Q9BU89 (DOHH_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Deoxyhypusine hydroxylase
Short name=hDOHH
EC=1.14.99.29

Alternative name(s):
Deoxyhypusine dioxygenase
Deoxyhypusine monooxygenase
HEAT-like repeat-containing protein 1

Gene names

Name:	DOHH
Synonyms:	HLRC1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	302 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the hydroxylation of the N(6)-(4-aminobutyl)-L-lysine intermediate to form hypusine, an essential post-translational modification only found in mature eIF-5A factor. Ref.4 Ref.5
Catalytic activity	Protein N(6)-(4-aminobutyl)-L-lysine + AH2 + O2 = protein N(6)-((R)-4-amino-2-hydroxybutyl)-L-lysine + A + H2O. Ref.4
Cofactor	Binds 2 Fe2+ ions per subunit. Ref.3 Ref.5
Pathway	Protein modification; eIF5A hypusination.
Sequence similarities	Belongs to the deoxyhypusine hydroxylase family. Contains 5 HEAT-like PBS-type repeats.

Ontologies

Keywords
Biological process	Hypusine biosynthesis
Domain	Repeat
Ligand	Iron Metal-binding
Molecular function	Monooxygenase Oxidoreductase
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	peptidyl-lysine modification to hypusine Inferred from mutant phenotype Ref.4. Source: UniProtKB post-translational protein modification Traceable author statement. Source: Reactome
Cellular component	cytosol Traceable author statement. Source: Reactome
Molecular function	deoxyhypusine monooxygenase activity Inferred from mutant phenotype Ref.4. Source: UniProtKB metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 302	302	Deoxyhypusine hydroxylase		PRO_0000248575
Regions
	Repeat	54 – 80	27	HEAT-like PBS-type 1
	Repeat	87 – 113	27	HEAT-like PBS-type 2
	Repeat	174 – 200	27	HEAT-like PBS-type 3
	Repeat	205 – 231	27	HEAT-like PBS-type 4
	Repeat	238 – 264	27	HEAT-like PBS-type 5
Sites
	Metal binding	56	1	Iron 1
	Metal binding	57	1	Iron 1
	Metal binding	89	1	Iron 1
	Metal binding	90	1	Iron 1
	Metal binding	207	1	Iron 2
	Metal binding	208	1	Iron 2
	Metal binding	240	1	Iron 2
	Metal binding	241	1	Iron 2
Experimental info
	Mutagenesis	56	1	H → A: Abolishes both iron-binding and enzyme activity. Ref.3
	Mutagenesis	57	1	E → A: Abolishes enzyme activity and impairs iron-binding. Ref.3
	Mutagenesis	89	1	H → A: Abolishes both iron-binding and enzyme activity. Ref.3
	Mutagenesis	90	1	E → A: Abolishes both iron-binding and enzyme activity. Ref.3
	Mutagenesis	207	1	H → A: Abolishes both iron-binding and enzyme activity. Ref.3
	Mutagenesis	208	1	E → A: Abolishes enzyme activity and impairs iron-binding. Ref.3
	Mutagenesis	240	1	H → A: Abolishes both iron-binding and enzyme activity. Ref.3
	Mutagenesis	241	1	E → A: Abolishes both iron-binding and enzyme activity. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q9BU89 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: CDA86E5549B98A2F	FASTA	302	32,904
	10 20 30 40 50 60 MVTEQEVDAI GQTLVDPKQP LQARFRALFT LRGLGGPGAI AWISQAFDDD SALLKHELAY 70 80 90 100 110 120 CLGQMQDARA IPMLVDVLQD TRQEPMVRHE AGEALGAIGD PEVLEILKQY SSDPVIEVAE 130 140 150 160 170 180 TCQLAVRRLE WLQQHGGEPA AGPYLSVDPA PPAEERDVGR LREALLDESR PLFERYRAMF 190 200 210 220 230 240 ALRNAGGEEA ALALAEGLHC GSALFRHEVG YVLGQLQHEA AVPQLAAALA RCTENPMVRH 250 260 270 280 290 300 ECAEALGAIA RPACLAALQA HADDPERVVR ESCEVALDMY EHETGRAFQY ADGLEQLRGA PS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The DNA sequence and biology of human chromosome 19." Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M. Nature 428:529-535(2004) [PubMed: 15057824] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Lung and Lymph.
[3]	"Deoxyhypusine hydroxylase is an Fe(II)-dependent, HEAT-repeat enzyme. Identification of amino acid residues critical for Fe(II) binding and catalysis." Kim Y.S., Kang K.R., Wolff E.C., Bell J.K., McPhie P., Park M.H. J. Biol. Chem. 281:13217-13225(2006) [PubMed: 16533814] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-7, COFACTOR, MUTAGENESIS OF HIS-56; GLU-57; HIS-89; GLU-90; HIS-207; GLU-208; HIS-240 AND GLU-241.
[4]	"Molecular cloning, expression, and structural prediction of deoxyhypusine hydroxylase: a HEAT-repeat-containing metalloenzyme." Park J.-H., Aravind L., Wolff E.C., Kaevel J., Kim Y.S., Park M.H. Proc. Natl. Acad. Sci. U.S.A. 103:51-56(2006) [PubMed: 16371467] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY.
[5]	"Human deoxyhypusine hydroxylase, an enzyme involved in regulating cell growth, activates O(2) with a nonheme diiron center." Vu V.V., Emerson J.P., Martinho M., Kim Y.S., Munck E., Park M.H., Que L. Jr. Proc. Natl. Acad. Sci. U.S.A. 106:14814-14819(2009) [PubMed: 19706422] [Abstract] Cited for: FUNCTION, COFACTOR.
[6]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AC005551 Genomic DNA. Translation: AAC33193.1. AC093052 Genomic DNA. No translation available. BC002817 mRNA. Translation: AAH02817.1. BC009863 mRNA. Translation: AAH09863.1.
IPI	IPI00171856.
RefSeq	NP_001138637.1. NM_001145165.1. NP_112594.1. NM_031304.4.
UniGene	Hs.515064. Hs.609012.
3D structure databases
ProteinModelPortal	Q9BU89.
SMR	Q9BU89. Positions 2-284.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9BU89.
PTM databases
PhosphoSite	Q9BU89.
Polymorphism databases
DMDM	74733193.
Proteomic databases
PeptideAtlas	Q9BU89.
PRIDE	Q9BU89.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000250937; ENSP00000250937; ENSG00000129932. ENST00000427575; ENSP00000398882; ENSG00000129932.
GeneID	83475.
KEGG	hsa:83475.
UCSC	uc002lxs.1. human.
Organism-specific databases
CTD	83475.
GeneCards	GC19M003443.
H-InvDB	HIX0014639.
HGNC	HGNC:28662. DOHH.
HPA	HPA041953.
MIM	611262. gene.
neXtProt	NX_Q9BU89.
PharmGKB	PA142671678.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG12900.
GeneTree	ENSGT00500000044957.
HOGENOM	HBG434986.
HOVERGEN	HBG081460.
InParanoid	Q9BU89.
OMA	PEFQYAD.
OrthoDB	EOG46WZ94.
PhylomeDB	Q9BU89.
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-13918.
Reactome	REACT_17015. Metabolism of proteins.
Gene expression databases
ArrayExpress	Q9BU89.
Bgee	Q9BU89.
CleanEx	HS_DOHH.
Genevestigator	Q9BU89.
GermOnline	ENSG00000129932. Homo sapiens.
Family and domain databases
InterPro	IPR011989. ARM-like. IPR016024. ARM-type_fold. IPR021133. HEAT_type_2. IPR004155. PBS_lyase_HEAT. [Graphical view]
Gene3D	G3DSA:1.25.10.10. ARM-like. 1 hit.
KO	K06072.
Pfam	PF03130. HEAT_PBS. 4 hits. [Graphical view]
SMART	SM00567. EZ_HEAT. 6 hits. [Graphical view]
SUPFAM	SSF48371. ARM-type_fold. 1 hit.
PROSITE	PS50077. HEAT_REPEAT. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	72407.
SOURCE	Search...

Entry information

Entry name

DOHH_HUMAN

Accession

Primary (citable) accession number: Q9BU89
Secondary accession number(s): O75265

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 5, 2006
Last sequence update:	June 1, 2001
Last modified:	January 25, 2012
This is version 92 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.