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,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).
SIMILARITY: Belongs to the JHDM1 histone demethylase family.
SIMILARITY: Contains 1 JmjC domain.

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

CR380956; CAG60777.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

XP_447828.1; -.

3D structure databases

ModBase

Q6FPL6.

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: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:0016568;	Biological process: chromatin modification (inferred from electronic annotation from UniProtKB-KW).
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.
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

Q6FPL6.

Genome annotation databases

GeneID

2889738; -.

KEGG

cgr:CAGL0J02860g; -.

Phylogenomic databases

HOGENOM

Q6FPL6; -.

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`	`1 403`	`403`	`JmjC domain-containing histone demethylation protein 1.`	`PRO_0000226794`
`DOMAIN`	`141 328`	`188`	`JmjC.`
`METAL`	`224 224`		`Iron; catalytic (By similarity).`
`METAL`	`226 226`		`Iron; catalytic (By similarity).`
`METAL`	`296 296`		`Iron; catalytic (By similarity).`
`BINDING`	`221 221`		`Substrate (By similarity).`
`BINDING`	`241 241`		`Substrate (By similarity).`

Sequence information

Length: 403 AA [This is the length of the unprocessed precursor]

Molecular weight: 47030 Da [This is the MW of the unprocessed precursor]

CRC64: F327A0D7EB1217BD [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAVKIEQALG EKRSLNDNDE VPRKKRYNFR KKVELDYSAL NEGEDKKSKF FHPHIALFEK 

        70         80         90        100        110        120 
EFEKCLSNVT EDMSMTCSEY CKRFDDIDFP LKISDPENSG MVVSTNNKTT RDLTVDDITQ 

       130        140        150        160        170        180 
AVGDDYFVNV MDVQSQENER WSLREWCNYF NKPAEEKDRI RNVISLEVSH VEDLQYDRPD 

       190        200        210        220        230        240 
IVDDKDLVDI VWNNVENLDT ENDPRPKVTK YCLMSVKNAF TDYHLDFAGT SVYYNLAFGK 

       250        260        270        280        290        300 
KKFILYPPTP ENIENYIEWS TSTYQNMLFL GEKLTGGVAM ELNGGDLFMI PSGYIHVVYT 

       310        320        330        340        350        360 
PEDSLIFGGN YLTFRDISQQ LKIVDVEKQT GVTKRYTFPM FDEVMGRTCE WLCQNQKKGK 

       370        380        390        400 
QMQVKKETVN DLISYMKSGK TKYKPTNFIN KKQMLQELSN LYL

Q6FPL6 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