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P47120

- DOHH_YEAST

UniProt

P47120 - DOHH_YEAST

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Protein

Deoxyhypusine hydroxylase

Gene
LIA1, MMD1, YJR070C, J1814
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - 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 By similarity.2 Publications

Catalytic activityi

[eIF5A]-deoxyhypusine + AH2 + O2 = [eIF5A]-hypusine + A + H2O.1 Publication

Cofactori

Binds 2 Fe2+ ions per subunit.1 Publication

pH dependencei

Optimum pH is 7.5. Active from pH 6 to 10.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi79 – 791Iron 1
Metal bindingi80 – 801Iron 1
Metal bindingi112 – 1121Iron 1
Metal bindingi113 – 1131Iron 1
Metal bindingi237 – 2371Iron 2
Metal bindingi238 – 2381Iron 2
Metal bindingi270 – 2701Iron 2
Metal bindingi271 – 2711Iron 2

GO - Molecular functioni

  1. deoxyhypusine monooxygenase activity Source: SGD
  2. metal ion binding Source: UniProtKB-KW
  3. protein binding Source: IntAct

GO - Biological processi

  1. microtubule cytoskeleton organization Source: SGD
  2. peptidyl-lysine modification to peptidyl-hypusine Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Monooxygenase, Oxidoreductase

Keywords - Biological processi

Hypusine biosynthesis

Keywords - Ligandi

Iron, Metal-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-31703-MONOMER.
UniPathwayiUPA00354.

Names & Taxonomyi

Protein namesi
Recommended name:
Deoxyhypusine hydroxylase (EC:1.14.99.29)
Short name:
DOHH
Alternative name(s):
Deoxyhypusine dioxygenase
Deoxyhypusine monooxygenase
Ligand of eIF5A protein 1
Gene namesi
Name:LIA1
Synonyms:MMD1
Ordered Locus Names:YJR070C
ORF Names:J1814
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome X

Organism-specific databases

CYGDiYJR070c.
SGDiS000003831. LIA1.

Subcellular locationi

Cytoplasm. Nucleus 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi79 – 791H → A: Abolishes both iron-binding and enzyme activity. 1 Publication
Mutagenesisi80 – 801E → A: Abolishes enzyme activity and impairs iron-binding. 1 Publication
Mutagenesisi112 – 1121H → A: Abolishes both iron-binding and enzyme activity. 1 Publication
Mutagenesisi113 – 1131E → A: Abolishes iron-binding, substrate-binding, and enzyme activity. 1 Publication
Mutagenesisi116 – 1161E → A: Abolishes substrate-binding and enzyme activity. 1 Publication
Mutagenesisi116 – 1161E → D: Reduces enzyme activity by 97%. 1 Publication
Mutagenesisi237 – 2371H → A: Abolishes both iron-binding and enzyme activity. 1 Publication
Mutagenesisi238 – 2381E → A: Abolishes substrate-binding, enzyme activity, and impairs iron-binding. 1 Publication
Mutagenesisi270 – 2701H → A: Abolishes iron-binding, substrate-binding, and enzyme activity. 1 Publication
Mutagenesisi271 – 2711E → A: Abolishes iron-binding, substrate-binding, and enzyme activity. 1 Publication
Mutagenesisi274 – 2741E → A: Abolishes substrate-binding. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedUniRule annotation
Chaini2 – 325324Deoxyhypusine hydroxylaseUniRule annotationPRO_0000203100Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Modified residuei126 – 1261Phosphoserine1 Publication
Modified residuei187 – 1871Phosphothreonine1 Publication
Modified residuei281 – 2811Phosphoserine3 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP47120.
PaxDbiP47120.
PeptideAtlasiP47120.

Expressioni

Gene expression databases

GenevestigatoriP47120.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
HYP2P233012EBI-25526,EBI-9033

Protein-protein interaction databases

BioGridi33827. 67 interactions.
DIPiDIP-2829N.
IntActiP47120. 6 interactions.
MINTiMINT-539495.
STRINGi4932.YJR070C.

Structurei

3D structure databases

ProteinModelPortaliP47120.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati77 – 10327HEAT-like PBS-type 1UniRule annotationAdd
BLAST
Repeati110 – 13627HEAT-like PBS-type 2UniRule annotationAdd
BLAST
Repeati202 – 23130HEAT-like PBS-type 3UniRule annotationAdd
BLAST
Repeati235 – 26127HEAT-like PBS-type 4UniRule annotationAdd
BLAST
Repeati268 – 29427HEAT-like PBS-type 5UniRule annotationAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG1413.
GeneTreeiENSGT00500000044957.
HOGENOMiHOG000248665.
KOiK06072.
OMAiRESCQVA.
OrthoDBiEOG7QC85Z.

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]
PfamiPF03130. HEAT_PBS. 3 hits.
[Graphical view]
SMARTiSM00567. EZ_HEAT. 5 hits.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P47120-1 [UniParc]FASTAAdd to Basket

« Hide

MSTNFEKHFQ ENVDECTLEQ LRDILVNKSG KTVLANRFRA LFNLKTVAEE    50
FATKPEEAKK AIEYIAESFV NDKSELLKHE VAYVLGQTKN LDAAPTLRHV 100
MLDQNQEPMV RHEAAEALGA LGDKDSLDDL NKAAKEDPHV AVRETCELAI 150
NRINWTHGGA KDKENLQQSL YSSIDPAPPL PLEKDATIPE LQALLNDPKQ 200
PLFQRYRAMF RLRDIGTDEA ILALATGFSA ESSLFKHEIA YVFGQIGSPA 250
AVPSLIEVLG RKEEAPMVRH EAAEALGAIA SPEVVDVLKS YLNDEVDVVR 300
ESCIVALDMY DYENSNELEY APTAN 325
Length:325
Mass (Da):36,165
Last modified:February 1, 1996 - v1
Checksum:iAB36A73B40466CD5
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z49570 Genomic DNA. Translation: CAA89598.1.
L47993 Genomic DNA. Translation: AAB39296.1.
BK006943 Genomic DNA. Translation: DAA08857.1.
PIRiS57089.
RefSeqiNP_012604.1. NM_001181728.1.

Genome annotation databases

EnsemblFungiiYJR070C; YJR070C; YJR070C.
GeneIDi853534.
KEGGisce:YJR070C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z49570 Genomic DNA. Translation: CAA89598.1 .
L47993 Genomic DNA. Translation: AAB39296.1 .
BK006943 Genomic DNA. Translation: DAA08857.1 .
PIRi S57089.
RefSeqi NP_012604.1. NM_001181728.1.

3D structure databases

ProteinModelPortali P47120.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 33827. 67 interactions.
DIPi DIP-2829N.
IntActi P47120. 6 interactions.
MINTi MINT-539495.
STRINGi 4932.YJR070C.

Proteomic databases

MaxQBi P47120.
PaxDbi P47120.
PeptideAtlasi P47120.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YJR070C ; YJR070C ; YJR070C .
GeneIDi 853534.
KEGGi sce:YJR070C.

Organism-specific databases

CYGDi YJR070c.
SGDi S000003831. LIA1.

Phylogenomic databases

eggNOGi COG1413.
GeneTreei ENSGT00500000044957.
HOGENOMi HOG000248665.
KOi K06072.
OMAi RESCQVA.
OrthoDBi EOG7QC85Z.

Enzyme and pathway databases

UniPathwayi UPA00354 .
BioCyci YEAST:G3O-31703-MONOMER.

Miscellaneous databases

NextBioi 974236.
PROi P47120.

Gene expression databases

Genevestigatori P47120.

Family and domain databases

Gene3Di 1.25.10.10. 1 hit.
HAMAPi MF_03101. Deoxyhypusine_hydroxylase.
InterProi IPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR027517. Deoxyhypusine_hydroxylase.
IPR004155. PBS_lyase_HEAT.
[Graphical view ]
Pfami PF03130. HEAT_PBS. 3 hits.
[Graphical view ]
SMARTi SM00567. EZ_HEAT. 5 hits.
[Graphical view ]
SUPFAMi SSF48371. SSF48371. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  7. 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.

Entry informationi

Entry nameiDOHH_YEAST
AccessioniPrimary (citable) accession number: P47120
Secondary accession number(s): D6VWP1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: September 3, 2014
This is version 128 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome X
    Yeast (Saccharomyces cerevisiae) chromosome X: entries and gene names

External Data

Dasty 3

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