Q9UQB9 (AURKC_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Aurora kinase C
EC=2.7.11.1

Alternative name(s):
Aurora 3
Aurora/IPL1-related kinase 3
Short name=ARK-3
Short name=Aurora-related kinase 3
Aurora/IPL1/Eg2 protein 2
Serine/threonine-protein kinase 13
Serine/threonine-protein kinase aurora-C

Gene names

Name:	AURKC
Synonyms:	AIE2, AIK3, AIRK3, ARK3, STK13

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

General annotation (Comments)

Function	Serine/threonine-protein kinase component of the chromosomal passenger complex (CPC), a complex that acts as a key regulator of mitosis. The CPC complex has essential functions at the centromere in ensuring correct chromosome alignment and segregation and is required for chromatin-induced microtubule stabilization and spindle assembly. Plays also a role in meiosis and more particularly in spermatogenesis. Has redundant cellular functions with AURKB and can rescue an AURKB knockdown. Like AURKB, AURKC phosphorylates histone H3 at 'Ser-10' and 'Ser-28'. Phosphorylates TACC1, another protein involved in cell division, at 'Ser-228'. Ref.4 Ref.8 Ref.9 Ref.10 Ref.12 Ref.13
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Enzyme regulation	Okadaic acid, an inhibitor of protein phosphatase 1 (PP1), protein phosphatase 2A (PP2A) and protein phosphatase 5 (PP5), increases AURKC activity. AURKC is also stabilized through its interaction with INCENP, which acts also as an activator. Ref.9
Subunit structure	Component of the chromosomal passenger complex (CPC) composed of at least BIRC5/survivin, CDCA8/borealin, INCENP, AURKB and AURKC. Interacts directly with BIRC5/survivin and INCENP. Interacts with TACC1. Ref.8 Ref.9 Ref.10 Ref.12
Subcellular location	Nucleus. Chromosome. Chromosome › centromere. Cytoplasm › cytoskeleton › spindle. Note: Distributes in the condensed chromosomes during prophase to metaphase. After entering anaphase, there is a dissociation from separated chromosomes and a redistribution to midzone microtubules, and finally remains in the midbody during cytokinesis. Ref.1 Ref.3 Ref.4 Ref.8 Ref.9 Ref.10 Ref.12 Ref.13
Tissue specificity	Isoform 1 and isoform 2 are expressed in testis. Elevated expression levels were seen only in a subset of cancer cell lines such as Hep-G2, Huh-7 and HeLa. Expression is maximum at M phase. Ref.4
Induction	Expression is cell cycle-regulated, with an increase during G2 and M phases. Ref.3 Ref.8 Ref.9
Involvement in disease	Spermatogenic failure 5 (SPGF5) [MIM:243060]: An infertility disorder caused by spermatogenesis defects. Semen from affected men show close to 100% morphologically abnormal multiflagellar spermatozoa with low motility, oversized irregular heads, and abnormal midpiece and acrosome. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.11 Ref.14
Sequence similarities	Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. Aurora subfamily. Contains 1 protein kinase domain.

Ontologies

Keywords
Biological process	Cell cycle Cell division Meiosis Mitosis
Cellular component	Centromere Chromosome Cytoplasm Cytoskeleton Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	attachment of spindle microtubules to kinetochore Traceable author statement PubMed 19774610. Source: UniProtKB cytokinesis Traceable author statement Ref.3. Source: ProtInc histone modification Traceable author statement PubMed 19774610. Source: UniProtKB meiosis Inferred from electronic annotation. Source: UniProtKB-KW positive regulation of cell cycle cytokinesis Traceable author statement PubMed 19774610. Source: UniProtKB spindle midzone assembly involved in mitosis Traceable author statement PubMed 19774610. Source: UniProtKB
Cellular_component	chromosome passenger complex Traceable author statement PubMed 19774610. Source: UniProtKB chromosome, centromeric region Inferred from electronic annotation. Source: UniProtKB-SubCell condensed chromosome Inferred from direct assay Ref.4. Source: UniProtKB cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW midbody Inferred from direct assay Ref.4. Source: UniProtKB nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell spindle midzone Inferred from direct assay Ref.4. Source: UniProtKB
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein serine/threonine kinase activity Inferred from electronic annotation. Source: UniProtKB-KW protein serine/threonine/tyrosine kinase activity Traceable author statement PubMed 19774610. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9UQB9-1)

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: Q9UQB9-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-34: Missing.

Isoform 3 (identifier: Q9UQB9-3)

Also known as: Aurora C-SV;

The sequence of this isoform differs from the canonical sequence as follows:
     1-20: MSSPRAVVQLGKAQPAGEEL → M

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 309	309	Aurora kinase C		PRO_0000085660
Regions
	Domain	43 – 293	251	Protein kinase
	Nucleotide binding	49 – 57	9	ATP By similarity
Sites
	Active site	166	1	Proton acceptor By similarity
	Binding site	72	1	ATP By similarity
Amino acid modifications
	Modified residue	198	1	Phosphothreonine; by PKA By similarity
Natural variations
	Alternative sequence	1 – 34	34	Missing in isoform 2.		VSP_004872
	Alternative sequence	1 – 20	20	MSSPR…AGEEL → M in isoform 3.		VSP_041095
	Natural variant	52	1	G → E in a lung adenocarcinoma sample; somatic mutation. Ref.15		VAR_040385
	Natural variant	148	1	E → Q in a lung squamous cell carcinoma sample; somatic mutation. Ref.15		VAR_040386
	Natural variant	244	1	H → Q in a lung adenocarcinoma sample; somatic mutation. Ref.15		VAR_040387
Experimental info
	Mutagenesis	72	1	K → R: Impairs kinase activity. Ref.8 Ref.9
	Mutagenesis	166	1	D → Y: Impairs kinase activity, and keeps AURKC with the chromosomes until the end of mitosis. Ref.10
	Mutagenesis	198	1	T → A: Impairs kinase activity. Ref.4 Ref.9
	Sequence conflict	109	1	Y → H in AAC25955. Ref.1
	Sequence conflict	150	1	L → V in AAC77369. Ref.2
	Sequence conflict	193 – 195	3	SLR → LPE in AAC77369. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 41B7DFCA91704201	FASTA	309	35,591
	10 20 30 40 50 60 MSSPRAVVQL GKAQPAGEEL ATANQTAQQP SSPAMRRLTV DDFEIGRPLG KGKFGNVYLA 70 80 90 100 110 120 RLKESHFIVA LKVLFKSQIE KEGLEHQLRR EIEIQAHLQH PNILRLYNYF HDARRVYLIL 130 140 150 160 170 180 EYAPRGELYK ELQKSEKLDE QRTATIIEEL ADALTYCHDK KVIHRDIKPE NLLLGFRGEV 190 200 210 220 230 240 KIADFGWSVH TPSLRRKTMC GTLDYLPPEM IEGRTYDEKV DLWCIGVLCY ELLVGYPPFE 250 260 270 280 290 300 SASHSETYRR ILKVDVRFPL SMPLGARDLI SRLLRYQPLE RLPLAQILKH PWVQAHSRRV LPPCAQMAS
	Isoform 2 [UniParc]. Checksum: 8DF2BDC1F436E266	FASTA	275	32,187
	10 20 30 40 50 60 MRRLTVDDFE IGRPLGKGKF GNVYLARLKE SHFIVALKVL FKSQIEKEGL EHQLRREIEI 70 80 90 100 110 120 QAHLQHPNIL RLYNYFHDAR RVYLILEYAP RGELYKELQK SEKLDEQRTA TIIEELADAL 130 140 150 160 170 180 TYCHDKKVIH RDIKPENLLL GFRGEVKIAD FGWSVHTPSL RRKTMCGTLD YLPPEMIEGR 190 200 210 220 230 240 TYDEKVDLWC IGVLCYELLV GYPPFESASH SETYRRILKV DVRFPLSMPL GARDLISRLL 250 260 270 RYQPLERLPL AQILKHPWVQ AHSRRVLPPC AQMAS
	Isoform 3 (Aurora C-SV) [UniParc]. Checksum: D07FD6988B208140	FASTA	290	33,672
	10 20 30 40 50 60 MATANQTAQQ PSSPAMRRLT VDDFEIGRPL GKGKFGNVYL ARLKESHFIV ALKVLFKSQI 70 80 90 100 110 120 EKEGLEHQLR REIEIQAHLQ HPNILRLYNY FHDARRVYLI LEYAPRGELY KELQKSEKLD 130 140 150 160 170 180 EQRTATIIEE LADALTYCHD KKVIHRDIKP ENLLLGFRGE VKIADFGWSV HTPSLRRKTM 190 200 210 220 230 240 CGTLDYLPPE MIEGRTYDEK VDLWCIGVLC YELLVGYPPF ESASHSETYR RILKVDVRFP 250 260 270 280 290 LSMPLGARDL ISRLLRYQPL ERLPLAQILK HPWVQAHSRR VLPPCAQMAS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Protein kinase profile of sperm and eggs: cloning and characterization of two novel testis-specific protein kinases (AIE1, AIE2) related to yeast and fly chromosome segregation regulators." Tseng T.-C., Chen S.-H., Hsu Y.-P.P., Tang T.K. DNA Cell Biol. 17:823-833(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION. Tissue: Testis.
[2]	"Cloning of STK13, a third human protein kinase related to Drosophila aurora and budding yeast Ipl1 that maps on chromosome 19q13.3-ter." Bernard M., Sanseau P., Henry C., Couturier A., Prigent C. Genomics 53:406-409(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). Tissue: Placenta.
[3]	"Cell cycle-dependent expression and centrosome localization of a third human Aurora/Ipl1-related protein kinase, AIK3." Kimura M., Matsuda Y., Yoshioka T., Okano Y. J. Biol. Chem. 274:7334-7340(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INDUCTION, SUBCELLULAR LOCATION. Tissue: Testis.
[4]	"Cloning and characterization of a novel human Aurora C splicing variant." Yan X., Wu Y., Li Q., Cao L., Liu X., Saiyin H., Yu L. Biochem. Biophys. Res. Commun. 328:353-361(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), TISSUE SPECIFICITY, FUNCTION, MUTAGENESIS OF THR-198, SUBCELLULAR LOCATION.
[5]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	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].
[7]	"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 2). Tissue: Brain.
[8]	"Aurora-C kinase is a novel chromosomal passenger protein that can complement Aurora-B kinase function in mitotic cells." Sasai K., Katayama H., Stenoien D.L., Fujii S., Honda R., Kimura M., Okano Y., Tatsuka M., Suzuki F., Nigg E.A., Earnshaw W.C., Brinkley W.R., Sen S. Cell Motil. Cytoskeleton 59:249-263(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INDUCTION, FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH INCENP, MUTAGENESIS OF LYS-72.
[9]	"Direct association with inner centromere protein (INCENP) activates the novel chromosomal passenger protein, Aurora-C." Li X., Sakashita G., Matsuzaki H., Sugimoto K., Kimura K., Hanaoka F., Taniguchi H., Furukawa K., Urano T. J. Biol. Chem. 279:47201-47211(2004) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE CDC COMPLEX, SUBCELLULAR LOCATION, ENZYME REGULATION, FUNCTION, MUTAGENESIS OF LYS-72 AND THR-198.
[10]	"Aurora C is directly associated with Survivin and required for cytokinesis." Yan X., Cao L., Li Q., Wu Y., Zhang H., Saiyin H., Liu X., Zhang X., Shi Q., Yu L. Genes Cells 10:617-626(2005) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE CDC COMPLEX, INTERACTION WITH BIRC5, SUBCELLULAR LOCATION, FUNCTION, MUTAGENESIS OF ASP-166.
[11]	"Homozygous mutation of AURKC yields large-headed polyploid spermatozoa and causes male infertility." Dieterich K., Soto Rifo R., Faure A.K., Hennebicq S., Ben Amar B., Zahi M., Perrin J., Martinez D., Sele B., Jouk P.-S., Ohlmann T., Rousseaux S., Lunardi J., Ray P.F. Nat. Genet. 39:661-665(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN SPGF5.
[12]	"Aurora-C interacts with and phosphorylates the transforming acidic coiled-coil 1 protein." Gabillard J.C., Ulisse S., Baldini E., Sorrenti S., Cremet J.Y., Coccaro C., Prigent C., D'Armiento M., Arlot-Bonnemains Y. Biochem. Biophys. Res. Commun. 408:647-653(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH TACC1.
[13]	"A role for Aurora C in the chromosomal passenger complex during human preimplantation embryo development." Avo Santos M., van de Werken C., de Vries M., Jahr H., Vromans M.J., Laven J.S., Fauser B.C., Kops G.J., Lens S.M., Baart E.B. Hum. Reprod. 26:1868-1881(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[14]	"A new AURKC mutation causing macrozoospermia: implications for human spermatogenesis and clinical diagnosis." Ben Khelifa M., Zouari R., Harbuz R., Halouani L., Arnoult C., Lunardi J., Ray P.F. Mol. Hum. Reprod. 17:762-768(2011) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN SPGF5.
[15]	"Patterns of somatic mutation in human cancer genomes." Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R. Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] GLU-52; GLN-148 AND GLN-244.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF054621 mRNA. Translation: AAC25955.1. AF059681 mRNA. Translation: AAC77369.1. AB017332 mRNA. Translation: BAA76292.1. AY661554 mRNA. Translation: AAT64422.1. AC005261 Genomic DNA. No translation available. CH471135 Genomic DNA. Translation: EAW72485.1. BC075064 mRNA. Translation: AAH75064.2.
IPI	IPI00099756. IPI00332343. IPI00555808.
RefSeq	NP_001015878.1. NM_001015878.1. NP_001015879.1. NM_001015879.1. NP_003151.2. NM_003160.2.
UniGene	Hs.98338.
3D structure databases
ProteinModelPortal	Q9UQB9.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9UQB9. 2 interactions.
STRING	9606.ENSP00000302898.
PTM databases
PhosphoSite	Q9UQB9.
Polymorphism databases
DMDM	27805738.
Proteomic databases
PaxDb	Q9UQB9.
PRIDE	Q9UQB9.
Protocols and materials databases
DNASU	6795.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000302804; ENSP00000302898; ENSG00000105146. ENST00000415300; ENSP00000407162; ENSG00000105146. ENST00000448930; ENSP00000406798; ENSG00000105146. ENST00000598785; ENSP00000471830; ENSG00000105146.
GeneID	6795.
KEGG	hsa:6795.
UCSC	uc002qoc.3. human. uc002qod.3. human.
Organism-specific databases
CTD	6795.
GeneCards	GC19P057743.
HGNC	HGNC:11391. AURKC.
HPA	HPA034859.
MIM	243060. phenotype. 603495. gene.
neXtProt	NX_Q9UQB9.
Orphanet	137893. Male infertility associated with large-headed multiflagellar polyploid spermatozoa.
PharmGKB	PA36200.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0515.
HOGENOM	HOG000233016.
HOVERGEN	HBG108519.
InParanoid	Q9UQB9.
KO	K11480.
OMA	ILKHPWV.
Enzyme and pathway databases
Pathway_Interaction_DB	aurora_b_pathway. Aurora B signaling. aurora_c_pathway. Aurora C signaling. aurora_kinase_pathway. Signaling by Aurora kinases.
Gene expression databases
Bgee	Q9UQB9.
CleanEx	HS_AURKC.
Genevestigator	Q9UQB9.
GermOnline	ENSG00000105146. Homo sapiens.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR002290. Ser/Thr_dual-sp_kinase_dom. IPR008271. Ser/Thr_kinase_AS. [Graphical view]
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
SMART	SM00220. S_TKc. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
PROSITE	PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	Q9UQB9.
ChEMBL	CHEMBL3935.
GenomeRNAi	6795.
NextBio	26545.
SOURCE	Search...

Entry information

Entry name

AURKC_HUMAN

Accession

Primary (citable) accession number: Q9UQB9
Secondary accession number(s): O60681 , O75442, Q6AZY8, Q6DLZ0, Q9UPK5

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 17, 2003
Last sequence update:	May 1, 2000
Last modified:	May 1, 2013
This is version 123 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.