Q9UNY4 (TTF2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Transcription termination factor 2
EC=3.6.4.-

Alternative name(s):
Lodestar homolog
RNA polymerase II termination factor
Transcription release factor 2
Short name=F2
Short name=HuF2

Gene names

Name:

TTF2

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	1162 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	DsDNA-dependent ATPase which acts as a transcription termination factor by coupling ATP hydrolysis with removal of RNA polymerase II from the DNA template. May contribute to mitotic transcription repression. May also be involved in pre-mRNA splicing. Ref.1 Ref.2 Ref.6 Ref.7
Subunit structure	Interacts with CDC5L. Part of the spliceosome. Ref.2
Subcellular location	Cytoplasm. Nucleus. Note: Cytoplasmic during interphase. Relocates to the nucleus as cells enter mitosis. Ref.7
Sequence similarities	Belongs to the SNF2/RAD54 helicase family. Contains 1 helicase ATP-binding domain. Contains 1 helicase C-terminal domain.

Ontologies

Keywords
Biological process	Transcription Transcription regulation Transcription termination mRNA processing mRNA splicing
Cellular component	Cytoplasm Nucleus Spliceosome
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	ATP-binding DNA-binding Nucleotide-binding
Molecular function	Helicase Hydrolase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	RNA splicing Inferred from electronic annotation. Source: UniProtKB-KW mRNA processing Inferred from electronic annotation. Source: UniProtKB-KW regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW termination of RNA polymerase II transcription Traceable author statement Ref.1. Source: ProtInc
Cellular_component	cytoplasm Inferred from direct assay. Source: HPA spliceosomal complex Inferred from electronic annotation. Source: UniProtKB-KW transcription elongation factor complex Traceable author statement Ref.1. Source: ProtInc
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATP-dependent helicase activity Inferred from electronic annotation. Source: InterPro DNA binding Inferred from electronic annotation. Source: UniProtKB-KW DNA-dependent ATPase activity Traceable author statement Ref.1. Source: ProtInc zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

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

Isoform 1 (identifier: Q9UNY4-1)

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: Q9UNY4-2)

The sequence of this isoform differs from the canonical sequence as follows:
     635-676: DSCDFTSHGT...NKLRVYLYHG → GRQKCLNSLP...YLITLLENQY
     677-1162: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1162	1162	Transcription termination factor 2		PRO_0000074376
Regions
	Domain	583 – 786	204	Helicase ATP-binding
	Domain	995 – 1157	163	Helicase C-terminal
	Nucleotide binding	596 – 603	8	ATP Potential
	Motif	737 – 740	4	DEAH box
Amino acid modifications
	Modified residue	460	1	Phosphoserine Ref.9 Ref.10
	Modified residue	883	1	Phosphoserine Ref.9
	Modified residue	908	1	Phosphoserine Ref.10
Natural variations
	Alternative sequence	635 – 676	42	DSCDF…YLYHG → GRQKCLNSLPFPTSFEPPKR GTSSAKKGHLWSYLITLLEN QY in isoform 2.		VSP_015370
	Alternative sequence	677 – 1162	486	Missing in isoform 2.		VSP_015371
	Natural variant	167	1	K → E. Ref.3 Corresponds to variant rs998532 [ dbSNP | Ensembl ].		VAR_023393
	Natural variant	213	1	K → R. Corresponds to variant rs7535524 [ dbSNP | Ensembl ].		VAR_034431
	Natural variant	256	1	E → G. Corresponds to variant rs34334470 [ dbSNP | Ensembl ].		VAR_061234
	Natural variant	1134	1	K → R. Corresponds to variant rs41276572 [ dbSNP | Ensembl ].		VAR_061235
	Natural variant	1155	1	D → H. Ref.2 Corresponds to variant rs34236116 [ dbSNP | Ensembl ].		VAR_061236
Experimental info
	Sequence conflict	64	1	L → P in AAD49435. Ref.2
	Sequence conflict	80	1	R → G in AAD49435. Ref.2
	Sequence conflict	675	1	H → R in AAC64044. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified August 30, 2005. Version 2. Checksum: 858BAA22B2D2D5C9	FASTA	1,162	129,588
	10 20 30 40 50 60 MEEVRCPEHG TFCFLKTGVR DGPNKGKSFY VCRADTCSFV RATDIPVSHC LLHEDFVVEL 70 80 90 100 110 120 QGLLLPQDKK EYRLFFRCIR SKAEGKRWCG SIPWQDPDSK EHSVSNKSQH ASETFHHSSN 130 140 150 160 170 180 WLRNPFKVLD KNQEPALWKQ LIKGEGEEKK ADKKQREKGD QLFDQKKEQK PEMMEKDLSS 190 200 210 220 230 240 GLVPKKKQSV VQEKKQEEGA EIQCEAETGG THKRDFSEIK SQQCQGNELT RPSASSQEKS 250 260 270 280 290 300 SGKSQDVQRE SEPLREKVTQ LLPQNVHSHN SISKPQKGGP LNKEYTNWEA KETKAKDGPS 310 320 330 340 350 360 IQATQKSLPQ GHFQERPETH SVPAPGGPAA QAAPAAPGLS LGEGREAATS SDDEEEDDVV 370 380 390 400 410 420 FVSSKPGSPL LFDSTLDLET KENLQFPDRS VQRKVSPASG VSKKVEPSDP VARRVYLTTQ 430 440 450 460 470 480 LKQKKSTLAS VNIQALPDKG QKLIKQIQEL EEVLSGLTLS PEQGTNEKSN SQVPQQSHFT 490 500 510 520 530 540 KTTTGPPHLV PPQPLPRRGT QPVGSLELKS ACQVTAGGSS QCYRGHTNQD HVHAVWKITS 550 560 570 580 590 600 EAIGQLHRSL ESCPGETVVA EDPAGLKVPL LLHQKQALAW LLWRESQKPQ GGILADDMGL 610 620 630 640 650 660 GKTLTMIALI LTQKNQEKKE EKEKSTALTW LSKDDSCDFT SHGTLIICPA SLIHHWKNEV 670 680 690 700 710 720 EKRVNSNKLR VYLYHGPNRD SRARVLSTYD IVITTYSLVA KEIPTNKQEA EIPGANLNVE 730 740 750 760 770 780 GTSTPLLRIA WARIILDEAH NVKNPRVQTS IAVCKLQACA RWAVTGTPIQ NNLLDMYSLL 790 800 810 820 830 840 KFLRCSPFDE FNLWRSQVDN GSKKGGERLS ILTKSLLLRR TKDQLDSTGR PLVILPQRKF 850 860 870 880 890 900 QLHHLKLSED EETVYNVFFA RSRSALQSYL KRHESRGNQS GRSPNNPFSR VALEFGSEEP 910 920 930 940 950 960 RHSEAADSPR SSTVHILSQL LRLRQCCCHL SLLKSALDPM ELKGEGLVLS LEEQLSALTL 970 980 990 1000 1010 1020 SELRDSEPSS TVSLNGTFFK MELFEGMRES TKISSLLAEL EAIQRNSASQ KSVIVSQWTN 1030 1040 1050 1060 1070 1080 MLKVVALHLK KHGLTYATID GSVNPKQRMD LVEAFNHSRG PQVMLISLLA GGVGLNLTGG 1090 1100 1110 1120 1130 1140 NHLFLLDMHW NPSLEDQACD RIYRVGQQKD VVIHRFVCEG TVEEKILQLQ EKKKDLAKQV 1150 1160 LSGSGESVTK LTLADLRVLF GI
	Isoform 2 [UniParc]. Checksum: 9CB5D331F1848C97	FASTA	676	75,128
	10 20 30 40 50 60 MEEVRCPEHG TFCFLKTGVR DGPNKGKSFY VCRADTCSFV RATDIPVSHC LLHEDFVVEL 70 80 90 100 110 120 QGLLLPQDKK EYRLFFRCIR SKAEGKRWCG SIPWQDPDSK EHSVSNKSQH ASETFHHSSN 130 140 150 160 170 180 WLRNPFKVLD KNQEPALWKQ LIKGEGEEKK ADKKQREKGD QLFDQKKEQK PEMMEKDLSS 190 200 210 220 230 240 GLVPKKKQSV VQEKKQEEGA EIQCEAETGG THKRDFSEIK SQQCQGNELT RPSASSQEKS 250 260 270 280 290 300 SGKSQDVQRE SEPLREKVTQ LLPQNVHSHN SISKPQKGGP LNKEYTNWEA KETKAKDGPS 310 320 330 340 350 360 IQATQKSLPQ GHFQERPETH SVPAPGGPAA QAAPAAPGLS LGEGREAATS SDDEEEDDVV 370 380 390 400 410 420 FVSSKPGSPL LFDSTLDLET KENLQFPDRS VQRKVSPASG VSKKVEPSDP VARRVYLTTQ 430 440 450 460 470 480 LKQKKSTLAS VNIQALPDKG QKLIKQIQEL EEVLSGLTLS PEQGTNEKSN SQVPQQSHFT 490 500 510 520 530 540 KTTTGPPHLV PPQPLPRRGT QPVGSLELKS ACQVTAGGSS QCYRGHTNQD HVHAVWKITS 550 560 570 580 590 600 EAIGQLHRSL ESCPGETVVA EDPAGLKVPL LLHQKQALAW LLWRESQKPQ GGILADDMGL 610 620 630 640 650 660 GKTLTMIALI LTQKNQEKKE EKEKSTALTW LSKDGRQKCL NSLPFPTSFE PPKRGTSSAK 670 KGHLWSYLIT LLENQY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A human RNA polymerase II transcription termination factor is a SWI2/SNF2 family member." Liu M., Xie Z., Price D.H. J. Biol. Chem. 273:25541-25544(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION.
[2]	"hLodestar/HuF2 interacts with CDC5L and is involved in pre-mRNA splicing." Leonard D., Ajuh P., Lamond A.I., Legerski R.J. Biochem. Biophys. Res. Commun. 308:793-801(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH CDC5L, IDENTIFICATION AS PART OF THE SPLICEOSOME, VARIANT HIS-1155.
[3]	"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] (ISOFORM 1), VARIANT GLU-167.
[4]	"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].
[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 2). Tissue: Brain.
[6]	"Human transcription release factor 2 dissociates RNA polymerases I and II stalled at a cyclobutane thymine dimer." Hara R., Selby C.P., Liu M., Price D.H., Sancar A. J. Biol. Chem. 274:24779-24786(1999) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[7]	"Involvement of transcription termination factor 2 in mitotic repression of transcription elongation." Jiang Y., Liu M., Spencer C.A., Price D.H. Mol. Cell 14:375-385(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[8]	"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[9]	"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-460 AND SER-883, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"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-460 AND SER-908, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"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].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF073771 mRNA. Translation: AAC64044.1. AF080255 mRNA. Translation: AAD49435.1. AK291017 mRNA. Translation: BAF83706.1. AL445231, AL391476 Genomic DNA. Translation: CAH71961.1. AL391476, AL445231 Genomic DNA. Translation: CAI12738.1. AL391476 Genomic DNA. Translation: CAI12731.1. BC030058 mRNA. Translation: AAH30058.1.
IPI	IPI00290812. IPI00640904.
RefSeq	NP_003585.3. NM_003594.3.
UniGene	Hs.486818. Hs.735195.
3D structure databases
ProteinModelPortal	Q9UNY4.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9UNY4. 2 interactions.
MINT	MINT-272557.
STRING	9606.ENSP00000358478.
PTM databases
PhosphoSite	Q9UNY4.
Polymorphism databases
DMDM	73920148.
Proteomic databases
PaxDb	Q9UNY4.
PRIDE	Q9UNY4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000369466; ENSP00000358478; ENSG00000116830. ENST00000427271; ENSP00000408111; ENSG00000116830.
GeneID	8458.
KEGG	hsa:8458.
UCSC	uc001egx.1. human. uc001egy.3. human.
Organism-specific databases
CTD	8458.
GeneCards	GC01P117602.
H-InvDB	HIX0000933.
HGNC	HGNC:12398. TTF2.
HPA	HPA005776.
MIM	604718. gene.
neXtProt	NX_Q9UNY4.
PharmGKB	PA37063.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0553.
HOGENOM	HOG000154708.
HOVERGEN	HBG053179.
InParanoid	Q9UNY4.
KO	K15173.
OMA	WCGSIPW.
OrthoDB	EOG4GMTWH.
PhylomeDB	Q9UNY4.
Gene expression databases
Bgee	Q9UNY4.
CleanEx	HS_TTF2.
Genevestigator	Q9UNY4.
GermOnline	ENSG00000116830. Homo sapiens.
Family and domain databases
InterPro	IPR002464. DNA/RNA_helicase_DEAH_CS. IPR014001. Helicase_ATP-bd. IPR001650. Helicase_C. IPR027417. P-loop_NTPase. IPR000330. SNF2_N. IPR010666. Znf_GRF. [Graphical view]
Pfam	PF00271. Helicase_C. 1 hit. PF00176. SNF2_N. 1 hit. PF06839. zf-GRF. 1 hit. [Graphical view]
SMART	SM00487. DEXDc. 1 hit. SM00490. HELICc. 1 hit. [Graphical view]
SUPFAM	SSF52540. SSF52540. 2 hits.
PROSITE	PS00690. DEAH_ATP_HELICASE. 1 hit. PS51192. HELICASE_ATP_BIND_1. 1 hit. PS51194. HELICASE_CTER. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	TTF2. human.
GenomeRNAi	8458.
NextBio	31654.
SOURCE	Search...

Entry information

Entry name

TTF2_HUMAN

Accession

Primary (citable) accession number: Q9UNY4
Secondary accession number(s): A8K4Q2 , O75921, Q5T2K7, Q5VVU8, Q8N6I8

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 30, 2005
Last sequence update:	August 30, 2005
Last modified:	May 29, 2013
This is version 112 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.