[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=ATCC 38366 / 972; DOI=10.1038/nature724; PubMed=11859360 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "The genome sequence of Schizosaccharomyces pombe."; Nature 415:871-880(2002).
[2]	FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF TYR-307. DOI=10.1128/MCB.23.12.4356-4370.2003; PubMed=12773576 [NCBI, ExPASy, EBI, Israel, Japan] Ayoub N., Noma K., Isaac S., Kahan T., Grewal S.I.S., Cohen A.; "A novel jmjC domain protein modulates heterochromatization in fission yeast."; Mol. Cell. Biol. 23:4356-4370(2003).
[3]	POSSIBLE FUNCTION AS A DEMETHYLASE. DOI=10.1038/sj.embor.7400379; PubMed=15809658 [NCBI, ExPASy, EBI, Israel, Japan] Trewick S.C., McLaughlin P.J., Allshire R.C.; "Methylation: lost in hydroxylation?"; EMBO Rep. 6:315-320(2005).
[4]	LACK OF DEMETHYLASE ACTIVITY IN VITRO. DOI=10.1038/nature04433; PubMed=16362057 [NCBI, ExPASy, EBI, Israel, Japan] Tsukada Y., Fang J., Erdjument-Bromage H., Warren M.E., Borchers C.H., Tempst P., Zhang Y.; "Histone demethylation by a family of JmjC domain-containing proteins."; Nature 439:811-816(2006).

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,N⁶-dimethyl-L-lysine + 2-oxoglutarate + O₂ = protein N⁶-methyl-L-lysine + succinate + formaldehyde + CO₂.
CATALYTIC ACTIVITY: Protein N⁶-methyl-L-lysine + 2-oxoglutarate + O₂ = protein L-lysine + succinate + formaldehyde + CO₂.
COFACTOR: Binds 1 Fe(2+) ion per subunit (By similarity).
SUBCELLULAR LOCATION: Nucleus.
DOMAIN: The JmjC domain mediates the demethylation activity (By similarity).
SIMILARITY: Belongs to the JHDM1 histone demethylase family.
SIMILARITY: 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.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

CU329672; CAA21872.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

T41496; T41496.

RefSeq

NP_588188.1; -.

3D structure databases

ModBase

O94603.

Enzyme and pathway databases

BioCyc

SPOM-XXX-01:SPOM-XXX-01-000127-MON; -.

Organism-specific databases

GeneDB_Spombe

SPCC622.16c; -.

Gene expression databases

ArrayExpress

O94603; -.

Ontologies

GO:0005720;	Cellular component: nuclear heterochromatin (inferred from direct assay from GeneDB_SPombe).
GO:0051864;	Molecular function: histone demethylase activity (H3-K36 specific) (inferred from electronic annotation from EC).
GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0016702;	Molecular function: oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen (inferred from electronic annotation from UniProtKB-KW).
GO:0005515;	Molecular function: protein binding (inferred from physical interaction from GeneDB_SPombe).
GO:0030702;	Biological process: chromatin silencing at centromere (inferred from mutant phenotype from GeneDB_SPombe).
GO:0030466;	Biological process: chromatin silencing at silent mating-type cassette (inferred from mutant phenotype from GeneDB_SPombe).
GO:0007059;	Biological process: chromosome segregation (inferred from mutant phenotype from GeneDB_SPombe).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0031454;	Biological process: regulation of extent of heterochromatin formation (inferred from mutant phenotype from GeneDB_SPombe).
GO:0006357;	Biological process: regulation of transcription from RNA polymerase II promoter (inferred from mutant phenotype from GeneDB_SPombe).
QuickGo view.

Family and domain databases

InterPro

IPR013129; TF_JmjC.
IPR003347; TF_JmjC_AAH.
Graphical view of domain structure.

Pfam

PF02373; JmjC; 1.
Pfam graphical view of domain structure.

SMART

SM00558; JmjC; 1.
SMART graphical view of domain structure.

PROSITE

PS51184; JMJC; 1.
PROSITE graphical view of domain structure (profiles).

ProtoNet

O94603.

Genome annotation databases

GeneID

2539481; -.

KEGG

spo:SPCC622.16c; -.

NMPDR

fig|4896.1.peg.526; -.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Chromatin regulator; Complete proteome; Dioxygenase; Iron; Metal-binding; Nucleus; Oxidoreductase; Transcription; Transcription regulation.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 948`	`948`	`Putative JmjC domain-containing histone demethylation protein 1.`	`PRO_0000086985`
`DOMAIN`	`243 402`	`160`	`JmjC.`
`METAL`	`297 297`		`Iron; catalytic (By similarity).`
`METAL`	`299 299`		`Iron; catalytic (By similarity).`
`BINDING`	`294 294`		`Substrate (By similarity).`
`BINDING`	`314 314`		`Substrate (By similarity).`
`MUTAGEN`	`307 307`		`Y->A: Loss of function.`

Sequence information

Length: 948 AA [This is the length of the unprocessed precursor]

Molecular weight: 108653 Da [This is the MW of the unprocessed precursor]

CRC64: 5CACC9C1F39751C4 [This is a checksum on the sequence]

        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

O94603 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools