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P47120 (DOHH_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 124. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Deoxyhypusine hydroxylase

Short name=DOHH
EC=1.14.99.29
Alternative name(s):
Deoxyhypusine dioxygenase
Deoxyhypusine monooxygenase
Ligand of eIF5A protein 1
Gene names
Name:LIA1
Synonyms:MMD1
Ordered Locus Names:YJR070C
ORF Names:J1814
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length325 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 By similarity. Ref.8 Ref.12

Catalytic activity

[eIF5A]-deoxyhypusine + AH2 + O2 = [eIF5A]-hypusine + A + H2O. Ref.8

Cofactor

Binds 2 Fe2+ ions per subunit. Ref.12

Pathway

Protein modification; eIF5A hypusination. HAMAP-Rule MF_03101

Subcellular location

Cytoplasm. Nucleus Ref.6.

Miscellaneous

Present with 39900 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the deoxyhypusine hydroxylase family.

Contains 5 HEAT-like PBS-type repeats.

Biophysicochemical properties

pH dependence:

Optimum pH is 7.5. Active from pH 6 to 10. Ref.12

Binary interactions

With

Entry

#Exp.

IntAct

Notes

HYP2P233012EBI-25526,EBI-9033

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed HAMAP-Rule MF_03101
Chain2 – 325324Deoxyhypusine hydroxylase HAMAP-Rule MF_03101
PRO_0000203100

Regions

Repeat77 – 10327HEAT-like PBS-type 1 HAMAP-Rule MF_03101
Repeat110 – 13627HEAT-like PBS-type 2 HAMAP-Rule MF_03101
Repeat202 – 23130HEAT-like PBS-type 3 HAMAP-Rule MF_03101
Repeat235 – 26127HEAT-like PBS-type 4 HAMAP-Rule MF_03101
Repeat268 – 29427HEAT-like PBS-type 5 HAMAP-Rule MF_03101

Sites

Metal binding791Iron 1
Metal binding801Iron 1
Metal binding1121Iron 1
Metal binding1131Iron 1
Metal binding2371Iron 2
Metal binding2381Iron 2
Metal binding2701Iron 2
Metal binding2711Iron 2

Amino acid modifications

Modified residue21N-acetylserine Ref.5
Modified residue1261Phosphoserine Ref.11
Modified residue1871Phosphothreonine Ref.11
Modified residue2811Phosphoserine Ref.9 Ref.10 Ref.11

Experimental info

Mutagenesis791H → A: Abolishes both iron-binding and enzyme activity. Ref.12
Mutagenesis801E → A: Abolishes enzyme activity and impairs iron-binding. Ref.12
Mutagenesis1121H → A: Abolishes both iron-binding and enzyme activity. Ref.12
Mutagenesis1131E → A: Abolishes iron-binding, substrate-binding, and enzyme activity. Ref.12
Mutagenesis1161E → A: Abolishes substrate-binding and enzyme activity. Ref.12
Mutagenesis1161E → D: Reduces enzyme activity by 97%. Ref.12
Mutagenesis2371H → A: Abolishes both iron-binding and enzyme activity. Ref.12
Mutagenesis2381E → A: Abolishes substrate-binding, enzyme activity, and impairs iron-binding. Ref.12
Mutagenesis2701H → A: Abolishes iron-binding, substrate-binding, and enzyme activity. Ref.12
Mutagenesis2711E → A: Abolishes iron-binding, substrate-binding, and enzyme activity. Ref.12
Mutagenesis2741E → A: Abolishes substrate-binding. Ref.12

Sequences

Sequence LengthMass (Da)Tools
P47120 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: AB36A73B40466CD5

FASTA32536,165
        10         20         30         40         50         60 
MSTNFEKHFQ ENVDECTLEQ LRDILVNKSG KTVLANRFRA LFNLKTVAEE FATKPEEAKK 

        70         80         90        100        110        120 
AIEYIAESFV NDKSELLKHE VAYVLGQTKN LDAAPTLRHV MLDQNQEPMV RHEAAEALGA 

       130        140        150        160        170        180 
LGDKDSLDDL NKAAKEDPHV AVRETCELAI NRINWTHGGA KDKENLQQSL YSSIDPAPPL 

       190        200        210        220        230        240 
PLEKDATIPE LQALLNDPKQ PLFQRYRAMF RLRDIGTDEA ILALATGFSA ESSLFKHEIA 

       250        260        270        280        290        300 
YVFGQIGSPA AVPSLIEVLG RKEEAPMVRH EAAEALGAIA SPEVVDVLKS YLNDEVDVVR 

       310        320 
ESCIVALDMY DYENSNELEY APTAN 

« Hide

References

« Hide 'large scale' references
[1]"Analysis of a 62 kb DNA sequence of chromosome X reveals 36 open reading frames and a gene cluster with a counterpart on chromosome XI."
Huang M.-E., Manus V., Chuat J.-C., Galibert F.
Yeast 12:869-875(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[2]"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X."
Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C., Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D., Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J., Heumann K. expand/collapse author list , Hilger F., Hollenberg C.P., Huang M.-E., Jacq C., Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E., Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T., Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R., Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N., To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H., von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.
EMBO J. 15:2031-2049(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"Linking genome and proteome by mass spectrometry: large-scale identification of yeast proteins from two dimensional gels."
Shevchenko A., Jensen O.N., Podtelejnikov A.V., Sagliocco F., Wilm M., Vorm O., Mortensen P., Shevchenko A., Boucherie H., Mann M.
Proc. Natl. Acad. Sci. U.S.A. 93:14440-14445(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY.
[5]"Proteome studies of Saccharomyces cerevisiae: identification and characterization of abundant proteins."
Garrels J.I., McLaughlin C.S., Warner J.R., Futcher B., Latter G.I., Kobayashi R., Schwender B., Volpe T., Anderson D.S., Mesquita-Fuentes R., Payne W.E.
Electrophoresis 18:1347-1360(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION AT SER-2.
[6]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[7]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[8]"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.
[9]"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-281, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ADR376.
[10]"A multidimensional chromatography technology for in-depth phosphoproteome analysis."
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-281, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-126; THR-187 AND SER-281, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"Evidence for conformational changes in the yeast deoxyhypusine hydroxylase Lia1 upon iron displacement from its active site."
Cano V.S., Medrano F.J., Park M.H., Valentini S.R.
Amino Acids 38:479-490(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, COFACTOR, MUTAGENESIS OF HIS-79; GLU-80; HIS-112; GLU-113; GLU-116; HIS-237; GLU-238; HIS-270; GLU-271 AND GLU-274, BIOPHYSICOCHEMICAL PROPERTIES.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z49570 Genomic DNA. Translation: CAA89598.1.
L47993 Genomic DNA. Translation: AAB39296.1.
BK006943 Genomic DNA. Translation: DAA08857.1.
PIRS57089.
RefSeqNP_012604.1. NM_001181728.1.

3D structure databases

ProteinModelPortalP47120.
SMRP47120. Positions 6-313.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid33827. 66 interactions.
DIPDIP-2829N.
IntActP47120. 6 interactions.
MINTMINT-539495.
STRING4932.YJR070C.

Proteomic databases

PaxDbP47120.
PeptideAtlasP47120.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYJR070C; YJR070C; YJR070C.
GeneID853534.
KEGGsce:YJR070C.

Organism-specific databases

CYGDYJR070c.
SGDS000003831. LIA1.

Phylogenomic databases

eggNOGCOG1413.
GeneTreeENSGT00500000044957.
HOGENOMHOG000248665.
KOK06072.
OMARESCQVA.
OrthoDBEOG7QC85Z.

Enzyme and pathway databases

BioCycYEAST:G3O-31703-MONOMER.
UniPathwayUPA00354.

Gene expression databases

GenevestigatorP47120.

Family and domain databases

Gene3D1.25.10.10. 1 hit.
HAMAPMF_03101. Deoxyhypusine_hydroxylase.
InterProIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR027517. Deoxyhypusine_hydroxylase.
IPR004155. PBS_lyase_HEAT.
[Graphical view]
PfamPF03130. HEAT_PBS. 3 hits.
[Graphical view]
SMARTSM00567. EZ_HEAT. 5 hits.
[Graphical view]
SUPFAMSSF48371. SSF48371. 1 hit.
ProtoNetSearch...

Other

NextBio974236.
PROP47120.

Entry information

Entry nameDOHH_YEAST
AccessionPrimary (citable) accession number: P47120
Secondary accession number(s): D6VWP1
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: March 19, 2014
This is version 124 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome X

Yeast (Saccharomyces cerevisiae) chromosome X: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways