P22234 (PUR6_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Multifunctional protein ADE2

Including the following 2 domains:

1. Phosphoribosylaminoimidazole-succinocarboxamide synthase
   EC=6.3.2.6
   Alternative name(s):
   SAICAR synthetase
2. Phosphoribosylaminoimidazole carboxylase
   EC=4.1.1.21
   Alternative name(s):
   AIR carboxylase
   Short name=AIRC

Gene names

Name:	PAICS
Synonyms:	ADE2, AIRC, PAIS

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	425 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)

Catalytic activity	ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-aspartate = ADP + phosphate + (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido)succinate. 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate = 5-amino-1-(5-phospho-D-ribosyl)imidazole + CO2.
Pathway	Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate: step 1/2. Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate from 5-amino-1-(5-phospho-D-ribosyl)imidazole (carboxylase route): step 1/1.
Subunit structure	Homooctamer. Ref.17
Sequence similarities	In the N-terminal section; belongs to the SAICAR synthetase family. In the C-terminal section; belongs to the AIR carboxylase family.

Ontologies

Keywords
Biological process	Purine biosynthesis
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	ATP-binding Nucleotide-binding
Molecular function	Decarboxylase Ligase Lyase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Multifunctional enzyme Reference proteome
Gene Ontology (GO)
Biological_process	'de novo' IMP biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway purine nucleobase biosynthetic process Traceable author statement Ref.1. Source: ProtInc purine ribonucleoside monophosphate biosynthetic process Traceable author statement. Source: Reactome
Cellular_component	cytosol Traceable author statement. Source: Reactome
Molecular_function	5-(carboxyamino)imidazole ribonucleotide mutase activity Inferred from electronic annotation. Source: InterPro ATP binding Inferred from electronic annotation. Source: UniProtKB-KW phosphoribosylaminoimidazole carboxylase activity Traceable author statement. Source: Reactome phosphoribosylaminoimidazolesuccinocarboxamide synthase activity Traceable author statement. Source: Reactome
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		3	EBI-712261,EBI-712261
FXR2	P51116	3	EBI-712261,EBI-740459
NUDT18	Q6ZVK8	3	EBI-712261,EBI-740486

Alternative products

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

Isoform 1 (identifier: P22234-1)

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: P22234-2)

The sequence of this isoform differs from the canonical sequence as follows:
     72-72: G → VTSYKSNR

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.6

Chain

2 – 425

424

Multifunctional protein ADE2

PRO_0000075030

Regions

Region

2 – 260

259

SAICAR synthetase

Region

261 – 266

6

Linker

Region

267 – 425

159

AIR carboxylase

Sites

Active site

101

1

For SAICAR synthetase activity Ref.17

Active site

107

1

For SAICAR synthetase activity Ref.17

Active site

215

1

For SAICAR synthetase activity Ref.17

Active site

303

1

For AIR carboxylase activity Ref.17

Active site

332

1

For AIR carboxylase activity Ref.17

Site

334

1

Essential for AIR carboxylase activity

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.6

Modified residue

22

1

Phosphotyrosine By similarity

Modified residue

27

1

Phosphoserine Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.14 Ref.16

Modified residue

107

1

Phosphoserine Ref.10

Modified residue

238

1

Phosphothreonine Ref.9

Modified residue

247

1

N6-acetyllysine Ref.13

Natural variations

Alternative sequence

72

1

G → VTSYKSNR in isoform 2.

VSP_041265

Natural variant

201

1

K → N.
Corresponds to variant rs11549976 [ dbSNP | Ensembl ].

VAR_051884

Experimental info

Mutagenesis

303

1

H → Y: Loss of AIR carboxylase activity. Ref.17

Mutagenesis

332

1

S → A: Loss of AIR carboxylase activity. Ref.17

Mutagenesis

334

1

G → A: Loss of AIR carboxylase activity. Ref.17

Mutagenesis

400

1

S → A: No change of AIR carboxylase activity.

Sequence conflict

217

1

W → R in CAH18683. Ref.3

Sequence conflict

340

1

S → T in CAH18683. Ref.3

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

425

Helix Strand Turn

Details...

Beta strand

20 – 22

3

Beta strand

32 – 35

4

Helix

54 – 71

18

Beta strand

82 – 88

7

Beta strand

91 – 93

3

Beta strand

97 – 103

7

Helix

106 – 111

6

Beta strand

126 – 130

5

Helix

142 – 146

5

Turn

147 – 149

3

Helix

159 – 180

22

Helix

181 – 183

3

Beta strand

186 – 192

7

Beta strand

194 – 197

4

Turn

198 – 200

3

Beta strand

203 – 205

3

Beta strand

213 – 217

5

Beta strand

241 – 243

3

Helix

249 – 253

5

Helix

256 – 260

5

Beta strand

267 – 273

7

Helix

275 – 277

3

Helix

278 – 290

13

Beta strand

295 – 299

5

Turn

302 – 304

3

Helix

306 – 317

12

Beta strand

323 – 328

6

Helix

335 – 342

8

Beta strand

347 – 349

3

Turn

355 – 357

3

Helix

358 – 361

4

Helix

362 – 364

3

Helix

380 – 392

13

Helix

396 – 421

26

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: E08CF19BC8898F29	FASTA	425	47,079
	10 20 30 40 50 60 MATAEVLNIG KKLYEGKTKE VYELLDSPGK VLLQSKDQIT AGNAARKNHL EGKAAISNKI 70 80 90 100 110 120 TSCIFQLLQE AGIKTAFTRK CGETAFIAPQ CEMIPIEWVC RRIATGSFLK RNPGVKEGYK 130 140 150 160 170 180 FYPPKVELFF KDDANNDPQW SEEQLIAAKF CFAGLLIGQT EVDIMSHATQ AIFEILEKSW 190 200 210 220 230 240 LPQNCTLVDM KIEFGVDVTT KEIVLADVID NDSWRLWPSG DRSQQKDKQS YRDLKEVTPE 250 260 270 280 290 300 GLQMVKKNFE WVAERVELLL KSESQCRVVV LMGSTSDLGH CEKIKKACGN FGIPCELRVT 310 320 330 340 350 360 SAHKGPDETL RIKAEYEGDG IPTVFVAVAG RSNGLGPVMS GNTAYPVISC PPLTPDWGVQ 370 380 390 400 410 420 DVWSSLRLPS GLGCSTVLSP EGSAQFAAQI FGLSNHLVWS KLRASILNTW ISLKQADKKI RECNL
	Isoform 2 [UniParc]. Checksum: 1F8F3B240AD1C137	FASTA	432	47,958
	10 20 30 40 50 60 MATAEVLNIG KKLYEGKTKE VYELLDSPGK VLLQSKDQIT AGNAARKNHL EGKAAISNKI 70 80 90 100 110 120 TSCIFQLLQE AVTSYKSNRI KTAFTRKCGE TAFIAPQCEM IPIEWVCRRI ATGSFLKRNP 130 140 150 160 170 180 GVKEGYKFYP PKVELFFKDD ANNDPQWSEE QLIAAKFCFA GLLIGQTEVD IMSHATQAIF 190 200 210 220 230 240 EILEKSWLPQ NCTLVDMKIE FGVDVTTKEI VLADVIDNDS WRLWPSGDRS QQKDKQSYRD 250 260 270 280 290 300 LKEVTPEGLQ MVKKNFEWVA ERVELLLKSE SQCRVVVLMG STSDLGHCEK IKKACGNFGI 310 320 330 340 350 360 PCELRVTSAH KGPDETLRIK AEYEGDGIPT VFVAVAGRSN GLGPVMSGNT AYPVISCPPL 370 380 390 400 410 420 TPDWGVQDVW SSLRLPSGLG CSTVLSPEGS AQFAAQIFGL SNHLVWSKLR ASILNTWISL 430 KQADKKIREC NL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and sequencing of a human cDNA coding for a multifunctional polypeptide of the purine pathway by complementation of the ade2-101 mutant in Saccharomyces cerevisiae." Minet M., Lacroute F. Curr. Genet. 18:287-291(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[3]	"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 2). Tissue: Retina.
[4]	"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] [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: Lung and Placenta.
[6]	Bienvenut W.V., Potts A., Brablan J., Quadroni M. Submitted (JUL-2004) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-11, ACETYLATION AT ALA-2, MASS SPECTROMETRY. Tissue: B-cell lymphoma.
[7]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27 AND THR-238, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"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-27 AND SER-107, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27, MASS SPECTROMETRY.
[12]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[13]	"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-247, MASS SPECTROMETRY.
[14]	"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-27, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[15]	"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].
[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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27, MASS SPECTROMETRY.
[17]	"Octameric structure of the human bifunctional enzyme PAICS in purine biosynthesis." Li S.-X., Tong Y.-P., Xie X.-C., Wang Q.-H., Zhou H.-N., Han Y., Zhang Z.-Y., Gao W., Li S.-G., Zhang X.C., Bi R.-C. J. Mol. Biol. 366:1603-1614(2007) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), SUBUNIT, ACTIVE SITE, MUTAGENESIS OF HIS-303; SER-332 AND GLY-334.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X53793 mRNA. Translation: CAA37801.1.
BT006988 mRNA. Translation: AAP35634.1.
CR749824 mRNA. Translation: CAH18683.1.
AC068620 Genomic DNA. No translation available.
AC114766 Genomic DNA. No translation available.
BC010273 mRNA. Translation: AAH10273.1.
BC019255 mRNA. Translation: AAH19255.1.

IPI

IPI00217223.
IPI00815732.

PIR

S14147.

RefSeq

NP_001072992.1. NM_001079524.1.
NP_001072993.1. NM_001079525.1.
NP_006443.1. NM_006452.3.

UniGene

Hs.518774.
Hs.709570.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2H31	X-ray	2.80	A	1-425	[»]

ProteinModelPortal

P22234.

ModBase

Search...

Protein-protein interaction databases

IntAct

P22234. 16 interactions.

MINT

MINT-1374364.

STRING

9606.ENSP00000382595.

PTM databases

PhosphoSite

P22234.

Polymorphism databases

DMDM

131628.

Proteomic databases

PaxDb

P22234.

PRIDE

P22234.

Protocols and materials databases

DNASU

10606.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000264221; ENSP00000264221; ENSG00000128050.
ENST00000399688; ENSP00000382595; ENSG00000128050.
ENST00000512576; ENSP00000421096; ENSG00000128050.

GeneID

10606.

KEGG

hsa:10606.

UCSC

uc003hbs.1. human.
uc003hbt.1. human.

Organism-specific databases

CTD

10606.

GeneCards

GC04P057301.

HGNC

HGNC:8587. PAICS.

HPA

HPA035895.

MIM

172439. gene.

neXtProt

NX_P22234.

PharmGKB

PA32914.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0041.

HOGENOM

HOG000082628.

HOVERGEN

HBG008335.

InParanoid

P22234.

KO

K01587.

OMA

TAFTRKC.

Enzyme and pathway databases

Reactome

REACT_111217. Metabolism.

UniPathway

UPA00074; UER00130.
UPA00074; UER00131.

Gene expression databases

ArrayExpress

P22234.

Bgee

P22234.

CleanEx

HS_PAICS.

Genevestigator

P22234.

GermOnline

ENSG00000128050. Homo sapiens.

Family and domain databases

Gene3D

3.30.470.20. 1 hit.
3.40.50.7700. 1 hit.

InterPro

IPR013816. ATP_grasp_subdomain_2.
IPR000031. N5-CAIR_Mutase_PurE_dom.
IPR001636. SAICAR_synth.
IPR018236. SAICAR_synthetase_CS.
[Graphical view]

PANTHER

PTHR11609. PTHR11609. 1 hit.

Pfam

PF00731. AIRC. 1 hit.
PF01259. SAICAR_synt. 1 hit.
[Graphical view]

SMART

SM01001. AIRC. 1 hit.
[Graphical view]

SUPFAM

SSF52255. AIR_carboxyl. 1 hit.

TIGRFAMs

TIGR01162. purE. 1 hit.

PROSITE

PS01057. SAICAR_SYNTHETASE_1. 1 hit.
PS01058. SAICAR_SYNTHETASE_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChEMBL

CHEMBL5922.

ChiTaRS

PAICS. human.

DrugBank

DB00128. L-Aspartic Acid.

EvolutionaryTrace

P22234.

GenomeRNAi

10606.

NextBio

40280.

SOURCE

Search...

Entry information

Entry name

PUR6_HUMAN

Accession

Primary (citable) accession number: P22234
Secondary accession number(s): E9PDH9, Q68CQ5

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1991
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 143 of the entry and version 3 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.