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Protein

Deoxyhypusine hydroxylase

Gene

Dohh

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 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 annotation1 Publication

Catalytic activityi

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

Cofactori

Fe2+UniRule annotationNote: Binds 2 Fe2+ ions per subunit.UniRule annotation

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 1UniRule annotation
Metal bindingi57 – 571Iron 1UniRule annotation
Metal bindingi89 – 891Iron 1UniRule annotation
Metal bindingi90 – 901Iron 1UniRule annotation
Metal bindingi208 – 2081Iron 2UniRule annotation
Metal bindingi209 – 2091Iron 2UniRule annotation
Metal bindingi241 – 2411Iron 2UniRule annotation
Metal bindingi242 – 2421Iron 2UniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Monooxygenase, Oxidoreductase

Keywords - Biological processi

Hypusine biosynthesis

Keywords - Ligandi

Iron, Metal-binding

Enzyme and pathway databases

ReactomeiR-MMU-204626. Hypusine synthesis from eIF5A-lysine.
UniPathwayiUPA00354.

Names & Taxonomyi

Protein namesi
Recommended name:
Deoxyhypusine hydroxylaseUniRule annotation (EC:1.14.99.29UniRule annotation1 Publication)
Short name:
DOHHUniRule annotation
Alternative name(s):
Deoxyhypusine dioxygenaseUniRule annotation
Deoxyhypusine monooxygenaseUniRule annotation
Gene namesi
Name:DohhImported
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 10

Organism-specific databases

MGIiMGI:1915964. Dohh.

Pathology & Biotechi

Disruption phenotypei

Embryonic lethal between E3.5 and E9.5.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 302302Deoxyhypusine hydroxylasePRO_0000248576Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ99LN9.
MaxQBiQ99LN9.
PaxDbiQ99LN9.
PeptideAtlasiQ99LN9.
PRIDEiQ99LN9.

PTM databases

PhosphoSiteiQ99LN9.

Expressioni

Gene expression databases

BgeeiQ99LN9.
CleanExiMM_DOHH.
ExpressionAtlasiQ99LN9. baseline and differential.
GenevisibleiQ99LN9. MM.

Interactioni

Protein-protein interaction databases

IntActiQ99LN9. 1 interaction.
MINTiMINT-4124284.
STRINGi10090.ENSMUSP00000072534.

Structurei

3D structure databases

ProteinModelPortaliQ99LN9.
SMRiQ99LN9. 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
Repeati175 – 20127HEAT-like PBS-type 3Add
BLAST
Repeati206 – 23227HEAT-like PBS-type 4Add
BLAST
Repeati239 – 26527HEAT-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.
InParanoidiQ99LN9.
KOiK06072.
OMAiPEFQYAD.
OrthoDBiEOG75TMCH.
PhylomeDBiQ99LN9.
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.
IPR004155. PBS_lyase_HEAT.
[Graphical view]
SMARTiSM00567. EZ_HEAT. 6 hits.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q99LN9-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MVTEQEIEAI GKTLVDPKQP LQARFRALFT LRGLGGPDAI SWISRGFEDS
60 70 80 90 100
SALLKHELAY CLGQMRDARA IPVLADVLQD TSQEPMVRHE AGEALGAIGN
110 120 130 140 150
PEVLGLLKQY STDPVVEVAE TCQLAVGRLE WLQQHPGEAT CAGPYLSVDP
160 170 180 190 200
APPAAEQDVG RLREALLDEA RPLFERYRAM FALRNVGGKE AALALAEGLQ
210 220 230 240 250
CGSALFRHEV GYVLGQLQHE AAVPGLAATL ARTTESPMVR HECAEALGAI
260 270 280 290 300
ARPACLAALR EHIEDPEQVV RESCEVALDM YEYESSQDFQ YADGLERLRP

PP
Length:302
Mass (Da):32,905
Last modified:September 5, 2006 - v2
Checksum:i524712E1EABF90C9
GO
Isoform 2 (identifier: Q99LN9-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     199-200: LQ → SC
     201-302: Missing.

Note: No experimental confirmation available.
Show »
Length:200
Mass (Da):21,663
Checksum:iC49099A0533AA971
GO

Sequence cautioni

The sequence BAC25064.1 differs from that shown. Reason: Frameshift at positions 171 and 302. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti68 – 681A → V in AAH02295 (PubMed:15489334).Curated
Sequence conflicti75 – 762AD → VG in AAH02295 (PubMed:15489334).Curated
Sequence conflicti298 – 2981L → V in BAC25064 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei199 – 2002LQ → SC in isoform 2. 1 PublicationVSP_020315
Alternative sequencei201 – 302102Missing in isoform 2. 1 PublicationVSP_020316Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK004052 mRNA. Translation: BAC25064.1. Frameshift.
AK080664 mRNA. Translation: BAC37972.1.
BC002295 mRNA. Translation: AAH02295.1.
CCDSiCCDS35997.1. [Q99LN9-1]
RefSeqiNP_598725.2. NM_133964.2. [Q99LN9-1]
UniGeneiMm.294975.

Genome annotation databases

EnsembliENSMUST00000072751; ENSMUSP00000072534; ENSMUSG00000078440. [Q99LN9-1]
ENSMUST00000144647; ENSMUSP00000116074; ENSMUSG00000078440. [Q99LN9-2]
GeneIDi102115.
KEGGimmu:102115.
UCSCiuc007ghu.2. mouse. [Q99LN9-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK004052 mRNA. Translation: BAC25064.1. Frameshift.
AK080664 mRNA. Translation: BAC37972.1.
BC002295 mRNA. Translation: AAH02295.1.
CCDSiCCDS35997.1. [Q99LN9-1]
RefSeqiNP_598725.2. NM_133964.2. [Q99LN9-1]
UniGeneiMm.294975.

3D structure databases

ProteinModelPortaliQ99LN9.
SMRiQ99LN9. Positions 1-285.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ99LN9. 1 interaction.
MINTiMINT-4124284.
STRINGi10090.ENSMUSP00000072534.

PTM databases

PhosphoSiteiQ99LN9.

Proteomic databases

EPDiQ99LN9.
MaxQBiQ99LN9.
PaxDbiQ99LN9.
PeptideAtlasiQ99LN9.
PRIDEiQ99LN9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000072751; ENSMUSP00000072534; ENSMUSG00000078440. [Q99LN9-1]
ENSMUST00000144647; ENSMUSP00000116074; ENSMUSG00000078440. [Q99LN9-2]
GeneIDi102115.
KEGGimmu:102115.
UCSCiuc007ghu.2. mouse. [Q99LN9-1]

Organism-specific databases

CTDi83475.
MGIiMGI:1915964. Dohh.

Phylogenomic databases

eggNOGiKOG0567. Eukaryota.
COG1413. LUCA.
GeneTreeiENSGT00500000044957.
HOGENOMiHOG000248665.
HOVERGENiHBG081460.
InParanoidiQ99LN9.
KOiK06072.
OMAiPEFQYAD.
OrthoDBiEOG75TMCH.
PhylomeDBiQ99LN9.
TreeFamiTF105626.

Enzyme and pathway databases

UniPathwayiUPA00354.
ReactomeiR-MMU-204626. Hypusine synthesis from eIF5A-lysine.

Miscellaneous databases

PROiQ99LN9.
SOURCEiSearch...

Gene expression databases

BgeeiQ99LN9.
CleanExiMM_DOHH.
ExpressionAtlasiQ99LN9. baseline and differential.
GenevisibleiQ99LN9. MM.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Strain: C57BL/6J.
    Tissue: Brain cortex.
  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] (ISOFORM 1).
    Strain: Czech II.
    Tissue: Mammary tumor.
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  4. "A novel mouse model for inhibition of DOHH-mediated hypusine modification reveals a crucial function in embryonic development, proliferation and oncogenic transformation."
    Sievert H., Paellmann N., Miller K.K., Hermans-Borgmeyer I., Venz S., Sendoel A., Preukschas M., Schweizer M., Boettcher S., Janiesch P.C., Streichert T., Walther R., Hengartner M.O., Manz M.G., Bruemmendorf T.H., Bokemeyer C., Braig M., Hauber J., Duncan K.E., Balabanov S.
    Dis. Model. Mech. 7:963-976(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiDOHH_MOUSE
AccessioniPrimary (citable) accession number: Q99LN9
Secondary accession number(s): Q8BNT3, Q8BTD5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: September 5, 2006
Last modified: July 6, 2016
This is version 119 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. 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.