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Q9BQA1 (MEP50_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 119. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Methylosome protein 50

Short name=MEP-50
Alternative name(s):
Androgen receptor cofactor p44
WD repeat-containing protein 77
p44/Mep50
Gene names
Name:WDR77
Synonyms:MEP50, WD45
ORF Names:HKMT1069, Nbla10071
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

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. 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.1 Ref.20

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. Ref.1 Ref.2 Ref.10 Ref.11 Ref.12 Ref.14 Ref.16 Ref.20

Subcellular location

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. Ref.10 Ref.12 Ref.13 Ref.16

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. Ref.2 Ref.13

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. Ref.13

Sequence similarities

Contains 7 WD repeats.

Ontologies

Keywords
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityPolymorphism
   DomainRepeat
WD repeat
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processRNA metabolic process

Traceable author statement. Source: Reactome

gene expression

Traceable author statement. Source: Reactome

ncRNA metabolic process

Traceable author statement. Source: Reactome

negative regulation of epithelial cell proliferation involved in prostate gland development

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

secretory columnal luminar epithelial cell differentiation involved in prostate glandular acinus development

Inferred from electronic annotation. Source: Ensembl

spliceosomal snRNP assembly

Traceable author statement. Source: Reactome

   Cellular_componentGolgi apparatus

Inferred from direct assay. Source: HPA

cytoplasm

Inferred from direct assay Ref.16. Source: UniProtKB

cytosol

Inferred from direct assay Ref.14. Source: UniProtKB

methylosome

Inferred from direct assay Ref.14. Source: UniProtKB

nucleus

Inferred from direct assay. Source: HPA

   Molecular_functionligand-dependent nuclear receptor transcription coactivator activity

Inferred from genetic interaction Ref.2. Source: MGI

protein binding

Inferred from physical interaction Ref.11Ref.16. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PRMT5O147446EBI-1237307,EBI-351098

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 342342Methylosome protein 50
PRO_0000051074

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 Ref.8 Ref.17 Ref.18

Natural variations

Natural variant481S → I.
Corresponds to variant rs7416672 [ dbSNP | Ensembl ].
VAR_042903

Experimental info

Sequence conflict2441S → N in BAD96909. Ref.2
Sequence conflict313 – 34230LTTVG…ASVTE → DLQVLLSRLDLRQKASPP in AAH09411. Ref.7

Secondary structure

.................................................................. 342
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9BQA1 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 3D355AEC68491ECB

FASTA34236,724
        10         20         30         40         50         60 
MRKETPPPLV PPAAREWNLP PNAPACMERQ LEAARYRSDG ALLLGASSLS GRCWAGSLWL 

        70         80         90        100        110        120 
FKDPCAAPNE GFCSAGVQTE AGVADLTWVG ERGILVASDS GAVELWELDE NETLIVSKFC 

       130        140        150        160        170        180 
KYEHDDIVST VSVLSSGTQA VSGSKDICIK VWDLAQQVVL SSYRAHAAQV TCVAASPHKD 

       190        200        210        220        230        240 
SVFLSCSEDN RILLWDTRCP KPASQIGCSA PGYLPTSLAW HPQQSEVFVF GDENGTVSLV 

       250        260        270        280        290        300 
DTKSTSCVLS SAVHSQCVTG LVFSPHSVPF LASLSEDCSL AVLDSSLSEL FRSQAHRDFV 

       310        320        330        340 
RDATWSPLNH SLLTTVGWDH QVVHHVVPTE PLPAPGPASV TE 

« Hide

References

« Hide 'large scale' references
[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], 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], 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. expand/collapse author list , 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].
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].
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. expand/collapse author list , 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]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. expand/collapse author list , 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
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].
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.
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"Crystal structure of the human PRMT5:MEP50 complex."
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.
Proc. Natl. Acad. Sci. U.S.A. 109:17960-17965(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.06 ANGSTROMS) OF 2-342 IN COMPLEX WITH PRMT5, FUNCTION, WD REPEATS, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF478464 mRNA. Translation: AAL79917.1.
AK022860 mRNA. Translation: BAG51128.1.
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.
CCDSCCDS835.1.
RefSeqNP_077007.1. NM_024102.2.
UniGeneHs.204773.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4GQBX-ray2.06B2-342[»]
ProteinModelPortalQ9BQA1.
SMRQ9BQA1. Positions 21-329.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid122532. 80 interactions.
DIPDIP-38172N.
IntActQ9BQA1. 43 interactions.
MINTMINT-1217135.
STRING9606.ENSP00000235090.

PTM databases

PhosphoSiteQ9BQA1.

Polymorphism databases

DMDM32171507.

2D gel databases

REPRODUCTION-2DPAGEIPI00012202.

Proteomic databases

MaxQBQ9BQA1.
PaxDbQ9BQA1.
PeptideAtlasQ9BQA1.
PRIDEQ9BQA1.

Protocols and materials databases

DNASU79084.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000235090; ENSP00000235090; ENSG00000116455.
GeneID79084.
KEGGhsa:79084.
UCSCuc001ebb.3. human.

Organism-specific databases

CTD79084.
GeneCardsGC01M111983.
HGNCHGNC:29652. WDR77.
HPAHPA026437.
HPA026448.
HPA027271.
MIM611734. gene.
neXtProtNX_Q9BQA1.
PharmGKBPA142670581.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2319.
HOVERGENHBG052458.
InParanoidQ9BQA1.
KOK13221.
OMAMRKETPP.
OrthoDBEOG7KSX99.
PhylomeDBQ9BQA1.
TreeFamTF325967.

Enzyme and pathway databases

ReactomeREACT_21257. Metabolism of RNA.
REACT_71. Gene Expression.
SignaLinkQ9BQA1.

Gene expression databases

ArrayExpressQ9BQA1.
BgeeQ9BQA1.
CleanExHS_WDR77.
GenevestigatorQ9BQA1.

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. 3 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

GeneWikiWD_repeat-containing_protein_77.
GenomeRNAi79084.
NextBio67897.
PROQ9BQA1.
SOURCESearch...

Entry information

Entry nameMEP50_HUMAN
AccessionPrimary (citable) accession number: Q9BQA1
Secondary accession number(s): B3KMW6 expand/collapse secondary AC list , Q3LID2, Q53FU2, Q6JZZ5, Q96GK4, Q9BWY3
Entry history
Integrated into UniProtKB/Swiss-Prot: June 20, 2003
Last sequence update: June 1, 2001
Last modified: July 9, 2014
This is version 119 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM