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P49366

- DHYS_HUMAN

UniProt

P49366 - DHYS_HUMAN

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Protein

Deoxyhypusine synthase

Gene

DHPS

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

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

GO - Biological processi

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

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
Complete GO annotation...

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

BgeeiP49366.
CleanExiHS_DHPS.
ExpressionAtlasiP49366. baseline and differential.
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. 30 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 – 177Combined sources
Helixi36 – 383Combined sources
Helixi42 – 476Combined sources
Helixi48 – 514Combined sources
Helixi54 – 7320Combined sources
Helixi79 – 857Combined sources
Beta strandi96 – 1038Combined sources
Helixi106 – 1094Combined sources
Helixi112 – 12110Combined sources
Beta strandi126 – 1305Combined sources
Helixi132 – 1409Combined sources
Turni141 – 1433Combined sources
Helixi155 – 1606Combined sources
Beta strandi163 – 1664Combined sources
Beta strandi169 – 1724Combined sources
Helixi174 – 19623Combined sources
Helixi203 – 21412Combined sources
Helixi220 – 2267Combined sources
Turni234 – 2374Combined sources
Helixi240 – 25112Combined sources
Helixi260 – 27112Combined sources
Beta strandi274 – 2829Combined sources
Helixi284 – 29512Combined sources
Turni296 – 2983Combined sources
Beta strandi299 – 3079Combined sources
Helixi321 – 3277Combined sources
Beta strandi337 – 3415Combined sources
Helixi343 – 35311Combined sources
Helixi355 – 3584Combined sources
Helixi359 – 3657Combined sources

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.
GeneTreeiENSGT00390000008063.
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

        10         20         30         40         50
MEGSLEREAP AGALAAVLKH SSTLPPESTQ VRGYDFNRGV NYRALLEAFG
60 70 80 90 100
TTGFQATNFG RAVQQVNAMI EKKLEPLSQD EDQHADLTQS RRPLTSCTIF
110 120 130 140 150
LGYTSNLISS GIRETIRYLV QHNMVDVLVT TAGGVEEDLI KCLAPTYLGE
160 170 180 190 200
FSLRGKELRE NGINRIGNLL VPNENYCKFE DWLMPILDQM VMEQNTEGVK
210 220 230 240 250
WTPSKMIARL GKEINNPESV YYWAQKNHIP VFSPALTDGS LGDMIFFHSY
260 270 280 290 300
KNPGLVLDIV EDLRLINTQA IFAKCTGMII LGGGVVKHHI ANANLMRNGA
310 320 330 340 350
DYAVYINTAQ EFDGSDSGAR PDEAVSWGKI RVDAQPVKVY ADASLVFPLL
360
VAETFAQKMD AFMHEKNED
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. 30 interactions.
IntActi P49366. 7 interactions.
MINTi MINT-1436761.
STRINGi 9606.ENSP00000210060.

Chemistry

ChEMBLi CHEMBL4415.

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.
GeneTreei ENSGT00390000008063.
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

Bgeei P49366.
CleanExi HS_DHPS.
ExpressionAtlasi P49366. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 145 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