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P49366

- DHYS_HUMAN

UniProt

P49366 - DHYS_HUMAN

Protein

Deoxyhypusine synthase

Gene

DHPS

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 144 (01 Oct 2014)
      Sequence version 1 (01 Feb 1996)
      Previous versions | rss
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    Functioni

    Catalyzes the NAD-dependent oxidative cleavage of spermidine and the subsequent transfer of the butylamine moiety of spermidine to the epsilon-amino group of a specific lysine residue of the eIF-5A precursor protein to form the intermediate deoxyhypusine residue.

    Catalytic activityi

    [eIF5A-precursor]-lysine + spermidine = [eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine.

    Cofactori

    NAD.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei137 – 1371NAD1 Publication
    Binding sitei238 – 2381NAD1 Publication
    Binding sitei243 – 2431SpermidineCurated
    Binding sitei283 – 2831NAD; via amide nitrogen1 Publication
    Binding sitei288 – 2881SpermidineCurated
    Active sitei329 – 3291Nucleophile1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi105 – 1095NAD1 Publication
    Nucleotide bindingi131 – 1333NAD1 Publication
    Nucleotide bindingi308 – 3092NAD1 Publication
    Nucleotide bindingi342 – 3432NAD1 Publication

    GO - Molecular functioni

    1. deoxyhypusine synthase activity Source: Reactome
    2. protein binding Source: UniProtKB

    GO - Biological processi

    1. cellular protein metabolic process Source: Reactome
    2. deoxyhypusine biosynthetic process from spermidine Source: ProtInc
    3. peptidyl-lysine modification to peptidyl-hypusine Source: Reactome
    4. positive regulation of cell proliferation Source: ProtInc
    5. post-translational protein modification Source: Reactome
    6. protein homotetramerization Source: Ensembl
    7. translation Source: ProtInc

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    Hypusine biosynthesis

    Keywords - Ligandi

    NAD

    Enzyme and pathway databases

    BioCyciMetaCyc:HS01810-MONOMER.
    ReactomeiREACT_12469. Hypusine synthesis from eIF5A-lysine.
    SABIO-RKP49366.
    UniPathwayiUPA00354.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Deoxyhypusine synthase (EC:2.5.1.46)
    Short name:
    DHS
    Gene namesi
    Name:DHPS
    Synonyms:DS
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:2869. DHPS.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi106 – 1061N → A: Strongly reduced NAD and spermidine binding. Reduced activity. 1 Publication
    Mutagenesisi109 – 1091S → A: Strongly reduced spermidine binding. Reduced activity. 1 Publication
    Mutagenesisi137 – 1371E → A: Strongly reduced NAD binding. Strongly reduced formation of covalent intermediate. 1 Publication
    Mutagenesisi238 – 2381D → A: Strongly reduced NAD binding. Strongly reduced formation of covalent intermediate. 1 Publication
    Mutagenesisi243 – 2431D → A: Reduces spermidine binding by 98%. Strongly reduced formation of covalent intermediate. 1 Publication
    Mutagenesisi287 – 2871K → A: Reduces covalent intermediate formation and deoxyhypusine synthesis by 99.5%. Retains low spermidine cleavage activity. 1 Publication
    Mutagenesisi288 – 2881H → A: Reduces spermidine binding by 98%. Strongly reduced NAD binding. Strongly reduced formation of covalent intermediate. 1 Publication
    Mutagenesisi305 – 3051Y → A: Strongly reduced NAD binding. No effect on enzyme activity. 1 Publication
    Mutagenesisi313 – 3131D → A: Strongly reduced NAD binding. 1 Publication
    Mutagenesisi316 – 3161D → A: Reduces spermidine binding by 98%. Loss of covalent intermediate formation and deoxyhypusine synthesis. 1 Publication
    Mutagenesisi317 – 3171S → A: Strongly reduced NAD binding. No effect on enzyme activity. 1 Publication
    Mutagenesisi323 – 3231E → A: Reduces spermidine binding by 98%. Strongly reduced formation of covalent intermediate. 1 Publication
    Mutagenesisi327 – 3271W → A: Reduces spermidine binding by 98%. Loss of covalent intermediate formation and deoxyhypusine synthesis. 1 Publication
    Mutagenesisi329 – 3291K → A or R: Loss of covalent intermediate formation and deoxyhypusine synthesis. 1 Publication
    Mutagenesisi342 – 3421D → A: Strongly reduced NAD binding. Strongly reduced activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA27329.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 369369Deoxyhypusine synthasePRO_0000134469Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei78 – 781Phosphoserine2 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP49366.
    PaxDbiP49366.
    PRIDEiP49366.

    PTM databases

    PhosphoSiteiP49366.

    Expressioni

    Gene expression databases

    ArrayExpressiP49366.
    BgeeiP49366.
    CleanExiHS_DHPS.
    GenevestigatoriP49366.

    Organism-specific databases

    HPAiHPA014461.
    HPA029413.

    Interactioni

    Subunit structurei

    Homotetramer formed by a dimer of dimers.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    NIF3L1Q9GZT83EBI-741925,EBI-740897
    NUDT18Q6ZVK83EBI-741925,EBI-740486

    Protein-protein interaction databases

    BioGridi108070. 24 interactions.
    IntActiP49366. 7 interactions.
    MINTiMINT-1436761.
    STRINGi9606.ENSP00000210060.

    Structurei

    Secondary structure

    1
    369
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi11 – 177
    Helixi36 – 383
    Helixi42 – 476
    Helixi48 – 514
    Helixi54 – 7320
    Helixi79 – 857
    Beta strandi96 – 1038
    Helixi106 – 1094
    Helixi112 – 12110
    Beta strandi126 – 1305
    Helixi132 – 1409
    Turni141 – 1433
    Helixi155 – 1606
    Beta strandi163 – 1664
    Beta strandi169 – 1724
    Helixi174 – 19623
    Helixi203 – 21412
    Helixi220 – 2267
    Turni234 – 2374
    Helixi240 – 25112
    Helixi260 – 27112
    Beta strandi274 – 2829
    Helixi284 – 29512
    Turni296 – 2983
    Beta strandi299 – 3079
    Helixi321 – 3277
    Beta strandi337 – 3415
    Helixi343 – 35311
    Helixi355 – 3584
    Helixi359 – 3657

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1DHSX-ray2.20A9-369[»]
    1RLZX-ray2.15A1-369[»]
    1ROZX-ray2.21A/B1-369[»]
    1RQDX-ray3.00A/B1-369[»]
    ProteinModelPortaliP49366.
    SMRiP49366. Positions 28-364.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP49366.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni136 – 1372Spermidine bindingCurated
    Regioni314 – 3163Spermidine bindingCurated
    Regioni323 – 3297Spermidine bindingCurated

    Sequence similaritiesi

    Belongs to the deoxyhypusine synthase family.Curated

    Phylogenomic databases

    eggNOGiCOG1899.
    HOGENOMiHOG000228838.
    HOVERGENiHBG000852.
    InParanoidiP49366.
    KOiK00809.
    OMAiKRAGMII.
    PhylomeDBiP49366.
    TreeFamiTF300625.

    Family and domain databases

    Gene3Di3.40.910.10. 1 hit.
    InterProiIPR002773. Deoxyhypusine_synthase.
    IPR029035. DHS-like_NAD/FAD-binding_dom.
    [Graphical view]
    PANTHERiPTHR11703. PTHR11703. 1 hit.
    PfamiPF01916. DS. 1 hit.
    [Graphical view]
    SUPFAMiSSF52467. SSF52467. 1 hit.
    TIGRFAMsiTIGR00321. dhys. 1 hit.

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform Long (identifier: P49366-1) [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

    MEGSLEREAP AGALAAVLKH SSTLPPESTQ VRGYDFNRGV NYRALLEAFG    50
    TTGFQATNFG RAVQQVNAMI EKKLEPLSQD EDQHADLTQS RRPLTSCTIF 100
    LGYTSNLISS GIRETIRYLV QHNMVDVLVT TAGGVEEDLI KCLAPTYLGE 150
    FSLRGKELRE NGINRIGNLL VPNENYCKFE DWLMPILDQM VMEQNTEGVK 200
    WTPSKMIARL GKEINNPESV YYWAQKNHIP VFSPALTDGS LGDMIFFHSY 250
    KNPGLVLDIV EDLRLINTQA IFAKCTGMII LGGGVVKHHI ANANLMRNGA 300
    DYAVYINTAQ EFDGSDSGAR PDEAVSWGKI RVDAQPVKVY ADASLVFPLL 350
    VAETFAQKMD AFMHEKNED 369
    Length:369
    Mass (Da):40,971
    Last modified:February 1, 1996 - v1
    Checksum:i5314FED620AC9EE7
    GO
    Isoform Short (identifier: P49366-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         262-308: Missing.

    Note: Inactive.

    Show »
    Length:322
    Mass (Da):35,916
    Checksum:i1F44CC2AB89F7A2E
    GO
    Isoform 3 (identifier: P49366-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-68: MEGSLEREAP...FGRAVQQVNA → MPIIPAFWEAEAGGSREEEFETSLAN

    Note: No experimental confirmation available.

    Show »
    Length:327
    Mass (Da):36,583
    Checksum:i313374BBDB63A758
    GO

    Sequence cautioni

    The sequence AL520040 differs from that shown. Reason: Frameshift at positions 329, 344 and 355.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti11 – 111A → R in AAB02175. (PubMed:8615810)Curated
    Sequence conflicti11 – 111A → R in AAB02179. (PubMed:8615810)Curated
    Sequence conflicti13 – 142AL → R in AAB02175. (PubMed:8615810)Curated
    Sequence conflicti13 – 142AL → R in AAB02179. (PubMed:8615810)Curated
    Sequence conflicti85 – 851A → G in AAB02175. (PubMed:8615810)Curated
    Sequence conflicti85 – 851A → G in AAB02179. (PubMed:8615810)Curated
    Sequence conflicti196 – 1961T → I in AAB02175. (PubMed:8615810)Curated
    Sequence conflicti196 – 1961T → I in AAB02179. (PubMed:8615810)Curated
    Sequence conflicti199 – 1991V → A in AAB02175. (PubMed:8615810)Curated
    Sequence conflicti199 – 1991V → A in AAB02179. (PubMed:8615810)Curated
    Sequence conflicti220 – 2201V → A in AAB02175. (PubMed:8615810)Curated
    Sequence conflicti220 – 2201V → A in AAB02179. (PubMed:8615810)Curated
    Sequence conflicti228 – 2281H → K AA sequence (PubMed:7750572)Curated
    Sequence conflicti296 – 2972MR → SG in AAB02179. (PubMed:8615810)Curated
    Sequence conflicti311 – 3111E → EE in AAB02179. (PubMed:8615810)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti174 – 1741E → D.
    Corresponds to variant rs10425108 [ dbSNP | Ensembl ].
    VAR_043005

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 6868MEGSL…QQVNA → MPIIPAFWEAEAGGSREEEF ETSLAN in isoform 3. 1 PublicationVSP_047564Add
    BLAST
    Alternative sequencei262 – 30847Missing in isoform Short. 1 PublicationVSP_001351Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L39068 mRNA. Translation: AAA86282.1.
    U40579 mRNA. Translation: AAA96151.1.
    U32178 mRNA. Translation: AAB02179.1.
    U26266 mRNA. Translation: AAB02175.1.
    AJ001701
    , AJ001702, AJ001703, AJ001704 Genomic DNA. Translation: CAA04940.1.
    U79262 mRNA. Translation: AAB50208.1.
    AL520040 mRNA. No translation available.
    AK291553 mRNA. Translation: BAF84242.1.
    AC010422 Genomic DNA. No translation available.
    CH471106 Genomic DNA. Translation: EAW84288.1.
    BC000333 mRNA. Translation: AAH00333.1.
    BC014016 mRNA. Translation: AAH14016.1.
    CCDSiCCDS12276.1. [P49366-1]
    CCDS12277.1. [P49366-2]
    CCDS59354.1. [P49366-3]
    PIRiS68692.
    RefSeqiNP_001193903.1. NM_001206974.1. [P49366-3]
    NP_001921.1. NM_001930.3. [P49366-1]
    NP_037538.1. NM_013406.2. [P49366-2]
    UniGeneiHs.79064.

    Genome annotation databases

    EnsembliENST00000210060; ENSP00000210060; ENSG00000095059. [P49366-1]
    ENST00000351660; ENSP00000221303; ENSG00000095059. [P49366-2]
    ENST00000594424; ENSP00000471886; ENSG00000095059. [P49366-3]
    GeneIDi1725.
    KEGGihsa:1725.
    UCSCiuc002mug.2. human. [P49366-1]
    uc002mui.2. human. [P49366-2]

    Polymorphism databases

    DMDMi1352267.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L39068 mRNA. Translation: AAA86282.1 .
    U40579 mRNA. Translation: AAA96151.1 .
    U32178 mRNA. Translation: AAB02179.1 .
    U26266 mRNA. Translation: AAB02175.1 .
    AJ001701
    , AJ001702 , AJ001703 , AJ001704 Genomic DNA. Translation: CAA04940.1 .
    U79262 mRNA. Translation: AAB50208.1 .
    AL520040 mRNA. No translation available.
    AK291553 mRNA. Translation: BAF84242.1 .
    AC010422 Genomic DNA. No translation available.
    CH471106 Genomic DNA. Translation: EAW84288.1 .
    BC000333 mRNA. Translation: AAH00333.1 .
    BC014016 mRNA. Translation: AAH14016.1 .
    CCDSi CCDS12276.1. [P49366-1 ]
    CCDS12277.1. [P49366-2 ]
    CCDS59354.1. [P49366-3 ]
    PIRi S68692.
    RefSeqi NP_001193903.1. NM_001206974.1. [P49366-3 ]
    NP_001921.1. NM_001930.3. [P49366-1 ]
    NP_037538.1. NM_013406.2. [P49366-2 ]
    UniGenei Hs.79064.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1DHS X-ray 2.20 A 9-369 [» ]
    1RLZ X-ray 2.15 A 1-369 [» ]
    1ROZ X-ray 2.21 A/B 1-369 [» ]
    1RQD X-ray 3.00 A/B 1-369 [» ]
    ProteinModelPortali P49366.
    SMRi P49366. Positions 28-364.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108070. 24 interactions.
    IntActi P49366. 7 interactions.
    MINTi MINT-1436761.
    STRINGi 9606.ENSP00000210060.

    Chemistry

    ChEMBLi CHEMBL4415.
    DrugBanki DB01299. Sulfadoxine.

    PTM databases

    PhosphoSitei P49366.

    Polymorphism databases

    DMDMi 1352267.

    Proteomic databases

    MaxQBi P49366.
    PaxDbi P49366.
    PRIDEi P49366.

    Protocols and materials databases

    DNASUi 1725.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000210060 ; ENSP00000210060 ; ENSG00000095059 . [P49366-1 ]
    ENST00000351660 ; ENSP00000221303 ; ENSG00000095059 . [P49366-2 ]
    ENST00000594424 ; ENSP00000471886 ; ENSG00000095059 . [P49366-3 ]
    GeneIDi 1725.
    KEGGi hsa:1725.
    UCSCi uc002mug.2. human. [P49366-1 ]
    uc002mui.2. human. [P49366-2 ]

    Organism-specific databases

    CTDi 1725.
    GeneCardsi GC19M012786.
    HGNCi HGNC:2869. DHPS.
    HPAi HPA014461.
    HPA029413.
    MIMi 600944. gene.
    neXtProti NX_P49366.
    PharmGKBi PA27329.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1899.
    HOGENOMi HOG000228838.
    HOVERGENi HBG000852.
    InParanoidi P49366.
    KOi K00809.
    OMAi KRAGMII.
    PhylomeDBi P49366.
    TreeFami TF300625.

    Enzyme and pathway databases

    UniPathwayi UPA00354 .
    BioCyci MetaCyc:HS01810-MONOMER.
    Reactomei REACT_12469. Hypusine synthesis from eIF5A-lysine.
    SABIO-RK P49366.

    Miscellaneous databases

    EvolutionaryTracei P49366.
    GeneWikii DHPS.
    GenomeRNAii 1725.
    NextBioi 6975.
    PROi P49366.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P49366.
    Bgeei P49366.
    CleanExi HS_DHPS.
    Genevestigatori P49366.

    Family and domain databases

    Gene3Di 3.40.910.10. 1 hit.
    InterProi IPR002773. Deoxyhypusine_synthase.
    IPR029035. DHS-like_NAD/FAD-binding_dom.
    [Graphical view ]
    PANTHERi PTHR11703. PTHR11703. 1 hit.
    Pfami PF01916. DS. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52467. SSF52467. 1 hit.
    TIGRFAMsi TIGR00321. dhys. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and expression of human deoxyhypusine synthase cDNA. Structure-function studies with the recombinant enzyme and mutant proteins."
      Joe Y.A., Wolff E.C., Park M.H.
      J. Biol. Chem. 270:22386-22392(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
    2. "Molecular characterization of a cDNA encoding functional human deoxyhypusine synthase and chromosomal mapping of the corresponding gene locus."
      Bevec D., Kappel B., Jaksche H., Csonga R., Hauber J., Klier H., Steinkasserer A.
      FEBS Lett. 378:195-198(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
      Tissue: Blood.
    3. "Molecular cloning and functional expression of human deoxyhypusine synthase cDNA based on expressed sequence tag information."
      Yan Y.P., Tao Y., Chen K.Y.
      Biochem. J. 315:429-434(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT).
    4. "Localization and genomic structure of human deoxyhypusine synthase gene on chromosome 19p13.2-distal 19p13.1."
      Mantuano E., Trettel F., Olsen A.S., Lennin G., Frontali M., Jodice C.
      Gene 215:153-157(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    5. "Large-scale concatenation cDNA sequencing."
      Yu W., Andersson B., Worley K.C., Muzny D.M., Ding Y., Liu W., Ricafrente J.Y., Wentland M.A., Lennon G., Gibbs R.A.
      Genome Res. 7:353-358(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
      Tissue: Brain.
    6. "Full-length cDNA libraries and normalization."
      Li W.B., Gruber C., Jessee J., Polayes D.
      Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
      Tissue: Neuroblastoma.
    7. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
      Tissue: Placenta.
    8. "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].
    9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    10. "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 LONG).
      Tissue: Brain and Lung.
    11. "Purification and characterization of human deoxyhypusine synthase from HeLa cells."
      Klier H., Csonga R., Steinkasserer A., Woehl T., Lottspeich F., Eder J.
      FEBS Lett. 364:207-210(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 184-189; 192-204; 206-232 AND 278-296 (ISOFORM LONG).
      Tissue: Cervix carcinoma.
    12. "Enzyme-substrate intermediate at a specific lysine residue is required for deoxyhypusine synthesis. The role of Lys329 in human deoxyhypusine synthase."
      Joe Y.A., Wolff E.C., Lee Y.B., Park M.H.
      J. Biol. Chem. 272:32679-32685(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF LYS-287 AND LYS-329, SUBUNIT, ACTIVE SITE.
    13. "Structure-function studies of human deoxyhypusine synthase: identification of amino acid residues critical for the binding of spermidine and NAD."
      Lee C.H., Um P.Y., Park M.H.
      Biochem. J. 355:841-849(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF ASN-106; SER-109; GLU-137; ASP-238; ASP-243; HIS-288; TYR-305; ASP-313; ASP-316; SER-317; GLU-323; TRP-327 AND ASP-342.
    14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-78, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    15. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-78, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "Crystal structure of the NAD complex of human deoxyhypusine synthase: an enzyme with a ball-and-chain mechanism for blocking the active site."
      Liao D.-I., Wolff E.C., Park M.H., Davies D.R.
      Structure 6:23-32(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH NAD, SUBUNIT.
    18. "A new crystal structure of deoxyhypusine synthase reveals the configuration of the active enzyme and of an enzyme.NAD.inhibitor ternary complex."
      Umland T.C., Wolff E.C., Park M.H., Davies D.R.
      J. Biol. Chem. 279:28697-28705(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) IN COMPLEXES WITH NAD AND COMPETITIVE INHIBITOR, IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT.

    Entry informationi

    Entry nameiDHYS_HUMAN
    AccessioniPrimary (citable) accession number: P49366
    Secondary accession number(s): A8K688
    , M0R1I5, Q13184, Q13276, Q9UDG0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: February 1, 1996
    Last modified: October 1, 2014
    This is version 144 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. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3