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Q7K4H4 (NO66_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 48. 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:
Lysine-specific demethylase NO66

EC=1.14.11.27
Alternative name(s):
Nucleolar protein 66
Gene names
ORF Names:CG2982
OrganismDrosophila melanogaster (Fruit fly)
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length653 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Histone demethylase that specifically demethylates 'Lys-4' (H3K4me) and 'Lys-36' (H3K36me) of histone H3, thereby playing a central role in histone code By similarity.

Catalytic activity

Protein N6,N(6)-dimethyl-L-lysine + 2-oxoglutarate + O2 = protein N(6)-methyl-L-lysine + succinate + formaldehyde + CO2.

Protein N(6)-methyl-L-lysine + 2-oxoglutarate + O2 = protein L-lysine + succinate + formaldehyde + CO2.

Cofactor

Binds 1 Fe2+ ion per subunit By similarity.

Subcellular location

Nucleus By similarity.

Sequence similarities

Belongs to the MINA53/NO66 family. NO66 subfamily.

Contains 1 JmjC domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 653653Lysine-specific demethylase NO66
PRO_0000348221

Regions

Domain300 – 450151JmjC

Sites

Metal binding3511Iron; catalytic By similarity
Metal binding3531Iron; catalytic By similarity
Metal binding4161Iron; catalytic By similarity

Amino acid modifications

Modified residue441Phosphoserine Ref.5
Modified residue1311Phosphoserine Ref.5
Modified residue1371Phosphothreonine Ref.4
Modified residue1381Phosphoserine Ref.4 Ref.5

Sequences

Sequence LengthMass (Da)Tools
Q7K4H4 [UniParc].

Last modified October 3, 2006. Version 1.
Checksum: 87A4C50A35578313

FASTA65373,098
        10         20         30         40         50         60 
MKKATTSAAA KSQGNSKMQK NANNGTAKDK KKPNLDKESN DSNSVSDMLA VTKDQEVHAF 

        70         80         90        100        110        120 
FSKLFDDDAG PSTSKKTQSG SAAAAKTADR KRRLQAEADA NNNDTGKAGK LTKESEATQG 

       130        140        150        160        170        180 
ARATKRKQAR SLGLERTSPI QVNGAALACP LVRKSLPPGE ANSCPQPPKK DPAAVNSLVK 

       190        200        210        220        230        240 
IIKAEPTEEG NNNNDEKETE TIETHKADSV EEGRRVLQWI LFPVQTKVFF KDFWEHTACL 

       250        260        270        280        290        300 
VQRSNPKYFQ SMISFKMLDE ILIRHHLDFT VNVDVTTYKN GKRETLNPEG RALPPAVWGF 

       310        320        330        340        350        360 
YSDGCSIRLL NPSTYLIRLR QVCTVLQEFF HCKVGANLYL TPPNSQGFAP HYDDIEAFVI 

       370        380        390        400        410        420 
QVEGRKRWLL YEPPKKADQL ARISSGNYDQ EQLGKPIIDE VLSAGDVLYF PRGAVHQAIT 

       430        440        450        460        470        480 
EEQQHSLHIT LSVYQQQAYA NLLETLMPMV LKKAVDRSVA LRRGLPLHTF QVLGNAYKGN 

       490        500        510        520        530        540 
DCGSRKQLVE NVQKLVTNYL MPSEDDIDEA VDQMAKKFQH EALPPIVLPS EEVRTVHGAR 

       550        560        570        580        590        600 
SDADEQGNCV CDYKFNKKTS VRLLRANILR LVTESDGSVR IYHHVDNGLD YCKYEPYFME 

       610        620        630        640        650 
ILPEEAKAVE LLISAYPFYL TIDQLPLESS ARKIEVATAL WEHGLLMTEK PFK 

« Hide

References

« Hide 'large scale' references
[1]"The genome sequence of Drosophila melanogaster."
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. expand/collapse author list , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
Science 287:2185-2195(2000) [PubMed: 10731132] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[2]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: Berkeley.
[3]"A Drosophila full-length cDNA resource."
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed: 12537569] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.
Tissue: Embryo.
[4]"An integrated chemical, mass spectrometric and computational strategy for (quantitative) phosphoproteomics: application to Drosophila melanogaster Kc167 cells."
Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A., Eng J.K., Aebersold R., Tao W.A.
Mol. Biosyst. 3:275-286(2007) [PubMed: 17372656] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-137 AND SER-138, MASS SPECTROMETRY.
[5]"Phosphoproteome analysis of Drosophila melanogaster embryos."
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
J. Proteome Res. 7:1675-1682(2008) [PubMed: 18327897] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44; SER-131 AND SER-138, MASS SPECTROMETRY.
Tissue: Embryo.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE014298 Genomic DNA. Translation: AAN09120.1.
AY051917 mRNA. Translation: AAK93341.1.
RefSeqNP_572160.1. NM_131932.3.
UniGeneDm.76.

3D structure databases

ProteinModelPortalQ7K4H4.
SMRQ7K4H4. Positions 213-648.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ7K4H4.

Proteomic databases

PRIDEQ7K4H4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0070648; FBpp0070616; FBgn0029704.
GeneID31374.
KEGGdme:Dmel_CG2982.
UCSCCG2982-RA. d. melanogaster.

Organism-specific databases

FlyBaseFBgn0029704. CG2982.

Phylogenomic databases

eggNOGinNOG04469.
GeneTreeEMGT00050000000838.
InParanoidQ7K4H4.
OMARGFIHQA.
OrthoDBEOG4ZW3SP.
PhylomeDBQ7K4H4.

Gene expression databases

ArrayExpressQ7K4H4.
BgeeQ7K4H4.

Family and domain databases

InterProIPR013109. Cupin_4.
IPR022777. Cupin_JmjC.
IPR014710. RmlC-like_jellyroll.
IPR003347. TF_JmjC_AAH.
[Graphical view]
Gene3DG3DSA:2.60.120.10. RmlC-like_jellyroll. 1 hit.
PANTHERPTHR13096. Cupin_4. 1 hit.
PfamPF08007. Cupin_4. 1 hit.
[Graphical view]
SMARTSM00558. JmjC. 1 hit.
[Graphical view]
PROSITEPS51184. JMJC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio773313.

Entry information

Entry nameNO66_DROME
AccessionPrimary (citable) accession number: Q7K4H4
Entry history
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: October 3, 2006
Last modified: January 25, 2012
This is version 48 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase

SIMILARITY comments

Index of protein domains and families