Reviewed, UniProtKB/Swiss-Prot P35611 (ADDA_HUMAN)

Names and origin

Protein names

Recommended name:
    Alpha-adducin
Alternative name(s):
    Erythrocyte adducin subunit alpha

Gene names

Name:	ADD1
Synonyms:	ADDA

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	737 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Membrane-cytoskeleton-associated protein that promotes the assembly of the spectrin-actin network. Binds to calmodulin.
Subunit structure	Heterodimer of an alpha and a beta subunit or an alpha and a gamma subunit. Binds ROCK1.
Subcellular location	Cytoplasm › cytoskeleton. Cell membrane; Peripheral membrane protein; Cytoplasmic side.
Tissue specificity	Expressed in all tissues. Found in much higher levels in reticulocytes than the beta subunit.
Domain	Each subunit is comprised of three regions: a NH2-terminal protease-resistant globular head region, a short connecting subdomain, and a protease-sensitive tail region.
Post-translational modification	The N-terminus is blocked.
Sequence similarities	Belongs to the aldolase class II family. Adducin subfamily.
Sequence caution	The sequence CAA98970.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Cellular component	Cell membrane Cytoplasm Cytoskeleton Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	Actin-binding Calmodulin-binding
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	actin filament bundle formation Inferred from direct assay. Source: UniProtKB barbed-end actin filament capping Inferred from direct assay. Source: UniProtKB positive regulation of protein binding Inferred from direct assay. Source: UniProtKB
Cellular component	F-actin capping protein complex Inferred from direct assay. Source: UniProtKB cytosol Inferred from Experiment. Source: Reactome internal side of plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from direct assay. Source: UniProtKB
Molecular function	actin filament binding Inferred from direct assay. Source: UniProtKB calmodulin binding Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: InterPro protein heterodimerization activity Inferred from physical interaction. Source: UniProtKB protein homodimerization activity Inferred from physical interaction. Source: UniProtKB spectrin binding Inferred from direct assay. Source: UniProtKB transcription factor binding Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

Alternative products

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

Note: Additional isoforms seem to exist.

Isoform 1 (identifier: P35611-1)

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: P35611-2)

The sequence of this isoform differs from the canonical sequence as follows:
     621-631: DLVPEPTTGDD → GDGCAREYLLP
     632-737: Missing.

Isoform 3 (identifier: P35611-3)

The sequence of this isoform differs from the canonical sequence as follows:
     471-471: K → KVWTNITHDHVKPLLQSLSSGVCVPSCITNCL

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 737	737	Alpha-adducin		PRO_0000218530
Regions
	Region	717 – 734	18	Interaction with calmodulin Potential
Amino acid modifications
	Modified residue	12	1	Phosphoserine Ref.11 Ref.12
	Modified residue	59	1	Phosphoserine; by PKA Ref.5
	Modified residue	331	1	Phosphothreonine Ref.12
	Modified residue	334	1	Phosphoserine Ref.12
	Modified residue	353	1	Phosphoserine Ref.10
	Modified residue	355	1	Phosphoserine Ref.10 Ref.8
	Modified residue	358	1	Phosphoserine Ref.11 Ref.12 Ref.10 Ref.8 Ref.7
	Modified residue	408	1	Phosphoserine; by PKA Ref.5
	Modified residue	431	1	Phosphoserine Ref.12
	Modified residue	436	1	Phosphoserine; by PKA Ref.12 Ref.5
	Modified residue	445	1	Phosphothreonine; by ROCK1 Ref.6
	Modified residue	465	1	Phosphoserine Ref.12 Ref.10 Ref.7
	Modified residue	480	1	Phosphothreonine; by ROCK1 Ref.6
	Modified residue	481	1	Phosphoserine; by PKA Ref.5
	Modified residue	483	1	Phosphoserine By similarity
	Modified residue	586	1	Phosphoserine By similarity
	Modified residue	614	1	Phosphothreonine By similarity
	Modified residue	707	1	Phosphoserine Ref.9
	Modified residue	710	1	Phosphoserine Ref.9
	Modified residue	716	1	Phosphoserine; by PKC Ref.5 Ref.9
	Modified residue	726	1	Phosphoserine; by PKA and PKC Ref.5
Natural variations
	Alternative sequence	471	1	K → KVWTNITHDHVKPLLQSLSS GVCVPSCITNCL in isoform 3.		VSP_000174
	Alternative sequence	621 – 631	11	DLVPEPTTGDD → GDGCAREYLLP in isoform 2.		VSP_000175
	Alternative sequence	632 – 737	106	Missing in isoform 2.		VSP_000176
	Natural variant	6	1	R → C: dbSNP rs2295497.		VAR_022108
	Natural variant	270	1	Y → N: dbSNP rs4971.		VAR_014863
	Natural variant	376	1	E → D: dbSNP rs4972.		VAR_014864
	Natural variant	460	1	G → W: dbSNP rs4961. Ref.13 Ref.14		VAR_014184
	Natural variant	510	1	N → I: dbSNP rs4962.		VAR_014865
	Natural variant	586	1	S → C: dbSNP rs4963. Ref.14 Ref.1		VAR_014185
Experimental info
	Mutagenesis	445	1	T → D: Abolishes phosphorylation by ROCK1; when associated with D-480. Ref.6
	Mutagenesis	480	1	T → D: Abolishes phosphorylation by ROCK1; when associated with D-445. Ref.6
	Sequence conflict	606	1	A → E in AAB05645. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified December 1, 2000. Version 2. Checksum: DF13AB30B12F20B6	FASTA	737	80,955
	10 20 30 40 50 60 MNGDSRAAVV TSPPPTTAPH KERYFDRVDE NNPEYLRERN MAPDLRQDFN MMEQKKRVSM 70 80 90 100 110 120 ILQSPAFCEE LESMIQEQFK KGKNPTGLLA LQQIADFMTT NVPNVYPAAP QGGMAALNMS 130 140 150 160 170 180 LGMVTPVNDL RGSDSIAYDK GEKLLRCKLA AFYRLADLFG WSQLIYNHIT TRVNSEQEHF 190 200 210 220 230 240 LIVPFGLLYS EVTASSLVKI NLQGDIVDRG STNLGVNQAG FTLHSAIYAA RPDVKCVVHI 250 260 270 280 290 300 HTPAGAAVSA MKCGLLPISP EALSLGEVAY HDYHGILVDE EEKVLIQKNL GPKSKVLILR 310 320 330 340 350 360 NHGLVSVGES VEEAFYYIHN LVVACEIQVR TLASAGGPDN LVLLNPEKYK AKSRSPGSPV 370 380 390 400 410 420 GEGTGSPPKW QIGEQEFEAL MRMLDNLGYR TGYPYRYPAL REKSKKYSDV EVPASVTGYS 430 440 450 460 470 480 FASDGDSGTC SPLRHSFQKQ QREKTRWLNS GRGDEASEEG QNGSSPKSKT KWTKEDGHRT 490 500 510 520 530 540 STSAVPNLFV PLNTNPKEVQ EMRNKIREQN LQDIKTAGPQ SQVLCGVVMD RSLVQGELVT 550 560 570 580 590 600 ASKAIIEKEY QPHVIVSTTG PNPFTTLTDR ELEEYRREVE RKQKGSEENL DEAREQKEKS 610 620 630 640 650 660 PPDQPAVPHP PPSTPIKLEE DLVPEPTTGD DSDAATFKPT LPDLSPDEPS EALGFPMLEK 670 680 690 700 710 720 EEEAHRPPSP TEAPTEASPE PAPDPAPVAE EAAPSAVEEG AAADPGSDGS PGKSPSKKKK 730 KFRTPSFLKK SKKKSDS
	Isoform 2. Checksum: 350DDCF58AB61357	FASTA	631	69,985
	10 20 30 40 50 60 MNGDSRAAVV TSPPPTTAPH KERYFDRVDE NNPEYLRERN MAPDLRQDFN MMEQKKRVSM 70 80 90 100 110 120 ILQSPAFCEE LESMIQEQFK KGKNPTGLLA LQQIADFMTT NVPNVYPAAP QGGMAALNMS 130 140 150 160 170 180 LGMVTPVNDL RGSDSIAYDK GEKLLRCKLA AFYRLADLFG WSQLIYNHIT TRVNSEQEHF 190 200 210 220 230 240 LIVPFGLLYS EVTASSLVKI NLQGDIVDRG STNLGVNQAG FTLHSAIYAA RPDVKCVVHI 250 260 270 280 290 300 HTPAGAAVSA MKCGLLPISP EALSLGEVAY HDYHGILVDE EEKVLIQKNL GPKSKVLILR 310 320 330 340 350 360 NHGLVSVGES VEEAFYYIHN LVVACEIQVR TLASAGGPDN LVLLNPEKYK AKSRSPGSPV 370 380 390 400 410 420 GEGTGSPPKW QIGEQEFEAL MRMLDNLGYR TGYPYRYPAL REKSKKYSDV EVPASVTGYS 430 440 450 460 470 480 FASDGDSGTC SPLRHSFQKQ QREKTRWLNS GRGDEASEEG QNGSSPKSKT KWTKEDGHRT 490 500 510 520 530 540 STSAVPNLFV PLNTNPKEVQ EMRNKIREQN LQDIKTAGPQ SQVLCGVVMD RSLVQGELVT 550 560 570 580 590 600 ASKAIIEKEY QPHVIVSTTG PNPFTTLTDR ELEEYRREVE RKQKGSEENL DEAREQKEKS 610 620 630 PPDQPAVPHP PPSTPIKLEE GDGCAREYLL P
	Isoform 3. Checksum: D97BFFA790F661CA	FASTA	768	84,303
	10 20 30 40 50 60 MNGDSRAAVV TSPPPTTAPH KERYFDRVDE NNPEYLRERN MAPDLRQDFN MMEQKKRVSM 70 80 90 100 110 120 ILQSPAFCEE LESMIQEQFK KGKNPTGLLA LQQIADFMTT NVPNVYPAAP QGGMAALNMS 130 140 150 160 170 180 LGMVTPVNDL RGSDSIAYDK GEKLLRCKLA AFYRLADLFG WSQLIYNHIT TRVNSEQEHF 190 200 210 220 230 240 LIVPFGLLYS EVTASSLVKI NLQGDIVDRG STNLGVNQAG FTLHSAIYAA RPDVKCVVHI 250 260 270 280 290 300 HTPAGAAVSA MKCGLLPISP EALSLGEVAY HDYHGILVDE EEKVLIQKNL GPKSKVLILR 310 320 330 340 350 360 NHGLVSVGES VEEAFYYIHN LVVACEIQVR TLASAGGPDN LVLLNPEKYK AKSRSPGSPV 370 380 390 400 410 420 GEGTGSPPKW QIGEQEFEAL MRMLDNLGYR TGYPYRYPAL REKSKKYSDV EVPASVTGYS 430 440 450 460 470 480 FASDGDSGTC SPLRHSFQKQ QREKTRWLNS GRGDEASEEG QNGSSPKSKT KVWTNITHDH 490 500 510 520 530 540 VKPLLQSLSS GVCVPSCITN CLWTKEDGHR TSTSAVPNLF VPLNTNPKEV QEMRNKIREQ 550 560 570 580 590 600 NLQDIKTAGP QSQVLCGVVM DRSLVQGELV TASKAIIEKE YQPHVIVSTT GPNPFTTLTD 610 620 630 640 650 660 RELEEYRREV ERKQKGSEEN LDEAREQKEK SPPDQPAVPH PPPSTPIKLE EDLVPEPTTG 670 680 690 700 710 720 DDSDAATFKP TLPDLSPDEP SEALGFPMLE KEEEAHRPPS PTEAPTEASP EPAPDPAPVA 730 740 750 760 EEAAPSAVEE GAAADPGSDG SPGKSPSKKK KKFRTPSFLK KSKKKSDS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Primary structure and domain organization of human alpha and beta adducin." Joshi R.L., Gilligan D.M., Otto E., McLaughlin T., Bennett V.D. J. Cell Biol. 115:665-675(1991) [PubMed: 1840603] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 24-36; 41-47; 516-569 AND 722-729, VARIANT CYS-586. Tissue: Reticulocyte.
[2]	"Genomic organization of the human alpha-adducin gene and its alternately spliced isoforms." Lin B., Nasir J., McDonald H., Graham R., Rommens J.M., Goldberg Y.P., Hayden M.R. Genomics 25:93-99(1995) [PubMed: 7774961] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING.
[3]	"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: 15815621] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"Cloning of the alpha-adducin gene from the Huntington's disease candidate region of chromosome 4 by exon amplification." Taylor S.A., Snell R.G., Buckler A., Ambrose C., Duyao M., Church D., Lin C.S., Altherr M., Bates G.P., Groot N. Nat. Genet. 2:223-227(1992) [PubMed: 1345173] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 531-737 (ISOFORM 1/3).
[5]	"Adducin regulation. Definition of the calmodulin-binding domain and sites of phosphorylation by protein kinases A and C." Matsuoka Y., Hughes C.A., Bennett V. J. Biol. Chem. 271:25157-25166(1996) [PubMed: 8810272] [Abstract] Cited for: PHOSPHORYLATION AT SER-59; SER-408; SER-436; SER-481; SER-716 AND SER-726, PARTIAL PROTEIN SEQUENCE.
[6]	"Phosphorylation of adducin by Rho-kinase plays a crucial role in cell motility." Fukata Y., Oshiro N., Kinoshita N., Kawano Y., Matsuoka Y., Bennett V., Matsuura Y., Kaibuchi K. J. Cell Biol. 145:347-361(1999) [PubMed: 10209029] [Abstract] Cited for: PHOSPHORYLATION AT THR-445 AND THR-480, MUTAGENESIS OF THR-445 AND THR-480.
[7]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-358 AND SER-465, MASS SPECTROMETRY. Tissue: Epithelium.
[8]	"Phosphoproteomic analysis of synaptosomes from human cerebral cortex." DeGiorgis J.A., Jaffe H., Moreira J.E., Carlotti C.G. Jr., Leite J.P., Pant H.C., Dosemeci A. J. Proteome Res. 4:306-315(2005) [PubMed: 15822905] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-355 AND SER-358, MASS SPECTROMETRY. Tissue: Brain cortex.
[9]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-707; SER-710 AND SER-716, MASS SPECTROMETRY. Tissue: Epithelium.
[10]	"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-353; SER-355; SER-358 AND SER-465, MASS SPECTROMETRY.
[11]	"Phosphoproteome of resting human platelets." Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A. J. Proteome Res. 7:526-534(2008) [PubMed: 18088087] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12 AND SER-358, MASS SPECTROMETRY. Tissue: Platelet.
[12]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12; THR-331; SER-334; SER-358; SER-431; SER-436 AND SER-465, MASS SPECTROMETRY.
[13]	"Human alpha-adducin gene, blood pressure, and sodium metabolism." Kamitani A., Wong Z.Y., Fraser R., Davies D.L., Connor J.M., Foy C.J., Watt G.C., Harrap S.B. Hypertension 32:138-143(1998) [PubMed: 9674650] [Abstract] Cited for: VARIANT TRP-460.
[14]	"Patterns of single-nucleotide polymorphisms in candidate genes for blood-pressure homeostasis." Halushka M.K., Fan J.-B., Bentley K., Hsie L., Shen N., Weder A., Cooper R., Lipshutz R., Chakravarti A. Nat. Genet. 22:239-247(1999) [PubMed: 10391210] [Abstract] Cited for: VARIANTS TRP-460 AND CYS-586.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X58141 mRNA. Translation: CAA41149.1. L29296 , L29286, L29287, L29289, L29290, L29291, L29292, L29293, L29294, L29295, L29297, L29298 Genomic DNA. Translation: AAB05645.1. Z74617 Genomic DNA. Translation: CAA98970.1. Sequence problems. Z68280 Genomic DNA. No translation available. S70314 mRNA. Translation: AAB30914.2.
IPI	IPI00019901. IPI00220158. IPI00253279.
PIR	S18207.
RefSeq	NP_001110.2. NP_054908.2. NP_054909.2.
UniGene	Hs.183706 Hs.701490
3D structure databases
DisProt	DP00240.
ModBase	Search...
Protein-protein interaction databases
STRING	P35611.
PTM databases
PhosphoSite	P35611.
Proteomic databases
PRIDE	P35611.
Genome annotation databases
Ensembl	ENST00000264758; ENSP00000264758; ENSG00000087274; Homo sapiens. [Genome view] ENST00000355842; ENSP00000348100; ENSG00000087274; Homo sapiens. [Genome view] ENST00000398123; ENSP00000381191; ENSG00000087274; Homo sapiens. [Genome view] ENST00000398124; ENSP00000381192; ENSG00000087274; Homo sapiens. [Genome view] ENST00000398125; ENSP00000381193; ENSG00000087274; Homo sapiens. [Genome view] ENST00000398129; ENSP00000381197; ENSG00000087274; Homo sapiens. [Genome view] ENST00000446856; ENSP00000399828; ENSG00000087274; Homo sapiens. [Genome view]
GeneID	118.
KEGG	hsa:118.
UCSC	uc003gfp.1. human. uc003gfq.1. human. uc003gfr.1. human.
Organism-specific databases
CTD	118.
GeneCards	GC04P002882.
HGNC	HGNC:243. ADD1.
HPA	CAB009794.
MIM	102680. gene.
PharmGKB	PA31.
GenAtlas	Search...
Phylogenomic databases
HOVERGEN	P35611.
OMA	NSGRGDE.
Enzyme and pathway databases
Reactome	REACT_578. Apoptosis.
Gene expression databases
ArrayExpress	P35611.
Bgee	P35611.
CleanEx	HS_ADD1.
Genevestigator	P35611.
Family and domain databases
InterPro	IPR001303. Aldolase_II/adducin_N. [Graphical view]
Gene3D	G3DSA:3.40.225.10. Aldolase_II/adducin_N. 1 hit.
Pfam	PF00596. Aldolase_II. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	459.
PMAP-CutDB	P35611.
SOURCE	Search...

Entry information

Entry name

ADDA_HUMAN

Accession

Primary (citable) accession number: P35611
Secondary accession number(s): Q13734 , Q14729, Q16156, Q9UJB6

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	December 1, 2000
Last modified:	November 3, 2009
This is version 100 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.