[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. STRAIN=AB; NIH - Zebrafish Gene Collection (ZGC) project; Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.

Comments

FUNCTION: Hydroxylates HIF-1 alpha in the C-terminal transactivation domain (CAD). The hydroxylation prevents interaction of HIF-1 with transcriptional coactivators (By similarity).
CATALYTIC ACTIVITY: Peptide L-aspartate + 2-oxoglutarate + O₂ = peptide 3-hydroxy-L-aspartate + succinate + CO₂.
COFACTOR: Iron (By similarity).
SUBCELLULAR LOCATION: Nucleus (Potential).
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

BC044475; AAH44475.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_958904.1; -.

UniGene

Dr.13371

3D structure databases

HSSP

Q9NWT6; 1MZE. [HSSP ENTRY / PDB]

SMR

P59723; 16-340.

ModBase

P59723.

Organism-specific databases

ZFIN

ZDB-GENE-030826-19; hif1an.

Gene expression databases

ArrayExpress

P59723; -.

Ontologies

GO:0005634;	Cellular component: nucleus (inferred from electronic annotation from UniProtKB-KW).
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:0004597;	Molecular function: peptide-aspartate beta-dioxygenase activity (inferred from electronic annotation from EC).
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

P59723.

Genome annotation databases

Ensembl

ENSDARG00000031915; Danio rerio. [Contig view]

GeneID

373126; -.

KEGG

dre:373126; -.

Phylogenomic databases

HOGENOM

P59723; -.

HOVERGEN

P59723; -.

Other

UniRef

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

Keywords

Dioxygenase; Iron; Metal-binding; Nucleus; Oxidoreductase; Transcription; Transcription regulation.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 344`	`344`	`Hypoxia-inducible factor 1-alpha inhibitor.`	`PRO_0000083973`
`DOMAIN`	`133 303`	`171`	`JmjC.`
`METAL`	`190 190`		`Iron; catalytic (By similarity).`
`METAL`	`192 192`		`Iron; catalytic (By similarity).`
`METAL`	`270 270`		`Iron; catalytic (By similarity).`
`BINDING`	`136 136`		`2-oxoglutarate (By similarity).`
`BINDING`	`187 187`		`2-oxoglutarate (By similarity).`
`BINDING`	`205 205`		`2-oxoglutarate (By similarity).`

Sequence information

Length: 344 AA [This is the length of the unprocessed precursor]

Molecular weight: 39876 Da [This is the MW of the unprocessed precursor]

CRC64: FA9E2DC8B173B64C [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAETDGAAAF TELRDPGWDG SQLRQYTFPT RQIPRLSHTD PRAEVLINNE EPVVLTDTSL 

        70         80         90        100        110        120 
VYPALKWDIP YLQENIGNGD FSVYIAENHK FLYYDEKKMV NFQDFVPKSR RIEMKFSEFV 

       130        140        150        160        170        180 
DKMHQTEEQG GKGRVYLQQT LNDTVGRKIV VDFLGFNWNW INKQQAKRNW GPLTSNLLLI 

       190        200        210        220        230        240 
GMEGNVTPAH YDEQQNFFAQ IKGHKRCILF PPEQFDCLYP YPVHHPCDRQ SQVDFENPDY 

       250        260        270        280        290        300 
DKFPNFKNAV GYEAVVGPGD VLYIPMYWWH HIESLLNGGE TITVNFWYKG APTPKRIEYP 

       310        320        330        340 
LKAHQKVAIM RNIEKMLGEA LGDPHEVGPL LNMMIKGRYD HGLS

P59723 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	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