P55084 (ECHB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Trifunctional enzyme subunit beta, mitochondrial

Alternative name(s):
TP-beta

Including the following 1 domains:

1. 3-ketoacyl-CoA thiolase
   EC=2.3.1.16
   Alternative name(s):
   Acetyl-CoA acyltransferase
   Beta-ketothiolase

Gene names

Name:	HADHB
ORF Names:	MSTP029

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	474 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)

Catalytic activity	Acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA. Ref.8
Pathway	Lipid metabolism; fatty acid beta-oxidation.
Subunit structure	Octamer of 4 alpha (HADHA) and 4 beta (HADHB) subunits. Interacts with RSAD2/viperin. Ref.10 Ref.13
Subcellular location	Mitochondrion. Mitochondrion inner membrane. Mitochondrion outer membrane. Endoplasmic reticulum Ref.13.
Involvement in disease	Trifunctional protein deficiency (TFP deficiency) [MIM:609015]: The clinical manifestations are very variable and include hypoglycemia, cardiomyopathy and sudden death. Phenotypes with mainly hepatic and neuromyopathic involvement can also be distinguished. Biochemically, TFP deficiency is defined by the loss of all three enzyme activities of the TFP complex. Note: The disease is caused by mutations affecting the gene represented in this entry.
Sequence similarities	Belongs to the thiolase family.
Sequence caution	The sequence BAA22061.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Fatty acid metabolism Lipid metabolism
Cellular component	Endoplasmic reticulum Membrane Mitochondrion Mitochondrion inner membrane Mitochondrion outer membrane
Coding sequence diversity	Polymorphism
Disease	Disease mutation
Domain	Transit peptide
Molecular function	Acyltransferase Transferase
PTM	Acetylation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cardiolipin acyl-chain remodeling Traceable author statement. Source: Reactome fatty acid beta-oxidation Traceable author statement. Source: Reactome glycerophospholipid biosynthetic process Traceable author statement. Source: Reactome
Cellular_component	endoplasmic reticulum Inferred from direct assay Ref.13. Source: UniProtKB mitochondrial fatty acid beta-oxidation multienzyme complex Inferred from electronic annotation. Source: Compara mitochondrial inner membrane Inferred from direct assay Ref.13. Source: UniProtKB mitochondrial nucleoid Inferred from direct assay PubMed 18063578. Source: BHF-UCL mitochondrial outer membrane Inferred from direct assay Ref.13. Source: UniProtKB
Molecular_function	3-hydroxyacyl-CoA dehydrogenase activity Traceable author statement PubMed 1550553. Source: ProtInc NAD binding Inferred from electronic annotation. Source: Compara acetyl-CoA C-acyltransferase activity Traceable author statement Ref.1. Source: ProtInc enoyl-CoA hydratase activity Traceable author statement PubMed 1550553. Source: ProtInc fatty-acyl-CoA binding Inferred from electronic annotation. Source: Compara long-chain-3-hydroxyacyl-CoA dehydrogenase activity Inferred from electronic annotation. Source: Compara long-chain-enoyl-CoA hydratase activity Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
GABARAPL1	Q9H0R8	4	EBI-356635,EBI-746969

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 33	33	Mitochondrion Ref.7
	Chain	34 – 474	441	Trifunctional enzyme subunit beta, mitochondrial		PRO_0000034080
Sites
	Active site	138	1	Acyl-thioester intermediate By similarity
	Active site	428	1	Proton acceptor By similarity
	Active site	458	1	Proton acceptor By similarity
Amino acid modifications
	Modified residue	72	1	N6-acetyllysine Ref.11
	Modified residue	188	1	N6-acetyllysine Ref.11
	Modified residue	201	1	N6-acetyllysine By similarity
	Modified residue	348	1	N6-acetyllysine By similarity
Natural variations
	Natural variant	59	1	G → D in TFP deficiency. Ref.15		VAR_021128
	Natural variant	61	1	R → C in TFP deficiency. Ref.15		VAR_021129
	Natural variant	61	1	R → H in TFP deficiency. Ref.14 Ref.15		VAR_007493
	Natural variant	117	1	R → G in TFP deficiency. Ref.15		VAR_021130
	Natural variant	119	1	A → V in a breast cancer sample; somatic mutation. Ref.16		VAR_035705
	Natural variant	121	1	L → P in TFP deficiency. Ref.15		VAR_021131
	Natural variant	133	1	T → P in TFP deficiency. Ref.15		VAR_021132
	Natural variant	209	1	P → S. Ref.6 Corresponds to variant rs17851200 [ dbSNP | Ensembl ].		VAR_028231
	Natural variant	242	1	D → G in TFP deficiency. Ref.15		VAR_021133
	Natural variant	247	1	R → H in TFP deficiency. Ref.14 Ref.15		VAR_007494
	Natural variant	259 – 270	12	Missing in TFP deficiency.		VAR_021134
	Natural variant	263	1	D → G in TFP deficiency. Ref.14 Ref.15		VAR_007495
	Natural variant	277	1	K → R. Corresponds to variant rs57969630 [ dbSNP | Ensembl ].		VAR_061897
	Natural variant	280	1	G → D in TFP deficiency. Ref.15		VAR_021135
	Natural variant	294	1	P → L in TFP deficiency. Ref.15		VAR_021136
	Natural variant	294	1	P → R in TFP deficiency. Ref.15		VAR_021137
	Natural variant	301	1	G → S in TFP deficiency. Ref.15		VAR_021138
	Natural variant	444	1	R → K in TFP deficiency. Ref.2 Ref.15		VAR_017409
Experimental info
	Sequence conflict	1	1	M → MT in AAG39280. Ref.3
	Sequence conflict	1	1	M → MT in AAH14572. Ref.6
	Sequence conflict	1	1	M → MT in AAH17564. Ref.6
	Sequence conflict	1	1	M → MT in AAH30824. Ref.6
	Sequence conflict	1	1	M → MT in AAH66963. Ref.6

Sequences

	Sequence		Length	Mass (Da)
	P55084 [UniParc]. Last modified October 17, 2006. Version 3. Checksum: A7B41C37BEC1E6AD	FASTA	474	51,294
	10 20 30 40 50 60 MTILTYPFKN LPTASKWALR FSIRPLSCSS QLRAAPAVQT KTKKTLAKPN IRNVVVVDGV 70 80 90 100 110 120 RTPFLLSGTS YKDLMPHDLA RAALTGLLHR TSVPKEVVDY IIFGTVIQEV KTSNVAREAA 130 140 150 160 170 180 LGAGFSDKTP AHTVTMACIS ANQAMTTGVG LIASGQCDVI VAGGVELMSD VPIRHSRKMR 190 200 210 220 230 240 KLMLDLNKAK SMGQRLSLIS KFRFNFLAPE LPAVSEFSTS ETMGHSADRL AAAFAVSRLE 250 260 270 280 290 300 QDEYALRSHS LAKKAQDEGL LSDVVPFKVP GKDTVTKDNG IRPSSLEQMA KLKPAFIKPY 310 320 330 340 350 360 GTVTAANSSF LTDGASAMLI MAEEKALAMG YKPKAYLRDF MYVSQDPKDQ LLLGPTYATP 370 380 390 400 410 420 KVLEKAGLTM NDIDAFEFHE AFSGQILANF KAMDSDWFAE NYMGRKTKVG LPPLEKFNNW 430 440 450 460 470 GGSLSLGHPF GATGCRLVMA AANRLRKEGG QYGLVAACAA GGQGHAMIVE AYPK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structural analysis of cDNAs for subunits of human mitochondrial fatty acid beta-oxidation trifunctional protein." Kamijo T., Aoyama T., Komiyama A., Hashimoto T. Biochem. Biophys. Res. Commun. 199:818-825(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Genomic and mutational analysis of the mitochondrial trifunctional protein beta-subunit (HADHB) gene in patients with trifunctional protein deficiency." Orii K.E., Aoyama T., Wakui K., Fukushima Y., Miyajima H., Yamaguchi S., Orii T., Kondo N., Hashimoto T. Hum. Mol. Genet. 6:1215-1224(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT TFP DEFICIENCY LYS-444. Tissue: Blood.
[3]	Liu B., Liu Y.Q., Wang X.Y., Zhao B., Sheng H., Zhao X.W., Liu S., Xu Y.Y., Ye J., Song L., Gao Y., Zhang C.L., Zhang J., Wei Y.J., Cao H.Q., Zhao Y., Liu L.S., Ding J.F. , Gao R.L., Wu Q.Y., Qiang B.Q., Yuan J.G., Liew C.C., Zhao M.S., Hui R.T. Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Heart.
[4]	"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: Tongue.
[5]	"Generation and annotation of the DNA sequences of human chromosomes 2 and 4." Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K. Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract] 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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT SER-209. Tissue: Colon, Hypothalamus, Skeletal muscle and Urinary bladder.
[7]	"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] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 34-52. Tissue: Platelet.
[8]	"The mitochondrial long-chain trifunctional enzyme: 2-enoyl-CoA hydratase, 3-hydroxyacyl-CoA dehydrogenase and 3-oxoacyl-CoA thiolase." Middleton B. Biochem. Soc. Trans. 22:427-431(1994) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 48-63, CATALYTIC ACTIVITY. Tissue: Liver.
[9]	"Vectorial proteomics reveal targeting, phosphorylation and specific fragmentation of polymerase I and transcript release factor (PTRF) at the surface of caveolae in human adipocytes." Aboulaich N., Vainonen J.P., Stralfors P., Vener A.V. Biochem. J. 383:237-248(2004) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 62-72 AND 96-111. Tissue: Adipocyte.
[10]	"Mitochondrial trifunctional protein deficiency. Catalytic heterogeneity of the mutant enzyme in two patients." Kamijo T., Wanders R.J., Saudubray J.-M., Aoyama T., Komiyama A., Hashimoto T. J. Clin. Invest. 93:1740-1747(1994) [PubMed] [Europe PMC] [Abstract] Cited for: SUBUNIT.
[11]	"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-72 AND LYS-188, MASS SPECTROMETRY.
[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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]	"Human cytomegalovirus directly induces the antiviral protein viperin to enhance infectivity." Seo J.Y., Yaneva R., Hinson E.R., Cresswell P. Science 332:1093-1097(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, INTERACTION WITH RSAD2.
[14]	"Molecular characterization of mitochondrial trifunctional protein deficiency: formation of the enzyme complex is important for stabilization of both alpha- and beta-subunits." Ushikubo S., Aoyama T., Kamijo T., Wanders R.J.A., Rinaldo P., Vockley J., Hashimoto T. Am. J. Hum. Genet. 58:979-988(1996) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS TFP DEFICIENCY HIS-61; HIS-247 AND GLY-263.
[15]	"Molecular and phenotypic heterogeneity in mitochondrial trifunctional protein deficiency due to beta-subunit mutations." Spiekerkoetter U., Sun B., Khuchua Z., Bennett M.J., Strauss A.W. Hum. Mutat. 21:598-607(2003) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS TFP DEFICIENCY ASP-59; CYS-61; HIS-61; GLY-117; PRO-121; PRO-133; GLY-242; HIS-247; 259-GLY--PRO-270 DEL; GLY-263; ASP-280; ARG-294; LEU-294; SER-301 AND LYS-444.
[16]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] VAL-119.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases
EMBL GenBank DDBJ	D16481 mRNA. Translation: BAA03942.1. D86850 Genomic DNA. Translation: BAA22061.1. Sequence problems. AF113209 mRNA. Translation: AAG39280.1. AK314455 mRNA. Translation: BAG37063.1. AC010896 Genomic DNA. Translation: AAY14644.1. BC014572 mRNA. Translation: AAH14572.1. BC017564 mRNA. Translation: AAH17564.1. BC030824 mRNA. Translation: AAH30824.1. BC066963 mRNA. Translation: AAH66963.1.
IPI	IPI00022793.
PIR	JC2109.
RefSeq	NP_000174.1. NM_000183.2.
UniGene	Hs.515848.
3D structure databases
ProteinModelPortal	P55084.
ModBase	Search...
Protein-protein interaction databases
IntAct	P55084. 24 interactions.
MINT	MINT-1154861.
STRING	9606.ENSP00000325136.
PTM databases
PhosphoSite	P55084.
Polymorphism databases
DMDM	116241345.
2D gel databases
UCD-2DPAGE	P55084.
Proteomic databases
PaxDb	P55084.
PRIDE	P55084.
Protocols and materials databases
DNASU	3032.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000317799; ENSP00000325136; ENSG00000138029.
GeneID	3032.
KEGG	hsa:3032.
UCSC	uc002rgz.3. human.
Organism-specific databases
CTD	3032.
GeneCards	GC02P026466.
HGNC	HGNC:4803. HADHB.
HPA	HPA037539.
MIM	143450. gene. 609015. phenotype.
neXtProt	NX_P55084.
Orphanet	746. Mitochondrial trifunctional protein deficiency.
PharmGKB	PA29177.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0183.
HOGENOM	HOG000012240.
HOVERGEN	HBG104782.
InParanoid	P55084.
KO	K07509.
OMA	CRQNTAY.
PhylomeDB	P55084.
Enzyme and pathway databases
Reactome	REACT_111217. Metabolism.
UniPathway	UPA00659.
Gene expression databases
ArrayExpress	P55084.
Bgee	P55084.
CleanEx	HS_HADHB.
Genevestigator	P55084.
GermOnline	ENSG00000138029. Homo sapiens.
Family and domain databases
Gene3D	3.40.47.10. 4 hits.
InterPro	IPR002155. Thiolase. IPR016039. Thiolase-like. IPR016038. Thiolase-like_subgr. IPR020615. Thiolase_acyl_enz_int_AS. IPR020610. Thiolase_AS. IPR020617. Thiolase_C. IPR020613. Thiolase_CS. IPR020616. Thiolase_N. [Graphical view]
PANTHER	PTHR18919. PTHR18919. 1 hit.
Pfam	PF02803. Thiolase_C. 1 hit. PF00108. Thiolase_N. 1 hit. [Graphical view]
SUPFAM	SSF53901. Thiolase-like. 2 hits.
TIGRFAMs	TIGR01930. AcCoA-C-Actrans. 1 hit.
PROSITE	PS00098. THIOLASE_1. 1 hit. PS00737. THIOLASE_2. 1 hit. PS00099. THIOLASE_3. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	HADHB. human.
GenomeRNAi	3032.
NextBio	12002.
SOURCE	Search...

Entry information

Entry name

ECHB_HUMAN

Accession

Primary (citable) accession number: P55084
Secondary accession number(s): B2RB16 , O14969, Q53TA6, Q96C77, Q9H3F5, Q9T2V8

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 17, 2006
Last modified:	May 1, 2013
This is version 133 of the entry and version 3 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.