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Protein

Probable lysine-specific demethylase 4A

Gene

Kdm4A

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Probable histone demethylase that specifically demethylates 'Lys-9' and 'Lys-36' residues of histone H3, thereby playing a central role in histone code. Demethylation of Lys residue generates formaldehyde and succinate (By similarity).By similarity

Cofactori

Fe2+By similarityNote: Binds 1 Fe2+ ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei139 – 1391Alpha-ketoglutarateBy similarity
Metal bindingi195 – 1951Iron; catalyticPROSITE-ProRule annotation
Metal bindingi197 – 1971Iron; catalyticPROSITE-ProRule annotation
Binding sitei205 – 2051Alpha-ketoglutarateBy similarity
Binding sitei213 – 2131Alpha-ketoglutarateBy similarity
Metal bindingi241 – 2411ZincBy similarity
Metal bindingi247 – 2471ZincBy similarity
Metal bindingi283 – 2831Iron; catalyticPROSITE-ProRule annotation
Metal bindingi313 – 3131ZincBy similarity
Metal bindingi315 – 3151ZincBy similarity

GO - Molecular functioni

  • histone demethylase activity (H3-K36 specific) Source: UniProtKB
  • histone demethylase activity (H3-K9 specific) Source: FlyBase
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • histone demethylation Source: UniProtKB
  • histone H3-K36 demethylation Source: FlyBase
  • histone H3-K9 demethylation Source: FlyBase
  • negative regulation of transcription, DNA-templated Source: UniProtKB
  • positive regulation of gene expression Source: FlyBase
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Dioxygenase, Oxidoreductase

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

Iron, Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi1.14.11.27. 1994.
1.14.11.B1. 1994.
ReactomeiR-DME-3214842. HDMs demethylate histones.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable lysine-specific demethylase 4A (EC:1.14.11.-)
Alternative name(s):
Probable JmjC domain-containing histone demethylation protein 3A
Gene namesi
Name:Kdm4A
ORF Names:CG15835
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0033233. Kdm4A.

Subcellular locationi

  • Nucleus PROSITE-ProRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 495495Probable lysine-specific demethylase 4APRO_0000234379Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei409 – 4091Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ9V333.
PRIDEiQ9V333.

PTM databases

iPTMnetiQ9V333.

Expressioni

Gene expression databases

BgeeiQ9V333.
GenevisibleiQ9V333. DM.

Interactioni

Protein-protein interaction databases

BioGridi61608. 3 interactions.
IntActiQ9V333. 1 interaction.
MINTiMINT-800097.
STRINGi7227.FBpp0087961.

Structurei

3D structure databases

ProteinModelPortaliQ9V333.
SMRiQ9V333. Positions 13-406.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini18 – 6043JmjNPROSITE-ProRule annotationAdd
BLAST
Domaini149 – 315167JmjCPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the JHDM3 histone demethylase family.Curated
Contains 1 JmjC domain.PROSITE-ProRule annotation
Contains 1 JmjN domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0958. Eukaryota.
ENOG410XP0T. LUCA.
GeneTreeiENSGT00530000063342.
InParanoidiQ9V333.
KOiK06709.
OMAiTENYQEC.
OrthoDBiEOG7TQV03.
PhylomeDBiQ9V333.

Family and domain databases

InterProiIPR003347. JmjC_dom.
IPR003349. JmjN.
[Graphical view]
PfamiPF02373. JmjC. 1 hit.
PF02375. JmjN. 1 hit.
[Graphical view]
SMARTiSM00558. JmjC. 1 hit.
SM00545. JmjN. 1 hit.
[Graphical view]
PROSITEiPS51184. JMJC. 1 hit.
PS51183. JMJN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9V333-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTRSSFADE EQNKVPRIMT FRPSYEEFQN FSAYIEYIES RGAHLAGLAK
60 70 80 90 100
IQPPAEWVPR KSGYDIDNIN MTIPAPICQV VTGAHGVYQQ INIQQRRQMT
110 120 130 140 150
LRQFMEKANS ELHQTPRHFD YDDLERKYWK NITYISPLYA ADVKGSLSDE
160 170 180 190 200
DLDVWNIGRL DTILNLVNTD YNIIIDGVNT AYLYFGMWKS SFAWHTEDMD
210 220 230 240 250
LYSINYLHFG APKTWYAIPP AYGRRLEKLA NETFSENYQE CNAYLRHKMT
260 270 280 290 300
MISPKVLRQH NIPYNKITQE AGEIMITFPF GYHAGFNHGF NGAESTNFAS
310 320 330 340 350
KRWIEYGKRA SICRCRSDMV KISMETFVRR FQPERYDNWL KGQDMGCHPE
360 370 380 390 400
EPGKICAAAP PTLNEYEKQE NLRAAKSEEE SPQKRGCSLA GNGCERNAES
410 420 430 440 450
AEDVDDKASV SSYSSCRQLQ PVVKLRKLPT IASVPEPSSA PKRYDFNTEA
460 470 480 490
VVRVKRLWNE LPCPDRGANL LTNGVVKNTK RMRFQTKVLT LDDED
Length:495
Mass (Da):56,990
Last modified:May 1, 2000 - v1
Checksum:i75EF4AC188C834A9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE013599 Genomic DNA. Translation: AAF59172.1.
AY058636 mRNA. Translation: AAL13865.1.
RefSeqiNP_610331.1. NM_136487.4.
UniGeneiDm.4139.

Genome annotation databases

EnsemblMetazoaiFBtr0088886; FBpp0087961; FBgn0033233.
GeneIDi35744.
KEGGidme:Dmel_CG15835.
UCSCiCG15835-RA. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE013599 Genomic DNA. Translation: AAF59172.1.
AY058636 mRNA. Translation: AAL13865.1.
RefSeqiNP_610331.1. NM_136487.4.
UniGeneiDm.4139.

3D structure databases

ProteinModelPortaliQ9V333.
SMRiQ9V333. Positions 13-406.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi61608. 3 interactions.
IntActiQ9V333. 1 interaction.
MINTiMINT-800097.
STRINGi7227.FBpp0087961.

PTM databases

iPTMnetiQ9V333.

Proteomic databases

PaxDbiQ9V333.
PRIDEiQ9V333.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0088886; FBpp0087961; FBgn0033233.
GeneIDi35744.
KEGGidme:Dmel_CG15835.
UCSCiCG15835-RA. d. melanogaster.

Organism-specific databases

CTDi9682.
FlyBaseiFBgn0033233. Kdm4A.

Phylogenomic databases

eggNOGiKOG0958. Eukaryota.
ENOG410XP0T. LUCA.
GeneTreeiENSGT00530000063342.
InParanoidiQ9V333.
KOiK06709.
OMAiTENYQEC.
OrthoDBiEOG7TQV03.
PhylomeDBiQ9V333.

Enzyme and pathway databases

BRENDAi1.14.11.27. 1994.
1.14.11.B1. 1994.
ReactomeiR-DME-3214842. HDMs demethylate histones.

Miscellaneous databases

ChiTaRSiKdm4A. fly.
GenomeRNAii35744.
PROiQ9V333.

Gene expression databases

BgeeiQ9V333.
GenevisibleiQ9V333. DM.

Family and domain databases

InterProiIPR003347. JmjC_dom.
IPR003349. JmjN.
[Graphical view]
PfamiPF02373. JmjC. 1 hit.
PF02375. JmjN. 1 hit.
[Graphical view]
SMARTiSM00558. JmjC. 1 hit.
SM00545. JmjN. 1 hit.
[Graphical view]
PROSITEiPS51184. JMJC. 1 hit.
PS51183. JMJN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  2. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Embryo.
  4. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-409, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryo.

Entry informationi

Entry nameiKDM4A_DROME
AccessioniPrimary (citable) accession number: Q9V333
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 16, 2006
Last sequence update: May 1, 2000
Last modified: July 6, 2016
This is version 108 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.