P26599 (PTBP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Polypyrimidine tract-binding protein 1
Short name=PTB

Alternative name(s):
57 kDa RNA-binding protein PPTB-1
Heterogeneous nuclear ribonucleoprotein I
Short name=hnRNP I

Gene names

Name:	PTBP1
Synonyms:	PTB

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	531 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Plays a role in pre-mRNA splicing and in the regulation of alternative splicing events. Activates exon skipping of its own pre-mRNA during muscle cell differentiation. Binds to the polypyrimidine tract of introns. May promote RNA looping when bound to two separate polypyrimidine tracts in the same pre-mRNA. May promote the binding of U2 snRNP to pre-mRNA. Cooperates with RAVER1 to modulate switching between mutually exclusive exons during maturation of the TPM1 pre-mRNA. Represses the splicing of MAPT/Tau exon 10. Ref.9 Ref.10 Ref.11 Ref.19 Ref.22
Subunit structure	Monomer. Part of a ternary complex containing KHSRP, PTBP1, PTBP2 and HNRPH1. Interacts with RAVER1 and SFPQ. Ref.8 Ref.9 Ref.21
Subcellular location	Nucleus.
Sequence similarities	Contains 4 RRM (RNA recognition motif) domains.

Ontologies

Keywords
Biological process	mRNA processing mRNA splicing
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Domain	Repeat
Ligand	RNA-binding
Molecular function	Activator Repressor
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	negative regulation of muscle cell differentiation Inferred from direct assay Ref.19. Source: UniProtKB negative regulation of nuclear mRNA splicing, via spliceosome Inferred from direct assay Ref.10. Source: UniProtKB nuclear mRNA splicing, via spliceosome Traceable author statement. Source: Reactome regulation of alternative nuclear mRNA splicing, via spliceosome Inferred from direct assay Ref.11Ref.19. Source: UniProtKB
Cellular component	heterogeneous nuclear ribonucleoprotein complex Traceable author statement. Source: ProtInc nucleolus Traceable author statement. Source: ProtInc nucleoplasm Traceable author statement. Source: Reactome
Molecular function	nucleotide binding Inferred from electronic annotation. Source: InterPro poly-pyrimidine tract binding Traceable author statement. Source: ProtInc pre-mRNA binding Inferred from direct assay Ref.11. Source: UniProtKB protein binding Inferred from physical interaction Ref.8. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
hnrnpab	Q7ZYE9	4	EBI-350540,EBI-1086317	From a different organism.
PCBP1	Q15365	2	EBI-350540,EBI-946095
QKI	Q96PU8	2	EBI-350540,EBI-945792
SFPQ	P23246	2	EBI-350540,EBI-355453

Alternative products

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

Note: Additional isoforms seem to exist.

Isoform 1 (identifier: P26599-1)

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: P26599-2)

Also known as: PTB2;

The sequence of this isoform differs from the canonical sequence as follows:
     297-297: F → FASPYAGAGFPPTFAIPQAA

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 531

531

Polypyrimidine tract-binding protein 1

PRO_0000081737

Regions

Domain

59 – 143

85

RRM 1

Domain

184 – 260

77

RRM 2

Domain

337 – 411

75

RRM 3

Domain

454 – 529

76

RRM 4

Compositional bias

316 – 323

8

Poly-Ala

Amino acid modifications

Modified residue

1

1

N-acetylmethionine Ref.6 Ref.16

Modified residue

16

1

Phosphoserine Ref.15

Modified residue

127

1

Phosphotyrosine Ref.12

Modified residue

141

1

Phosphoserine Ref.13 Ref.15 Ref.17

Modified residue

433

1

Phosphoserine Ref.13 Ref.14

Natural variations

Alternative sequence

297

1

F → FASPYAGAGFPPTFAIPQAA in isoform 2.

VSP_005802

Secondary structure

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531

Helix Strand Turn

Details...

Beta strand

60 – 63

4

Helix

72 – 82

11

Beta strand

85 – 91

7

Turn

92 – 95

4

Beta strand

96 – 103

8

Helix

104 – 114

11

Beta strand

132 – 135

4

Turn

142 – 145

4

Beta strand

183 – 188

6

Helix

197 – 207

11

Beta strand

210 – 220

11

Beta strand

222 – 229

8

Helix

231 – 240

10

Beta strand

246 – 249

4

Beta strand

253 – 257

5

Beta strand

259 – 262

4

Beta strand

269 – 276

8

Helix

329 – 332

4

Beta strand

339 – 342

4

Beta strand

346 – 348

3

Helix

351 – 359

9

Beta strand

365 – 368

4

Beta strand

378 – 380

3

Turn

382 – 384

3

Helix

385 – 394

10

Beta strand

405 – 408

4

Beta strand

417 – 425

9

Beta strand

427 – 431

5

Beta strand

437 – 440

4

Beta strand

455 – 458

4

Helix

467 – 476

10

Beta strand

483 – 488

6

Beta strand

494 – 497

4

Helix

501 – 511

11

Beta strand

524 – 527

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified August 1, 1992. Version 1. Checksum: BE12D5EA21537BED	FASTA	531	57,221
	10 20 30 40 50 60 MDGIVPDIAV GTKRGSDELF STCVTNGPFI MSSNSASAAN GNDSKKFKGD SRSAGVPSRV 70 80 90 100 110 120 IHIRKLPIDV TEGEVISLGL PFGKVTNLLM LKGKNQAFIE MNTEEAANTM VNYYTSVTPV 130 140 150 160 170 180 LRGQPIYIQF SNHKELKTDS SPNQARAQAA LQAVNSVQSG NLALAASAAA VDAGMAMAGQ 190 200 210 220 230 240 SPVLRIIVEN LFYPVTLDVL HQIFSKFGTV LKIITFTKNN QFQALLQYAD PVSAQHAKLS 250 260 270 280 290 300 LDGQNIYNAC CTLRIDFSKL TSLNVKYNND KSRDYTRPDL PSGDSQPSLD QTMAAAFGLS 310 320 330 340 350 360 VPNVHGALAP LAIPSAAAAA AAAGRIAIPG LAGAGNSVLL VSNLNPERVT PQSLFILFGV 370 380 390 400 410 420 YGDVQRVKIL FNKKENALVQ MADGNQAQLA MSHLNGHKLH GKPIRITLSK HQNVQLPREG 430 440 450 460 470 480 QEDQGLTKDY GNSPLHRFKK PGSKNFQNIF PPSATLHLSN IPPSVSEEDL KVLFSSNGGV 490 500 510 520 530 VKGFKFFQKD RKMALIQMGS VEEAVQALID LHNHDLGENH HLRVSFSKST I
	Isoform 2 (PTB2) [UniParc]. Checksum: 70CB96D0530CA091	FASTA	550	59,037
	10 20 30 40 50 60 MDGIVPDIAV GTKRGSDELF STCVTNGPFI MSSNSASAAN GNDSKKFKGD SRSAGVPSRV 70 80 90 100 110 120 IHIRKLPIDV TEGEVISLGL PFGKVTNLLM LKGKNQAFIE MNTEEAANTM VNYYTSVTPV 130 140 150 160 170 180 LRGQPIYIQF SNHKELKTDS SPNQARAQAA LQAVNSVQSG NLALAASAAA VDAGMAMAGQ 190 200 210 220 230 240 SPVLRIIVEN LFYPVTLDVL HQIFSKFGTV LKIITFTKNN QFQALLQYAD PVSAQHAKLS 250 260 270 280 290 300 LDGQNIYNAC CTLRIDFSKL TSLNVKYNND KSRDYTRPDL PSGDSQPSLD QTMAAAFASP 310 320 330 340 350 360 YAGAGFPPTF AIPQAAGLSV PNVHGALAPL AIPSAAAAAA AAGRIAIPGL AGAGNSVLLV 370 380 390 400 410 420 SNLNPERVTP QSLFILFGVY GDVQRVKILF NKKENALVQM ADGNQAQLAM SHLNGHKLHG 430 440 450 460 470 480 KPIRITLSKH QNVQLPREGQ EDQGLTKDYG NSPLHRFKKP GSKNFQNIFP PSATLHLSNI 490 500 510 520 530 540 PPSVSEEDLK VLFSSNGGVV KGFKFFQKDR KMALIQMGSV EEAVQALIDL HNHDLGENHH 550 LRVSFSKSTI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of cDNAs encoding the polypyrimidine tract-binding protein." Gil A., Sharp P.A., Jamison S.F., Garcia-Blanco M.A. Genes Dev. 5:1224-1236(1991) [PubMed: 1906035] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 123-130 AND 219-238. Tissue: Placenta.
[2]	"Characterization and molecular cloning of polypyrimidine tract-binding protein: a component of a complex necessary for pre-mRNA splicing." Patton J.G., Mayer S.A., Tempst P., Nadal-Ginard B. Genes Dev. 5:1237-1251(1991) [PubMed: 1906036] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"hnRNP I, the polypyrimidine tract-binding protein: distinct nuclear localization and association with hnRNAs." Ghetti A., Pinol-Roma S., Michael W., Morandi C., Dreyfuss G. Nucleic Acids Res. 20:3671-3678(1992) [PubMed: 1641332] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[4]	"The DNA sequence and biology of human chromosome 19." Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M. Nature 428:529-535(2004) [PubMed: 15057824] [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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Skin.
[6]	Bienvenut W.V., Heiserich L., Boulahbel H., Gottlieb E., Matallanas D., Cooper W.N., Boldt K., von Kriegsheim A.F., Kolch W. Submitted (JUL-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 1-13; 65-92; 123-134; 219-238; 326-348; 411-418; 429-437 AND 472-482, ACETYLATION AT MET-1, MASS SPECTROMETRY. Tissue: Colon carcinoma, Hepatoma and Mammary carcinoma.
[7]	"Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes." Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E., Vandekerckhove J. Electrophoresis 13:960-969(1992) [PubMed: 1286667] [Abstract] Cited for: PROTEIN SEQUENCE OF 123-129; 399-405; 411-426 AND 429-437. Tissue: Keratinocyte.
[8]	"Differential nuclear localization and nuclear matrix association of the splicing factors PSF and PTB." Meissner M., Dechat T., Gerner C., Grimm R., Foisner R., Sauermann G. J. Cell. Biochem. 76:559-566(2000) [PubMed: 10653975] [Abstract] Cited for: INTERACTION WITH SFPQ.
[9]	"Cooperative assembly of an hnRNP complex induced by a tissue-specific homolog of polypyrimidine tract binding protein." Markovtsov V., Nikolic J.M., Goldman J.A., Turck C.W., Chou M.-Y., Black D.L. Mol. Cell. Biol. 20:7463-7479(2000) [PubMed: 11003644] [Abstract] Cited for: FUNCTION, INTERACTION WITH HNRPH1; PTBP2 AND KHSRP.
[10]	"Tau exon 10, whose missplicing causes frontotemporal dementia, is regulated by an intricate interplay of cis elements and trans factors." Wang J., Gao Q.S., Wang Y., Lafyatis R., Stamm S., Andreadis A. J. Neurochem. 88:1078-1090(2004) [PubMed: 15009664] [Abstract] Cited for: FUNCTION.
[11]	"Exon selection in alpha-tropomyosin mRNA is regulated by the antagonistic action of RBM4 and PTB." Lin J.C., Tarn W.Y. Mol. Cell. Biol. 25:10111-10121(2005) [PubMed: 16260624] [Abstract] Cited for: FUNCTION, RNA-BINDING.
[12]	"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-127, MASS SPECTROMETRY. Tissue: Lung carcinoma.
[13]	"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra." Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D. J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-141 AND SER-433, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-433, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[15]	"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-16 AND SER-141, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[16]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[17]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed: 19369195] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-141, MASS SPECTROMETRY.
[18]	"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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]	"RBM4 down-regulates PTB and antagonizes its activity in muscle cell-specific alternative splicing." Lin J.C., Tarn W.Y. J. Cell Biol. 193:509-520(2011) [PubMed: 21518792] [Abstract] Cited for: FUNCTION.
[20]	"Structure of tandem RNA recognition motifs from polypyrimidine tract binding protein reveals novel features of the RRM fold." Conte M.R., Gruene T., Ghuman J., Kelly G., Ladas A., Matthews S., Curry S. EMBO J. 19:3132-3141(2000) [PubMed: 10856256] [Abstract] Cited for: STRUCTURE BY NMR OF 335-531, RNA-BINDING.
[21]	"Structure and RNA interactions of the N-terminal RRM domains of PTB." Simpson P.J., Monie T.P., Szendroei A., Davydova N., Tyzack J.K., Conte M.R., Read C.M., Cary P.D., Svergun D.I., Konarev P.V., Curry S., Matthews S. Structure 12:1631-1643(2004) [PubMed: 15341728] [Abstract] Cited for: STRUCTURE BY NMR OF 55-301, SUBUNIT, RNA-BINDING.
[22]	"Structure of PTB bound to RNA: specific binding and implications for splicing regulation." Oberstrass F.C., Auweter S.D., Erat M., Hargous Y., Henning A., Wenter P., Reymond L., Amir-Ahmady B., Pitsch S., Black D.L., Allain F.H. Science 309:2054-2057(2005) [PubMed: 16179478] [Abstract] Cited for: STRUCTURE BY NMR OF 49-531 IN COMPLEXES WITH RNA, FUNCTION.
[23]	"Structure of the two most C-terminal RNA recognition motifs of PTB using segmental isotope labeling." Vitali F., Henning A., Oberstrass F.C., Hargous Y., Auweter S.D., Erat M., Allain F.H. EMBO J. 25:150-162(2006) [PubMed: 16362043] [Abstract] Cited for: STRUCTURE BY NMR OF 324-531.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X62006 mRNA. Translation: CAA43973.1.
X65371 mRNA. Translation: CAA46443.1.
X65372 mRNA. Translation: CAA46444.1.
X60648 mRNA. Translation: CAA43056.1.
X66975 mRNA. Translation: CAA47386.1.
AC006273 Genomic DNA. Translation: AAC99798.1.
BC004383 mRNA. Translation: AAH04383.1.

IPI

IPI00179964.
IPI00334175.

PIR

S23016.

RefSeq

NP_002810.1. NM_002819.4.
NP_114367.1. NM_031990.3.
NP_114368.1. NM_031991.3.
NP_787041.1. NM_175847.2.

UniGene

Hs.172550.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1QM9	NMR	-	A	335-531	[»]
1SJQ	NMR	-	A	55-147	[»]
1SJR	NMR	-	A	147-301	[»]
2AD9	NMR	-	A	49-146	[»]
2ADB	NMR	-	A	172-298	[»]
2ADC	NMR	-	A	324-531	[»]
2EVZ	NMR	-	A	324-531	[»]

ProteinModelPortal

P26599.

SMR

P26599. Positions 49-531.

ModBase

Search...

Protein-protein interaction databases

IntAct

P26599. 20 interactions.

MINT

MINT-1348690.

STRING

P26599.

PTM databases

PhosphoSite

P26599.

Polymorphism databases

DMDM

131528.

2D gel databases

SWISS-2DPAGE

P26599.

Aarhus/Ghent-2DPAGE

1505. NEPHGE.

Proteomic databases

PRIDE

P26599.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000349038; ENSP00000014112; ENSG00000011304.

GeneID

5725.

KEGG

hsa:5725.

UCSC

uc002lpq.1. human.
uc002lpr.1. human.

Organism-specific databases

CTD

5725.

GeneCards

GC19P000797.

HGNC

HGNC:9583. PTBP1.

HPA

CAB013507.

MIM

600693. gene.

neXtProt

NX_P26599.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG10547.

HOVERGEN

HBG069548.

PhylomeDB

P26599.

Enzyme and pathway databases

Reactome

REACT_1675. mRNA Processing.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpress

P26599.

Bgee

P26599.

CleanEx

HS_PTBP1.

Genevestigator

P26599.

GermOnline

ENSG00000011304. Homo sapiens.

Family and domain databases

InterPro

IPR006536. HnRNP-L_PTB.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]

Gene3D

G3DSA:3.30.70.330. a_b_plait_nuc_bd. 4 hits.

KO

K13218.

Pfam

PF00076. RRM_1. 3 hits.
[Graphical view]

SMART

SM00360. RRM. 4 hits.
[Graphical view]

TIGRFAMs

TIGR01649. HnRNP-L_PTB. 1 hit.

PROSITE

PS50102. RRM. 4 hits.
[Graphical view]

ProtoNet

Search...

Other

NextBio

22252.

PMAP-CutDB

P26599.

SOURCE

Search...

Entry information

Entry name

PTBP1_HUMAN

Accession

Primary (citable) accession number: P26599

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	August 1, 1992
Last modified:	January 25, 2012
This is version 142 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.