Q8WXF1 (PSPC1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Paraspeckle component 1

Alternative name(s):
Paraspeckle protein 1

Gene names

Name:	PSPC1
Synonyms:	PSP1

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

General annotation (Comments)

Function	Regulates, cooperatively with NONO and SFPQ, androgen receptor-mediated gene transcription activity in Sertoli cell line By similarity. Binds to poly(A), poly(G) and poly(U) RNA homopolymers By similarity. Together with NONO, required for the formation of nuclear paraspeckles. Ref.12
Subunit structure	Forms heterodimers with NONO; this involves formation of a coiled coil domain by helices from both proteins. Found in a RNP complex with CAT2 transcribed nuclear RNA (CTN-RNA). Interaction with NONO is required for its targeting to paraspeckles and perinucleolar caps. Interacts with SFPQ By similarity. Ref.8
Subcellular location	Nucleus › nucleolus. Nucleus matrix By similarity. Cytoplasm By similarity. Nucleus speckle. Note: In punctate subnuclear structures often located adjacent to splicing speckles, called paraspeckles. Colocalizes with NONO and SFPQ in paraspeckles and perinucleolar caps in a RNA-dependent manner. May cycles between paraspeckles and nucleolus. In telophase, when daughter nuclei form, localizes to perinucleolar caps. Ref.1 Ref.8 Ref.12
Tissue specificity	Expressed in pancreas, kidney, skeletal muscle, liver, lung, placenta, brain and heart. Ref.1
Sequence similarities	Belongs to the PSPC family. Contains 2 RRM (RNA recognition motif) domains.
Sequence caution	The sequence BAA91924.1 differs from that shown. Reason: Erroneous termination at position 14. Translated as Lys.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing
Domain	Coiled coil Repeat
Ligand	RNA-binding
Molecular function	Activator
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nuclear matrix Inferred from electronic annotation. Source: UniProtKB-SubCell nuclear speck Inferred from electronic annotation. Source: UniProtKB-SubCell nucleolus Inferred from direct assay. Source: HPA paraspeckles Inferred from electronic annotation. Source: Compara
Molecular_function	RNA binding Inferred from electronic annotation. Source: UniProtKB-KW nucleotide binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
NONO	Q15233	6	EBI-1392258,EBI-350527

Alternative products

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

Isoform 1 (identifier: Q8WXF1-1)

Also known as: PSP1-alpha;

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: Q8WXF1-2)

Also known as: PSP1-beta;

The sequence of this isoform differs from the canonical sequence as follows:
     387-393: REQEMRM → GDKRKCG
     394-523: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 523

523

Paraspeckle component 1

PRO_0000297540

Regions

Domain

82 – 154

73

RRM 1

Domain

156 – 237

82

RRM 2

Region

125 – 358

234

Sufficient for paraspeckles localization

Region

231 – 358

128

Sufficient for perinucleolar caps localization and interaction with NONO

Coiled coil

283 – 377

95

Potential

Compositional bias

394 – 516

123

Gly-rich

Amino acid modifications

Modified residue

409

1

Phosphoserine Ref.10

Modified residue

473

1

Phosphoserine Ref.10

Modified residue

477

1

Phosphoserine Ref.10

Modified residue

509

1

Phosphoserine Ref.9

Natural variations

Alternative sequence

387 – 393

7

REQEMRM → GDKRKCG in isoform 2.

VSP_027274

Alternative sequence

394 – 523

130

Missing in isoform 2.

VSP_027275

Experimental info

Mutagenesis

119

1

F → A: Abolishes accumulation in paraspeckles, but not in perinucleolar caps; when associated with A-121; A-198 and A-200. Ref.8

Mutagenesis

121

1

F → A: Abolishes accumulation in paraspeckles, but not in perinucleolar caps; when associated with A-119; A-198 and A-200. Ref.8

Mutagenesis

198

1

K → A: Abolishes accumulation in paraspeckles, but not in perinucleolar caps; when associated with A-119; A-121 and A-200. Ref.8

Mutagenesis

200

1

F → A: Abolishes accumulation in paraspeckles, but not in perinucleolar caps; when associated with A-119; A-121 and A-198. Ref.8

Mutagenesis

275

1

Y → A: Abolishes interaction with NONO and localization in nuclear paraspeckles; when associated with A-279. Ref.12

Mutagenesis

279

1

W → A: Abolishes interaction with NONO and localization in nuclear paraspeckles; when associated with A-275. Ref.12

Secondary structure

1

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523

Helix Strand Turn

Details...

Helix

80 – 82

3

Beta strand

83 – 88

6

Helix

95 – 101

7

Helix

102 – 105

4

Beta strand

109 – 114

6

Turn

115 – 118

4

Beta strand

119 – 123

5

Helix

127 – 137

11

Beta strand

148 – 151

4

Beta strand

155 – 162

8

Helix

169 – 176

8

Helix

177 – 179

3

Beta strand

182 – 190

9

Beta strand

195 – 205

11

Helix

206 – 218

13

Beta strand

221 – 226

6

Beta strand

231 – 234

4

Beta strand

238 – 242

5

Helix

246 – 248

3

Helix

253 – 259

7

Beta strand

263 – 265

3

Helix

271 – 318

48

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (PSP1-alpha) [UniParc]. Last modified March 1, 2002. Version 1. Checksum: 3A8C44079D64BBF0	FASTA	523	58,744
	10 20 30 40 50 60 MMLRGNLKQV RIEKNPARLR ALESAVGESE PAAAAAMALA LAGEPAPPAP APPEDHPDEE 70 80 90 100 110 120 MGFTIDIKSF LKPGEKTYTQ RCRLFVGNLP TDITEEDFKR LFERYGEPSE VFINRDRGFG 130 140 150 160 170 180 FIRLESRTLA EIAKAELDGT ILKSRPLRIR FATHGAALTV KNLSPVVSNE LLEQAFSQFG 190 200 210 220 230 240 PVEKAVVVVD DRGRATGKGF VEFAAKPPAR KALERCGDGA FLLTTTPRPV IVEPMEQFDD 250 260 270 280 290 300 EDGLPEKLMQ KTQQYHKERE QPPRFAQPGT FEFEYASRWK ALDEMEKQQR EQVDRNIREA 310 320 330 340 350 360 KEKLEAEMEA ARHEHQLMLM RQDLMRRQEE LRRLEELRNQ ELQKRKQIQL RHEEEHRRRE 370 380 390 400 410 420 EEMIRHREQE ELRRQQEGFK PNYMENREQE MRMGDMGPRG AINMGDAFSP APAGNQGPPP 430 440 450 460 470 480 MMGMNMNNRA TIPGPPMGPG PAMGPEGAAN MGTPMMPDNG AVHNDRFPQG PPSQMGSPMG 490 500 510 520 SRTGSETPQA PMSGVGPVSG GPGGFGRGSQ GGNFEGPNKR RRY
	Isoform 2 (PSP1-beta) [UniParc]. Checksum: 67F1A7EBF93050B2	FASTA	393	45,571
	10 20 30 40 50 60 MMLRGNLKQV RIEKNPARLR ALESAVGESE PAAAAAMALA LAGEPAPPAP APPEDHPDEE 70 80 90 100 110 120 MGFTIDIKSF LKPGEKTYTQ RCRLFVGNLP TDITEEDFKR LFERYGEPSE VFINRDRGFG 130 140 150 160 170 180 FIRLESRTLA EIAKAELDGT ILKSRPLRIR FATHGAALTV KNLSPVVSNE LLEQAFSQFG 190 200 210 220 230 240 PVEKAVVVVD DRGRATGKGF VEFAAKPPAR KALERCGDGA FLLTTTPRPV IVEPMEQFDD 250 260 270 280 290 300 EDGLPEKLMQ KTQQYHKERE QPPRFAQPGT FEFEYASRWK ALDEMEKQQR EQVDRNIREA 310 320 330 340 350 360 KEKLEAEMEA ARHEHQLMLM RQDLMRRQEE LRRLEELRNQ ELQKRKQIQL RHEEEHRRRE 370 380 390 EEMIRHREQE ELRRQQEGFK PNYMENGDKR KCG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Paraspeckles: a novel nuclear domain." Fox A.H., Lam Y.W., Leung A.K.L., Lyon C.E., Andersen J., Mann M., Lamond A.I. Curr. Biol. 12:13-25(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), PROTEIN SEQUENCE OF 21-83; 105-124; 135-143; 185-194; 199-210; 252-259; 265-289; 327-345; 352-357; 366-374 AND 483-507, MASS SPECTROMETRY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[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 2). Tissue: Placenta.
[3]	"The DNA sequence and analysis of human chromosome 13." Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T. , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T. Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	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 (SEP-2005) to the EMBL/GenBank/DDBJ databases 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 2). Tissue: Skin.
[6]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 37-523 (ISOFORM 2).
[7]	"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] OF 192-523 (ISOFORM 2). Tissue: Kidney.
[8]	"P54nrb forms a heterodimer with PSP1 that localizes to paraspeckles in an RNA-dependent manner." Fox A.H., Bond C.S., Lamond A.I. Mol. Biol. Cell 16:5304-5315(2005) [PubMed] [Europe PMC] [Abstract] Cited for: SUBUNIT, INTERACTION WITH NONO, MUTAGENESIS OF PHE-119; PHE-121; LYS-198 AND PHE-200, SUBCELLULAR LOCATION.
[9]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-509, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[10]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-409; SER-473 AND SER-477, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[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]	"Structure of the heterodimer of human NONO and paraspeckle protein component 1 and analysis of its role in subnuclear body formation." Passon D.M., Lee M., Rackham O., Stanley W.A., Sadowska A., Filipovska A., Fox A.H., Bond C.S. Proc. Natl. Acad. Sci. U.S.A. 109:4846-4850(2012) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 61-320 IN COMPLEX WITH NONO, FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF TYR-275 AND TRP-279.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF448795 mRNA. Translation: AAL59601.1.
AF449627 mRNA. Translation: AAL59602.1.
AK001817 mRNA. Translation: BAA91924.1. Sequence problems.
AL354808 Genomic DNA. Translation: CAI41004.1.
AL354808 Genomic DNA. Translation: CAI41005.1.
CH471075 Genomic DNA. Translation: EAX08232.1.
BC014184 mRNA. Translation: AAH14184.2.
CR457272 mRNA. Translation: CAG33553.1.
AL834505 mRNA. Translation: CAD39162.1.

IPI

IPI00103525.
IPI00395775.

RefSeq

NP_001035879.1. NM_001042414.2.

UniGene

Hs.213198.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3SDE	X-ray	1.90	A	61-320	[»]

ProteinModelPortal

Q8WXF1.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q8WXF1. 8 interactions.

MINT

MINT-1395719.

STRING

9606.ENSP00000343966.

PTM databases

PhosphoSite

Q8WXF1.

Polymorphism databases

DMDM

74762636.

Proteomic databases

PaxDb

Q8WXF1.

PRIDE

Q8WXF1.

Protocols and materials databases

DNASU

55269.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000338910; ENSP00000343966; ENSG00000121390.
ENST00000427943; ENSP00000393069; ENSG00000121390.
ENST00000471658; ENSP00000436038; ENSG00000121390.
ENST00000492741; ENSP00000435921; ENSG00000121390.

GeneID

55269.

KEGG

hsa:55269.

UCSC

uc021rgx.1. human.

Organism-specific databases

CTD

55269.

GeneCards

GC13M020249.

H-InvDB

HIX0011177.

HGNC

HGNC:20320. PSPC1.

HPA

HPA038904.

MIM

612408. gene.

neXtProt

NX_Q8WXF1.

PharmGKB

PA134968603.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG298586.

HOGENOM

HOG000231095.

HOVERGEN

HBG009801.

InParanoid

Q8WXF1.

OMA

DNREQEM.

OrthoDB

EOG444KKN.

PhylomeDB

Q8WXF1.

Gene expression databases

ArrayExpress

Q8WXF1.

Bgee

Q8WXF1.

CleanEx

HS_PSPC1.

Genevestigator

Q8WXF1.

Family and domain databases

Gene3D

3.30.70.330. 2 hits.

InterPro

IPR012975. NOPS.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]

Pfam

PF08075. NOPS. 1 hit.
PF00076. RRM_1. 2 hits.
[Graphical view]

SMART

SM00360. RRM. 2 hits.
[Graphical view]

PROSITE

PS50102. RRM. 2 hits.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

PSPC1. human.

GenomeRNAi

55269.

NextBio

59380.

SOURCE

Search...

Entry information

Entry name

PSPC1_HUMAN

Accession

Primary (citable) accession number: Q8WXF1
Secondary accession number(s): Q5JTQ3 , Q8NCZ9, Q8WXE8, Q9NV36

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 21, 2007
Last sequence update:	March 1, 2002
Last modified:	May 1, 2013
This is version 107 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.