Kidney proximal tubule; 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Hepatoblastoma; RX PubMed=15221005; DOI=10.1038/sj.onc.1207782; RA Yamada S., Ohira M., Horie H., Ando K., Takayasu H., Suzuki Y., Sugano S., RA Hirata T., Goto T., Matsunaga T., Hiyama E., Hayashi Y., Ando H., Suita S., RA Kaneko M., Sasaki F., Hashizume K., Ohnuma N., Nakagawara A.; RT "Expression profiling and differential screening between hepatoblastomas RT and the corresponding normal livers: identification of high expression of RT the PLK1 oncogene as a poor-prognostic indicator of hepatoblastomas."; RL Oncogene 23:5901-5911(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Colon, Lung, and 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 [8] RP PROTEIN SEQUENCE OF 3-15; 36-52; 122-145; 151-179 AND 192-198, RP PHOSPHORYLATION AT THR-5, AND IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Colon carcinoma; RA Bienvenut W.V., Zebisch A., Kolch W.; RL Submitted (DEC-2008) to UniProtKB. RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 184-342 (ISOFORM 1). RC TISSUE=Neuroblastoma; RX PubMed=12880961; DOI=10.1016/s0304-3835(03)00085-5; RA Ohira M., Morohashi A., Nakamura Y., Isogai E., Furuya K., Hamano S., RA Machida T., Aoyama M., Fukumura M., Miyazaki K., Suzuki Y., Sugano S., RA Hirato J., Nakagawara A.; RT "Neuroblastoma oligo-capping cDNA project: toward the understanding of the RT genesis and biology of neuroblastoma."; RL Cancer Lett. 197:63-68(2003). RN [10] RP SUBCELLULAR LOCATION, AND INTERACTION WITH CTDP1. RX PubMed=12560496; DOI=10.1093/nar/gkg197; RA Licciardo P., Amente S., Ruggiero L., Monti M., Pucci P., Lania L., RA Majello B.; RT "The FCP1 phosphatase interacts with RNA polymerase II and with MEP50 a RT component of the methylosome complex involved in the assembly of snRNP."; RL Nucleic Acids Res. 31:999-1005(2003). RN [11] RP INTERACTION WITH LSM11. RX PubMed=16087681; DOI=10.1074/jbc.m505077200; RA Azzouz T.N., Pillai R.S., Dapp C., Chari A., Meister G., Kambach C., RA Fischer U., Schuemperli D.; RT "Toward an assembly line for U7 snRNPs: interactions of U7-specific Lsm RT proteins with PRMT5 and SMN complexes."; RL J. Biol. Chem. 280:34435-34440(2005). RN [12] RP SUBCELLULAR LOCATION, AND INTERACTION WITH H2AC20; PRMT5 AND SUZ12. RX PubMed=16712789; DOI=10.1016/j.bbrc.2006.05.014; RA Furuno K., Masatsugu T., Sonoda M., Sasazuki T., Yamamoto K.; RT "Association of Polycomb group SUZ12 with WD-repeat protein MEP50 that RT binds to histone H2A selectively in vitro."; RL Biochem. Biophys. Res. Commun. 345:1051-1058(2006). RN [13] RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE. RX PubMed=17437848; DOI=10.1016/j.juro.2007.01.017; RA Liang J.J., Wang Z., Chiriboga L., Greco M.A., Shapiro E., Huang H., RA Yang X.J., Huang J., Peng Y., Melamed J., Garabedian M.J., Lee P.; RT "The expression and function of androgen receptor coactivator p44 and RT protein arginine methyltransferase 5 in the developing testis and RT testicular tumors."; RL J. Urol. 177:1918-1922(2007). RN [14] RP IDENTIFICATION IN THE METHYLOSOME COMPLEX. RX PubMed=18984161; DOI=10.1016/j.cell.2008.09.020; RA Chari A., Golas M.M., Klingenhager M., Neuenkirchen N., Sander B., RA Englbrecht C., Sickmann A., Stark H., Fischer U.; RT "An assembly chaperone collaborates with the SMN complex to generate RT spliceosomal SnRNPs."; RL Cell 135:497-509(2008). RN [15] RP 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 [16] RP INTERACTION WITH APEX1, IDENTIFICATION BY MASS SPECTROMETRY, AND RP SUBCELLULAR LOCATION. RX PubMed=19188445; DOI=10.1128/mcb.01337-08; RA Vascotto C., Fantini D., Romanello M., Cesaratto L., Deganuto M., RA Leonardi A., Radicella J.P., Kelley M.R., D'Ambrosio C., Scaloni A., RA Quadrifoglio F., Tell G.; RT "APE1/Ref-1 interacts with NPM1 within nucleoli and plays a role in the RT rRNA quality control process."; RL Mol. Cell. Biol. 29:1834-1854(2009). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-5, AND IDENTIFICATION BY MASS RP 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 [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-5, AND IDENTIFICATION BY MASS RP 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 [19] 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 [20] RP SUBUNIT, SUBCELLULAR LOCATION, AND IDENTIFICATION IN A COMPLEX WITH PRTM5; RP WDR77; RIOK1 OR CLNS1A. RX PubMed=21081503; DOI=10.1074/jbc.m110.148486; RA Guderian G., Peter C., Wiesner J., Sickmann A., Schulze-Osthoff K., RA Fischer U., Grimmler M.; RT "RioK1, a new interactor of protein arginine methyltransferase 5 (PRMT5), RT competes with pICln for binding and modulates PRMT5 complex composition and RT substrate specificity."; RL J. Biol. Chem. 286:1976-1986(2011). RN [21] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-5, AND IDENTIFICATION BY MASS RP 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 [22] RP INTERACTION WITH CHTOP, AND IDENTIFICATION IN THE METHYLOSOME COMPLEX WITH RP PRMT1; PRMT5 AND ERH. RX PubMed=25284789; DOI=10.1016/j.celrep.2014.08.071; RA Takai H., Masuda K., Sato T., Sakaguchi Y., Suzuki T., Suzuki T., RA Koyama-Nasu R., Nasu-Nishimura Y., Katou Y., Ogawa H., Morishita Y., RA Kozuka-Hata H., Oyama M., Todo T., Ino Y., Mukasa A., Saito N., RA Toyoshima C., Shirahige K., Akiyama T.; RT "5-Hydroxymethylcytosine plays a critical role in glioblastomagenesis by RT recruiting the CHTOP-methylosome complex."; RL Cell Rep. 9:48-60(2014). RN [23] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-5, AND IDENTIFICATION BY MASS RP 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 [24] RP INTERACTION WITH PRMT5. RX PubMed=33376131; DOI=10.26508/lsa.202000699; RA Chakrapani B., Khan M.I.K., Kadumuri R.V., Gupta S., Verma M., Awasthi S., RA Govindaraju G., Mahesh A., Rajavelu A., Chavali S., Dhayalan A.; RT "The uncharacterized protein FAM47E interacts with PRMT5 and regulates its RT functions."; RL Life. Sci Alliance 4:e202000699-e202000699(2021). RN [25] RP X-RAY CRYSTALLOGRAPHY (2.06 ANGSTROMS) OF 2-342 IN COMPLEX WITH PRMT5, RP FUNCTION, WD REPEATS, AND SUBUNIT. RX PubMed=23071334; DOI=10.1073/pnas.1209814109; RA Antonysamy S., Bonday Z., Campbell R.M., Doyle B., Druzina Z., Gheyi T., RA Han B., Jungheim L.N., Qian Y., Rauch C., Russell M., Sauder J.M., RA Wasserman S.R., Weichert K., Willard F.S., Zhang A., Emtage S.; RT "Crystal structure of the human PRMT5:MEP50 complex."; RL Proc. Natl. Acad. Sci. U.S.A. 109:17960-17965(2012). CC -!- FUNCTION: Non-catalytic component of the methylosome complex, composed CC of PRMT5, WDR77 and CLNS1A, which modifies specific arginines to CC dimethylarginines in several spliceosomal Sm proteins and histones CC (PubMed:11756452). This modification targets Sm proteins to the CC survival of motor neurons (SMN) complex for assembly into small nuclear CC ribonucleoprotein core particles. Might play a role in transcription CC regulation. The methylosome complex also methylates the Piwi proteins CC (PIWIL1, PIWIL2 and PIWIL4), methylation of Piwi proteins being CC required for the interaction with Tudor domain-containing proteins and CC subsequent localization to the meiotic nuage (PubMed:23071334). CC {ECO:0000269|PubMed:11756452, ECO:0000269|PubMed:23071334}. CC -!- SUBUNIT: Component of the methylosome complex composed of PRMT5, WDR77 CC and CLNS1A (PubMed:21081503, PubMed:18984161). Found in a complex CC composed of PRMT5, WDR77 and RIOK1 (PubMed:21081503). RIOK1 and CLNS1A CC bound directly to PRMT5 at the same binding site, in a mutually CC exclusive manner, which allows the recruitment of distinct methylation CC substrates, such as nucleolin/NCL and Sm proteins, respectively CC (PubMed:21081503). Found in a complex with the component of the CC methylosome, PRMT5, CLNS1A, WDR77, PRMT1 and ERH (PubMed:25284789). CC Directly interacts with PRMT5, as well as with several Sm proteins, CC including SNRPB and SNRPD2 and, more weakly, SNRPD3 and SNRPE CC (PubMed:11756452, PubMed:33376131). Forms a compact hetero-octamer with CC PRMT5, decorating the outer surface of a PRMT5 tetramer. Interacts with CC SUZ12 and histone H2A/H2AC20, but not with histones H2B, H3 nor H4 CC (PubMed:16712789). Interacts with CTDP1 and LSM11 (PubMed:12560496, CC PubMed:16087681). Interacts with APEX1, AR and NKX3-1 (PubMed:19188445, CC PubMed:12972618). Interacts with CHTOP (PubMed:25284789). Interacts CC with FAM47E. {ECO:0000269|PubMed:11756452, ECO:0000269|PubMed:12560496, CC ECO:0000269|PubMed:12972618, ECO:0000269|PubMed:16087681, CC ECO:0000269|PubMed:16712789, ECO:0000269|PubMed:18984161, CC ECO:0000269|PubMed:19188445, ECO:0000269|PubMed:21081503, CC ECO:0000269|PubMed:23071334, ECO:0000269|PubMed:25284789, CC ECO:0000269|PubMed:33376131}. CC -!- INTERACTION: CC Q9BQA1; P55212: CASP6; NbExp=3; IntAct=EBI-1237307, EBI-718729; CC Q9BQA1; P04792: HSPB1; NbExp=3; IntAct=EBI-1237307, EBI-352682; CC Q9BQA1; O60333-2: KIF1B; NbExp=3; IntAct=EBI-1237307, EBI-10975473; CC Q9BQA1; P13473-2: LAMP2; NbExp=3; IntAct=EBI-1237307, EBI-21591415; CC Q9BQA1; O14744: PRMT5; NbExp=17; IntAct=EBI-1237307, EBI-351098; CC Q9BQA1; P62826: RAN; NbExp=3; IntAct=EBI-1237307, EBI-286642; CC Q9BQA1; Q9Y3C5: RNF11; NbExp=3; IntAct=EBI-1237307, EBI-396669; CC Q9BQA1; O76024: WFS1; NbExp=3; IntAct=EBI-1237307, EBI-720609; CC Q9BQA1; P03418: N; Xeno; NbExp=3; IntAct=EBI-1237307, EBI-6930799; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17437848, CC ECO:0000269|PubMed:21081503}. Cytoplasm {ECO:0000269|PubMed:17437848, CC ECO:0000269|PubMed:21081503}. Note=Nuclear in Leydig cells and CC cytoplasmic in germ cells during fetal testicular development. In adult CC testis, predominantly nuclear. Subcellular location varies from nuclear CC to cytoplasmic in various tumors (PubMed:17437848). CC {ECO:0000269|PubMed:17437848}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9BQA1-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9BQA1-2; Sequence=VSP_056166; CC -!- TISSUE SPECIFICITY: Highly expressed in heart, skeletal muscle, spleen, CC testis, uterus, prostate and thymus. In testis, expressed in germ cells CC and Leydig cells, but not in peritubular myocytes, nor in Sertoli CC cells. Expressed in prostate cancers, in seminomas and in Leydig cell CC tumors. {ECO:0000269|PubMed:12972618, ECO:0000269|PubMed:17437848}. CC -!- DEVELOPMENTAL STAGE: Expressed in Leydig cells during fetal testicular CC development, especially during the second semester. Germ cells CC expression is detected as early as 10 weeks of gestation. CC {ECO:0000269|PubMed:17437848}. CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="http://atlasgeneticsoncology.org/Genes/WDR77ID44142ch1p13.html"; 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; AF478464; AAL79917.1; -; mRNA. DR EMBL; AK022860; BAG51128.1; -; mRNA. DR EMBL; AK298179; BAG60450.1; -; mRNA. DR EMBL; AK223189; BAD96909.1; -; mRNA. DR EMBL; AY225316; AAP79114.1; -; mRNA. DR EMBL; AB073603; BAD38641.1; -; mRNA. DR EMBL; AL390195; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471122; EAW56493.1; -; Genomic_DNA. DR EMBL; BC001679; AAH01679.1; -; mRNA. DR EMBL; BC006477; AAH06477.1; -; mRNA. DR EMBL; BC009411; AAH09411.1; -; mRNA. DR EMBL; BC011778; AAH11778.1; -; mRNA. DR EMBL; BC016946; AAH16946.1; -; mRNA. DR EMBL; AB074171; BAE45736.1; -; mRNA. DR CCDS; CCDS835.1; -. [Q9BQA1-1] DR RefSeq; NP_001303991.1; NM_001317062.1. DR RefSeq; NP_001303992.1; NM_001317063.1. DR RefSeq; NP_001303993.1; NM_001317064.1. [Q9BQA1-2] DR RefSeq; NP_077007.1; NM_024102.3. [Q9BQA1-1] DR PDB; 4GQB; X-ray; 2.06 A; B=2-342. DR PDB; 4X60; X-ray; 2.35 A; B=2-342. DR PDB; 4X61; X-ray; 2.85 A; B=2-342. DR PDB; 4X63; X-ray; 3.05 A; B=2-342. DR PDB; 5C9Z; X-ray; 2.36 A; B=2-342. DR PDB; 5EMJ; X-ray; 2.27 A; B=2-342. DR PDB; 5EMK; X-ray; 2.52 A; B=2-342. DR PDB; 5EML; X-ray; 2.39 A; B=2-342. DR PDB; 5EMM; X-ray; 2.37 A; B=2-342. DR PDB; 5FA5; X-ray; 2.34 A; B=2-342. DR PDB; 6CKC; X-ray; 2.80 A; B=2-342. DR PDB; 6K1S; X-ray; 2.60 A; B=2-342. DR PDB; 6RLL; X-ray; 2.22 A; B=2-342. DR PDB; 6RLQ; X-ray; 2.53 A; B=2-342. DR PDB; 6UGH; EM; 3.40 A; B=2-342. DR PDB; 6UXX; X-ray; 2.69 A; B=2-342. DR PDB; 6UXY; X-ray; 2.57 A; B=2-342. DR PDB; 6V0N; X-ray; 2.11 A; B=2-342. DR PDB; 6V0O; X-ray; 2.86 A; B=2-342. DR PDB; 6V0P; X-ray; 1.88 A; B=2-342. DR PDBsum; 4GQB; -. DR PDBsum; 4X60; -. DR PDBsum; 4X61; -. DR PDBsum; 4X63; -. DR PDBsum; 5C9Z; -. DR PDBsum; 5EMJ; -. DR PDBsum; 5EMK; -. DR PDBsum; 5EML; -. DR PDBsum; 5EMM; -. DR PDBsum; 5FA5; -. DR PDBsum; 6CKC; -. DR PDBsum; 6K1S; -. DR PDBsum; 6RLL; -. DR PDBsum; 6RLQ; -. DR PDBsum; 6UGH; -. DR PDBsum; 6UXX; -. DR PDBsum; 6UXY; -. DR PDBsum; 6V0N; -. DR PDBsum; 6V0O; -. DR PDBsum; 6V0P; -. DR SMR; Q9BQA1; -. DR BioGRID; 122532; 307. DR ComplexPortal; CPX-696; PRMT5 methylosome complex. DR CORUM; Q9BQA1; -. DR DIP; DIP-38172N; -. DR IntAct; Q9BQA1; 96. DR MINT; Q9BQA1; -. DR STRING; 9606.ENSP00000235090; -. DR BindingDB; Q9BQA1; -. DR ChEMBL; CHEMBL3108649; -. DR iPTMnet; Q9BQA1; -. DR PhosphoSitePlus; Q9BQA1; -. DR SwissPalm; Q9BQA1; -. DR BioMuta; WDR77; -. DR DMDM; 32171507; -. DR REPRODUCTION-2DPAGE; IPI00012202; -. DR EPD; Q9BQA1; -. DR jPOST; Q9BQA1; -. DR MassIVE; Q9BQA1; -. DR MaxQB; Q9BQA1; -. DR PaxDb; Q9BQA1; -. DR PeptideAtlas; Q9BQA1; -. DR PRIDE; Q9BQA1; -. DR ProteomicsDB; 4753; -. DR ProteomicsDB; 78647; -. [Q9BQA1-1] DR Antibodypedia; 35257; 265 antibodies. DR DNASU; 79084; -. DR Ensembl; ENST00000235090; ENSP00000235090; ENSG00000116455. [Q9BQA1-1] DR GeneID; 79084; -. DR KEGG; hsa:79084; -. DR UCSC; uc001ebb.4; human. [Q9BQA1-1] DR CTD; 79084; -. DR DisGeNET; 79084; -. DR GeneCards; WDR77; -. DR HGNC; HGNC:29652; WDR77. DR HPA; ENSG00000116455; Tissue enhanced (fallopian). DR MIM; 611734; gene. DR neXtProt; NX_Q9BQA1; -. DR OpenTargets; ENSG00000116455; -. DR PharmGKB; PA142670581; -. DR VEuPathDB; HostDB:ENSG00000116455.13; -. DR eggNOG; KOG0284; Eukaryota. DR GeneTree; ENSGT00390000010711; -. DR HOGENOM; CLU_051285_0_0_1; -. DR InParanoid; Q9BQA1; -. DR OMA; HQVIHHV; -. DR OrthoDB; 774546at2759; -. DR PhylomeDB; Q9BQA1; -. DR TreeFam; TF325967; -. DR PathwayCommons; Q9BQA1; -. DR Reactome; R-HSA-191859; snRNP Assembly. DR Reactome; R-HSA-3214858; RMTs methylate histone arginines. DR SignaLink; Q9BQA1; -. DR BioGRID-ORCS; 79084; 720 hits in 1005 CRISPR screens. DR ChiTaRS; WDR77; human. DR GeneWiki; WD_repeat-containing_protein_77; -. DR GenomeRNAi; 79084; -. DR Pharos; Q9BQA1; Tbio. DR PRO; PR:Q9BQA1; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q9BQA1; protein. DR Bgee; ENSG00000116455; Expressed in right uterine tube and 232 other tissues. DR ExpressionAtlas; Q9BQA1; baseline and differential. DR Genevisible; Q9BQA1; HS. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:UniProtKB. DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA. DR GO; GO:0034709; C:methylosome; IDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0045495; C:pole plasm; IBA:GO_Central. DR GO; GO:0008327; F:methyl-CpG binding; IDA:UniProtKB. DR GO; GO:0030374; F:nuclear receptor coactivator activity; IGI:MGI. DR GO; GO:0060770; P:negative regulation of epithelial cell proliferation involved in prostate gland development; IBA:GO_Central. DR GO; GO:0007315; P:pole plasm assembly; IBA:GO_Central. DR GO; GO:0008284; P:positive regulation of cell population proliferation; IBA:GO_Central. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central. DR GO; GO:0060528; P:secretory columnal luminar epithelial cell differentiation involved in prostate glandular acinus development; IBA:GO_Central. DR GO; GO:0000387; P:spliceosomal snRNP assembly; TAS:Reactome. DR Gene3D; 2.130.10.10; -; 1. DR IDEAL; IID00583; -. DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf. DR InterPro; IPR001680; WD40_repeat. DR InterPro; IPR019775; WD40_repeat_CS. DR InterPro; IPR017986; WD40_repeat_dom. DR InterPro; IPR036322; WD40_repeat_dom_sf. DR Pfam; PF00400; WD40; 1. DR SMART; SM00320; WD40; 6. DR SUPFAM; SSF50978; SSF50978; 1. DR PROSITE; PS00678; WD_REPEATS_1; 1. DR PROSITE; PS50082; WD_REPEATS_2; 2. DR PROSITE; PS50294; WD_REPEATS_REGION; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cytoplasm; Direct protein sequencing; KW Nucleus; Phosphoprotein; Reference proteome; Repeat; WD repeat. FT CHAIN 1..342 FT /note="Methylosome protein 50" FT /id="PRO_0000051074" FT REPEAT 22..75 FT /note="WD 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221, FT ECO:0000269|PubMed:23071334" FT REPEAT 78..116 FT /note="WD 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221, FT ECO:0000269|PubMed:23071334" FT REPEAT 123..162 FT /note="WD 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221, FT ECO:0000269|PubMed:23071334" FT REPEAT 165..205 FT /note="WD 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221, FT ECO:0000269|PubMed:23071334" FT REPEAT 209..250 FT /note="WD 5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221, FT ECO:0000269|PubMed:23071334" FT REPEAT 253..293 FT /note="WD 6" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221, FT ECO:0000269|PubMed:23071334" FT REPEAT 295..330 FT /note="WD 7" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221, FT ECO:0000269|PubMed:23071334" FT MOD_RES 5 FT /note="Phosphothreonine" FT /evidence="ECO:0000269|Ref.8, ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT VAR_SEQ 101..164 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_056166" FT VARIANT 48 FT /note="S -> I (in dbSNP:rs7416672)" FT /id="VAR_042903" FT CONFLICT 244 FT /note="S -> N (in Ref. 2; BAD96909)" FT /evidence="ECO:0000305" FT CONFLICT 313..342 FT /note="LTTVGWDHQVVHHVVPTEPLPAPGPASVTE -> DLQVLLSRLDLRQKASPP FT (in Ref. 7; AAH09411)" FT /evidence="ECO:0000305" FT STRAND 29..36 FT /evidence="ECO:0007829|PDB:6V0P" FT STRAND 42..47 FT /evidence="ECO:0007829|PDB:6V0P" FT STRAND 50..52 FT /evidence="ECO:0007829|PDB:6V0P" FT STRAND 56..63 FT /evidence="ECO:0007829|PDB:6V0P" FT HELIX 64..66 FT /evidence="ECO:0007829|PDB:6V0P" FT HELIX 70..72 FT /evidence="ECO:0007829|PDB:6V0P" FT STRAND 74..81 FT /evidence="ECO:0007829|PDB:6V0P" FT STRAND 83..89 FT /evidence="ECO:0007829|PDB:6V0P" FT TURN 90..92 FT /evidence="ECO:0007829|PDB:6V0P" FT STRAND 93..98 FT /evidence="ECO:0007829|PDB:6V0P" FT STRAND 101..108 FT /evidence="ECO:0007829|PDB:6V0P" FT STRAND 110..112 FT /evidence="ECO:0007829|PDB:6V0P" FT STRAND 115..122 FT /evidence="ECO:0007829|PDB:6V0P" FT STRAND 124..126 FT /evidence="ECO:0007829|PDB:6RLL" FT STRAND 128..133 FT /evidence="ECO:0007829|PDB:6V0P" FT STRAND 137..144 FT /evidence="ECO:0007829|PDB:6V0P" FT STRAND 145..147 FT /evidence="ECO:0007829|PDB:6UGH" FT STRAND 149..153 FT /evidence="ECO:0007829|PDB:6V0P" FT TURN 154..157 FT /evidence="ECO:0007829|PDB:6V0P" FT STRAND 158..163 FT /evidence="ECO:0007829|PDB:6V0P" FT STRAND 170..175 FT /evidence="ECO:0007829|PDB:6V0P" FT STRAND 182..187 FT /evidence="ECO:0007829|PDB:6V0P" FT TURN 188..190 FT /evidence="ECO:0007829|PDB:6UXX" FT STRAND 192..196 FT /evidence="ECO:0007829|PDB:6V0P" FT STRAND 199..201 FT /evidence="ECO:0007829|PDB:6V0P" FT STRAND 203..205 FT /evidence="ECO:0007829|PDB:6V0P" FT STRAND 209..211 FT /evidence="ECO:0007829|PDB:6V0O" FT STRAND 215..220 FT /evidence="ECO:0007829|PDB:6V0P" FT STRAND 222..224 FT /evidence="ECO:0007829|PDB:5EMJ" FT STRAND 227..232 FT /evidence="ECO:0007829|PDB:6V0P" FT STRAND 235..242 FT /evidence="ECO:0007829|PDB:6V0P" FT STRAND 244..246 FT /evidence="ECO:0007829|PDB:6V0O" FT STRAND 249..252 FT /evidence="ECO:0007829|PDB:6V0P" FT STRAND 258..263 FT /evidence="ECO:0007829|PDB:6V0P" FT STRAND 265..268 FT /evidence="ECO:0007829|PDB:6V0P" FT STRAND 271..275 FT /evidence="ECO:0007829|PDB:6V0P" FT STRAND 280..283 FT /evidence="ECO:0007829|PDB:6V0P" FT STRAND 289..293 FT /evidence="ECO:0007829|PDB:6V0P" FT STRAND 300..305 FT /evidence="ECO:0007829|PDB:6V0P" FT STRAND 307..309 FT /evidence="ECO:0007829|PDB:6V0P" FT STRAND 312..317 FT /evidence="ECO:0007829|PDB:6V0P" FT STRAND 322..326 FT /evidence="ECO:0007829|PDB:6V0P" SQ SEQUENCE 342 AA; 36724 MW; 3D355AEC68491ECB CRC64; MRKETPPPLV PPAAREWNLP PNAPACMERQ LEAARYRSDG ALLLGASSLS GRCWAGSLWL FKDPCAAPNE GFCSAGVQTE AGVADLTWVG ERGILVASDS GAVELWELDE NETLIVSKFC KYEHDDIVST VSVLSSGTQA VSGSKDICIK VWDLAQQVVL SSYRAHAAQV TCVAASPHKD SVFLSCSEDN RILLWDTRCP KPASQIGCSA PGYLPTSLAW HPQQSEVFVF GDENGTVSLV DTKSTSCVLS SAVHSQCVTG LVFSPHSVPF LASLSEDCSL AVLDSSLSEL FRSQAHRDFV RDATWSPLNH SLLTTVGWDH QVVHHVVPTE PLPAPGPASV TE //