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UniProtKB - Q6FHX6 (Q6FHX6_HUMAN)

Entry version 149 (25 May 2022)
Sequence version 1 (10 May 2005)
Previous versions | rss
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Protein

Flap endonuclease 1

Gene

FEN1

Organism
Homo sapiens (Human)
Status
Unreviewed-Annotation score:

Annotation score:4 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at transcript leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Structure-specific nuclease with 5'-flap endonuclease and 5'-3' exonuclease activities involved in DNA replication and repair. During DNA replication, cleaves the 5'-overhanging flap structure that is generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment. It enters the flap from the 5'-end and then tracks to cleave the flap base, leaving a nick for ligation. Also involved in the long patch base excision repair (LP-BER) pathway, by cleaving within the apurinic/apyrimidinic (AP) site-terminated flap. Acts as a genome stabilization factor that prevents flaps from equilibrating into structures that lead to duplications and deletions. Also possesses 5'-3' exonuclease activity on nicked or gapped double-stranded DNA, and exhibits RNase H activity. Also involved in replication and repair of rDNA and in repairing mitochondrial DNA.

UniRule annotationARBA annotation

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Mg2+UniRule annotationNote: Binds 2 magnesium ions per subunit. They probably participate in the reaction catalyzed by the enzyme. May bind an additional third magnesium ion after substrate binding.UniRule annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi34Magnesium 1UniRule annotation1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei47DNA substrateUniRule annotation1
Binding sitei70DNA substrateUniRule annotation1
Metal bindingi86Magnesium 1UniRule annotation1
Metal bindingi158Magnesium 1UniRule annotation1
Binding sitei158DNA substrateUniRule annotation1
Metal bindingi160Magnesium 1UniRule annotation1
Metal bindingi179Magnesium 2UniRule annotation1
Metal bindingi181Magnesium 2UniRule annotation1
Binding sitei231DNA substrateUniRule annotation1
Metal bindingi233Magnesium 2UniRule annotation1
Binding sitei233DNA substrateUniRule annotation1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionEndonucleaseUniRule annotationARBA annotation, ExonucleaseUniRule annotationARBA annotation, Hydrolase, Nuclease
Biological processDNA damage, DNA repairUniRule annotationARBA annotation, DNA replicationUniRule annotationARBA annotation
LigandMagnesiumUniRule annotationARBA annotation, Metal-bindingUniRule annotationARBA annotation

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Flap endonuclease 1UniRule annotation (EC:3.1.-.-UniRule annotation)
Short name:
FEN-1UniRule annotation
Alternative name(s):
Flap structure-specific endonuclease 1UniRule annotation
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:FEN1UniRule annotationImported
ORF Names:hCG_40848Imported
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)Imported
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Organism-specific databases

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		HostDB:ENSG00000168496

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Keywords - Cellular componenti

MitochondrionUniRule annotation, NucleusUniRule annotation

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Organism-specific databases

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA28090

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei19Symmetric dimethylarginine; by PRMT5UniRule annotation1
Modified residuei100Symmetric dimethylarginine; by PRMT5UniRule annotation1
Modified residuei104Symmetric dimethylarginine; by PRMT5UniRule annotation1
Modified residuei187Phosphoserine; by CDK2UniRule annotation1
Modified residuei192Symmetric dimethylarginine; by PRMT5UniRule annotation1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Acetylated by EP300. Acetylation inhibits both endonuclease and exonuclease activity. Acetylation also reduces DNA-binding activity but does not affect interaction with PCNA or EP300.UniRule annotation
Methylation at Arg-192 by PRMT5 impedes Ser-187 phosphorylation and increases interaction with PCNA.UniRule annotation
Phosphorylation upon DNA damage induces relocalization to the nuclear plasma. Phosphorylation at Ser-187 by CDK2 occurs during late S-phase and results in dissociation from PCNA.UniRule annotation

Keywords - PTMi

MethylationUniRule annotation, PhosphoproteinUniRule annotationARBA annotation

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000168496, Expressed in amniotic fluid and 232 other tissues

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Interacts with PCNA. Three molecules of FEN1 bind to one PCNA trimer with each molecule binding to one PCNA monomer. PCNA stimulates the nuclease activity without altering cleavage specificity. The C-terminal domain binds EP300. Can bind simultaneously to both PCNA and EP300.

Interacts with DDX11.

UniRule annotation

Protein-protein interaction databases

Protein interaction database and analysis system

More...IntActi		Q6FHX6, 1 interactor

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini1 – 107XPGNInterPro annotationAdd BLAST107
Domaini146 – 218XPGIInterPro annotationAdd BLAST73

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1 – 104N-domainUniRule annotationAdd BLAST104
Regioni122 – 253I-domainUniRule annotationAdd BLAST132
Regioni327 – 380DisorderedSequence analysisAdd BLAST54
Regioni336 – 344Interaction with PCNAUniRule annotation9

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and domains' section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili97 – 136Sequence analysisAdd BLAST40

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi328 – 342Polar residuesSequence analysisAdd BLAST15
Compositional biasi352 – 366Basic and acidic residuesSequence analysisAdd BLAST15

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the XPG/RAD2 endonuclease family. FEN1 subfamily.UniRule annotation

Keywords - Domaini

Coiled coilSequence analysis

Phylogenomic databases

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_032444_2_0_1

Identification of Orthologs from Complete Genome Data

More...OMAi		GSQDYDS

Database of Orthologous Groups

More...OrthoDBi		1094524at2759

Family and domain databases

HAMAP database of protein families

More...HAMAPi		MF_00614, Fen, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR036279, 5-3_exonuclease_C_sf
IPR023426, Flap_endonuc
IPR008918, HhH2
IPR029060, PIN-like_dom_sf
IPR006086, XPG-I_dom
IPR006084, XPG/Rad2
IPR019974, XPG_CS
IPR006085, XPG_DNA_repair_N

The PANTHER Classification System

More...PANTHERi		PTHR11081, PTHR11081, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00867, XPG_I, 1 hit
PF00752, XPG_N, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00853, XPGRADSUPER

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00279, HhH2, 1 hit
SM00484, XPGI, 1 hit
SM00485, XPGN, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF47807, SSF47807, 1 hit
SSF88723, SSF88723, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00841, XPG_1, 1 hit
PS00842, XPG_2, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

Q6FHX6-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGIQGLAKLI ADVAPSAIRE NDIKSYFGRK VAIDASMSIY QFLIAVRQGG 
        60         70         80         90        100
DVLQNEEGET TSHLMGMFYR TIRMMENGIK PVYVFDGKPP QLKSGELAKR 
       110        120        130        140        150
SERRAEAEKQ LQQAQAAGAE QEVEKFTKRL VKVTKQHNDE CKHLLSLMGI 
       160        170        180        190        200
PYLDAPSEAE ASCAALVKAG KVYAAATEDM DCLTFGSPVL MRHLTASEAK 
       210        220        230        240        250
KLPIQEFHLS RILQELGLNQ EQFVDLCILL GSDYCESIRG IGPKRAVDLI 
       260        270        280        290        300
QKHKSIEEIV RRLDPNKYPV PENWLHKEAH QLFLEPEVLD PESVELKWSE 
       310        320        330        340        350
PNEEELIKFM CGEKQFSEER IRSGVKRLSK SRQGSTQGRL DDFFKVTGSL 
       360        370        380
SSAKRKEPEP KGSTKKKAKT GAAGKFKRGK
Length:380
Mass (Da):42,593
Last modified:May 10, 2005 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i5154F2F6E57592C5
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
BT019524 mRNA Translation: AAV38331.1
AK312761 mRNA Translation: BAG35627.1
CR536562 mRNA Translation: CAG38799.1
CH471076 Genomic DNA Translation: EAW73972.1

NCBI Reference Sequences

More...RefSeqi		NP_004102.1, NM_004111.5

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...GeneIDi		2237

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:2237

Matched Annotation from NCBI and EMBL-EBI (MANE) - Phase one

More...MANE-Selecti		ENST00000305885.3; ENSP00000305480.2; NM_004111.6; NP_004102.1

UCSC genome browser

More...UCSCi		uc001nsg.4, human

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BT019524 mRNA Translation: AAV38331.1
AK312761 mRNA Translation: BAG35627.1
CR536562 mRNA Translation: CAG38799.1
CH471076 Genomic DNA Translation: EAW73972.1
RefSeqiNP_004102.1, NM_004111.5

3D structure databases

Database of comparative protein structure models

More...ModBasei		Search...

SWISS-MODEL Interactive Workspace

More...SWISS-MODEL-Workspacei		Submit a new modelling project...

Protein-protein interaction databases

IntActiQ6FHX6, 1 interactor

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...Antibodypediai		1878, 577 antibodies from 39 providers

The DNASU plasmid repository

More...DNASUi		2237

Genome annotation databases

GeneIDi2237
KEGGihsa:2237
MANE-SelectiENST00000305885.3; ENSP00000305480.2; NM_004111.6; NP_004102.1
UCSCiuc001nsg.4, human

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		2237
PharmGKBiPA28090
VEuPathDBiHostDB:ENSG00000168496

Phylogenomic databases

HOGENOMiCLU_032444_2_0_1
OMAiGSQDYDS
OrthoDBi1094524at2759

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		2237, 517 hits in 1085 CRISPR screens

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...ChiTaRSi		FEN1, human

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...GenomeRNAii		2237

Gene expression databases

BgeeiENSG00000168496, Expressed in amniotic fluid and 232 other tissues

Family and domain databases

HAMAPiMF_00614, Fen, 1 hit
InterProiView protein in InterPro
IPR036279, 5-3_exonuclease_C_sf
IPR023426, Flap_endonuc
IPR008918, HhH2
IPR029060, PIN-like_dom_sf
IPR006086, XPG-I_dom
IPR006084, XPG/Rad2
IPR019974, XPG_CS
IPR006085, XPG_DNA_repair_N
PANTHERiPTHR11081, PTHR11081, 1 hit
PfamiView protein in Pfam
PF00867, XPG_I, 1 hit
PF00752, XPG_N, 1 hit
PRINTSiPR00853, XPGRADSUPER
SMARTiView protein in SMART
SM00279, HhH2, 1 hit
SM00484, XPGI, 1 hit
SM00485, XPGN, 1 hit
SUPFAMiSSF47807, SSF47807, 1 hit
SSF88723, SSF88723, 1 hit
PROSITEiView protein in PROSITE
PS00841, XPG_1, 1 hit
PS00842, XPG_2, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiQ6FHX6_HUMAN
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q6FHX6
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/TrEMBL: May 10, 2005
Last sequence update: May 10, 2005
Last modified: May 25, 2022
This is version 149 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiUnreviewed (UniProtKB/TrEMBL)
DisclaimerAny 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.
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