P52788 (SPSY_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Spermine synthase
Short name=SPMSY
EC=2.5.1.22

Alternative name(s):
Spermidine aminopropyltransferase

Gene names

Name:

SMS

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	366 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the production of spermine from spermidine and decarboxylated S-adenosylmethionine (dcSAM).
Catalytic activity	S-adenosylmethioninamine + spermidine = 5'-methylthioadenosine + spermine.
Pathway	Amine and polyamine biosynthesis; spermine biosynthesis; spermine from spermidine: step 1/1.
Subunit structure	Homodimer. Dimerization is mediated through the N-terminal domain and seems to be required for activity as deletion of the N-terminal domain causes complete loss of activity. Ref.13
Domain	Composed of 3 domains: the N-terminal domain has structural similarity to S-adenosylmethionine decarboxylase, the central domain is made up of four beta strands and the C-terminal domain is similar in structure to spermidine synthase. The N- and C-terminal domains are both required for activity.
Involvement in disease	Defects in SMS are the cause of X-linked syndromic mental retardation Snyder-Robinson type (MRXSSR) [MIM:309583]. Characterized by moderate intellectual deficit, hypotonia, an unsteady gait, osteoporosis, kyphoscoliosis and facial asymmetry. Transmission is X-linked recessive. Ref.9
Sequence similarities	Belongs to the spermidine/spermine synthase family.

Ontologies

Keywords
Coding sequence diversity	Alternative splicing
Disease	Mental retardation
Molecular function	Transferase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	methionine metabolic process Traceable author statement. Source: ProtInc spermine biosynthetic process Inferred from electronic annotation. Source: InterPro
Cellular component	cytosol Traceable author statement. Source: Reactome
Molecular function	spermidine synthase activity Traceable author statement. Source: ProtInc spermine synthase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Alternative products

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

Isoform 1 (identifier: P52788-1)

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 2 (identifier: P52788-2)

The sequence of this isoform differs from the canonical sequence as follows:
     57-109: Missing.

Note: Gene prediction confirmed by EST data.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed

Chain

2 – 366

365

Spermine synthase

PRO_0000156538

Regions

Region

255 – 256

2

S-adenosylmethioninamine binding

Sites

Active site

276

1

Proton acceptor Probable

Binding site

148

1

S-adenosylmethioninamine

Binding site

177

1

Spermidine

Binding site

201

1

Spermidine

Binding site

220

1

S-adenosylmethioninamine

Binding site

351

1

Spermidine

Binding site

353

1

Spermidine

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.11

Modified residue

147

1

Phosphotyrosine Ref.10

Natural variations

Alternative sequence

57 – 109

53

Missing in isoform 2.

VSP_034406

Experimental info

Mutagenesis

201

1

D → A or N: 100,000-fold decrease in catalytic efficiency. Ref.13

Mutagenesis

276

1

D → N: 200,000-fold decrease in catalytic efficiency. Ref.13

Mutagenesis

353

1

E → Q: 800-fold decrease in catalytic efficiency. Ref.13

Sequence conflict

1

1

M → MPG in CAA88921. Ref.1

Secondary structure

1

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366

Helix Strand Turn

Details...

Beta strand

5 – 12

8

Helix

21 – 32

12

Beta strand

36 – 42

7

Turn

43 – 45

3

Beta strand

46 – 52

7

Beta strand

58 – 63

6

Beta strand

67 – 75

9

Helix

85 – 98

14

Beta strand

114 – 117

4

Beta strand

136 – 144

9

Beta strand

149 – 155

7

Turn

156 – 158

3

Beta strand

159 – 164

6

Beta strand

167 – 171

5

Helix

175 – 181

7

Turn

182 – 185

4

Beta strand

193 – 198

6

Helix

203 – 209

7

Beta strand

214 – 221

8

Helix

223 – 232

10

Beta strand

242 – 246

5

Beta strand

249 – 254

6

Helix

256 – 266

11

Beta strand

270 – 276

7

Helix

291 – 304

14

Beta strand

306 – 318

13

Helix

322 – 332

11

Beta strand

335 – 337

3

Beta strand

339 – 346

8

Helix

349 – 351

3

Beta strand

355 – 362

8

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 30, 2000. Version 2. Checksum: D5B23EF61DE66443	FASTA	366	41,268
	10 20 30 40 50 60 MAAARHSTLD FMLGAKADGE TILKGLQSIF QEQGMAESVH TWQDHGYLAT YTNKNGSFAN 70 80 90 100 110 120 LRIYPHGLVL LDLQSYDGDA QGKEEIDSIL NKVEERMKEL SQDSTGRVKR LPPIVRGGAI 130 140 150 160 170 180 DRYWPTADGR LVEYDIDEVV YDEDSPYQNI KILHSKQFGN ILILSGDVNL AESDLAYTRA 190 200 210 220 230 240 IMGSGKEDYT GKDVLILGGG DGGILCEIVK LKPKMVTMVE IDQMVIDGCK KYMRKTCGDV 250 260 270 280 290 300 LDNLKGDCYQ VLIEDCIPVL KRYAKEGREF DYVINDLTAV PISTSPEEDS TWEFLRLILD 310 320 330 340 350 360 LSMKVLKQDG KYFTQGNCVN LTEALSLYEE QLGRLYCPVE FSKEIVCVPS YLELWVFYTV WKKAKP
	Isoform 2 [UniParc]. Checksum: 7D237FC4CD55D3E6	FASTA	313	35,278
	10 20 30 40 50 60 MAAARHSTLD FMLGAKADGE TILKGLQSIF QEQGMAESVH TWQDHGYLAT YTNKNGRLPP 70 80 90 100 110 120 IVRGGAIDRY WPTADGRLVE YDIDEVVYDE DSPYQNIKIL HSKQFGNILI LSGDVNLAES 130 140 150 160 170 180 DLAYTRAIMG SGKEDYTGKD VLILGGGDGG ILCEIVKLKP KMVTMVEIDQ MVIDGCKKYM 190 200 210 220 230 240 RKTCGDVLDN LKGDCYQVLI EDCIPVLKRY AKEGREFDYV INDLTAVPIS TSPEEDSTWE 250 260 270 280 290 300 FLRLILDLSM KVLKQDGKYF TQGNCVNLTE ALSLYEEQLG RLYCPVEFSK EIVCVPSYLE 310 LWVFYTVWKK AKP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning of a cDNA encoding human spermine synthase." Korhonen V.-P., Halmekytoe M., Kauppinen L., Myoehaenen S., Wahlfors J., Keinaenen T., Hyvoenen T., Alhonen L., Eloranta T., Jaenne J. DNA Cell Biol. 14:841-847(1995) [PubMed: 7546290] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	"Sequence analysis of 139 kb in Xp22.1 containing spermine synthase and the 5' region of PEX." Grieff M., Whyte M.P., Thakker R.V., Mazzarella R. Genomics 44:227-231(1997) [PubMed: 9299240] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Colon.
[3]	"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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[4]	"The DNA sequence of the human X chromosome." Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R. Nature 434:325-337(2005) [PubMed: 15772651] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	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].
[6]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Kidney and Skin.
[7]	Eloranta T., Kajander O., Kauppinen L., Hyvoenen T., Linnala-Kankkunen A., Kalkkinen N., Kulomaa M., Alhonen L., Jaenne J. (In) Goldemberg S.H., Algranati I.D. (eds.); Proceedings of the international symposium on the biology and chemistry of polyamines, pp.91-98, ICSU Press, New York (1988) Cited for: PARTIAL PROTEIN SEQUENCE.
[8]	"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides." Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J. Nat. Biotechnol. 21:566-569(2003) [PubMed: 12665801] [Abstract] Cited for: PROTEIN SEQUENCE OF 97-107 (ISOFORM 1). Tissue: Platelet.
[9]	"X-linked spermine synthase gene (SMS) defect: the first polyamine deficiency syndrome." Cason A.L., Ikeguchi Y., Skinner C., Wood T.C., Holden K.R., Lubs H.A., Martinez F., Simensen R.J., Stevenson R.E., Pegg A.E., Schwartz C.E. Eur. J. Hum. Genet. 11:937-944(2003) [PubMed: 14508504] [Abstract] Cited for: INVOLVEMENT IN MRXSSR.
[10]	"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells." Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J. Nat. Biotechnol. 23:94-101(2005) [PubMed: 15592455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-147, MASS SPECTROMETRY.
[11]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[12]	"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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]	"Crystal structure of human spermine synthase: implications of substrate binding and catalytic mechanism." Wu H., Min J., Zeng H., McCloskey D.E., Ikeguchi Y., Loppnau P., Michael A.J., Pegg A.E., Plotnikov A.N. J. Biol. Chem. 283:16135-16146(2008) [PubMed: 18367445] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 5-366 (ISOFORM 1) IN COMPLEX WITH SPERMIDINE AND 5-METHYLTHIOADENOSINE, SUBUNIT, MUTAGENESIS OF ASP-201; ASP-276 AND GLU-353.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Z49099 mRNA. Translation: CAA88921.1.
AD001528 mRNA. Translation: AAB61308.1.
AK313834 mRNA. Translation: BAG36567.1.
U53331 Genomic DNA. Translation: AAD08634.1.
U73023 Genomic DNA. No translation available.
CH471074 Genomic DNA. Translation: EAW98984.1.
BC009898 mRNA. Translation: AAH09898.1.
BC085621 mRNA. Translation: AAH85621.1.

IPI

IPI00005102.
IPI00642393.

PIR

S54160.

RefSeq

NP_004586.2. NM_004595.3.

UniGene

Hs.727552.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3C6K	X-ray	1.95	A/B/C/D	5-366	[»]
3C6M	X-ray	2.45	A/B/C/D	5-366	[»]

ProteinModelPortal

P52788.

SMR

P52788. Positions 3-365.

ModBase

Search...

Protein-protein interaction databases

IntAct

P52788. 1 interaction.

MINT

MINT-5002620.

STRING

P52788.

PTM databases

PhosphoSite

P52788.

Polymorphism databases

DMDM

8247960.

2D gel databases

OGP

P52788.

Proteomic databases

PRIDE

P52788.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000404933; ENSP00000385746; ENSG00000102172.

GeneID

6611.

KEGG

hsa:6611.

NMPDR

fig|9606.3.peg.32544.

UCSC

uc004dag.1. human.

Organism-specific databases

CTD

6611.

GeneCards

GC0XP021958.

H-InvDB

HIX0016698.

HGNC

HGNC:11123. SMS.

HPA

HPA029849.
HPA029852.

MIM

300105. gene.
309583. phenotype.

neXtProt

NX_P52788.

Orphanet

3063. Intellectual deficit, X-linked, Snyder type.

PharmGKB

PA35972.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG05010.

GeneTree

ENSGT00530000063329.

HOGENOM

HBG445292.

HOVERGEN

HBG004512.

InParanoid

P52788.

OMA

PSYMELW.

OrthoDB

EOG479F7N.

PhylomeDB

P52788.

Enzyme and pathway databases

BioCyc

MetaCyc:MONOMER-11579.

Reactome

REACT_111217. Metabolism.

Gene expression databases

Bgee

P52788.

CleanEx

HS_SMS.

Genevestigator

P52788.

GermOnline

ENSG00000102172. Homo sapiens.

Family and domain databases

InterPro

IPR015576. Spermine_synthase-related.
IPR001045. Sprmine_synthase.
[Graphical view]

KO

K00802.

PANTHER

PTHR11558:SF1. Spermine_synth-rel. 1 hit.
PTHR11558. Sprmine_synthase. 1 hit.

Pfam

PF01564. Spermine_synth. 1 hit.
[Graphical view]

PROSITE

PS01330. SPERMIDINE_SYNTHASE_1. 1 hit.
PS51006. SPERMIDINE_SYNTHASE_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

DrugBank

DB00127. Spermine.

NextBio

25739.

SOURCE

Search...

Entry information

Entry name

SPSY_HUMAN

Accession

Primary (citable) accession number: P52788
Secondary accession number(s): A6NHA7 , A6NI34, B2R9M0, O00544, Q9UQS1

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	May 30, 2000
Last modified:	January 25, 2012
This is version 107 of the entry and version 2 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.