P21953 (ODBB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
2-oxoisovalerate dehydrogenase subunit beta, mitochondrial
EC=1.2.4.4

Alternative name(s):
Branched-chain alpha-keto acid dehydrogenase E1 component beta chain
Short name=BCKDE1B
Short name=BCKDH E1-beta

Gene names

Name:

BCKDHB

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	392 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	The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO2. It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3).
Catalytic activity	3-methyl-2-oxobutanoate + [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] lipoyllysine = [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(2-methylpropanoyl)dihydrolipoyllysine + CO2.
Subunit structure	Heterotetramer of 2 alpha and 2 beta chains.
Subcellular location	Mitochondrion matrix.
Involvement in disease	Maple syrup urine disease type IB (MSUD1B) [MIM:248600]: Autosomal recessive disorder characterized by mental and physical retardation, feeding problems, and a maple syrup odor to the urine. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.12 Ref.13 Ref.14

Ontologies

Keywords
Cellular component	Mitochondrion
Coding sequence diversity	Polymorphism
Disease	Disease mutation Maple syrup urine disease
Domain	Transit peptide
Molecular function	Oxidoreductase
PTM	Acetylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	branched-chain amino acid catabolic process Inferred from mutant phenotype PubMed 2022752. Source: HGNC cellular nitrogen compound metabolic process Traceable author statement. Source: Reactome response to cAMP Inferred from electronic annotation. Source: Compara response to glucocorticoid stimulus Inferred from electronic annotation. Source: Compara response to nutrient Inferred from electronic annotation. Source: Compara
Cellular_component	mitochondrial alpha-ketoglutarate dehydrogenase complex Inferred from mutant phenotype PubMed 2022752. Source: HGNC
Molecular_function	3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) activity Traceable author statement Ref.1. Source: ProtInc alpha-ketoacid dehydrogenase activity Inferred from electronic annotation. Source: Compara carboxy-lyase activity Traceable author statement PubMed 11839747. Source: HGNC
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
BCKDHA	P12694	14	EBI-1029067,EBI-1029053

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 50

50

Mitochondrion

Chain

51 – 392

342

2-oxoisovalerate dehydrogenase subunit beta, mitochondrial

PRO_0000020470

Amino acid modifications

Modified residue

241

1

N6-acetyllysine Ref.10

Natural variations

Natural variant

41

1

T → I.
Corresponds to variant rs35470366 [ dbSNP | Ensembl ].

VAR_050437

Natural variant

170

1

R → H in MSUD1B. Ref.14

VAR_068348

Natural variant

183

1

R → P in MSUD1B. Ref.13
Corresponds to variant rs28934895 [ dbSNP | Ensembl ].

VAR_024851

Natural variant

206

1

H → R in MSUD1B. Ref.12

VAR_004974

Natural variant

278

1

G → S in MSUD1B. Ref.13

VAR_024852

Natural variant

346

1

Q → R in MSUD1B. Ref.14

VAR_068349

Experimental info

Sequence conflict

20 – 23

4

EGHW → RLPP Ref.8

Sequence conflict

322

1

T → S in CAA36685. Ref.8

Secondary structure

1

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392

Helix Strand Turn

Details...

Beta strand

68 – 71

4

Helix

73 – 87

15

Beta strand

92 – 95

4

Turn

96 – 101

6

Turn

106 – 109

4

Helix

110 – 114

5

Turn

116 – 118

3

Beta strand

119 – 121

3

Helix

126 – 138

13

Beta strand

143 – 146

4

Helix

150 – 152

3

Helix

154 – 156

3

Helix

157 – 161

5

Helix

164 – 166

3

Helix

167 – 170

4

Turn

171 – 173

3

Beta strand

180 – 187

8

Helix

193 – 195

3

Helix

201 – 205

5

Beta strand

211 – 213

3

Helix

218 – 230

13

Beta strand

231 – 233

3

Beta strand

235 – 240

6

Helix

241 – 243

3

Turn

244 – 246

3

Beta strand

249 – 254

6

Beta strand

264 – 267

4

Beta strand

270 – 276

7

Helix

280 – 295

16

Beta strand

299 – 303

5

Beta strand

306 – 309

4

Helix

312 – 322

11

Beta strand

325 – 333

9

Helix

337 – 349

13

Helix

350 – 352

3

Beta strand

358 – 362

5

Helix

372 – 375

4

Helix

379 – 390

12

Sequences

	Sequence		Length	Mass (Da)
	P21953 [UniParc]. Last modified August 1, 1992. Version 2. Checksum: D78097834D063BB7	FASTA	392	43,122
	10 20 30 40 50 60 MAVVAAAAGW LLRLRAAGAE GHWRRLPGAG LARGFLHPAA TVEDAAQRRQ VAHFTFQPDP 70 80 90 100 110 120 EPREYGQTQK MNLFQSVTSA LDNSLAKDPT AVIFGEDVAF GGVFRCTVGL RDKYGKDRVF 130 140 150 160 170 180 NTPLCEQGIV GFGIGIAVTG ATAIAEIQFA DYIFPAFDQI VNEAAKYRYR SGDLFNCGSL 190 200 210 220 230 240 TIRSPWGCVG HGALYHSQSP EAFFAHCPGI KVVIPRSPFQ AKGLLLSCIE DKNPCIFFEP 250 260 270 280 290 300 KILYRAAAEE VPIEPYNIPL SQAEVIQEGS DVTLVAWGTQ VHVIREVASM AKEKLGVSCE 310 320 330 340 350 360 VIDLRTIIPW DVDTICKSVI KTGRLLISHE APLTGGFASE ISSTVQEECF LNLEAPISRV 370 380 390 CGYDTPFPHI FEPFYIPDKW KCYDALRKMI NY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Maple syrup urine disease. Complete primary structure of the E1 beta subunit of human branched chain alpha-ketoacid dehydrogenase complex deduced from the nucleotide sequence and a gene analysis of patients with this disease." Matsuda I., Asaka J., Akaboshi I., Endo F., Mitsubuchi H., Nobukuni Y. J. Clin. Invest. 86:242-247(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Maple syrup urine disease: the E1beta gene of human branched-chain alpha-ketoacid dehydrogenase complex has 11 rather than 10 exons, and the 3' UTR in one of the two E1beta mRNAs arises from intronic sequences." Chuang J.L., Cox R.P., Chuang D.T. Am. J. Hum. Genet. 58:1373-1377(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Placenta.
[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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Hippocampus.
[4]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]	"The DNA sequence and analysis of human chromosome 6." Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S. Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	Mural R.J., Istrail S., Sutton 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"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]. Tissue: Eye.
[8]	"Molecular cloning of the mature E1b-beta subunit of human branched-chain alpha-keto acid dehydrogenase complex." Chuang J.L., Cox R.P., Chuang D.T. FEBS Lett. 262:305-309(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 20-392.
[9]	"Differential processing of human and rat E1 alpha precursors of the branched-chain alpha-keto acid dehydrogenase complex caused by an N-terminal proline in the rat sequence." Wynn R.M., Kochi H., Cox R.P., Chuang D.T. Biochim. Biophys. Acta 1201:125-128(1994) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 36-62.
[10]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-241, MASS SPECTROMETRY.
[11]	"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].
[12]	"Heterogeneity of mutations in maple syrup urine disease (MSUD): screening and identification of affected E1 alpha and E1 beta subunits of the branched-chain alpha-keto-acid dehydrogenase multienzyme complex." Nobukuni Y., Mitsubuchi H., Hayashida Y., Ohta K., Indo Y., Ichiba Y., Endo F., Matsuda I. Biochim. Biophys. Acta 1225:64-70(1993) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT MSUD1B ARG-206.
[13]	"Maple syrup urine disease: identification and carrier-frequency determination of a novel founder mutation in the Ashkenazi Jewish population." Edelmann L., Wasserstein M.P., Kornreich R., Sansaricq C., Snyderman S.E., Diaz G.A. Am. J. Hum. Genet. 69:863-868(2001) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS MSUD1B PRO-183 AND SER-278.
[14]	"Two novel mutations in the BCKDHB gene (R170H, Q346R) cause the classic form of maple syrup urine disease (MSUD)." Wang Y.P., Qi M.L., Li T.T., Zhao Y.J. Gene 498:112-115(2012) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS MSUD1B HIS-170 AND ARG-346.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M55575 mRNA. Translation: AAA51812.1.
D90391 Genomic DNA. Translation: BAA14389.1.
AK289977 mRNA. Translation: BAF82666.1.
BT020063 mRNA. Translation: AAV38866.1.
AL049696, AL391595 Genomic DNA. Translation: CAC36881.2.
AL391595, AL049696 Genomic DNA. Translation: CAI15049.1.
CH471051 Genomic DNA. Translation: EAW48696.1.
CH471051 Genomic DNA. Translation: EAW48697.1.
BC040139 mRNA. Translation: AAH40139.1.
U50708 mRNA. Translation: AAB16763.1.
X52446 mRNA. Translation: CAA36685.1.

IPI

IPI00011276.

PIR

A37157.

RefSeq

NP_000047.1. NM_000056.3.
NP_898871.1. NM_183050.2.

UniGene

Hs.654441.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1DTW	X-ray	2.70	B	51-392	[»]
1OLS	X-ray	1.85	B	51-392	[»]
1OLU	X-ray	1.90	B	51-392	[»]
1OLX	X-ray	2.25	B	51-392	[»]
1U5B	X-ray	1.83	B	51-392	[»]
1V11	X-ray	1.95	B	51-392	[»]
1V16	X-ray	1.90	B	51-392	[»]
1V1M	X-ray	2.00	B	51-392	[»]
1V1R	X-ray	1.80	B	51-392	[»]
1WCI	X-ray	1.84	B	51-392	[»]
1X7W	X-ray	1.73	B	51-392	[»]
1X7X	X-ray	2.10	B	51-392	[»]
1X7Y	X-ray	1.57	B	51-392	[»]
1X7Z	X-ray	1.72	B	51-392	[»]
1X80	X-ray	2.00	B	51-392	[»]
2BEU	X-ray	1.89	B	51-392	[»]
2BEV	X-ray	1.80	B	51-392	[»]
2BEW	X-ray	1.79	B	51-392	[»]
2BFB	X-ray	1.77	B	51-392	[»]
2BFC	X-ray	1.64	B	51-392	[»]
2BFD	X-ray	1.39	B	51-392	[»]
2BFE	X-ray	1.69	B	51-392	[»]
2BFF	X-ray	1.46	B	51-392	[»]
2J9F	X-ray	1.88	B/D	51-392	[»]

ProteinModelPortal

P21953.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-6147N.

IntAct

P21953. 1 interaction.

MINT

MINT-271857.

STRING

9606.ENSP00000318351.

PTM databases

PhosphoSite

P21953.

Polymorphism databases

DMDM

129034.

2D gel databases

REPRODUCTION-2DPAGE

IPI00011276.

Proteomic databases

PaxDb

P21953.

PeptideAtlas

P21953.

PRIDE

P21953.

Protocols and materials databases

DNASU

594.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000320393; ENSP00000318351; ENSG00000083123.
ENST00000356489; ENSP00000348880; ENSG00000083123.

GeneID

594.

KEGG

hsa:594.

UCSC

uc003pjd.2. human.

Organism-specific databases

CTD

594.

GeneCards

GC06P080873.

HGNC

HGNC:987. BCKDHB.

HPA

HPA031580.

MIM

248600. phenotype.
248611. gene.

neXtProt

NX_P21953.

Orphanet

268145. Classic maple syrup urine disease.
268162. Intermediate maple syrup urine disease.
268173. Intermittent maple syrup urine disease.
268184. Thiamin-responsive maple syrup urine disease.

PharmGKB

PA25298.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0022.

HOGENOM

HOG000281451.

HOVERGEN

HBG108210.

InParanoid

P21953.

KO

K00167.

OMA

IQEECFL.

OrthoDB

EOG4HQDJN.

PhylomeDB

P21953.

Enzyme and pathway databases

BioCyc

MetaCyc:MONOMER-12006.

Reactome

REACT_111217. Metabolism.

SABIO-RK

P21953.

Gene expression databases

ArrayExpress

P21953.

Bgee

P21953.

CleanEx

HS_BCKDHB.

Genevestigator

P21953.

GermOnline

ENSG00000083123. Homo sapiens.

Family and domain databases

Gene3D

3.40.50.920. 1 hit.

InterPro

IPR009014. Transketo_C/Pyr-ferredox_oxred.
IPR015941. Transketolase-like_C.
IPR005475. Transketolase-like_Pyr-bd.
IPR005476. Transketolase_C.
[Graphical view]

Pfam

PF02779. Transket_pyr. 1 hit.
PF02780. Transketolase_C. 1 hit.
[Graphical view]

SMART

SM00861. Transket_pyr. 1 hit.
[Graphical view]

SUPFAM

SSF52922. Transketo_C_like. 1 hit.

ProtoNet

Search...

Other

ChiTaRS

BCKDHB. human.

EvolutionaryTrace

P21953.

GenomeRNAi

594.

NextBio

2413.

SOURCE

Search...

Entry information

Entry name

ODBB_HUMAN

Accession

Primary (citable) accession number: P21953
Secondary accession number(s): Q9BQL0

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1991
Last sequence update:	August 1, 1992
Last modified:	May 29, 2013
This is version 147 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.