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Q99J09 (MEP50_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Methylosome protein 50

Short name=MEP-50
Alternative name(s):
WD repeat-containing protein 77
Gene names
Name:Wdr77
Synonyms:Mep50
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length342 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 By similarity. 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. Ref.4

Subunit structure

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 By similarity. Ref.3

Subcellular location

Nucleus By similarity. Cytoplasm By similarity.

Sequence similarities

Contains 7 WD repeats.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 342342Methylosome protein 50
PRO_0000051075

Regions

Repeat22 – 7554WD 1
Repeat78 – 11639WD 2
Repeat123 – 16240WD 3
Repeat165 – 20541WD 4
Repeat209 – 25042WD 5
Repeat253 – 29341WD 6
Repeat295 – 33036WD 7

Amino acid modifications

Modified residue51Phosphothreonine By similarity

Experimental info

Sequence conflict267 – 28519SVPLL…AVLDS → RCCVSPGTWKGWVGTVVKE in AAH05755. Ref.2
Sequence conflict286 – 34257Missing in AAH05755. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q99J09 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: E9C52BC4D6E5AC36

FASTA34236,943
        10         20         30         40         50         60 
MRKDTPPPLV PPAAREWNLP PNAPACMERQ LEAARYRSDG SLLLGVSSLS GRCWVGSLWF 

        70         80         90        100        110        120 
FKDPSAAPNE GFCSAGVQTE AGVADLTWVG DKGILVASDS GAVELWELDE NETLIVSKFC 

       130        140        150        160        170        180 
KYEHDDIVST VTVLSSGTQA VSGSKDCCIK IWDLAQQVSL NSYRAHAGQV TCVAASPHKD 

       190        200        210        220        230        240 
SVFLSCSEDS RILLWDTRCP KPASQMACNA SGYLPTALAW HPQQSEVFVF GDENGSVSLV 

       250        260        270        280        290        300 
DTKNASCTLS SAVHSQGVTR LVFSPHSVPL LTSLSEDCSL AVLDSSLSEV FRSRAHRDFV 

       310        320        330        340 
RDATWSPLNH SLLTTVGWDH QVIHHVVPLE PLPNPGPDSV VE 

« Hide

References

« Hide 'large scale' references
[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Amnion, Embryo, Head, Liver and Mesonephros.
[2]"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].
Tissue: Mammary tumor.
[3]"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: INTERACTION WITH SUZ12.
[4]"Proteomic analysis of murine Piwi proteins reveals a role for arginine methylation in specifying interaction with Tudor family members."
Vagin V.V., Wohlschlegel J., Qu J., Jonsson Z., Huang X., Chuma S., Girard A., Sachidanandam R., Hannon G.J., Aravin A.A.
Genes Dev. 23:1749-1762(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN METHYLATION OF PIWI PROTEINS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK012014 mRNA. Translation: BAB27975.1.
AK032897 mRNA. Translation: BAC28076.1.
AK048488 mRNA. Translation: BAC33350.1.
AK050391 mRNA. Translation: BAC34232.1.
AK163839 mRNA. Translation: BAE37512.1.
AK169128 mRNA. Translation: BAE40907.1.
BC005755 mRNA. Translation: AAH05755.1.
CCDSCCDS17715.1.
RefSeqNP_081708.1. NM_027432.3.
UniGeneMm.5110.

3D structure databases

ProteinModelPortalQ99J09.
SMRQ99J09. Positions 21-328.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ99J09. 4 interactions.
MINTMINT-4101776.

PTM databases

PhosphoSiteQ99J09.

Proteomic databases

MaxQBQ99J09.
PaxDbQ99J09.
PRIDEQ99J09.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000010278; ENSMUSP00000010278; ENSMUSG00000000561.
GeneID70465.
KEGGmmu:70465.
UCSCuc008qvo.1. mouse.

Organism-specific databases

CTD79084.
MGIMGI:1917715. Wdr77.

Phylogenomic databases

eggNOGCOG2319.
GeneTreeENSGT00390000010711.
HOGENOMHOG000035094.
HOVERGENHBG052458.
InParanoidQ99J09.
KOK13221.
OMAMRKETPP.
OrthoDBEOG7KSX99.
PhylomeDBQ99J09.
TreeFamTF325967.

Gene expression databases

ArrayExpressQ99J09.
BgeeQ99J09.
CleanExMM_WDR77.
GenevestigatorQ99J09.

Family and domain databases

Gene3D2.130.10.10. 1 hit.
InterProIPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamPF00400. WD40. 2 hits.
[Graphical view]
SMARTSM00320. WD40. 6 hits.
[Graphical view]
SUPFAMSSF50978. SSF50978. 1 hit.
PROSITEPS00678. WD_REPEATS_1. 1 hit.
PS50082. WD_REPEATS_2. 2 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSWDR77. mouse.
NextBio331685.
PROQ99J09.
SOURCESearch...

Entry information

Entry nameMEP50_MOUSE
AccessionPrimary (citable) accession number: Q99J09
Secondary accession number(s): Q3TFJ1, Q8BSH8, Q9CZY5
Entry history
Integrated into UniProtKB/Swiss-Prot: June 20, 2003
Last sequence update: June 1, 2001
Last modified: July 9, 2014
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot