P49366 (DHYS_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Deoxyhypusine synthase
Short name=DHS
EC=2.5.1.46

Gene names

Name:	DHPS
Synonyms:	DS

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	369 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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 activity	[eIF5A-precursor]-lysine + spermidine = [eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine.
Cofactor	NAD.
Pathway	Protein modification; eIF5A hypusination.
Subunit structure	Homotetramer formed by a dimer of dimers. Ref.10 Ref.15 Ref.16
Sequence similarities	Belongs to the deoxyhypusine synthase family.

Ontologies

Keywords
Biological process	Hypusine biosynthesis
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	NAD
Molecular function	Transferase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	deoxyhypusine biosynthetic process from spermidine Traceable author statement Ref.2. Source: ProtInc peptidyl-lysine modification to hypusine Traceable author statement. Source: Reactome positive regulation of cell proliferation Traceable author statement Ref.2. Source: ProtInc post-translational protein modification Traceable author statement. Source: Reactome protein homotetramerization Inferred from electronic annotation. Source: Compara translation Traceable author statement Ref.1. Source: ProtInc
Cellular_component	cytosol Traceable author statement. Source: Reactome
Molecular_function	deoxyhypusine synthase activity Traceable author statement. Source: Reactome
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
NIF3L1	Q9GZT8	3	EBI-741925,EBI-740897
NUDT18	Q6ZVK8	3	EBI-741925,EBI-740486

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform Long (identifier: P49366-1)

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.

Isoform Short (identifier: P49366-2)

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

Note: Inactive.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 369

369

Deoxyhypusine synthase

PRO_0000134469

Regions

Nucleotide binding

105 – 109

5

NAD

Nucleotide binding

131 – 133

3

NAD

Nucleotide binding

308 – 309

2

NAD

Nucleotide binding

342 – 343

2

NAD

Region

136 – 137

2

Spermidine binding Probable

Region

314 – 316

3

Spermidine binding Probable

Region

323 – 329

7

Spermidine binding Probable

Sites

Active site

329

1

Nucleophile Ref.10

Binding site

137

1

NAD

Binding site

238

1

NAD

Binding site

243

1

Spermidine Probable

Binding site

283

1

NAD; via amide nitrogen

Binding site

288

1

Spermidine Probable

Amino acid modifications

Modified residue

78

1

Phosphoserine Ref.12 Ref.13

Natural variations

Alternative sequence

262 – 308

47

Missing in isoform Short.

VSP_001351

Natural variant

174

1

E → D.
Corresponds to variant rs10425108 [ dbSNP | Ensembl ].

VAR_043005

Experimental info

Mutagenesis

106

1

N → A: Strongly reduced NAD and spermidine binding. Reduced activity. Ref.11

Mutagenesis

109

1

S → A: Strongly reduced spermidine binding. Reduced activity. Ref.11

Mutagenesis

137

1

E → A: Strongly reduced NAD binding. Strongly reduced formation of covalent intermediate. Ref.11

Mutagenesis

238

1

D → A: Strongly reduced NAD binding. Strongly reduced formation of covalent intermediate. Ref.11

Mutagenesis

243

1

D → A: Reduces spermidine binding by 98%. Strongly reduced formation of covalent intermediate. Ref.11

Mutagenesis

287

1

K → A: Reduces covalent intermediate formation and deoxyhypusine synthesis by 99.5%. Retains low spermidine cleavage activity. Ref.10

Mutagenesis

288

1

H → A: Reduces spermidine binding by 98%. Strongly reduced NAD binding. Strongly reduced formation of covalent intermediate. Ref.11

Mutagenesis

305

1

Y → A: Strongly reduced NAD binding. No effect on enzyme activity. Ref.11

Mutagenesis

313

1

D → A: Strongly reduced NAD binding. Ref.11

Mutagenesis

316

1

D → A: Reduces spermidine binding by 98%. Loss of covalent intermediate formation and deoxyhypusine synthesis. Ref.11

Mutagenesis

317

1

S → A: Strongly reduced NAD binding. No effect on enzyme activity. Ref.11

Mutagenesis

323

1

E → A: Reduces spermidine binding by 98%. Strongly reduced formation of covalent intermediate. Ref.11

Mutagenesis

327

1

W → A: Reduces spermidine binding by 98%. Loss of covalent intermediate formation and deoxyhypusine synthesis. Ref.11

Mutagenesis

329

1

K → A or R: Loss of covalent intermediate formation and deoxyhypusine synthesis. Ref.10

Mutagenesis

342

1

D → A: Strongly reduced NAD binding. Strongly reduced activity. Ref.11

Sequence conflict

11

1

A → R in AAB02175. Ref.3

Sequence conflict

11

1

A → R in AAB02179. Ref.3

Sequence conflict

13 – 14

2

AL → R in AAB02175. Ref.3

Sequence conflict

13 – 14

2

AL → R in AAB02179. Ref.3

Sequence conflict

85

1

A → G in AAB02175. Ref.3

Sequence conflict

85

1

A → G in AAB02179. Ref.3

Sequence conflict

196

1

T → I in AAB02175. Ref.3

Sequence conflict

196

1

T → I in AAB02179. Ref.3

Sequence conflict

199

1

V → A in AAB02175. Ref.3

Sequence conflict

199

1

V → A in AAB02179. Ref.3

Sequence conflict

220

1

V → A in AAB02175. Ref.3

Sequence conflict

220

1

V → A in AAB02179. Ref.3

Sequence conflict

228

1

H → K AA sequence Ref.9

Sequence conflict

296 – 297

2

MR → SG in AAB02179. Ref.3

Sequence conflict

311

1

E → EE in AAB02179. Ref.3

Secondary structure

1

.

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369

Helix Strand Turn

Details...

Helix

11 – 17

7

Helix

36 – 38

3

Helix

42 – 47

6

Helix

48 – 51

4

Helix

54 – 73

20

Helix

79 – 85

7

Beta strand

96 – 103

8

Helix

106 – 109

4

Helix

112 – 121

10

Beta strand

126 – 130

5

Helix

132 – 140

9

Turn

141 – 143

3

Helix

155 – 160

6

Beta strand

163 – 166

4

Beta strand

169 – 172

4

Helix

174 – 196

23

Helix

203 – 214

12

Helix

220 – 226

7

Turn

234 – 237

4

Helix

240 – 251

12

Helix

260 – 271

12

Beta strand

274 – 282

9

Helix

284 – 295

12

Turn

296 – 298

3

Beta strand

299 – 307

9

Helix

321 – 327

7

Beta strand

337 – 341

5

Helix

343 – 353

11

Helix

355 – 358

4

Helix

359 – 365

7

Sequences

	Sequence		Length	Mass (Da)
	Isoform Long [UniParc]. Last modified February 1, 1996. Version 1. Checksum: 5314FED620AC9EE7	FASTA	369	40,971
	10 20 30 40 50 60 MEGSLEREAP AGALAAVLKH SSTLPPESTQ VRGYDFNRGV NYRALLEAFG TTGFQATNFG 70 80 90 100 110 120 RAVQQVNAMI EKKLEPLSQD EDQHADLTQS RRPLTSCTIF LGYTSNLISS GIRETIRYLV 130 140 150 160 170 180 QHNMVDVLVT TAGGVEEDLI KCLAPTYLGE FSLRGKELRE NGINRIGNLL VPNENYCKFE 190 200 210 220 230 240 DWLMPILDQM VMEQNTEGVK WTPSKMIARL GKEINNPESV YYWAQKNHIP VFSPALTDGS 250 260 270 280 290 300 LGDMIFFHSY KNPGLVLDIV EDLRLINTQA IFAKCTGMII LGGGVVKHHI ANANLMRNGA 310 320 330 340 350 360 DYAVYINTAQ EFDGSDSGAR PDEAVSWGKI RVDAQPVKVY ADASLVFPLL VAETFAQKMD AFMHEKNED
	Isoform Short [UniParc]. Checksum: 1F44CC2AB89F7A2E	FASTA	322	35,916
	10 20 30 40 50 60 MEGSLEREAP AGALAAVLKH SSTLPPESTQ VRGYDFNRGV NYRALLEAFG TTGFQATNFG 70 80 90 100 110 120 RAVQQVNAMI EKKLEPLSQD EDQHADLTQS RRPLTSCTIF LGYTSNLISS GIRETIRYLV 130 140 150 160 170 180 QHNMVDVLVT TAGGVEEDLI KCLAPTYLGE FSLRGKELRE NGINRIGNLL VPNENYCKFE 190 200 210 220 230 240 DWLMPILDQM VMEQNTEGVK WTPSKMIARL GKEINNPESV YYWAQKNHIP VFSPALTDGS 250 260 270 280 290 300 LGDMIFFHSY KNPGLVLDIV EAQEFDGSDS GARPDEAVSW GKIRVDAQPV KVYADASLVF 310 320 PLLVAETFAQ KMDAFMHEKN ED

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"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.
[7]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	"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.
[9]	"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.
[10]	"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.
[11]	"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.
[12]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-78, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[13]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]	"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.
[16]	"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, MASS SPECTROMETRY, SUBUNIT.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.
AK291553 mRNA. Translation: BAF84242.1.
CH471106 Genomic DNA. Translation: EAW84288.1.
BC000333 mRNA. Translation: AAH00333.1.
BC014016 mRNA. Translation: AAH14016.1.

IPI

IPI00026829.
IPI00215771.

PIR

S68692.

RefSeq

NP_001921.1. NM_001930.3.
NP_037538.1. NM_013406.2.

UniGene

Hs.79064.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P49366.

ModBase

Search...

Protein-protein interaction databases

IntAct

P49366. 5 interactions.

MINT

MINT-1436761.

STRING

9606.ENSP00000210060.

PTM databases

PhosphoSite

P49366.

Polymorphism databases

DMDM

1352267.

Proteomic databases

PaxDb

P49366.

PRIDE

P49366.

Protocols and materials databases

DNASU

1725.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000210060; ENSP00000210060; ENSG00000095059.
ENST00000351660; ENSP00000221303; ENSG00000095059.

GeneID

1725.

KEGG

hsa:1725.

UCSC

uc002mug.2. human.
uc002mui.2. human.

Organism-specific databases

CTD

1725.

GeneCards

GC19M012786.

HGNC

HGNC:2869. DHPS.

HPA

HPA014461.
HPA029413.

MIM

600944. gene.

neXtProt

NX_P49366.

PharmGKB

PA27329.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG1899.

HOGENOM

HOG000228838.

HOVERGEN

HBG000852.

InParanoid

P49366.

KO

K00809.

OMA

DTYIDED.

OrthoDB

EOG405S18.

Enzyme and pathway databases

BioCyc

MetaCyc:HS01810-MONOMER.

Reactome

REACT_17015. Metabolism of proteins.

SABIO-RK

P49366.

UniPathway

UPA00354.

Gene expression databases

Bgee

P49366.

CleanEx

HS_DHPS.

Genevestigator

P49366.

GermOnline

ENSG00000095059. Homo sapiens.

Family and domain databases

Gene3D

3.40.910.10. 1 hit.

InterPro

IPR002773. Deoxyhypusine_synthase.
[Graphical view]

PANTHER

PTHR11703. PTHR11703. 1 hit.

Pfam

PF01916. DS. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00321. dhys. 1 hit.

ProtoNet

Search...

Other

ChEMBL

CHEMBL4415.

DrugBank

DB01299. Sulfadoxine.

EvolutionaryTrace

P49366.

GenomeRNAi

1725.

NextBio

6975.

SOURCE

Search...

Entry information

Entry name

DHYS_HUMAN

Accession

Primary (citable) accession number: P49366
Secondary accession number(s): A8K688 , Q13184, Q13276, Q9UDG0

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	February 1, 1996
Last modified:	May 1, 2013
This is version 129 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.