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Methylosome protein 50 (MEP-50) (Androgen receptor cofactor p44) (WD repeat-containing protein 77) (p44/Mep50)

 MEP50_HUMAN             Reviewed;         342 AA.
Q9BQA1; B3KMW6; B4DP38; Q3LID2; Q53FU2; Q6JZZ5; Q96GK4; Q9BWY3;
20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
01-JUN-2001, sequence version 1.
18-JUL-2018, entry version 160.
RecName: Full=Methylosome protein 50;
Short=MEP-50;
AltName: Full=Androgen receptor cofactor p44;
AltName: Full=WD repeat-containing protein 77;
AltName: Full=p44/Mep50;
Name=WDR77; Synonyms=MEP50, WD45; ORFNames=HKMT1069, Nbla10071;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 4-15;
38-52; 122-145; 151-164 AND 192-198, FUNCTION, INTERACTION WITH PRMT5;
SNRPB; SNRPD2; SNRPD3 AND SNRPE, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=11756452; DOI=10.1074/jbc.M109984200;
Friesen W.J., Wyce A., Paushkin S., Abel L., Rappsilber J., Mann M.,
Dreyfuss G.;
"A novel WD repeat protein component of the methylosome binds Sm
proteins.";
J. Biol. Chem. 277:8243-8247(2002).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 3-15,
TISSUE SPECIFICITY, AND INTERACTION WITH AR AND NKX3-1.
PubMed=12972618; DOI=10.1128/MCB.23.19.7019-7029.2003;
Hosohata K., Li P., Hosohata Y., Qin J., Roeder R.G., Wang Z.;
"Purification and identification of a novel complex which is involved
in androgen receptor-dependent transcription.";
Mol. Cell. Biol. 23:7019-7029(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Kidney proximal tubule;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Hepatoblastoma;
PubMed=15221005; DOI=10.1038/sj.onc.1207782;
Yamada S., Ohira M., Horie H., Ando K., Takayasu H., Suzuki Y.,
Sugano S., Hirata T., Goto T., Matsunaga T., Hiyama E., Hayashi Y.,
Ando H., Suita S., Kaneko M., Sasaki F., Hashizume K., Ohnuma N.,
Nakagawara A.;
"Expression profiling and differential screening between
hepatoblastomas and the corresponding normal livers: identification of
high expression of the PLK1 oncogene as a poor-prognostic indicator of
hepatoblastomas.";
Oncogene 23:5901-5911(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Colon, Lung, and Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
PROTEIN SEQUENCE OF 3-15; 36-52; 122-145; 151-179 AND 192-198,
PHOSPHORYLATION AT THR-5, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Colon carcinoma;
Bienvenut W.V., Zebisch A., Kolch W.;
Submitted (DEC-2008) to UniProtKB.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 184-342 (ISOFORM 1).
TISSUE=Neuroblastoma;
PubMed=12880961; DOI=10.1016/S0304-3835(03)00085-5;
Ohira M., Morohashi A., Nakamura Y., Isogai E., Furuya K., Hamano S.,
Machida T., Aoyama M., Fukumura M., Miyazaki K., Suzuki Y., Sugano S.,
Hirato J., Nakagawara A.;
"Neuroblastoma oligo-capping cDNA project: toward the understanding of
the genesis and biology of neuroblastoma.";
Cancer Lett. 197:63-68(2003).
[10]
SUBCELLULAR LOCATION, AND INTERACTION WITH CTDP1.
PubMed=12560496; DOI=10.1093/nar/gkg197;
Licciardo P., Amente S., Ruggiero L., Monti M., Pucci P., Lania L.,
Majello B.;
"The FCP1 phosphatase interacts with RNA polymerase II and with MEP50
a component of the methylosome complex involved in the assembly of
snRNP.";
Nucleic Acids Res. 31:999-1005(2003).
[11]
INTERACTION WITH LSM11.
PubMed=16087681; DOI=10.1074/jbc.M505077200;
Azzouz T.N., Pillai R.S., Dapp C., Chari A., Meister G., Kambach C.,
Fischer U., Schuemperli D.;
"Toward an assembly line for U7 snRNPs: interactions of U7-specific
Lsm proteins with PRMT5 and SMN complexes.";
J. Biol. Chem. 280:34435-34440(2005).
[12]
SUBCELLULAR LOCATION, AND INTERACTION WITH HIST2H2AC; PRMT5 AND SUZ12.
PubMed=16712789; DOI=10.1016/j.bbrc.2006.05.014;
Furuno K., Masatsugu T., Sonoda M., Sasazuki T., Yamamoto K.;
"Association of Polycomb group SUZ12 with WD-repeat protein MEP50 that
binds to histone H2A selectively in vitro.";
Biochem. Biophys. Res. Commun. 345:1051-1058(2006).
[13]
SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=17437848; DOI=10.1016/j.juro.2007.01.017;
Liang J.J., Wang Z., Chiriboga L., Greco M.A., Shapiro E., Huang H.,
Yang X.J., Huang J., Peng Y., Melamed J., Garabedian M.J., Lee P.;
"The expression and function of androgen receptor coactivator p44 and
protein arginine methyltransferase 5 in the developing testis and
testicular tumors.";
J. Urol. 177:1918-1922(2007).
[14]
IDENTIFICATION IN THE METHYLOSOME COMPLEX.
PubMed=18984161; DOI=10.1016/j.cell.2008.09.020;
Chari A., Golas M.M., Klingenhager M., Neuenkirchen N., Sander B.,
Englbrecht C., Sickmann A., Stark H., Fischer U.;
"An assembly chaperone collaborates with the SMN complex to generate
spliceosomal SnRNPs.";
Cell 135:497-509(2008).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[16]
INTERACTION WITH APEX1, IDENTIFICATION BY MASS SPECTROMETRY, AND
SUBCELLULAR LOCATION.
PubMed=19188445; DOI=10.1128/MCB.01337-08;
Vascotto C., Fantini D., Romanello M., Cesaratto L., Deganuto M.,
Leonardi A., Radicella J.P., Kelley M.R., D'Ambrosio C., Scaloni A.,
Quadrifoglio F., Tell G.;
"APE1/Ref-1 interacts with NPM1 within nucleoli and plays a role in
the rRNA quality control process.";
Mol. Cell. Biol. 29:1834-1854(2009).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-5, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-5, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[20]
SUBUNIT, SUBCELLULAR LOCATION, AND IDENDTIFICATION IN A COMPLEX WITH
PRTM5; WDR77; RIOK1 OR CLNS1A.
PubMed=21081503; DOI=10.1074/jbc.M110.148486;
Guderian G., Peter C., Wiesner J., Sickmann A., Schulze-Osthoff K.,
Fischer U., Grimmler M.;
"RioK1, a new interactor of protein arginine methyltransferase 5
(PRMT5), competes with pICln for binding and modulates PRMT5 complex
composition and substrate specificity.";
J. Biol. Chem. 286:1976-1986(2011).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-5, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[22]
INTERACTION WITH CHTOP, AND IDENTIFICATION IN THE METHYLOSOME COMPLEX
WITH PRMT1; PRMT5 AND ERH.
PubMed=25284789; DOI=10.1016/j.celrep.2014.08.071;
Takai H., Masuda K., Sato T., Sakaguchi Y., Suzuki T., Suzuki T.,
Koyama-Nasu R., Nasu-Nishimura Y., Katou Y., Ogawa H., Morishita Y.,
Kozuka-Hata H., Oyama M., Todo T., Ino Y., Mukasa A., Saito N.,
Toyoshima C., Shirahige K., Akiyama T.;
"5-Hydroxymethylcytosine plays a critical role in glioblastomagenesis
by recruiting the CHTOP-methylosome complex.";
Cell Rep. 9:48-60(2014).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-5, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[24]
X-RAY CRYSTALLOGRAPHY (2.06 ANGSTROMS) OF 2-342 IN COMPLEX WITH PRMT5,
FUNCTION, WD REPEATS, AND SUBUNIT.
PubMed=23071334; DOI=10.1073/pnas.1209814109;
Antonysamy S., Bonday Z., Campbell R.M., Doyle B., Druzina Z.,
Gheyi T., Han B., Jungheim L.N., Qian Y., Rauch C., Russell M.,
Sauder J.M., Wasserman S.R., Weichert K., Willard F.S., Zhang A.,
Emtage S.;
"Crystal structure of the human PRMT5:MEP50 complex.";
Proc. Natl. Acad. Sci. U.S.A. 109:17960-17965(2012).
-!- FUNCTION: Non-catalytic component of the methylosome complex,
composed of PRMT5, WDR77 and CLNS1A, which modifies specific
arginines to dimethylarginines in several spliceosomal Sm proteins
and histones (PubMed:11756452). This modification targets Sm
proteins to the survival of motor neurons (SMN) complex for
assembly into small nuclear ribonucleoprotein core particles.
Might play a role in transcription regulation. The methylosome
complex also methylates the Piwi proteins (PIWIL1, PIWIL2 and
PIWIL4), methylation of Piwi proteins being required for the
interaction with Tudor domain-containing proteins and subsequent
localization to the meiotic nuage (PubMed:23071334).
{ECO:0000269|PubMed:11756452, ECO:0000269|PubMed:23071334}.
-!- SUBUNIT: Component of the methylosome complex composed of PRMT5,
WDR77 and CLNS1A (PubMed:21081503, PubMed:18984161). Found in a
complex composed of PRMT5, WDR77 and RIOK1 (PubMed:21081503).
RIOK1 and CLNS1A bound directly to PRMT5 at the same binding site,
in a mutually exclusive manner, which allows the recruitment of
distinct methylation substrates, such as nucleolin/NCL and Sm
proteins, respectively (PubMed:21081503). Found in a complex with
the component of the methylosome, PRMT5, CLNS1A, WDR77, PRMT1 and
ERH (PubMed:25284789). Directly interacts with PRMT5, as well as
with several Sm proteins, including SNRPB and SNRPD2 and, more
weakly, SNRPD3 and SNRPE (PubMed:11756452). Forms a compact
hetero-octamer with PRMT5, decorating the outer surface of a PRMT5
tetramer. Interacts with SUZ12 and histone H2A/HIST2H2AC, but not
with histones H2B, H3 nor H4 (PubMed:16712789). Interacts with
CTDP1 and LSM11 (PubMed:12560496, PubMed:16087681). Interacts with
APEX1, AR and NKX3-1 (PubMed:19188445, PubMed:12972618). Interacts
with CHTOP (PubMed:25284789). {ECO:0000269|PubMed:11756452,
ECO:0000269|PubMed:12560496, ECO:0000269|PubMed:12972618,
ECO:0000269|PubMed:16087681, ECO:0000269|PubMed:16712789,
ECO:0000269|PubMed:18984161, ECO:0000269|PubMed:19188445,
ECO:0000269|PubMed:21081503, ECO:0000269|PubMed:23071334,
ECO:0000269|PubMed:25284789}.
-!- INTERACTION:
P03418:N (xeno); NbExp=3; IntAct=EBI-1237307, EBI-6930799;
O14744:PRMT5; NbExp=16; IntAct=EBI-1237307, EBI-351098;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17437848,
ECO:0000269|PubMed:21081503}. Cytoplasm
{ECO:0000269|PubMed:17437848, ECO:0000269|PubMed:21081503}.
Note=Nuclear in Leydig cells and cytoplasmic in germ cells during
fetal testicular development. In adult testis, predominantly
nuclear. Subcellular location varies from nuclear to cytoplasmic
in various tumors (PubMed:17437848).
{ECO:0000269|PubMed:17437848}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9BQA1-1; Sequence=Displayed;
Name=2;
IsoId=Q9BQA1-2; Sequence=VSP_056166;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Highly expressed in heart, skeletal muscle,
spleen, testis, uterus, prostate and thymus. In testis, expressed
in germ cells and Leydig cells, but not in peritubular myocytes,
nor in Sertoli cells. Expressed in prostate cancers, in seminomas
and in Leydig cell tumors. {ECO:0000269|PubMed:12972618,
ECO:0000269|PubMed:17437848}.
-!- DEVELOPMENTAL STAGE: Expressed in Leydig cells during fetal
testicular development, especially during the second semester.
Germ cells expression is detected as early as 10 weeks of
gestation. {ECO:0000269|PubMed:17437848}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/WDR77ID44142ch1p13.html";
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EMBL; AF478464; AAL79917.1; -; mRNA.
EMBL; AK022860; BAG51128.1; -; mRNA.
EMBL; AK298179; BAG60450.1; -; mRNA.
EMBL; AK223189; BAD96909.1; -; mRNA.
EMBL; AY225316; AAP79114.1; -; mRNA.
EMBL; AB073603; BAD38641.1; -; mRNA.
EMBL; AL390195; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471122; EAW56493.1; -; Genomic_DNA.
EMBL; BC001679; AAH01679.1; -; mRNA.
EMBL; BC006477; AAH06477.1; -; mRNA.
EMBL; BC009411; AAH09411.1; -; mRNA.
EMBL; BC011778; AAH11778.1; -; mRNA.
EMBL; BC016946; AAH16946.1; -; mRNA.
EMBL; AB074171; BAE45736.1; -; mRNA.
CCDS; CCDS835.1; -. [Q9BQA1-1]
RefSeq; NP_001303991.1; NM_001317062.1.
RefSeq; NP_001303992.1; NM_001317063.1.
RefSeq; NP_001303993.1; NM_001317064.1. [Q9BQA1-2]
RefSeq; NP_077007.1; NM_024102.3. [Q9BQA1-1]
UniGene; Hs.204773; -.
PDB; 4GQB; X-ray; 2.06 A; B=2-342.
PDB; 4X60; X-ray; 2.35 A; B=2-342.
PDB; 4X61; X-ray; 2.85 A; B=2-342.
PDB; 4X63; X-ray; 3.05 A; B=2-342.
PDB; 5C9Z; X-ray; 2.36 A; B=2-342.
PDB; 5EMJ; X-ray; 2.27 A; B=2-342.
PDB; 5EMK; X-ray; 2.52 A; B=2-342.
PDB; 5EML; X-ray; 2.39 A; B=2-342.
PDB; 5EMM; X-ray; 2.37 A; B=2-342.
PDB; 5FA5; X-ray; 2.34 A; B=2-342.
PDB; 6CKC; X-ray; 2.80 A; B=2-342.
PDBsum; 4GQB; -.
PDBsum; 4X60; -.
PDBsum; 4X61; -.
PDBsum; 4X63; -.
PDBsum; 5C9Z; -.
PDBsum; 5EMJ; -.
PDBsum; 5EMK; -.
PDBsum; 5EML; -.
PDBsum; 5EMM; -.
PDBsum; 5FA5; -.
PDBsum; 6CKC; -.
ProteinModelPortal; Q9BQA1; -.
SMR; Q9BQA1; -.
BioGrid; 122532; 125.
ComplexPortal; CPX-696; Methylosome.
CORUM; Q9BQA1; -.
DIP; DIP-38172N; -.
IntAct; Q9BQA1; 68.
MINT; Q9BQA1; -.
STRING; 9606.ENSP00000235090; -.
BindingDB; Q9BQA1; -.
ChEMBL; CHEMBL3137261; -.
iPTMnet; Q9BQA1; -.
PhosphoSitePlus; Q9BQA1; -.
BioMuta; WDR77; -.
DMDM; 32171507; -.
REPRODUCTION-2DPAGE; IPI00012202; -.
EPD; Q9BQA1; -.
MaxQB; Q9BQA1; -.
PaxDb; Q9BQA1; -.
PeptideAtlas; Q9BQA1; -.
PRIDE; Q9BQA1; -.
ProteomicsDB; 78647; -.
DNASU; 79084; -.
Ensembl; ENST00000235090; ENSP00000235090; ENSG00000116455. [Q9BQA1-1]
GeneID; 79084; -.
KEGG; hsa:79084; -.
UCSC; uc001ebb.4; human. [Q9BQA1-1]
CTD; 79084; -.
DisGeNET; 79084; -.
EuPathDB; HostDB:ENSG00000116455.13; -.
GeneCards; WDR77; -.
HGNC; HGNC:29652; WDR77.
HPA; HPA026437; -.
HPA; HPA026448; -.
HPA; HPA027271; -.
MIM; 611734; gene.
neXtProt; NX_Q9BQA1; -.
OpenTargets; ENSG00000116455; -.
PharmGKB; PA142670581; -.
eggNOG; ENOG410IP8S; Eukaryota.
eggNOG; ENOG4111F0R; LUCA.
GeneTree; ENSGT00390000010711; -.
HOGENOM; HOG000035094; -.
HOVERGEN; HBG052458; -.
InParanoid; Q9BQA1; -.
KO; K13221; -.
OMA; DTKSASC; -.
OrthoDB; EOG091G0T6F; -.
PhylomeDB; Q9BQA1; -.
TreeFam; TF325967; -.
Reactome; R-HSA-191859; snRNP Assembly.
Reactome; R-HSA-3214858; RMTs methylate histone arginines.
SignaLink; Q9BQA1; -.
ChiTaRS; WDR77; human.
GeneWiki; WD_repeat-containing_protein_77; -.
GenomeRNAi; 79084; -.
PRO; PR:Q9BQA1; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000116455; -.
CleanEx; HS_WDR77; -.
ExpressionAtlas; Q9BQA1; baseline and differential.
Genevisible; Q9BQA1; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
GO; GO:0034709; C:methylosome; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0030374; F:ligand-dependent nuclear receptor transcription coactivator activity; IGI:MGI.
GO; GO:0008327; F:methyl-CpG binding; IDA:UniProtKB.
GO; GO:0016274; F:protein-arginine N-methyltransferase activity; TAS:Reactome.
GO; GO:0060770; P:negative regulation of epithelial cell proliferation involved in prostate gland development; IEA:Ensembl.
GO; GO:0008284; P:positive regulation of cell proliferation; IEA:Ensembl.
GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:Ensembl.
GO; GO:0060528; P:secretory columnal luminar epithelial cell differentiation involved in prostate glandular acinus development; IEA:Ensembl.
Gene3D; 2.130.10.10; -; 1.
InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
InterPro; IPR001680; WD40_repeat.
InterPro; IPR019775; WD40_repeat_CS.
InterPro; IPR017986; WD40_repeat_dom.
InterPro; IPR036322; WD40_repeat_dom_sf.
Pfam; PF00400; WD40; 1.
SMART; SM00320; WD40; 6.
SUPFAM; SSF50978; SSF50978; 1.
PROSITE; PS00678; WD_REPEATS_1; 1.
PROSITE; PS50082; WD_REPEATS_2; 2.
PROSITE; PS50294; WD_REPEATS_REGION; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; Cytoplasm;
Direct protein sequencing; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Repeat; WD repeat.
CHAIN 1 342 Methylosome protein 50.
/FTId=PRO_0000051074.
REPEAT 22 75 WD 1. {ECO:0000255|PROSITE-
ProRule:PRU00221,
ECO:0000269|PubMed:23071334}.
REPEAT 78 116 WD 2. {ECO:0000255|PROSITE-
ProRule:PRU00221,
ECO:0000269|PubMed:23071334}.
REPEAT 123 162 WD 3. {ECO:0000255|PROSITE-
ProRule:PRU00221,
ECO:0000269|PubMed:23071334}.
REPEAT 165 205 WD 4. {ECO:0000255|PROSITE-
ProRule:PRU00221,
ECO:0000269|PubMed:23071334}.
REPEAT 209 250 WD 5. {ECO:0000255|PROSITE-
ProRule:PRU00221,
ECO:0000269|PubMed:23071334}.
REPEAT 253 293 WD 6. {ECO:0000255|PROSITE-
ProRule:PRU00221,
ECO:0000269|PubMed:23071334}.
REPEAT 295 330 WD 7. {ECO:0000255|PROSITE-
ProRule:PRU00221,
ECO:0000269|PubMed:23071334}.
MOD_RES 5 5 Phosphothreonine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569,
ECO:0000269|Ref.8}.
VAR_SEQ 101 164 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_056166.
VARIANT 48 48 S -> I (in dbSNP:rs7416672).
/FTId=VAR_042903.
CONFLICT 244 244 S -> N (in Ref. 2; BAD96909).
{ECO:0000305}.
CONFLICT 313 342 LTTVGWDHQVVHHVVPTEPLPAPGPASVTE -> DLQVLLS
RLDLRQKASPP (in Ref. 7; AAH09411).
{ECO:0000305}.
STRAND 29 36 {ECO:0000244|PDB:4GQB}.
STRAND 42 47 {ECO:0000244|PDB:4GQB}.
STRAND 50 52 {ECO:0000244|PDB:4GQB}.
STRAND 56 63 {ECO:0000244|PDB:4GQB}.
HELIX 64 66 {ECO:0000244|PDB:4GQB}.
HELIX 70 72 {ECO:0000244|PDB:4GQB}.
STRAND 74 81 {ECO:0000244|PDB:4GQB}.
STRAND 83 89 {ECO:0000244|PDB:4GQB}.
TURN 90 92 {ECO:0000244|PDB:4GQB}.
STRAND 93 98 {ECO:0000244|PDB:4GQB}.
STRAND 101 108 {ECO:0000244|PDB:4GQB}.
STRAND 110 113 {ECO:0000244|PDB:5EMJ}.
STRAND 115 122 {ECO:0000244|PDB:4GQB}.
STRAND 128 133 {ECO:0000244|PDB:4GQB}.
STRAND 137 144 {ECO:0000244|PDB:4GQB}.
STRAND 149 153 {ECO:0000244|PDB:4GQB}.
TURN 154 157 {ECO:0000244|PDB:4GQB}.
STRAND 158 163 {ECO:0000244|PDB:4GQB}.
STRAND 170 175 {ECO:0000244|PDB:4GQB}.
STRAND 182 187 {ECO:0000244|PDB:4GQB}.
STRAND 192 196 {ECO:0000244|PDB:4GQB}.
STRAND 199 201 {ECO:0000244|PDB:4GQB}.
STRAND 203 205 {ECO:0000244|PDB:4GQB}.
STRAND 208 211 {ECO:0000244|PDB:4X63}.
STRAND 215 220 {ECO:0000244|PDB:4GQB}.
STRAND 222 224 {ECO:0000244|PDB:5EMJ}.
STRAND 227 232 {ECO:0000244|PDB:4GQB}.
STRAND 235 242 {ECO:0000244|PDB:4GQB}.
STRAND 249 252 {ECO:0000244|PDB:4GQB}.
STRAND 258 263 {ECO:0000244|PDB:4GQB}.
STRAND 265 268 {ECO:0000244|PDB:4GQB}.
STRAND 271 275 {ECO:0000244|PDB:4GQB}.
STRAND 280 283 {ECO:0000244|PDB:4GQB}.
STRAND 289 293 {ECO:0000244|PDB:4GQB}.
STRAND 300 305 {ECO:0000244|PDB:4GQB}.
STRAND 307 309 {ECO:0000244|PDB:4GQB}.
STRAND 312 317 {ECO:0000244|PDB:4GQB}.
STRAND 322 326 {ECO:0000244|PDB:4GQB}.
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


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