Q9HAF1 (EAF6_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Chromatin modification-related protein MEAF6
Short name=MYST/Esa1-associated factor 6

Alternative name(s):
Esa1-associated factor 6 homolog
Short name=Protein EAF6 homolog
Short name=hEAF6
Sarcoma antigen NY-SAR-91

Gene names

Name:	MEAF6
Synonyms:	C1orf149, EAF6

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	191 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histone H4 and H2A. This modification may both alter nucleosome - DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription. Component of the HBO1 complex which has a histone H4-specific acetyltransferase activity, a reduced activity toward histone H3 and is responsible for the bulk of histone H4 acetylation in vivo. Component of the MOZ/MORF complex which has a histone H3 acetyltransferase activity. Ref.8 Ref.10 Ref.12
Subunit structure	Component of the NuA4 histone acetyltransferase complex which contains the catalytic subunit KAT5 and the subunits EP400, TRRAP, BRD8, EPC1, DMAP1, RUVBL1, RUVBL2, ING3, actin, ACTL6A, MORF4L1, MORF4L2, MRGBP, YEATS4, VPS72 and MEAF6. Component of the HBO1 complex composed at least of ING4 or ING5, KAT7/HBO1, MEAF6, and one of PHF15, PHF16 and PHF17. Component of the MOZ/MORF complex composed at least of ING5, KAT6A, KAT6B, MEAF6 and one of BRPF1, BRD1/BRPF2 and BRPF3. Ref.7 Ref.8 Ref.9 Ref.10 Ref.12
Subcellular location	Nucleus › nucleolus Ref.12.
Involvement in disease	A chromosomal aberration involving MEAF6 may be a cause of endometrial stromal tumors. Translocation t(1;6)(p34;p21) with PHF1. Ref.17
Sequence similarities	Belongs to the EAF6 family.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Chromosomal rearrangement
Domain	Coiled coil
Molecular function	Activator Chromatin regulator
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	histone H2A acetylation Inferred from direct assay Ref.8. Source: UniProtKB histone H3-K14 acetylation Inferred from direct assay Ref.10. Source: UniProtKB histone H4-K12 acetylation Inferred from direct assay Ref.10. Source: UniProtKB histone H4-K5 acetylation Inferred from direct assay Ref.10. Source: UniProtKB histone H4-K8 acetylation Inferred from direct assay Ref.10. Source: UniProtKB regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	MOZ/MORF histone acetyltransferase complex Inferred from direct assay Ref.10Ref.12. Source: UniProtKB NuA4 histone acetyltransferase complex Inferred from direct assay Ref.8Ref.10. Source: UniProtKB centrosome Inferred from direct assay. Source: HPA cytoplasm Inferred from direct assay. Source: HPA nucleolus Inferred from direct assay Ref.12. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
FXR2	P51116	3	EBI-399266,EBI-740459

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9HAF1-1)

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: Q9HAF1-2)

The sequence of this isoform differs from the canonical sequence as follows:
     178-191: RIDLKLNKKPRADY → SPSGMFDYDFEYVY

Note: No experimental confirmation available.

Isoform 3 (identifier: Q9HAF1-3)

The sequence of this isoform differs from the canonical sequence as follows:
     178-178: R → SPSGMFDYDFE

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 191	191	Chromatin modification-related protein MEAF6		PRO_0000272609
Regions
	Coiled coil	11 – 47	37	Potential
Amino acid modifications
	Modified residue	69	1	N6-acetyllysine Ref.14
	Modified residue	74	1	N6-acetyllysine Ref.14
	Modified residue	118	1	Phosphoserine Ref.13
	Modified residue	120	1	Phosphothreonine Ref.13
Natural variations
	Alternative sequence	178 – 191	14	RIDLK…PRADY → SPSGMFDYDFEYVY in isoform 2.		VSP_022450
	Alternative sequence	178	1	R → SPSGMFDYDFE in isoform 3.		VSP_022451
Experimental info
	Sequence conflict	2 – 3	2	AM → RG in AAO65179. Ref.6
	Sequence conflict	4	1	H → P in AAZ13760. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: C0FBC7566BAAF1F7	FASTA	191	21,635
	10 20 30 40 50 60 MAMHNKAAPP QIPDTRRELA ELVKRKQELA ETLANLERQI YAFEGSYLED TQMYGNIIRG 70 80 90 100 110 120 WDRYLTNQKN SNSKNDRRNR KFKEAERLFS KSSVTSAAAV SALAGVQDQL IEKREPGSGT 130 140 150 160 170 180 ESDTSPDFHN QENEPSQEDP EDLDGSVQGV KPQKAASSTS SGSHHSSHKK RKNKNRHRID 190 LKLNKKPRAD Y
	Isoform 2 [UniParc]. Checksum: 4A46263CF13F3C99	FASTA	191	21,625
	10 20 30 40 50 60 MAMHNKAAPP QIPDTRRELA ELVKRKQELA ETLANLERQI YAFEGSYLED TQMYGNIIRG 70 80 90 100 110 120 WDRYLTNQKN SNSKNDRRNR KFKEAERLFS KSSVTSAAAV SALAGVQDQL IEKREPGSGT 130 140 150 160 170 180 ESDTSPDFHN QENEPSQEDP EDLDGSVQGV KPQKAASSTS SGSHHSSHKK RKNKNRHSPS 190 GMFDYDFEYV Y
	Isoform 3 [UniParc]. Checksum: E30FC55A4AB5EBA0	FASTA	201	22,755
	10 20 30 40 50 60 MAMHNKAAPP QIPDTRRELA ELVKRKQELA ETLANLERQI YAFEGSYLED TQMYGNIIRG 70 80 90 100 110 120 WDRYLTNQKN SNSKNDRRNR KFKEAERLFS KSSVTSAAAV SALAGVQDQL IEKREPGSGT 130 140 150 160 170 180 ESDTSPDFHN QENEPSQEDP EDLDGSVQGV KPQKAASSTS SGSHHSSHKK RKNKNRHSPS 190 200 GMFDYDFEID LKLNKKPRAD Y

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). Tissue: Cerebellum and Fetal brain.
[2]	"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 1). Tissue: Embryo.
[3]	Lin L., Nong W., Zhou G., Ke R., Shen C., Zhong G., Zheng Z., Liang M., Li M., Li H., Yang S. Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[4]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"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 1). Tissue: Brain and Uterus.
[6]	"Immunomic analysis of human sarcoma." Lee S.-Y., Obata Y., Yoshida M., Stockert E., Williamson B., Jungbluth A.A., Chen Y.-T., Old L.J., Scanlan M.J. Proc. Natl. Acad. Sci. U.S.A. 100:2651-2656(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2-191 (ISOFORM 1).
[7]	"Identification of new subunits of the multiprotein mammalian TRRAP/TIP60-containing histone acetyltransferase complex." Cai Y., Jin J., Tomomori-Sato C., Sato S., Sorokina I., Parmely T.J., Conaway R.C., Conaway J.W. J. Biol. Chem. 278:42733-42736(2003) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE NUA4 HISTONE ACETYLTRANSFERASE COMPLEX.
[8]	"Structural and functional conservation of the NuA4 histone acetyltransferase complex from yeast to humans." Doyon Y., Selleck W., Lane W.S., Tan S., Cote J. Mol. Cell. Biol. 24:1884-1896(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE NUA4 HISTONE ACETYLTRANSFERASE COMPLEX.
[9]	"The mammalian YL1 protein is a shared subunit of the TRRAP/TIP60 histone acetyltransferase and SRCAP complexes." Cai Y., Jin J., Florens L., Swanson S.K., Kusch T., Li B., Workman J.L., Washburn M.P., Conaway R.C., Conaway J.W. J. Biol. Chem. 280:13665-13670(2005) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE NUA4 HISTONE ACETYLTRANSFERASE COMPLEX.
[10]	"ING tumor suppressor proteins are critical regulators of chromatin acetylation required for genome expression and perpetuation." Doyon Y., Cayrou C., Ullah M., Landry A.-J., Cote V., Selleck W., Lane W.S., Tan S., Yang X.-J., Cote J. Mol. Cell 21:51-64(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE NUA4 HISTONE ACETYLTRANSFERASE COMPLEX, IDENTIFICATION IN THE HBO1 COMPLEX, IDENTIFICATION IN THE MOZ/MORF COMPLEX.
[11]	"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Embryonic kidney.
[12]	"Molecular architecture of quartet MOZ/MORF histone acetyltransferase complexes." Ullah M., Pelletier N., Xiao L., Zhao S.P., Wang K., Degerny C., Tahmasebi S., Cayrou C., Doyon Y., Goh S.-L., Champagne N., Cote J., Yang X.-J. Mol. Cell. Biol. 28:6828-6843(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, IDENTIFICATION IN THE MOZ/MORF COMPLEX, INTERACTION WITH BRPF1, SUBCELLULAR LOCATION.
[13]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118 AND THR-120, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"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-69 AND LYS-74, MASS SPECTROMETRY.
[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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[16]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]	"Novel fusion of MYST/Esa1-associated factor 6 and PHF1 in endometrial stromal sarcoma." Panagopoulos I., Micci F., Thorsen J., Gorunova L., Eibak A.M., Bjerkehagen B., Davidson B., Heim S. PLoS ONE 7:E39354-E39354(2012) [PubMed] [Europe PMC] [Abstract] Cited for: DISEASE, CHROMOSOMAL TRANSLOCATION WITH PHF1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX538212 mRNA. Translation: CAD98071.1. BX640719 mRNA. Translation: CAE45838.1. AK021792 mRNA. Translation: BAB13898.1. DQ099384 mRNA. Translation: AAZ13760.1. AL034379 Genomic DNA. Translation: CAI20549.1. AL034379 Genomic DNA. Translation: CAI20550.1. BC056406 mRNA. Translation: AAH56406.1. BC016328 mRNA. Translation: AAH16328.1. AY211926 mRNA. Translation: AAO65179.1.
IPI	IPI00009373. IPI00642467. IPI00828199.
RefSeq	NP_001257804.1. NM_001270875.1. NP_073593.2. NM_022756.5.
UniGene	Hs.17118.
3D structure databases
ProteinModelPortal	Q9HAF1.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9HAF1. 7 interactions.
STRING	9606.ENSP00000362166.
PTM databases
PhosphoSite	Q9HAF1.
Polymorphism databases
DMDM	74752760.
Proteomic databases
PaxDb	Q9HAF1.
PRIDE	Q9HAF1.
Protocols and materials databases
DNASU	64769.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000296214; ENSP00000296214; ENSG00000163875. ENST00000373075; ENSP00000362166; ENSG00000163875. ENST00000448519; ENSP00000394966; ENSG00000163875.
GeneID	64769.
KEGG	hsa:64769.
UCSC	uc001cbe.1. human. uc001cbg.1. human. uc001cbh.1. human.
Organism-specific databases
CTD	64769.
GeneCards	GC01M037951.
HGNC	HGNC:25674. MEAF6.
HPA	HPA029599. HPA029600.
MIM	611001. gene.
neXtProt	NX_Q9HAF1.
PharmGKB	PA165751536.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG290756.
HOGENOM	HOG000290166.
KO	K11344.
OMA	SHHGSHK.
Gene expression databases
ArrayExpress	Q9HAF1.
Bgee	Q9HAF1.
CleanEx	HS_C1orf149.
Genevestigator	Q9HAF1.
Family and domain databases
InterPro	IPR015418. Hist_AcTrfase_NuA4_cplx. [Graphical view]
Pfam	PF09340. NuA4. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	64769.
NextBio	66769.
SOURCE	Search...

Entry information

Entry name

EAF6_HUMAN

Accession

Primary (citable) accession number: Q9HAF1
Secondary accession number(s): Q4F967, Q7Z311, Q86WE3

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 23, 2007
Last sequence update:	March 1, 2001
Last modified:	April 3, 2013
This is version 88 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.