[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=ATCC 204511 / S288c / AB972; PubMed=9169868 [NCBI, ExPASy, EBI, Israel, Japan] Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E., Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S., Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X., Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y., Botstein D., Davis R.W.; "The nucleotide sequence of Saccharomyces cerevisiae chromosome V."; Nature 387:78-81(1997).
[2]	LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. DOI=10.1038/nature02046; PubMed=14562106 [NCBI, ExPASy, EBI, Israel, Japan] Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.; "Global analysis of protein expression in yeast."; Nature 425:737-741(2003).
[3]	FUNCTION, ENZYME ACTIVITY, AND MUTAGENESIS OF HIS-305. 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: Histone demethylase that specifically demethylates 'Lys-36' of histone H3, thereby playing a central role in histone code. Does not demethylate H3 'Lys-4' nor 'Lys-79'.
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 (By similarity).
DOMAIN: The JmjC domain mediates the demethylation activity (By similarity).
MISCELLANEOUS: Present with 784 molecules/cell in log phase SD medium.
SIMILARITY: Belongs to the JHDM1 histone demethylase family.
SIMILARITY: Contains 1 JmjC domain.
SIMILARITY: Contains 1 PHD-type zinc finger.

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

U18796; AAB64586.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S50554; S50554.

RefSeq

NP_010971.1; -.

3D structure databases

ModBase

P40034.

Protein-protein interaction databases

DIP

DIP:5335N; -.

IntAct

P40034; -.

Organism-specific databases

YER051w; -.

S000000853; JHD1.

Gene expression databases

ArrayExpress

P40034; -.

GermOnline

YER051W; Saccharomyces cerevisiae.

Ontologies

GO:0005634;	Cellular component: nucleus (inferred from electronic annotation from UniProtKB-KW).
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:0035064;	Molecular function: methylated histone residue binding (inferred from direct assay from SGD).
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:0008270;	Molecular function: zinc ion binding (inferred from electronic annotation from InterPro).
GO:0016577;	Biological process: histone demethylation (inferred from direct assay from SGD).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0006355;	Biological process: regulation of transcription, DNA-dependent (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR003347; TF_JmjC_AAH.
IPR001965; Znf_PHD.
Graphical view of domain structure.

SMART

SM00558; JmjC; 1.
SM00249; PHD; 1.
SMART graphical view of domain structure.

PROSITE

PS51184; JMJC; 1.
PS01359; ZF_PHD_1; FALSE_NEG.
PS50016; ZF_PHD_2; FALSE_NEG.
PROSITE graphical view of domain structure (profiles).

ProtoNet

P40034.

Genome annotation databases

Ensembl

YER051W; Saccharomyces cerevisiae. [Contig view]

856777; -.

U00092_GR; YER051W.

sce:YER051W; -.

fig|4932.3.peg.2034; -.

Phylogenomic databases

HOGENOM

P40034; -.

Other

LinkHub

P40034; -.

NextBio

982979; -.

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; Zinc; Zinc-finger.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 492`	`492`	`JmjC domain-containing histone demethylation protein 1.`	`PRO_0000202630`
`DOMAIN`	`254 409`	`156`	`JmjC.`
`ZN_FING`	`4 72`	`69`	`PHD-type; atypical.`
`METAL`	`305 305`		`Iron; catalytic (Probable).`
`METAL`	`307 307`		`Iron; catalytic (By similarity).`
`METAL`	`377 377`		`Iron; catalytic (By similarity).`
`BINDING`	`302 302`		`Substrate (By similarity).`
`BINDING`	`322 322`		`Substrate (By similarity).`
`MUTAGEN`	`305 305`		`H->A: Abolishes histone demethylase activity.`

Sequence information

Length: 492 AA [This is the length of the unprocessed precursor]

Molecular weight: 56530 Da [This is the MW of the unprocessed precursor]

CRC64: 5CBD09352131692B [This is a checksum on the sequence]

        10         20         30         40         50         60 
MQDPNICQHC QLKDNPGALI WVKCDSCPQW VHVKCVPLKR IHYSNLTSSE VLSYPNSAKQ 

        70         80         90        100        110        120 
IKSYRCPNHK EGEYLTAYAL ITQKGKRQRN KENPEDSHIN KRYNFRKKKL LDYIALNEGE 

       130        140        150        160        170        180 
SKRDKMNHPH KESFMKSFEK WKNGSNIINA ADFAEKFDNI DVPYKIIDPL NSGVYVPNVG 

       190        200        210        220        230        240 
TDNGCLTVNY ITEMIGEDYH VDVMDVQSQM NENWNLGSWN EYFTNTEPDR RDRIRNVISL 

       250        260        270        280        290        300 
EVSNIEGLEL ERPTAVRQND LVDKIWSFNG HLEKVNGEKA EENDPKPKVT KYILMSVKDA 

       310        320        330        340        350        360 
YTDFHLDFAG TSVYYNVISG QKKFLLFPPT QSNIDKYIEW SLKEDQNSVF LGDILEDGIA 

       370        380        390        400        410        420 
MELDAGDLFM IPAGYIHAVY TPVDSLVFGG NFLTIRDLET HLKIVEIEKL TKVPRRFTFP 

       430        440        450        460        470        480 
KFDQVMGKLC EYLALDKNKI TSDVSDGDLL SRTTNCAIQS LHAYVIKPEV KYKPLNFTSK 

       490 
KHLAKALADL IS

P40034 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