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Q9BQA1

- MEP50_HUMAN

UniProt

Q9BQA1 - MEP50_HUMAN

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Protein

Methylosome protein 50

Gene

WDR77

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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

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
Complete GO annotation...

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
Complete GO annotation...

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

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. 80 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.
GeneTreeiENSGT00390000010711.
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. 4 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

        10         20         30         40         50
MRKETPPPLV PPAAREWNLP PNAPACMERQ LEAARYRSDG ALLLGASSLS
60 70 80 90 100
GRCWAGSLWL FKDPCAAPNE GFCSAGVQTE AGVADLTWVG ERGILVASDS
110 120 130 140 150
GAVELWELDE NETLIVSKFC KYEHDDIVST VSVLSSGTQA VSGSKDICIK
160 170 180 190 200
VWDLAQQVVL SSYRAHAAQV TCVAASPHKD SVFLSCSEDN RILLWDTRCP
210 220 230 240 250
KPASQIGCSA PGYLPTSLAW HPQQSEVFVF GDENGTVSLV DTKSTSCVLS
260 270 280 290 300
SAVHSQCVTG LVFSPHSVPF LASLSEDCSL AVLDSSLSEL FRSQAHRDFV
310 320 330 340
RDATWSPLNH SLLTTVGWDH QVVHHVVPTE PLPAPGPASV TE
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. [Q9BQA1-1]
RefSeqiNP_077007.1. NM_024102.2.
UniGeneiHs.204773.

Genome annotation databases

EnsembliENST00000235090; ENSP00000235090; ENSG00000116455. [Q9BQA1-1]
GeneIDi79084.
KEGGihsa:79084.
UCSCiuc001ebb.3. human. [Q9BQA1-1]

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. [Q9BQA1-1 ]
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. 80 interactions.
DIPi DIP-38172N.
IntActi Q9BQA1. 43 interactions.
MINTi MINT-1217135.
STRINGi 9606.ENSP00000235090.

Chemistry

ChEMBLi CHEMBL3137261.

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 . [Q9BQA1-1 ]
GeneIDi 79084.
KEGGi hsa:79084.
UCSCi uc001ebb.3. human. [Q9BQA1-1 ]

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.
GeneTreei ENSGT00390000010711.
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 35473777.
PROi Q9BQA1.
SOURCEi Search...

Gene expression databases

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. 4 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

« Hide 'large scale' publications
  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 29, 2014
This is version 122 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