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Protein

Deoxyhypusine hydroxylase

Gene

DOHH

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.UniRule annotation2 Publications

Catalytic activityi

[eIF5A]-deoxyhypusine + AH2 + O2 = [eIF5A]-hypusine + A + H2O.UniRule annotation1 Publication

Cofactori

Fe2+UniRule annotation2 PublicationsNote: Binds 2 Fe2+ ions per subunit.UniRule annotation2 Publications

Pathwayi: eIF5A hypusination

This protein is involved in the pathway eIF5A hypusination, which is part of Protein modification.UniRule annotation
View all proteins of this organism that are known to be involved in the pathway eIF5A hypusination and in Protein modification.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi56 – 561Iron 1
Metal bindingi57 – 571Iron 1
Metal bindingi89 – 891Iron 1
Metal bindingi90 – 901Iron 1
Metal bindingi207 – 2071Iron 2
Metal bindingi208 – 2081Iron 2
Metal bindingi240 – 2401Iron 2
Metal bindingi241 – 2411Iron 2

GO - Molecular functioni

  • deoxyhypusine monooxygenase activity Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • peptidyl-lysine modification to peptidyl-hypusine Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Monooxygenase, Oxidoreductase

Keywords - Biological processi

Hypusine biosynthesis

Keywords - Ligandi

Iron, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS05318-MONOMER.
BRENDAi1.14.99.29. 2681.
ReactomeiR-HSA-204626. Hypusine synthesis from eIF5A-lysine.
UniPathwayiUPA00354.

Names & Taxonomyi

Protein namesi
Recommended name:
Deoxyhypusine hydroxylaseUniRule annotation (EC:1.14.99.29UniRule annotation)
Short name:
hDOHH
Alternative name(s):
Deoxyhypusine dioxygenaseUniRule annotation
Deoxyhypusine monooxygenaseUniRule annotation
HEAT-like repeat-containing protein 1
Gene namesi
Name:DOHHUniRule annotation
Synonyms:HLRC1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:28662. DOHH.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi56 – 561H → A: Abolishes both iron-binding and enzyme activity. 1 Publication
Mutagenesisi57 – 571E → A: Abolishes enzyme activity and impairs iron-binding. 1 Publication
Mutagenesisi89 – 891H → A: Abolishes both iron-binding and enzyme activity. 1 Publication
Mutagenesisi90 – 901E → A: Abolishes both iron-binding and enzyme activity. 1 Publication
Mutagenesisi207 – 2071H → A: Abolishes both iron-binding and enzyme activity. 1 Publication
Mutagenesisi208 – 2081E → A: Abolishes enzyme activity and impairs iron-binding. 1 Publication
Mutagenesisi240 – 2401H → A: Abolishes both iron-binding and enzyme activity. 1 Publication
Mutagenesisi241 – 2411E → A: Abolishes both iron-binding and enzyme activity. 1 Publication

Organism-specific databases

PharmGKBiPA142671678.

Polymorphism and mutation databases

BioMutaiDOHH.
DMDMi74733193.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 302302Deoxyhypusine hydroxylasePRO_0000248575Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineCombined sources

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ9BU89.
MaxQBiQ9BU89.
PaxDbiQ9BU89.
PeptideAtlasiQ9BU89.
PRIDEiQ9BU89.

PTM databases

iPTMnetiQ9BU89.
PhosphoSiteiQ9BU89.

Expressioni

Gene expression databases

BgeeiQ9BU89.
CleanExiHS_DOHH.
ExpressionAtlasiQ9BU89. baseline and differential.
GenevisibleiQ9BU89. HS.

Organism-specific databases

HPAiHPA041953.

Interactioni

Protein-protein interaction databases

BioGridi123662. 12 interactions.
IntActiQ9BU89. 1 interaction.
STRINGi9606.ENSP00000250937.

Structurei

Secondary structure

302
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi1 – 1515Combined sources
Helixi21 – 3414Combined sources
Helixi37 – 459Combined sources
Helixi46 – 483Combined sources
Helixi52 – 6514Combined sources
Helixi68 – 703Combined sources
Helixi71 – 799Combined sources
Helixi85 – 9814Combined sources
Helixi101 – 1033Combined sources
Helixi104 – 1107Combined sources
Helixi116 – 13520Combined sources
Helixi158 – 1669Combined sources
Helixi172 – 18514Combined sources
Helixi187 – 19610Combined sources
Helixi197 – 1993Combined sources
Helixi203 – 21614Combined sources
Helixi219 – 2213Combined sources
Helixi222 – 2309Combined sources
Helixi236 – 24914Combined sources
Helixi252 – 26110Combined sources
Helixi267 – 28216Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4D4ZX-ray1.70A/B1-289[»]
4D50X-ray1.70A/B1-289[»]
ProteinModelPortaliQ9BU89.
SMRiQ9BU89. Positions 1-285.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati54 – 8027HEAT-like PBS-type 1Add
BLAST
Repeati87 – 11327HEAT-like PBS-type 2Add
BLAST
Repeati174 – 20027HEAT-like PBS-type 3Add
BLAST
Repeati205 – 23127HEAT-like PBS-type 4Add
BLAST
Repeati238 – 26427HEAT-like PBS-type 5Add
BLAST

Sequence similaritiesi

Belongs to the deoxyhypusine hydroxylase family.UniRule annotation
Contains 5 HEAT-like PBS-type repeats.UniRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0567. Eukaryota.
COG1413. LUCA.
GeneTreeiENSGT00500000044957.
HOGENOMiHOG000248665.
HOVERGENiHBG081460.
InParanoidiQ9BU89.
KOiK06072.
OMAiPEFQYAD.
OrthoDBiEOG75TMCH.
PhylomeDBiQ9BU89.
TreeFamiTF105626.

Family and domain databases

Gene3Di1.25.10.10. 1 hit.
HAMAPiMF_03101. Deoxyhypusine_hydroxylase.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR027517. Deoxyhypusine_hydroxylase.
IPR021133. HEAT_type_2.
IPR004155. PBS_lyase_HEAT.
[Graphical view]
SMARTiSM00567. EZ_HEAT. 6 hits.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.
PROSITEiPS50077. HEAT_REPEAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9BU89-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVTEQEVDAI GQTLVDPKQP LQARFRALFT LRGLGGPGAI AWISQAFDDD
60 70 80 90 100
SALLKHELAY CLGQMQDARA IPMLVDVLQD TRQEPMVRHE AGEALGAIGD
110 120 130 140 150
PEVLEILKQY SSDPVIEVAE TCQLAVRRLE WLQQHGGEPA AGPYLSVDPA
160 170 180 190 200
PPAEERDVGR LREALLDESR PLFERYRAMF ALRNAGGEEA ALALAEGLHC
210 220 230 240 250
GSALFRHEVG YVLGQLQHEA AVPQLAAALA RCTENPMVRH ECAEALGAIA
260 270 280 290 300
RPACLAALQA HADDPERVVR ESCEVALDMY EHETGRAFQY ADGLEQLRGA

PS
Length:302
Mass (Da):32,904
Last modified:June 1, 2001 - v1
Checksum:iCDA86E5549B98A2F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC005551 Genomic DNA. Translation: AAC33193.1.
AC093052 Genomic DNA. No translation available.
BC002817 mRNA. Translation: AAH02817.1.
BC009863 mRNA. Translation: AAH09863.1.
CCDSiCCDS12108.1.
RefSeqiNP_001138637.1. NM_001145165.1.
NP_112594.1. NM_031304.4.
XP_011526642.1. XM_011528340.1.
UniGeneiHs.515064.
Hs.609012.

Genome annotation databases

EnsembliENST00000250937; ENSP00000250937; ENSG00000129932.
ENST00000427575; ENSP00000398882; ENSG00000129932.
GeneIDi83475.
KEGGihsa:83475.
UCSCiuc002lxs.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC005551 Genomic DNA. Translation: AAC33193.1.
AC093052 Genomic DNA. No translation available.
BC002817 mRNA. Translation: AAH02817.1.
BC009863 mRNA. Translation: AAH09863.1.
CCDSiCCDS12108.1.
RefSeqiNP_001138637.1. NM_001145165.1.
NP_112594.1. NM_031304.4.
XP_011526642.1. XM_011528340.1.
UniGeneiHs.515064.
Hs.609012.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4D4ZX-ray1.70A/B1-289[»]
4D50X-ray1.70A/B1-289[»]
ProteinModelPortaliQ9BU89.
SMRiQ9BU89. Positions 1-285.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi123662. 12 interactions.
IntActiQ9BU89. 1 interaction.
STRINGi9606.ENSP00000250937.

PTM databases

iPTMnetiQ9BU89.
PhosphoSiteiQ9BU89.

Polymorphism and mutation databases

BioMutaiDOHH.
DMDMi74733193.

Proteomic databases

EPDiQ9BU89.
MaxQBiQ9BU89.
PaxDbiQ9BU89.
PeptideAtlasiQ9BU89.
PRIDEiQ9BU89.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000250937; ENSP00000250937; ENSG00000129932.
ENST00000427575; ENSP00000398882; ENSG00000129932.
GeneIDi83475.
KEGGihsa:83475.
UCSCiuc002lxs.4. human.

Organism-specific databases

CTDi83475.
GeneCardsiDOHH.
HGNCiHGNC:28662. DOHH.
HPAiHPA041953.
MIMi611262. gene.
neXtProtiNX_Q9BU89.
PharmGKBiPA142671678.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0567. Eukaryota.
COG1413. LUCA.
GeneTreeiENSGT00500000044957.
HOGENOMiHOG000248665.
HOVERGENiHBG081460.
InParanoidiQ9BU89.
KOiK06072.
OMAiPEFQYAD.
OrthoDBiEOG75TMCH.
PhylomeDBiQ9BU89.
TreeFamiTF105626.

Enzyme and pathway databases

UniPathwayiUPA00354.
BioCyciMetaCyc:HS05318-MONOMER.
BRENDAi1.14.99.29. 2681.
ReactomeiR-HSA-204626. Hypusine synthesis from eIF5A-lysine.

Miscellaneous databases

GenomeRNAii83475.
PROiQ9BU89.
SOURCEiSearch...

Gene expression databases

BgeeiQ9BU89.
CleanExiHS_DOHH.
ExpressionAtlasiQ9BU89. baseline and differential.
GenevisibleiQ9BU89. HS.

Family and domain databases

Gene3Di1.25.10.10. 1 hit.
HAMAPiMF_03101. Deoxyhypusine_hydroxylase.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR027517. Deoxyhypusine_hydroxylase.
IPR021133. HEAT_type_2.
IPR004155. PBS_lyase_HEAT.
[Graphical view]
SMARTiSM00567. EZ_HEAT. 6 hits.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.
PROSITEiPS50077. HEAT_REPEAT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, COFACTOR.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiDOHH_HUMAN
AccessioniPrimary (citable) accession number: Q9BU89
Secondary accession number(s): O75265
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: June 1, 2001
Last modified: June 8, 2016
This is version 133 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.