Q13526 (PIN1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1
EC=5.2.1.8

Alternative name(s):
Peptidyl-prolyl cis-trans isomerase Pin1
Short name=PPIase Pin1
Rotamase Pin1

Gene names

Name:

PIN1

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

General annotation (Comments)

Function	Essential PPIase that regulates mitosis presumably by interacting with NIMA and attenuating its mitosis-promoting activity. Displays a preference for an acidic residue N-terminal to the isomerized proline bond. Catalyzes pSer/Thr-Pro cis/trans isomerizations. Down-regulates kinase activity of BTK. Can transactivate multiple oncogenes and induce centrosome amplification, chromosome instability and cell transformation. Required for the efficient dephosphorylation and recycling of RAF1 after mitogen activation. Binds and targets PML for degradation in a phosphorylation-dependent manner. Ref.8 Ref.10 Ref.16 Ref.17
Catalytic activity	Peptidylproline (omega=180) = peptidylproline (omega=0).
Subunit structure	Interacts with STIL By similarity. Interacts with KIF20B. Interacts with NEK6. Interacts (via WW domain) with PRKX. Interacts with BTK. Interacts (via PpiC domain) with DAPK1. Interacts with the phosphorylated form of RAF1. Interacts (via WW domain) with ATCAY; upon NGF stimulation. Interacts with PML (isoform PML-4). Ref.7 Ref.8 Ref.9 Ref.10 Ref.12 Ref.13 Ref.16 Ref.17
Subcellular location	Nucleus. Nucleus speckle. Cytoplasm. Note: Co-localizes with NEK6 in the nucleus. Mainly localized in the nucleus but phosphorylation at Ser-71 by DAPK1 results in inhibition of its nuclear localization. Ref.9 Ref.17
Tissue specificity	The phosphorylated form at Ser-71 is expressed in normal breast tissue cells but not in breast cancer cells. Ref.17
Domain	The WW domain is required for the interaction with STIL and KIF20B.
Post-translational modification	Phosphorylation at Ser-71 by DAPK1 results in inhibition of its catalytic activity, nuclear localization, and its ability to induce centrosome amplification, chromosome instability and cell transformation.
Sequence similarities	Contains 1 PpiC domain. Contains 1 WW domain.

Ontologies

Keywords
Biological process	Cell cycle
Cellular component	Cytoplasm Nucleus
Molecular function	Isomerase Rotamase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell cycle Inferred from electronic annotation. Source: UniProtKB-KW cytokine-mediated signaling pathway Traceable author statement. Source: Reactome innate immune response Traceable author statement. Source: Reactome negative regulation of ERK1 and ERK2 cascade Inferred from direct assay PubMed 20179103. Source: BHF-UCL negative regulation of cell motility Inferred from direct assay PubMed 20179103. Source: BHF-UCL negative regulation of transforming growth factor beta receptor signaling pathway Inferred from direct assay PubMed 19122240. Source: BHF-UCL negative regulation of type I interferon production Traceable author statement. Source: Reactome positive regulation of Rho GTPase activity Inferred from mutant phenotype PubMed 20179103. Source: BHF-UCL positive regulation of protein phosphorylation Inferred from genetic interaction PubMed 19638580. Source: MGI positive regulation of ubiquitin-protein ligase activity Inferred from direct assay PubMed 19122240. Source: BHF-UCL protein folding Inferred from electronic annotation. Source: UniProtKB-KW regulation of cell proliferation Inferred from electronic annotation. Source: Compara regulation of cytokinesis Inferred from mutant phenotype PubMed 19638580. Source: MGI regulation of mitosis Traceable author statement PubMed 10391244. Source: ProtInc regulation of pathway-restricted SMAD protein phosphorylation Inferred from direct assay PubMed 19122240. Source: BHF-UCL
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell midbody Inferred from direct assay PubMed 19638580. Source: MGI nuclear speck Inferred from electronic annotation. Source: UniProtKB-SubCell nucleoplasm Traceable author statement. Source: Reactome
Molecular_function	peptidyl-prolyl cis-trans isomerase activity Inferred from direct assay PubMed 19122240. Source: BHF-UCL phosphoserine binding Inferred from direct assay PubMed 10037602. Source: BHF-UCL phosphothreonine binding Inferred from direct assay PubMed 10037602. Source: BHF-UCL
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
APP	P05067-4	2	EBI-714158,EBI-302641
CDK10	Q15131	5	EBI-714158,EBI-1646959
IRAK1	P51617	10	EBI-714158,EBI-358664
NEK6	Q9HC98	3	EBI-714158,EBI-740364
NOTCH1	P46531	9	EBI-714158,EBI-636374
TP53	P04637	11	EBI-714158,EBI-366083

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 163

163

Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1

PRO_0000193435

Regions

Domain

5 – 39

35

WW

Domain

52 – 163

112

PpiC

Amino acid modifications

Modified residue

46

1

N6-acetyllysine Ref.14

Modified residue

71

1

Phosphoserine; by DAPK1 Ref.17

Modified residue

108

1

Phosphoserine Ref.11

Experimental info

Mutagenesis

23

1

Y → A: Reduced affinity for KIF20B. Ref.7

Mutagenesis

71

1

S → D or E: Loss of activity, nuclear localization and cellular function. Ref.17

Secondary structure

1

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163

Helix Strand Turn

Details...

Beta strand

11 – 15

5

Turn

17 – 19

3

Beta strand

22 – 26

5

Turn

27 – 29

3

Beta strand

32 – 35

4

Beta strand

39 – 41

3

Beta strand

53 – 62

10

Beta strand

67 – 69

3

Beta strand

75 – 77

3

Helix

82 – 98

17

Beta strand

99 – 101

3

Helix

103 – 110

8

Helix

114 – 118

5

Beta strand

121 – 126

6

Helix

132 – 140

9

Beta strand

150 – 152

3

Beta strand

155 – 163

9

Sequences

	Sequence		Length	Mass (Da)
	Q13526 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 35391AF40B7D1E13	FASTA	163	18,243
	10 20 30 40 50 60 MADEEKLPPG WEKRMSRSSG RVYYFNHITN ASQWERPSGN SSSGGKNGQG EPARVRCSHL 70 80 90 100 110 120 LVKHSQSRRP SSWRQEKITR TKEEALELIN GYIQKIKSGE EDFESLASQF SDCSSAKARG 130 140 150 160 DLGAFSRGQM QKPFEDASFA LRTGEMSGPV FTDSGIHIIL RTE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A human peptidyl-prolyl isomerase essential for regulation of mitosis." Lu K.P., Hanes S.D., Hunter T. Nature 380:544-547(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"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 (MAY-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]	"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].
[4]	"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].
[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 (JUL-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]. Tissue: Lung.
[7]	"Identification of a novel kinesin-related protein, KRMP1, as a target for mitotic peptidyl-prolyl isomerase Pin1." Kamimoto T., Zama T., Aoki R., Muro Y., Hagiwara M. J. Biol. Chem. 276:37520-37528(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH KIF20B, MUTAGENESIS OF TYR-23.
[8]	"Regulation of Raf-1 by direct feedback phosphorylation." Dougherty M.K., Muller J., Ritt D.A., Zhou M., Zhou X.Z., Copeland T.D., Conrads T.P., Veenstra T.D., Lu K.P., Morrison D.K. Mol. Cell 17:215-224(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH RAF1.
[9]	"Interaction of Pin1 with Nek6 and characterization of their expression correlation in Chinese hepatocellular carcinoma patients." Chen J., Li L., Zhang Y., Yang H., Wei Y., Zhang L., Liu X., Yu L. Biochem. Biophys. Res. Commun. 341:1059-1065(2006) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, INTERACTION WITH NEK6.
[10]	"Regulation of Bruton tyrosine kinase by the peptidylprolyl isomerase Pin1." Yu L., Mohamed A.J., Vargas L., Berglof A., Finn G., Lu K.P., Smith C.I. J. Biol. Chem. 281:18201-18207(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH BTX, FUNCTION.
[11]	"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-108, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[12]	"Nerve growth factor stimulates interaction of Cayman ataxia protein BNIP-H/Caytaxin with peptidyl-prolyl isomerase Pin1 in differentiating neurons." Buschdorf J.P., Chew L.L., Soh U.J., Liou Y.C., Low B.C. PLoS ONE 3:E2686-E2686(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ATCAY.
[13]	"Protein kinase-X interacts with Pin-1 and Polycystin-1 during mouse kidney development." Li X., Hyink D.P., Radbill B., Sudol M., Zhang H., Zheleznova N.N., Wilson P.D. Kidney Int. 76:54-62(2009) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PRKX.
[14]	"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-46, MASS SPECTROMETRY.
[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]	"Mitogen-activated protein kinase extracellular signal-regulated kinase 2 phosphorylates and promotes Pin1 protein-dependent promyelocytic leukemia protein turnover." Lim J.H., Liu Y., Reineke E., Kao H.Y. J. Biol. Chem. 286:44403-44411(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH PML.
[17]	"Death-associated protein kinase 1 phosphorylates Pin1 and inhibits its prolyl isomerase activity and cellular function." Lee T.H., Chen C.H., Suizu F., Huang P., Schiene-Fischer C., Daum S., Zhang Y.J., Goate A., Chen R.H., Zhou X.Z., Lu K.P. Mol. Cell 42:147-159(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, PHOSPHORYLATION AT SER-71, INTERACTION WITH DAPK1, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-71, TISSUE SPECIFICITY.
[18]	"Structural and functional analysis of the mitotic rotamase Pin1 suggests substrate recognition is phosphorylation dependent." Ranganathan R., Lu K.P., Hunter T., Noel J.P. Cell 89:875-886(1997) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U49070 mRNA. Translation: AAC50492.1.
CR407654 mRNA. Translation: CAG28582.1.
BT019331 mRNA. Translation: AAV38138.1.
AK291074 mRNA. Translation: BAF83763.1.
CH471106 Genomic DNA. Translation: EAW84057.1.
BC002899 mRNA. Translation: AAH02899.1.

IPI

IPI00013723.

PIR

S68520.

RefSeq

NP_006212.1. NM_006221.3.

UniGene

Hs.465849.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1F8A	X-ray	1.84	B	1-163	[»]
1I6C	NMR	-	A	6-44	[»]
1I8G	NMR	-	B	6-44	[»]
1I8H	NMR	-	B	6-44	[»]
1NMV	NMR	-	A	1-163	[»]
1NMW	NMR	-	A	50-163	[»]
1PIN	X-ray	1.35	A	1-163	[»]
1ZCN	X-ray	1.90	A	1-161	[»]
2F21	X-ray	1.50	A	1-162	[»]
2ITK	X-ray	1.45	A	1-163	[»]
2KBU	NMR	-	A	6-39	[»]
2KCF	NMR	-	A	6-39	[»]
2LB3	NMR	-	A	6-41	[»]
2Q5A	X-ray	1.50	A	1-163	[»]
2XP3	X-ray	2.00	A	1-163	[»]
2XP4	X-ray	1.80	A	1-163	[»]
2XP5	X-ray	1.90	A	1-163	[»]
2XP6	X-ray	1.90	A	1-163	[»]
2XP7	X-ray	2.00	A	1-163	[»]
2XP8	X-ray	2.10	A	1-163	[»]
2XP9	X-ray	1.90	A	1-163	[»]
2XPA	X-ray	1.90	A	1-163	[»]
2XPB	X-ray	2.00	A	1-163	[»]
2ZQS	X-ray	1.90	A	1-163	[»]
2ZQT	X-ray	1.46	A	1-163	[»]
2ZQU	X-ray	2.50	A	1-163	[»]
2ZQV	X-ray	2.50	A	1-163	[»]
2ZR4	X-ray	2.00	A	1-163	[»]
2ZR5	X-ray	2.60	A	1-163	[»]
2ZR6	X-ray	3.20	A	1-163	[»]
3I6C	X-ray	1.30	A/B	45-163	[»]
3IK8	X-ray	1.85	A/B	45-163	[»]
3IKD	X-ray	2.00	A/B	45-163	[»]
3IKG	X-ray	1.86	A/B	45-163	[»]
3JYJ	X-ray	1.87	A/B	45-163	[»]
3KAB	X-ray	2.19	A	1-163	[»]
3KAC	X-ray	2.00	A/B	44-163	[»]
3KAD	X-ray	1.95	A	1-163	[»]
3KAF	X-ray	2.30	A	1-163	[»]
3KAG	X-ray	1.90	A	1-163	[»]
3KAH	X-ray	2.30	A	1-163	[»]
3KAI	X-ray	1.90	A	1-163	[»]
3KCE	X-ray	1.90	A	1-163	[»]
3NTP	X-ray	1.76	A	1-163	[»]
3ODK	X-ray	2.30	A	1-163	[»]
3OOB	X-ray	1.89	A	1-163	[»]
3TC5	X-ray	1.40	A	1-163	[»]
3TCZ	X-ray	2.10	A	6-163	[»]
3TDB	X-ray	2.27	A	6-163	[»]

ProteinModelPortal

Q13526.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29306N.

IntAct

Q13526. 44 interactions.

MINT

MINT-86298.

STRING

9606.ENSP00000247970.

PTM databases

PhosphoSite

Q13526.

Polymorphism databases

DMDM

3024406.

Proteomic databases

PaxDb

Q13526.

PeptideAtlas

Q13526.

PRIDE

Q13526.

Protocols and materials databases

DNASU

5300.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000247970; ENSP00000247970; ENSG00000127445.
ENST00000588695; ENSP00000466962; ENSG00000127445.

GeneID

5300.

KEGG

hsa:5300.

UCSC

uc002mml.2. human.

Organism-specific databases

CTD

5300.

GeneCards

GC19P009945.

HGNC

HGNC:8988. PIN1.

HPA

CAB004528.
CAB009326.

MIM

601052. gene.

neXtProt

NX_Q13526.

PharmGKB

PA33320.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0760.

HOGENOM

HOG000275331.

HOVERGEN

HBG002101.

InParanoid

Q13526.

KO

K09578.

OMA

DCSSARK.

OrthoDB

EOG4VMFGM.

PhylomeDB

Q13526.

Enzyme and pathway databases

BRENDA

5.2.1.8. 2681.

Reactome

REACT_6900. Immune System.

Gene expression databases

ArrayExpress

Q13526.

Bgee

Q13526.

CleanEx

HS_PIN1.

Genevestigator

Q13526.

GermOnline

ENSG00000127445. Homo sapiens.

Family and domain databases

InterPro

IPR000297. PPIase_PpiC.
IPR023058. PPIase_PpiC_CS.
IPR001202. WW_dom.
[Graphical view]

Pfam

PF00639. Rotamase. 1 hit.
PF00397. WW. 1 hit.
[Graphical view]

SMART

SM00456. WW. 1 hit.
[Graphical view]

SUPFAM

SSF51045. WW_Rsp5_WWP. 1 hit.

PROSITE

PS01096. PPIC_PPIASE_1. 1 hit.
PS50198. PPIC_PPIASE_2. 1 hit.
PS01159. WW_DOMAIN_1. 1 hit.
PS50020. WW_DOMAIN_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

Q13526.

ChEMBL

CHEMBL2288.

EvolutionaryTrace

Q13526.

GenomeRNAi

5300.

NextBio

20486.

SOURCE

Search...

Entry information

Entry name

PIN1_HUMAN

Accession

Primary (citable) accession number: Q13526
Secondary accession number(s): A8K4V9, Q53X75

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	November 1, 1996
Last modified:	May 1, 2013
This is version 135 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.