Q9HCE1 (MOV10_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Putative helicase MOV-10
EC=3.6.4.13

Alternative name(s):
Moloney leukemia virus 10 protein

Gene names

Name:	MOV10
Synonyms:	KIAA1631

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	1003 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Probable RNA helicase. Required for RNA-mediated gene silencing by the RNA-induced silencing complex (RISC). Required for both miRNA-mediated translational repression and miRNA-mediated cleavage of complementary mRNAs by RISC. Also required for RNA-directed transcription and replication of the human hepatitis delta virus (HDV). Interacts with small capped HDV RNAs derived from genomic hairpin structures that mark the initiation sites of RNA-dependent HDV RNA transcription. Ref.7 Ref.8 Ref.10 Ref.15
Catalytic activity	ATP + H2O = ADP + phosphate.
Subunit structure	Interacts with DICER1, EIF2C1/AGO1, EIF2C2/AGO2, EIF6 and TARBP2. Associates with the 60S ribosome. Interacts with the human hepatitis delta virus (HDV) antigen HDAg. Interacts with APOBEC3G in an RNA-dependent manner. Ref.7 Ref.8 Ref.15
Subcellular location	Cytoplasm › P-body Ref.7.
Sequence similarities	Belongs to the DNA2/NAM7 helicase family. SDE3 subfamily.
Sequence caution	The sequence BAB13457.1 differs from that shown. Reason: Erroneous translation. Wrong choice of CDS. The sequence BAB85000.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Biological process	RNA-mediated gene silencing Transcription Transcription regulation
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing
Ligand	ATP-binding Nucleotide-binding RNA-binding
Molecular function	Helicase Hydrolase
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	Notch signaling pathway Traceable author statement. Source: Reactome mRNA cleavage involved in gene silencing by miRNA Inferred from direct assay Ref.7. Source: UniProtKB regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasmic mRNA processing body Inferred from direct assay Ref.7. Source: UniProtKB cytosol Traceable author statement. Source: Reactome
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW RNA binding Inferred from electronic annotation. Source: UniProtKB-KW helicase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
EIF2AK2	P19525	2	EBI-1055820,EBI-640775

Alternative products

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

Isoform 1 (identifier: Q9HCE1-1)

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: Q9HCE1-2)

The sequence of this isoform differs from the canonical sequence as follows:
     838-900: EKIRYCITKL...DLDFNLGFLK → RSSVTSKGGA...PGLLPGSLLH
     901-1003: Missing.

Note: No experimental confirmation available.

Isoform 3 (identifier: Q9HCE1-3)

The sequence of this isoform differs from the canonical sequence as follows:
     47-56: FGTPAPGFSS → LASSKSILQS
     57-1003: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1003	1003	Putative helicase MOV-10		PRO_0000080704
Regions
	Nucleotide binding	524 – 531	8	ATP By similarity
	Region	921 – 965	45	Interaction with EIF2C2 and APOBEC3G
	Motif	645 – 648	4	DEAG box
Amino acid modifications
	Modified residue	148	1	N6-acetyllysine Ref.12
	Modified residue	160	1	Phosphothreonine Ref.9
	Modified residue	254	1	Phosphothreonine Ref.11 Ref.13
	Modified residue	969	1	Phosphoserine Ref.13
Natural variations
	Alternative sequence	47 – 56	10	FGTPAPGFSS → LASSKSILQS in isoform 3.		VSP_037305
	Alternative sequence	57 – 1003	947	Missing in isoform 3.		VSP_037306
	Alternative sequence	838 – 900	63	EKIRY…LGFLK → RSSVTSKGGAPPPDGTSLIS RPLGRGSRSLGLCWLRISEE HQGQLPPPFVPQLPGLLPGS LLH in isoform 2.		VSP_010943
	Alternative sequence	901 – 1003	103	Missing in isoform 2.		VSP_010944
Experimental info
	Sequence conflict	98	1	D → N in AL833353. Ref.4
	Sequence conflict	248	1	A → T in AL833353. Ref.4
	Sequence conflict	814	1	S → T in AL833353. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 1, 2002. Version 2. Checksum: 28A8B3BF9B5B54FC	FASTA	1,003	113,671
	10 20 30 40 50 60 MPSKFSCRQL REAGQCFESF LVVRGLDMET DRERLRTIYN RDFKISFGTP APGFSSMLYG 70 80 90 100 110 120 MKIANLAYVT KTRVRFFRLD RWADVRFPEK RRMKLGSDIS KHHKSLLAKI FYDRAEYLHG 130 140 150 160 170 180 KHGVDVEVQG PHEARDGQLL IRLDLNRKEV LTLRLRNGGT QSVTLTHLFP LCRTPQFAFY 190 200 210 220 230 240 NEDQELPCPL GPGECYELHV HCKTSFVGYF PATVLWELLG PGESGSEGAG TFYIARFLAA 250 260 270 280 290 300 VAHSPLAAQL KPMTPFKRTR ITGNPVVTNR IEEGERPDRA KGYDLELSMA LGTYYPPPRL 310 320 330 340 350 360 RQLLPMLLQG TSIFTAPKEI AEIKAQLETA LKWRNYEVKL RLLLHLEELQ MEHDIRHYDL 370 380 390 400 410 420 ESVPMTWDPV DQNPRLLTLE VPGVTESRPS VLRGDHLFAL LSSETHQEDP ITYKGFVHKV 430 440 450 460 470 480 ELDRVKLSFS MSLLSRFVDG LTFKVNFTFN RQPLRVQHRA LELTGRWLLW PMLFPVAPRD 490 500 510 520 530 540 VPLLPSDVKL KLYDRSLESN PEQLQAMRHI VTGTTRPAPY IIFGPPGTGK TVTLVEAIKQ 550 560 570 580 590 600 VVKHLPKAHI LACAPSNSGA DLLCQRLRVH LPSSIYRLLA PSRDIRMVPE DIKPCCNWDA 610 620 630 640 650 660 KKGEYVFPAK KKLQEYRVLI TTLITAGRLV SAQFPIDHFT HIFIDEAGHC MEPESLVAIA 670 680 690 700 710 720 GLMEVKETGD PGGQLVLAGD PRQLGPVLRS PLTQKHGLGY SLLERLLTYN SLYKKGPDGY 730 740 750 760 770 780 DPQFITKLLR NYRSHPTILD IPNQLYYEGE LQACADVVDR ERFCRWAGLP RQGFPIIFHG 790 800 810 820 830 840 VMGKDEREGN SPSFFNPEEA ATVTSYLKLL LAPSSKKGKA RLSPRSVGVI SPYRKQVEKI 850 860 870 880 890 900 RYCITKLDRE LRGLDDIKDL KVGSVEEFQG QERSVILIST VRSSQSFVQL DLDFNLGFLK 910 920 930 940 950 960 NPKRFNVAVT RAKALLIIVG NPLLLGHDPD WKVFLEFCKE NGGYTGCPFP AKLDLQQGQN 970 980 990 1000 LLQGLSKLSP STSGPHSHDY LPQEREGEGG LSLQVEPEWR NEL
	Isoform 2 [UniParc]. Checksum: 0CF3733285C48342	FASTA	900	101,598
	10 20 30 40 50 60 MPSKFSCRQL REAGQCFESF LVVRGLDMET DRERLRTIYN RDFKISFGTP APGFSSMLYG 70 80 90 100 110 120 MKIANLAYVT KTRVRFFRLD RWADVRFPEK RRMKLGSDIS KHHKSLLAKI FYDRAEYLHG 130 140 150 160 170 180 KHGVDVEVQG PHEARDGQLL IRLDLNRKEV LTLRLRNGGT QSVTLTHLFP LCRTPQFAFY 190 200 210 220 230 240 NEDQELPCPL GPGECYELHV HCKTSFVGYF PATVLWELLG PGESGSEGAG TFYIARFLAA 250 260 270 280 290 300 VAHSPLAAQL KPMTPFKRTR ITGNPVVTNR IEEGERPDRA KGYDLELSMA LGTYYPPPRL 310 320 330 340 350 360 RQLLPMLLQG TSIFTAPKEI AEIKAQLETA LKWRNYEVKL RLLLHLEELQ MEHDIRHYDL 370 380 390 400 410 420 ESVPMTWDPV DQNPRLLTLE VPGVTESRPS VLRGDHLFAL LSSETHQEDP ITYKGFVHKV 430 440 450 460 470 480 ELDRVKLSFS MSLLSRFVDG LTFKVNFTFN RQPLRVQHRA LELTGRWLLW PMLFPVAPRD 490 500 510 520 530 540 VPLLPSDVKL KLYDRSLESN PEQLQAMRHI VTGTTRPAPY IIFGPPGTGK TVTLVEAIKQ 550 560 570 580 590 600 VVKHLPKAHI LACAPSNSGA DLLCQRLRVH LPSSIYRLLA PSRDIRMVPE DIKPCCNWDA 610 620 630 640 650 660 KKGEYVFPAK KKLQEYRVLI TTLITAGRLV SAQFPIDHFT HIFIDEAGHC MEPESLVAIA 670 680 690 700 710 720 GLMEVKETGD PGGQLVLAGD PRQLGPVLRS PLTQKHGLGY SLLERLLTYN SLYKKGPDGY 730 740 750 760 770 780 DPQFITKLLR NYRSHPTILD IPNQLYYEGE LQACADVVDR ERFCRWAGLP RQGFPIIFHG 790 800 810 820 830 840 VMGKDEREGN SPSFFNPEEA ATVTSYLKLL LAPSSKKGKA RLSPRSVGVI SPYRKQVRSS 850 860 870 880 890 900 VTSKGGAPPP DGTSLISRPL GRGSRSLGLC WLRISEEHQG QLPPPFVPQL PGLLPGSLLH
	Isoform 3 [UniParc]. Checksum: 5FAEB3C0DC2A00F6	FASTA	56	6,546
	10 20 30 40 50 MPSKFSCRQL REAGQCFESF LVVRGLDMET DRERLRTIYN RDFKISLASS KSILQS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Prediction of the coding sequences of unidentified human genes. XVIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro." Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O. DNA Res. 7:273-281(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). Tissue: Brain.
[2]	"Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones." Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T. DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract] Cited for: SEQUENCE REVISION.
[3]	"The nucleotide sequence of a long cDNA clone isolated from human spleen." Jikuya H., Takano J., Nomura N., Kikuno R., Nagase T., Ohara O. Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Spleen.
[4]	"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 1). Tissue: Testis.
[5]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract] 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: Muscle, Placenta and Skin.
[7]	"Identification of novel argonaute-associated proteins." Meister G., Landthaler M., Peters L., Chen P.Y., Urlaub H., Luehrmann R., Tuschl T. Curr. Biol. 15:2149-2155(2005) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, INTERACTION WITH EIF2C1 AND EIF2C2, SUBCELLULAR LOCATION.
[8]	"MicroRNA silencing through RISC recruitment of eIF6." Chendrimada T.P., Finn K.J., Ji X., Baillat D., Gregory R.I., Liebhaber S.A., Pasquinelli A.E., Shiekhattar R. Nature 447:823-828(2007) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, INTERACTION WITH DICER1; EIF2C2; EIF6 AND TARBP2, ASSOCIATION WITH THE 60S RIBOSOME.
[9]	"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 THR-160, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[10]	"Capped small RNAs and MOV10 in human hepatitis delta virus replication." Haussecker D., Cao D., Huang Y., Parameswaran P., Fire A.Z., Kay M.A. Nat. Struct. Mol. Biol. 15:714-721(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, RNA-BINDING.
[11]	"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 THR-254, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"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-148, MASS SPECTROMETRY.
[13]	"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 THR-254 AND SER-969, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"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].
[15]	"APOBEC3G inhibits microRNA-mediated repression of translation by interfering with the interaction between Argonaute-2 and MOV10." Liu C., Zhang X., Huang F., Yang B., Li J., Liu B., Luo H., Zhang P., Zhang H. J. Biol. Chem. 287:29373-29383(2012) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH APOBEC3G AND EIF2C2.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB046851 mRNA. Translation: BAB13457.1. Sequence problems. AK074174 mRNA. Translation: BAB85000.1. Different initiation. AL833353 mRNA. No translation available. AL603832 Genomic DNA. Translation: CAI14055.1. BC002548 mRNA. Translation: AAH02548.1. BC004499 mRNA. Translation: AAH04499.2. BC009312 mRNA. Translation: AAH09312.1.
IPI	IPI00444452. IPI00444454. IPI00929442.
RefSeq	NP_001123551.1. NM_001130079.1. NP_066014.1. NM_020963.3.
UniGene	Hs.514941.
3D structure databases
ProteinModelPortal	Q9HCE1.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-44158N.
IntAct	Q9HCE1. 16 interactions.
STRING	9606.ENSP00000350028.
PTM databases
PhosphoSite	Q9HCE1.
Polymorphism databases
DMDM	24638063.
Proteomic databases
PaxDb	Q9HCE1.
PRIDE	Q9HCE1.
Protocols and materials databases
DNASU	4343.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000357443; ENSP00000350028; ENSG00000155363. ENST00000369645; ENSP00000358659; ENSG00000155363. ENST00000413052; ENSP00000399797; ENSG00000155363. ENST00000544796; ENSP00000439533; ENSG00000155363.
GeneID	4343.
KEGG	hsa:4343.
UCSC	uc001eck.3. human.
Organism-specific databases
CTD	4343.
GeneCards	GC01P113215.
HGNC	HGNC:7200. MOV10.
MIM	610742. gene.
neXtProt	NX_Q9HCE1.
PharmGKB	PA30908.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG1112.
HOGENOM	HOG000239755.
HOVERGEN	HBG052500.
InParanoid	Q9HCE1.
OMA	VRFFKLD.
OrthoDB	EOG4SXNC4.
PhylomeDB	Q9HCE1.
Enzyme and pathway databases
Reactome	REACT_111102. Signal Transduction. REACT_116125. Disease. REACT_6900. Immune System.
Gene expression databases
ArrayExpress	Q9HCE1.
Bgee	Q9HCE1.
CleanEx	HS_MOV10.
Genevestigator	Q9HCE1.
GermOnline	ENSG00000155363. Homo sapiens.
Family and domain databases
InterPro	IPR026122. MOV-10/Armitage. [Graphical view]
PANTHER	PTHR10887:SF17. PTHR10887:SF17. 1 hit.
ProtoNet	Search...
Other
ChiTaRS	MOV10. human.
GenomeRNAi	4343.
NextBio	17098.
SOURCE	Search...

Entry information

Entry name

MOV10_HUMAN

Accession

Primary (citable) accession number: Q9HCE1
Secondary accession number(s): Q5JR03 , Q8TEF0, Q9BSY3, Q9BUJ9

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 2002
Last sequence update:	November 1, 2002
Last modified:	May 1, 2013
This is version 103 of the entry and version 2 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.