Reviewed, UniProtKB/Swiss-Prot Q9VHH9 (JHD1_DROME)

Names and origin

Protein names

Recommended name:
    JmjC domain-containing histone demethylation protein 1
    EC=1.14.11.27
Alternative name(s):
    [Histone-H3]-lysine-36 demethylase 1

Gene names

Name:	Jhd1
ORF Names:	CG11033

Organism

Drosophila melanogaster (Fruit fly) [Complete proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	1345 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Histone demethylase that specifically demethylates 'Lys-36' 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.
Domain	The JmjC domain mediates the demethylation activity By similarity.
Sequence similarities	Belongs to the JHDM1 histone demethylase family. Contains 1 CXXC-type zinc finger. Contains 1 F-box domain. Contains 1 JmjC domain.
Sequence caution	The sequence AAF54335.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Domain	Zinc-finger
Ligand	Iron Metal-binding Zinc
Molecular function	Chromatin regulator Dioxygenase Oxidoreductase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	chromatin modification Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW regulation of transcription Inferred from electronic annotation. Source: UniProtKB-KW transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	DNA binding Inferred from electronic annotation. Source: InterPro histone demethylase activity (H3-K36 specific) Inferred from electronic annotation. Source: EC iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: IntAct zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
olf413	Q6NP60	1	EBI-158813,EBI-120478

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1345	1345	JmjC domain-containing histone demethylation protein 1		PRO_0000226790
Regions
	Domain	180 – 348	169	JmjC
	Domain	1059 – 1105	47	F-box
	Zinc finger	671 – 717	47	CXXC-type
	Compositional bias	592 – 669	78	Gly-rich
Sites
	Metal binding	244	1	Iron; catalytic By similarity
	Metal binding	246	1	Iron; catalytic By similarity
	Metal binding	316	1	Iron; catalytic By similarity
	Binding site	241	1	Substrate By similarity
	Binding site	261	1	Substrate By similarity
Amino acid modifications
	Modified residue	53	1	Phosphotyrosine Ref.4
	Modified residue	58	1	Phosphoserine Ref.4
	Modified residue	79	1	Phosphoserine Ref.4
Experimental info
	Sequence conflict	469	1	Q → L in AAQ22410. Ref.3
	Sequence conflict	950	1	N → T in AAQ22410. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q9VHH9-1 [UniParc]. Last modified March 7, 2006. Version 2. Checksum: 3157AD3B9E1AE619	FASTA	1,345	146,178
	10 20 30 40 50 60 MSTAVETGSS PAKSNSNNSS SGGNNNNGNG NLSPNAKGVQ RRQLRERKQR KLYLEEWSLG 70 80 90 100 110 120 DEDGEGTRGF SVAEKLESSK FAQAGMVREM RGCDLTVAFL QQHGFNIPLL FRDKAGLGLR 130 140 150 160 170 180 MPDPQEFTVN DVRLCVGSRR LLDVMDVNTQ KNLQMTMKEW QQYYDSPQKD RLLNVISLEF 190 200 210 220 230 240 SHTRLDRFVQ SPEIVRQIDW VDVVWPKQLK DAQREGTNLL GGMMYPKVQK YCLMSVKNCY 250 260 270 280 290 300 TDFHIDFGGT SVWYHILRGS KVFWLIPPTD RNLQLYEKWV LSGKQADIFF GDTVEKCARV 310 320 330 340 350 360 YLTAGNTFFI PTGWIHAVYT PTQSLVFGGN FLHSFGIVKQ LKTASVEDST KVPQKFRYPF 370 380 390 400 410 420 FTEMLWYVLA RYVHTLLGHS HLEGEASLSE DEMAARPHTH LTHHELFGLK EIVMYLYDLP 430 440 450 460 470 480 PQKKNVPSLV LDPVALIKDV RSLVERHCKD QQDLAITGVS VLKSPPGSQP PFLLYDRTRV 490 500 510 520 530 540 KQEIKQEIAR KNAEVIREQQ QLEAGRAREA ESDTSQSTGV GSVIGMGAGV EYSNGVMKKE 550 560 570 580 590 600 QLENGSGVTV GGHGSQPEAT FALPTDTLKY RPPKKMHLAT ALVAAAASSS SGGGGPVAGV 610 620 630 640 650 660 GGSAVVGSSH SPTGGGVGPV TGAGGAISVI ATSSSYIEGG QVGGILNMDN CHSPEGGGAK 670 680 690 700 710 720 LSPNLTGTGQ PRRRRTRCKN CAACQRSDCG TCPFCMDMVK FGGPGRAKQT CMMRQCLSPM 730 740 750 760 770 780 LPVTAQCVYC HLDGWRQTPV SPQTKQLASA DGPSALMECS VCYEIAHPDC ALSQLDGTED 790 800 810 820 830 840 AADAKGIVNE DLPNSWECPS CCRSGKNYDY KPRHFRARQK SSEVRRVSVS HGQGGAEGHA 850 860 870 880 890 900 DGNTLLPPPV GQYNDFVFTS ESEMESGTVS GHMTHWKHGM KRHHQLEVKT ERNNSCDTPS 910 920 930 940 950 960 PGISPNAIGG DSKVGKRRKS DDGTSVSSSM HESNDAPCGS SAEGAGGAGN ANVSTNQWSG 970 980 990 1000 1010 1020 SGGGGGSRKK NSIRSQLAQQ MLNSSTRVLK KPQYVVRPAS GTGSSSSSGN GGSASATNGI 1030 1040 1050 1060 1070 1080 SNGSNQSGAN SCGAGNGERG TNNGGLSGSN GLGNQHYSSS QNLALDPTVL KIIFRYLPQD 1090 1100 1110 1120 1130 1140 TLVTCCSVCK VWSNAAVDPD LWKKMNCSEH KMSASLLTAI VRRQPEHLIL DWTQIAKRQL 1150 1160 1170 1180 1190 1200 AWLVARLPAL KNLSLQNCPI QAVLALHTCL CPPLQTLDLS FVRGLNDAAI RDILSPPKDS 1210 1220 1230 1240 1250 1260 RPGLSDSKTR LRDLKVMKLA GTDISDVAVR YITQSLPYLR HLDLSSCQRI TDAGVAQIGT 1270 1280 1290 1300 1310 1320 STTATARLTE LNLSACRLVS ENALEHLAKC EGLIWLDLRH VPQVSTQSVI RFASNSKHDL 1330 1340 CVRDIKLVER RRRNSTTANR SWHHD

References

	« Hide 'large scale' referencesShow '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. , 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. , 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.
[3]	Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A. , Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E. Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases 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: 18327897] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-53; SER-58 AND SER-79, MASS SPECTROMETRY. Tissue: Embryo.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE014297 Genomic DNA. Translation: AAF54335.1. Sequence problems. BT009941 mRNA. Translation: AAQ22410.1.
RefSeq	NP_649864.2.
3D structure databases
SMR	Q9VHH9. Positions 68-465, 667-718, 1065-1315.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9VHH9. 1 interaction.
Genome annotation databases
Ensembl	FBtr0081970; FBpp0081450; FBgn0037659; Drosophila melanogaster. [Genome view]
GeneID	41090.
KEGG	dme:Dmel_CG11033.
UCSC	CG11033-RA. d. melanogaster.
Organism-specific databases
FlyBase	FBgn0037659. CG11033.
Phylogenomic databases
eggNOG	inNOG07003.
InParanoid	Q9VHH9.
OrthoDB	EOG9WDDJN.
PhylomeDB	Q9VHH9.
Enzyme and pathway databases
BRENDA	1.14.11.27. 48.
Gene expression databases
GermOnline	CG11033. Drosophila melanogaster.
Family and domain databases
InterPro	IPR001810. F-box. IPR006553. Leu-rich_rpt_Cys-con_subtyp. IPR013129. TF_JmjC. IPR003347. TF_JmjC_AAH. IPR002857. Znf_CXXC. [Graphical view]
Pfam	PF00646. F-box. 1 hit. PF02373. JmjC. 1 hit. PF02008. zf-CXXC. 1 hit. [Graphical view]
SMART	SM00256. FBOX. 1 hit. SM00558. JmjC. 1 hit. SM00367. LRR_CC. 1 hit. [Graphical view]
PROSITE	PS50181. FBOX. False negative. PS51184. JMJC. 1 hit. PS51058. ZF_CXXC. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	822112.

Entry information

Entry name

JHD1_DROME

Accession

Primary (citable) accession number: Q9VHH9
Secondary accession number(s): Q7YU79

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 7, 2006
Last sequence update:	March 7, 2006
Last modified:	February 9, 2010
This is version 70 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Drosophila annotation project