Q8IUX7 (AEBP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Adipocyte enhancer-binding protein 1
Short name=AE-binding protein 1

Alternative name(s):
Aortic carboxypeptidase-like protein

Gene names

Name:	AEBP1
Synonyms:	ACLP

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	1158 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)

Function	May positively regulate MAP-kinase activity in adipocytes, leading to enhanced adipocyte proliferation and reduced adipocyte differentiation By similarity. May also positively regulate NF-kappa-B activity in macrophages by promoting the phosphorylation and subsequent degradation of I-kappa-B-alpha (NFKBIA), leading to enhanced macrophage inflammatory responsiveness By similarity. Can act as a transcriptional repressor By similarity.
Subunit structure	Interacts with GNG5, NFKBIA, MAPK1, MAPK3 and PTEN By similarity. May interact with calmodulin By similarity. Binds to DNA in vitro By similarity.
Subcellular location	Isoform 1: Secreted By similarity. Isoform 2: Cytoplasm Probable. Nucleus Probable.
Tissue specificity	Expressed in osteoblast and visceral fat. Ref.7
Post-translational modification	Phosphorylated by MAPK1 in vitro By similarity.
Sequence similarities	Belongs to the peptidase M14 family. Contains 1 F5/8 type C domain.
Caution	Although related to peptidase M14 family, lacks the active sites residues and zinc-binding sites, suggesting that it has no carboxypeptidase activity.
Sequence caution	The sequence BAD92981.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus Secreted
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Signal
Ligand	Calmodulin-binding DNA-binding
Molecular function	Repressor
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell adhesion Inferred from electronic annotation. Source: InterPro muscle organ development Traceable author statement Ref.1. Source: ProtInc proteolysis Inferred from electronic annotation. Source: InterPro skeletal system development Traceable author statement Ref.7. Source: ProtInc transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell extracellular space Inferred from direct assay PubMed 20551380. Source: BHF-UCL nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW carboxypeptidase activity Traceable author statement Ref.7. Source: ProtInc metallocarboxypeptidase activity Inferred from electronic annotation. Source: InterPro sequence-specific DNA binding transcription factor activity Traceable author statement Ref.7. Source: ProtInc transcription corepressor activity Inferred from electronic annotation. Source: Compara zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

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

Isoform 1 (identifier: Q8IUX7-1)

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: Q8IUX7-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-457: Missing.
     458-495: ITQGRDSSIH...VMYTNGYEEM → MRKWWAPCPG...STALRPASPQ
     543-544: AP → ARECGGLAGALSGGGVLGWASRHPAKDNPASLAA

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 25	25	Potential
	Chain	26 – 1158	1133	Adipocyte enhancer-binding protein 1		PRO_0000333189
Regions
	Domain	383 – 540	158	F5/8 type C
	Region	390 – 555	166	Required for DNA-binding and interaction with NFKBIA By similarity
	Region	421 – 624	204	Interaction with MAPK1 and MAPK3 By similarity
	Region	555 – 985	431	Interaction with PTEN By similarity
	Region	941 – 1158	218	Required for transcriptional repression By similarity
	Region	1006 – 1158	153	Interaction with MAPK1 and MAPK3 By similarity
	Compositional bias	47 – 326	280	Pro-rich
	Compositional bias	1079 – 1136	58	Glu-rich
Amino acid modifications
	Glycosylation	528	1	N-linked (GlcNAc...) Ref.8
	Glycosylation	922	1	N-linked (GlcNAc...) Ref.8
Natural variations
	Alternative sequence	1 – 457	457	Missing in isoform 2.		VSP_033467
	Alternative sequence	458 – 495	38	ITQGR…GYEEM → MRKWWAPCPGSWLCSHCLGE GWALRGAGSTALRPASPQ in isoform 2.		VSP_033468
	Alternative sequence	543 – 544	2	AP → ARECGGLAGALSGGGVLGWA SRHPAKDNPASLAA in isoform 2.		VSP_033469
	Natural variant	273	1	P → T. Corresponds to variant rs2537188 [ dbSNP | Ensembl ].		VAR_043118
	Natural variant	648	1	D → E. Corresponds to variant rs11770649 [ dbSNP | Ensembl ].		VAR_043119
	Natural variant	1001	1	P → L. Corresponds to variant rs4724285 [ dbSNP | Ensembl ].		VAR_043120
	Natural variant	1133	1	K → E. Ref.3 Corresponds to variant rs13928 [ dbSNP | Ensembl ].		VAR_043121
	Natural variant	1148	1	V → I. Corresponds to variant rs13898 [ dbSNP | Ensembl ].		VAR_043122
Experimental info
	Sequence conflict	145	1	K → E in AAC25585. Ref.1
	Sequence conflict	218	1	R → Q in AAC25585. Ref.1
	Sequence conflict	569	1	D → G in BAC87026. Ref.2
	Sequence conflict	715	1	R → G in BAC87026. Ref.2
	Sequence conflict	884	1	S → G in BAC87026. Ref.2
	Sequence conflict	1079	1	E → G in BAD92981. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: 1D7F4A20451646AE	FASTA	1,158	130,929
	10 20 30 40 50 60 MAAVRGAPLL SCLLALLALC PGGRPQTVLT DDEIEEFLEG FLSELEPEPR EDDVEAPPPP 70 80 90 100 110 120 EPTPRVRKAQ AGGKPGKRPG TAAEVPPEKT KDKGKKGKKD KGPKVPKESL EGSPRPPKKG 130 140 150 160 170 180 KEKPPKATKK PKEKPPKATK KPKEKPPKAT KKPKEKPPKA TKKPPSGKRP PILAPSETLE 190 200 210 220 230 240 WPLPPPPSPG PEELPQEGGA PLSNNWQNPG EETHVEAREH QPEPEEETEQ PTLDYNDQIE 250 260 270 280 290 300 REDYEDFEYI RRQKQPRPPP SRRRRPERVW PEPPEEKAPA PAPEERIEPP VKPLLPPLPP 310 320 330 340 350 360 DYGDGYVIPN YDDMDYYFGP PPPQKPDAER QTDEEKEELK KPKKEDSSPK EETDKWAVEK 370 380 390 400 410 420 GKDHKEPRKG EELEEEWTPT EKVKCPPIGM ESHRIEDNQI RASSMLRHGL GAQRGRLNMQ 430 440 450 460 470 480 TGATEDDYYD GAWCAEDDAR TQWIEVDTRR TTRFTGVITQ GRDSSIHDDF VTTFFVGFSN 490 500 510 520 530 540 DSQTWVMYTN GYEEMTFHGN VDKDTPVLSE LPEPVVARFI RIYPLTWNGS LCMRLEVLGC 550 560 570 580 590 600 SVAPVYSYYA QNEVVATDDL DFRHHSYKDM RQLMKVVNEE CPTITRTYSL GKSSRGLKIY 610 620 630 640 650 660 AMEISDNPGE HELGEPEFRY TAGIHGNEVL GRELLLLLMQ YLCREYRDGN PRVRSLVQDT 670 680 690 700 710 720 RIHLVPSLNP DGYEVAAQMG SEFGNWALGL WTEEGFDIFE DFPDLNSVLW GAEERKWVPY 730 740 750 760 770 780 RVPNNNLPIP ERYLSPDATV STEVRAIIAW MEKNPFVLGA NLNGGERLVS YPYDMARTPT 790 800 810 820 830 840 QEQLLAAAMA AARGEDEDEV SEAQETPDHA IFRWLAISFA SAHLTLTEPY RGGCQAQDYT 850 860 870 880 890 900 GGMGIVNGAK WNPRTGTIND FSYLHTNCLE LSFYLGCDKF PHESELPREW ENNKEALLTF 910 920 930 940 950 960 MEQVHRGIKG VVTDEQGIPI ANATISVSGI NHGVKTASGG DYWRILNPGE YRVTAHAEGY 970 980 990 1000 1010 1020 TPSAKTCNVD YDIGATQCNF ILARSNWKRI REIMAMNGNR PIPHIDPSRP MTPQQRRLQQ 1030 1040 1050 1060 1070 1080 RRLQHRLRLR AQMRLRRLNA TTTLGPHTVP PTLPPAPATT LSTTIEPWGL IPPTTAGWEE 1090 1100 1110 1120 1130 1140 SETETYTEVV TEFGTEVEPE FGTKVEPEFE TQLEPEFETQ LEPEFEEEEE EEKEEEIATG 1150 QAFPFTTVET YTVNFGDF
	Isoform 2 [UniParc]. Checksum: A749B43E37811E45	FASTA	733	82,183
	10 20 30 40 50 60 MRKWWAPCPG SWLCSHCLGE GWALRGAGST ALRPASPQTF HGNVDKDTPV LSELPEPVVA 70 80 90 100 110 120 RFIRIYPLTW NGSLCMRLEV LGCSVARECG GLAGALSGGG VLGWASRHPA KDNPASLAAV 130 140 150 160 170 180 YSYYAQNEVV ATDDLDFRHH SYKDMRQLMK VVNEECPTIT RTYSLGKSSR GLKIYAMEIS 190 200 210 220 230 240 DNPGEHELGE PEFRYTAGIH GNEVLGRELL LLLMQYLCRE YRDGNPRVRS LVQDTRIHLV 250 260 270 280 290 300 PSLNPDGYEV AAQMGSEFGN WALGLWTEEG FDIFEDFPDL NSVLWGAEER KWVPYRVPNN 310 320 330 340 350 360 NLPIPERYLS PDATVSTEVR AIIAWMEKNP FVLGANLNGG ERLVSYPYDM ARTPTQEQLL 370 380 390 400 410 420 AAAMAAARGE DEDEVSEAQE TPDHAIFRWL AISFASAHLT LTEPYRGGCQ AQDYTGGMGI 430 440 450 460 470 480 VNGAKWNPRT GTINDFSYLH TNCLELSFYL GCDKFPHESE LPREWENNKE ALLTFMEQVH 490 500 510 520 530 540 RGIKGVVTDE QGIPIANATI SVSGINHGVK TASGGDYWRI LNPGEYRVTA HAEGYTPSAK 550 560 570 580 590 600 TCNVDYDIGA TQCNFILARS NWKRIREIMA MNGNRPIPHI DPSRPMTPQQ RRLQQRRLQH 610 620 630 640 650 660 RLRLRAQMRL RRLNATTTLG PHTVPPTLPP APATTLSTTI EPWGLIPPTT AGWEESETET 670 680 690 700 710 720 YTEVVTEFGT EVEPEFGTKV EPEFETQLEP EFETQLEPEF EEEEEEEKEE EIATGQAFPF 730 TTVETYTVNF GDF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Aortic carboxypeptidase-like protein, a novel protein with discoidin and carboxypeptidase-like domains, is up-regulated during vascular smooth muscle cell differentiation." Layne M.D., Endege W.O., Jain M.K., Yet S.-F., Hsieh C.-M., Chin M.T., Perrella M.A., Blanar M.A., Haber E., Lee M.-E. J. Biol. Chem. 273:15654-15660(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Aortic smooth muscle.
[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).
[3]	Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F. Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT GLU-1133. Tissue: Aortic endothelium.
[4]	"Human chromosome 7: DNA sequence and biology." Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S. , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C. Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	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].
[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] (ISOFORM 1). Tissue: Brain.
[7]	"A cDNA cloning of human AEBP1 from primary cultured osteoblasts and its expression in a differentiating osteoblastic cell line." Ohno I., Hashimoto J., Shimizu K., Takaoka K., Ochi T., Matsubara K., Okubo K. Biochem. Biophys. Res. Commun. 228:411-414(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 314-1158 (ISOFORM 1), TISSUE SPECIFICITY. Tissue: Cancellous bone.
[8]	"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry." Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H. J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-528 AND ASN-922, MASS SPECTROMETRY. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF053944 mRNA. Translation: AAC25585.1. AK127541 mRNA. Translation: BAC87026.1. AB209744 mRNA. Translation: BAD92981.1. Different initiation. CH236960 Genomic DNA. Translation: EAL23768.1. CH471128 Genomic DNA. Translation: EAW61119.1. BC038588 mRNA. Translation: AAH38588.1. D86479 mRNA. Translation: BAA13094.1.
IPI	IPI00745313. IPI00894097.
PIR	JC5256.
RefSeq	NP_001120.3. NM_001129.3.
UniGene	Hs.439463.
3D structure databases
HSSP	HSSP built from PDB template 1H8L based on UniProtKB P83852.
ProteinModelPortal	Q8IUX7.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q8IUX7. 1 interaction.
MINT	MINT-7034542.
STRING	9606.ENSP00000223357.
Protein family/group databases
MEROPS	M14.951.
PTM databases
PhosphoSite	Q8IUX7.
Polymorphism databases
DMDM	74728002.
Proteomic databases
PaxDb	Q8IUX7.
PRIDE	Q8IUX7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000223357; ENSP00000223357; ENSG00000106624. ENST00000450684; ENSP00000398878; ENSG00000106624.
GeneID	165.
KEGG	hsa:165.
UCSC	uc003tkb.3. human. uc003tkc.4. human.
Organism-specific databases
CTD	165.
GeneCards	GC07P044143.
HGNC	HGNC:303. AEBP1.
HPA	CAB009966.
MIM	602981. gene.
neXtProt	NX_Q8IUX7.
PharmGKB	PA24604.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG292169.
HOGENOM	HOG000232185.
HOVERGEN	HBG003410.
InParanoid	Q8IUX7.
OMA	MREQMRL.
OrthoDB	EOG4VQ9NT.
PhylomeDB	Q8IUX7.
Gene expression databases
ArrayExpress	Q8IUX7.
Bgee	Q8IUX7.
CleanEx	HS_AEBP1.
Genevestigator	Q8IUX7.
Family and domain databases
Gene3D	2.60.40.1120. 1 hit.
InterPro	IPR008969. CarboxyPept-like_regulatory. IPR014766. CarboxyPept_regulatory_dom. IPR000421. Coagulation_fac_5/8-C_type_dom. IPR008979. Galactose-bd-like. IPR000834. Peptidase_M14. [Graphical view]
Pfam	PF00754. F5_F8_type_C. 1 hit. PF00246. Peptidase_M14. 1 hit. [Graphical view]
PRINTS	PR00765. CRBOXYPTASEA.
SMART	SM00231. FA58C. 1 hit. SM00631. Zn_pept. 1 hit. [Graphical view]
SUPFAM	SSF49464. CarboxypepD_reg. 1 hit. SSF49785. Gal_bind_like. 1 hit.
PROSITE	PS00132. CARBOXYPEPT_ZN_1. 1 hit. PS01285. FA58C_1. 1 hit. PS01286. FA58C_2. 1 hit. PS50022. FA58C_3. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	AEBP1. human.
GenomeRNAi	165.
NextBio	665.
SOURCE	Search...

Entry information

Entry name

AEBP1_HUMAN

Accession

Primary (citable) accession number: Q8IUX7
Secondary accession number(s): Q14113 , Q59ER7, Q6ZSC7, Q7KZ79

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	March 1, 2003
Last modified:	May 1, 2013
This is version 98 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.