Reviewed, UniProtKB/Swiss-Prot O94603 (JHD1_SCHPO)

Names and origin

Protein names

Recommended name:
    Putative JmjC domain-containing histone demethylation protein 1
    EC=1.14.11.27
Alternative name(s):
    [Histone-H3]-lysine-36 demethylase 1
    Heterochromatin-destabilizing protein epe1

Gene names

Name:	jhd1
Synonyms:	epe1
ORF Names:	SPCC622.16c

Organism

Schizosaccharomyces pombe (Fission yeast) [Complete proteome]

Taxonomic identifier

4896 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	948 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	May have histone demethylase that specifically demethylates 'Lys-36' of histone H3, thereby playing a central role in histone code By similarity. Represses transcriptional silencing by negatively affecting heterochromatin stability.
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. Ref.2
Domain	The JmjC domain mediates the demethylation activity By similarity.
Sequence similarities	Belongs to the JHDM1 histone demethylase family. Contains 1 JmjC domain.
Caution	In contrast to other JHDM1 histone demethylases, it lacks the iron catalytic His in position 370 which is replaced by a Tyr residue and has no histone demethylase activity in vitro. It therefore may not be functional in vivo.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Ligand	Iron Metal-binding
Molecular function	Chromatin regulator Dioxygenase Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	chromatin remodeling Ref.2 Inferred from mutant phenotype. Source: GeneDB_SPombe chromatin silencing at centromere Ref.2 Inferred from mutant phenotype. Source: GeneDB_SPombe chromatin silencing at silent mating-type cassette Ref.2 Inferred from mutant phenotype. Source: GeneDB_SPombe chromosome segregation Inferred from mutant phenotype. Source: GeneDB_SPombe oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW regulation of extent of heterochromatin formation Inferred from mutant phenotype. Source: GeneDB_SPombe regulation of transcription from RNA polymerase II promoter Ref.2 Inferred from mutant phenotype. Source: GeneDB_SPombe transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	nuclear heterochromatin Inferred from direct assay. Source: GeneDB_SPombe
Molecular function	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: GeneDB_SPombe
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 948	948	Putative JmjC domain-containing histone demethylation protein 1		PRO_0000086985
Regions
	Domain	243 – 402	160	JmjC
Sites
	Metal binding	297	1	Iron; catalytic By similarity
	Metal binding	299	1	Iron; catalytic By similarity
	Binding site	294	1	Substrate By similarity
	Binding site	314	1	Substrate By similarity
Experimental info
	Mutagenesis	307	1	Y → A: Loss of function. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	O94603-1 [UniParc]. Last modified May 1, 1999. Version 1. Checksum: 5CACC9C1F39751C4	FASTA	948	108,653
	10 20 30 40 50 60 MDSWLEYDDI INQDIDIPSN DLSGSGTLCV GVHSSLLENS LNSIDSFISS KEEISWCGNQ 70 80 90 100 110 120 STPIATKSHL SCINPQYVNP FDTSPVSVDT EFQDTYLLDA PSFAQPHFSE RQSVDKTRSR 130 140 150 160 170 180 CLSRNRRRKR HPNLHKNHQR LLGMSFPQDG FRRMPAESVN FSYFRDTGFN EPTIFPSSDT 190 200 210 220 230 240 QNTRQLNLSK IATLIGYDCP LALVDVVTQK QIPNKMDMES WVKYMSLEPS KRGRIYDVLS 250 260 270 280 290 300 LEVSTTKLAY YVRKPNIVRD LDLVNTVWPP GSFALGEYPH VDTYCLMSAE NSYTEFHIEF 310 320 330 340 350 360 GGSSAYYNIL DGCKIFYLIP GTSKNWEAYT AWLTSSNDSD KKFLPNMVDV CYCVEVHSQQ 370 380 390 400 410 420 TILVPSGWIY AVVTPCDTIS IAGNFLTFLH IYPQLSIYNL ELQLGIEKEY QYPYFESIMW 430 440 450 460 470 480 YTAIHFYLAF PDNSSRDGID DIIAEYETGR LFDINAFTEQ ELDGFEELLN YLYIRAQILR 490 500 510 520 530 540 DCDIIIDIYN EPVKISKNNG YNSAYTMVPP DLDEICVDFV QKFGAWITYH HRRSAKHPSC 550 560 570 580 590 600 NCFSHLQTKL IDSGPKPANN SYQHQSNFIG VVISTNHNII KKCQESQIQT GKNNCSFQLV 610 620 630 640 650 660 KKRIKSTKKA PSWRSIIKAF KKRENTRCNF LSSLHATTFR EDIVVRPKIK SFVLEQLIFQ 670 680 690 700 710 720 ALFSFAINWT PSFFLNHSNF ENIALSKETF NFGGEANCEN TDTTLFTTWG DQGFRPSDSI 730 740 750 760 770 780 CYNDFNLLET ANSDAEASIH ELELQPLNAV NEREVDISQT DMTPSTALDT RVDTRVDSLP 790 800 810 820 830 840 EFSNLILSPS SNDDSFQLDD LLSPSSSNLK QQIQKVVPQN SLEFSVGEKE KKAAEYSLLH 850 860 870 880 890 900 TFSYKRLSME NEKPDTTKVP LKYNIQHEEM KAYRRKNDLE YIDQHFASSK SGISNGRNNN 910 920 930 940 KEVNLTKAEN VGIKKRRIMK NENNIYDFED HSPVREKWGH RLRSRGAS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P. Nature 415:871-880(2002) [PubMed: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 38366 / 972.
[2]	"A novel jmjC domain protein modulates heterochromatization in fission yeast." Ayoub N., Noma K., Isaac S., Kahan T., Grewal S.I.S., Cohen A. Mol. Cell. Biol. 23:4356-4370(2003) [PubMed: 12773576] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF TYR-307.
[3]	"Methylation: lost in hydroxylation?" Trewick S.C., McLaughlin P.J., Allshire R.C. EMBO Rep. 6:315-320(2005) [PubMed: 15809658] [Abstract] Cited for: POSSIBLE FUNCTION AS A DEMETHYLASE.
[4]	"Histone demethylation by a family of JmjC domain-containing proteins." Tsukada Y., Fang J., Erdjument-Bromage H., Warren M.E., Borchers C.H., Tempst P., Zhang Y. Nature 439:811-816(2006) [PubMed: 16362057] [Abstract] Cited for: LACK OF DEMETHYLASE ACTIVITY IN VITRO.

Cross-references

Sequence databases
EMBLGenBankDDBJ	CU329672 Genomic DNA. Translation: CAA21872.1.
PIR	T41496.
RefSeq	NP_588188.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	2539481.
KEGG	spo:SPCC622.16c.
NMPDR	fig|4896.1.peg.526.
Organism-specific databases
GeneDB_Spombe	SPCC622.16c.
Enzyme and pathway databases
BioCyc	SPOM-XXX-01:SPOM-XXX-01-000127-MON.
BRENDA	1.14.11.27. 653.
Gene expression databases
ArrayExpress	O94603.
Family and domain databases
InterPro	IPR013129. TF_JmjC. IPR003347. TF_JmjC_AAH. [Graphical view]
Pfam	PF02373. JmjC. 1 hit. [Graphical view]
SMART	SM00558. JmjC. 1 hit. [Graphical view]
PROSITE	PS51184. JMJC. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

JHD1_SCHPO

Accession

Primary (citable) accession number: O94603

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 13, 2004
Last sequence update:	May 1, 1999
Last modified:	June 16, 2009
This is version 52 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)