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Q9BQA1

- MEP50_HUMAN

UniProt

Q9BQA1 - MEP50_HUMAN

Protein

Methylosome protein 50

Gene

WDR77

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 121 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      Previous versions | rss
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    Functioni

    Non-catalytic component of the 20S PRMT5-containing methyltransferase complex, which modifies specific arginines to dimethylarginines in several spliceosomal Sm proteins and histones. 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 20S PRMT5-containing methyltransferase 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.2 Publications

    GO - Molecular functioni

    1. ligand-dependent nuclear receptor transcription coactivator activity Source: MGI
    2. protein binding Source: UniProtKB

    GO - Biological processi

    1. gene expression Source: Reactome
    2. ncRNA metabolic process Source: Reactome
    3. negative regulation of epithelial cell proliferation involved in prostate gland development Source: Ensembl
    4. positive regulation of cell proliferation Source: Ensembl
    5. regulation of transcription from RNA polymerase II promoter Source: Ensembl
    6. RNA metabolic process Source: Reactome
    7. secretory columnal luminar epithelial cell differentiation involved in prostate glandular acinus development Source: Ensembl
    8. spliceosomal snRNP assembly Source: Reactome

    Enzyme and pathway databases

    ReactomeiREACT_11066. snRNP Assembly.
    SignaLinkiQ9BQA1.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Methylosome protein 50
    Short name:
    MEP-50
    Alternative name(s):
    Androgen receptor cofactor p44
    WD repeat-containing protein 77
    p44/Mep50
    Gene namesi
    Name:WDR77
    Synonyms:MEP50, WD45
    ORF Names:HKMT1069, Nbla10071
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:29652. WDR77.

    Subcellular locationi

    Nucleus. Cytoplasm
    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.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: UniProtKB
    3. Golgi apparatus Source: HPA
    4. methylosome Source: UniProtKB
    5. nucleus Source: HPA

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA142670581.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 342342Methylosome protein 50PRO_0000051074Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei5 – 51Phosphothreonine3 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9BQA1.
    PaxDbiQ9BQA1.
    PeptideAtlasiQ9BQA1.
    PRIDEiQ9BQA1.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00012202.

    PTM databases

    PhosphoSiteiQ9BQA1.

    Expressioni

    Tissue specificityi

    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.2 Publications

    Developmental stagei

    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.1 Publication

    Gene expression databases

    ArrayExpressiQ9BQA1.
    BgeeiQ9BQA1.
    CleanExiHS_WDR77.
    GenevestigatoriQ9BQA1.

    Organism-specific databases

    HPAiHPA026437.
    HPA026448.
    HPA027271.

    Interactioni

    Subunit structurei

    Component of the methylosome, a 20S complex containing at least PRMT5, CLNS1A and WDR77. Directly interacts with PRMT5, as well as with several Sm proteins, including SNRPB and SNRPD2 and, more weakly, SNRPD3 and SNRPE. 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. Interacts with CTDP1 and LSM11. Interacts with APEX1, AR and NKX3-1.8 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PRMT5O147446EBI-1237307,EBI-351098

    Protein-protein interaction databases

    BioGridi122532. 79 interactions.
    DIPiDIP-38172N.
    IntActiQ9BQA1. 43 interactions.
    MINTiMINT-1217135.
    STRINGi9606.ENSP00000235090.

    Structurei

    Secondary structure

    1
    342
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi29 – 368
    Beta strandi42 – 476
    Beta strandi50 – 523
    Beta strandi56 – 638
    Helixi64 – 663
    Helixi70 – 723
    Beta strandi74 – 818
    Beta strandi83 – 897
    Turni90 – 923
    Beta strandi93 – 986
    Beta strandi101 – 1088
    Beta strandi115 – 1228
    Beta strandi128 – 1336
    Beta strandi137 – 1448
    Beta strandi149 – 1535
    Turni154 – 1574
    Beta strandi158 – 1636
    Beta strandi170 – 1756
    Beta strandi182 – 1876
    Beta strandi192 – 1965
    Beta strandi199 – 2013
    Beta strandi203 – 2053
    Beta strandi215 – 2206
    Beta strandi227 – 2326
    Beta strandi235 – 2428
    Beta strandi249 – 2524
    Beta strandi258 – 2636
    Beta strandi265 – 2684
    Beta strandi271 – 2755
    Beta strandi280 – 2834
    Beta strandi289 – 2935
    Beta strandi300 – 3056
    Beta strandi307 – 3093
    Beta strandi312 – 3176
    Beta strandi322 – 3265

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4GQBX-ray2.06B2-342[»]
    ProteinModelPortaliQ9BQA1.
    SMRiQ9BQA1. Positions 21-329.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati22 – 7554WD 11 PublicationPROSITE-ProRule annotationAdd
    BLAST
    Repeati78 – 11639WD 21 PublicationPROSITE-ProRule annotationAdd
    BLAST
    Repeati123 – 16240WD 31 PublicationPROSITE-ProRule annotationAdd
    BLAST
    Repeati165 – 20541WD 41 PublicationPROSITE-ProRule annotationAdd
    BLAST
    Repeati209 – 25042WD 51 PublicationPROSITE-ProRule annotationAdd
    BLAST
    Repeati253 – 29341WD 61 PublicationPROSITE-ProRule annotationAdd
    BLAST
    Repeati295 – 33036WD 71 PublicationPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 7 WD repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, WD repeat

    Phylogenomic databases

    eggNOGiCOG2319.
    HOVERGENiHBG052458.
    InParanoidiQ9BQA1.
    KOiK13221.
    OMAiMRKETPP.
    OrthoDBiEOG7KSX99.
    PhylomeDBiQ9BQA1.
    TreeFamiTF325967.

    Family and domain databases

    Gene3Di2.130.10.10. 1 hit.
    InterProiIPR015943. WD40/YVTN_repeat-like_dom.
    IPR001680. WD40_repeat.
    IPR019775. WD40_repeat_CS.
    IPR017986. WD40_repeat_dom.
    [Graphical view]
    PfamiPF00400. WD40. 3 hits.
    [Graphical view]
    SMARTiSM00320. WD40. 6 hits.
    [Graphical view]
    SUPFAMiSSF50978. SSF50978. 1 hit.
    PROSITEiPS00678. WD_REPEATS_1. 1 hit.
    PS50082. WD_REPEATS_2. 2 hits.
    PS50294. WD_REPEATS_REGION. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9BQA1-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MRKETPPPLV PPAAREWNLP PNAPACMERQ LEAARYRSDG ALLLGASSLS    50
    GRCWAGSLWL FKDPCAAPNE GFCSAGVQTE AGVADLTWVG ERGILVASDS 100
    GAVELWELDE NETLIVSKFC KYEHDDIVST VSVLSSGTQA VSGSKDICIK 150
    VWDLAQQVVL SSYRAHAAQV TCVAASPHKD SVFLSCSEDN RILLWDTRCP 200
    KPASQIGCSA PGYLPTSLAW HPQQSEVFVF GDENGTVSLV DTKSTSCVLS 250
    SAVHSQCVTG LVFSPHSVPF LASLSEDCSL AVLDSSLSEL FRSQAHRDFV 300
    RDATWSPLNH SLLTTVGWDH QVVHHVVPTE PLPAPGPASV TE 342
    Length:342
    Mass (Da):36,724
    Last modified:June 1, 2001 - v1
    Checksum:i3D355AEC68491ECB
    GO
    Isoform 2 (identifier: Q9BQA1-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         101-164: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:278
    Mass (Da):29,651
    Checksum:i1A8FE679CD05CB24
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti244 – 2441S → N in BAD96909. (PubMed:12972618)Curated
    Sequence conflicti313 – 34230LTTVG…ASVTE → DLQVLLSRLDLRQKASPP in AAH09411. (PubMed:15489334)CuratedAdd
    BLAST

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti48 – 481S → I.
    Corresponds to variant rs7416672 [ dbSNP | Ensembl ].
    VAR_042903

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei101 – 16464Missing in isoform 2. 1 PublicationVSP_056166Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF478464 mRNA. Translation: AAL79917.1.
    AK022860 mRNA. Translation: BAG51128.1.
    AK298179 mRNA. Translation: BAG60450.1.
    AK223189 mRNA. Translation: BAD96909.1.
    AY225316 mRNA. Translation: AAP79114.1.
    AB073603 mRNA. Translation: BAD38641.1.
    AL390195 Genomic DNA. Translation: CAC36041.1.
    CH471122 Genomic DNA. Translation: EAW56493.1.
    BC001679 mRNA. Translation: AAH01679.1.
    BC006477 mRNA. Translation: AAH06477.1.
    BC009411 mRNA. Translation: AAH09411.1.
    BC011778 mRNA. Translation: AAH11778.1.
    BC016946 mRNA. Translation: AAH16946.1.
    AB074171 mRNA. Translation: BAE45736.1.
    CCDSiCCDS835.1.
    RefSeqiNP_077007.1. NM_024102.2.
    UniGeneiHs.204773.

    Genome annotation databases

    EnsembliENST00000235090; ENSP00000235090; ENSG00000116455.
    ENST00000411751; ENSP00000400321; ENSG00000116455.
    GeneIDi79084.
    KEGGihsa:79084.
    UCSCiuc001ebb.3. human.

    Polymorphism databases

    DMDMi32171507.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF478464 mRNA. Translation: AAL79917.1 .
    AK022860 mRNA. Translation: BAG51128.1 .
    AK298179 mRNA. Translation: BAG60450.1 .
    AK223189 mRNA. Translation: BAD96909.1 .
    AY225316 mRNA. Translation: AAP79114.1 .
    AB073603 mRNA. Translation: BAD38641.1 .
    AL390195 Genomic DNA. Translation: CAC36041.1 .
    CH471122 Genomic DNA. Translation: EAW56493.1 .
    BC001679 mRNA. Translation: AAH01679.1 .
    BC006477 mRNA. Translation: AAH06477.1 .
    BC009411 mRNA. Translation: AAH09411.1 .
    BC011778 mRNA. Translation: AAH11778.1 .
    BC016946 mRNA. Translation: AAH16946.1 .
    AB074171 mRNA. Translation: BAE45736.1 .
    CCDSi CCDS835.1.
    RefSeqi NP_077007.1. NM_024102.2.
    UniGenei Hs.204773.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4GQB X-ray 2.06 B 2-342 [» ]
    ProteinModelPortali Q9BQA1.
    SMRi Q9BQA1. Positions 21-329.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 122532. 79 interactions.
    DIPi DIP-38172N.
    IntActi Q9BQA1. 43 interactions.
    MINTi MINT-1217135.
    STRINGi 9606.ENSP00000235090.

    PTM databases

    PhosphoSitei Q9BQA1.

    Polymorphism databases

    DMDMi 32171507.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00012202.

    Proteomic databases

    MaxQBi Q9BQA1.
    PaxDbi Q9BQA1.
    PeptideAtlasi Q9BQA1.
    PRIDEi Q9BQA1.

    Protocols and materials databases

    DNASUi 79084.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000235090 ; ENSP00000235090 ; ENSG00000116455 .
    ENST00000411751 ; ENSP00000400321 ; ENSG00000116455 .
    GeneIDi 79084.
    KEGGi hsa:79084.
    UCSCi uc001ebb.3. human.

    Organism-specific databases

    CTDi 79084.
    GeneCardsi GC01M111983.
    HGNCi HGNC:29652. WDR77.
    HPAi HPA026437.
    HPA026448.
    HPA027271.
    MIMi 611734. gene.
    neXtProti NX_Q9BQA1.
    PharmGKBi PA142670581.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2319.
    HOVERGENi HBG052458.
    InParanoidi Q9BQA1.
    KOi K13221.
    OMAi MRKETPP.
    OrthoDBi EOG7KSX99.
    PhylomeDBi Q9BQA1.
    TreeFami TF325967.

    Enzyme and pathway databases

    Reactomei REACT_11066. snRNP Assembly.
    SignaLinki Q9BQA1.

    Miscellaneous databases

    GeneWikii WD_repeat-containing_protein_77.
    GenomeRNAii 79084.
    NextBioi 67897.
    PROi Q9BQA1.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9BQA1.
    Bgeei Q9BQA1.
    CleanExi HS_WDR77.
    Genevestigatori Q9BQA1.

    Family and domain databases

    Gene3Di 2.130.10.10. 1 hit.
    InterProi IPR015943. WD40/YVTN_repeat-like_dom.
    IPR001680. WD40_repeat.
    IPR019775. WD40_repeat_CS.
    IPR017986. WD40_repeat_dom.
    [Graphical view ]
    Pfami PF00400. WD40. 3 hits.
    [Graphical view ]
    SMARTi SM00320. WD40. 6 hits.
    [Graphical view ]
    SUPFAMi SSF50978. SSF50978. 1 hit.
    PROSITEi PS00678. WD_REPEATS_1. 1 hit.
    PS50082. WD_REPEATS_2. 2 hits.
    PS50294. WD_REPEATS_REGION. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A novel WD repeat protein component of the methylosome binds Sm proteins."
      Friesen W.J., Wyce A., Paushkin S., Abel L., Rappsilber J., Mann M., Dreyfuss G.
      J. Biol. Chem. 277:8243-8247(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: 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, IDENTIFICATION BY MASS SPECTROMETRY.
    2. "Purification and identification of a novel complex which is involved in androgen receptor-dependent transcription."
      Hosohata K., Li P., Hosohata Y., Qin J., Roeder R.G., Wang Z.
      Mol. Cell. Biol. 23:7019-7029(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 3-15, TISSUE SPECIFICITY, INTERACTION WITH AR AND NKX3-1.
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      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.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
      Tissue: Kidney proximal tubule.
    4. "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."
      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.
      Oncogene 23:5901-5911(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Hepatoblastoma.
    5. "The DNA sequence and biological annotation of human chromosome 1."
      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.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Colon, Lung and Skin.
    8. Bienvenut W.V., Zebisch A., Kolch W.
      Submitted (DEC-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 3-15; 36-52; 122-145; 151-179 AND 192-198, PHOSPHORYLATION AT THR-5, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Colon carcinoma.
    9. "Neuroblastoma oligo-capping cDNA project: toward the understanding of the genesis and biology of neuroblastoma."
      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.
      Cancer Lett. 197:63-68(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 184-342 (ISOFORM 1).
      Tissue: Neuroblastoma.
    10. "The FCP1 phosphatase interacts with RNA polymerase II and with MEP50 a component of the methylosome complex involved in the assembly of snRNP."
      Licciardo P., Amente S., Ruggiero L., Monti M., Pucci P., Lania L., Majello B.
      Nucleic Acids Res. 31:999-1005(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH CTDP1.
    11. "Toward an assembly line for U7 snRNPs: interactions of U7-specific Lsm proteins with PRMT5 and SMN complexes."
      Azzouz T.N., Pillai R.S., Dapp C., Chari A., Meister G., Kambach C., Fischer U., Schuemperli D.
      J. Biol. Chem. 280:34435-34440(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH LSM11.
    12. "Association of Polycomb group SUZ12 with WD-repeat protein MEP50 that binds to histone H2A selectively in vitro."
      Furuno K., Masatsugu T., Sonoda M., Sasazuki T., Yamamoto K.
      Biochem. Biophys. Res. Commun. 345:1051-1058(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH HIST2H2AC; PRMT5 AND SUZ12.
    13. "The expression and function of androgen receptor coactivator p44 and protein arginine methyltransferase 5 in the developing testis and testicular tumors."
      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.
      J. Urol. 177:1918-1922(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    14. "An assembly chaperone collaborates with the SMN complex to generate spliceosomal SnRNPs."
      Chari A., Golas M.M., Klingenhager M., Neuenkirchen N., Sander B., Englbrecht C., Sickmann A., Stark H., Fischer U.
      Cell 135:497-509(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE METHYLOSOME COMPLEX.
    15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. "APE1/Ref-1 interacts with NPM1 within nucleoli and plays a role in the rRNA quality control process."
      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.
      Mol. Cell. Biol. 29:1834-1854(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH APEX1, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
    17. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-5, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    18. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      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.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-5, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. Cited for: X-RAY CRYSTALLOGRAPHY (2.06 ANGSTROMS) OF 2-342 IN COMPLEX WITH PRMT5, FUNCTION, WD REPEATS, SUBUNIT.

    Entry informationi

    Entry nameiMEP50_HUMAN
    AccessioniPrimary (citable) accession number: Q9BQA1
    Secondary accession number(s): B3KMW6
    , B4DP38, Q3LID2, Q53FU2, Q6JZZ5, Q96GK4, Q9BWY3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 20, 2003
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 121 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3