Q9H1I8 (ASCC2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Activating signal cointegrator 1 complex subunit 2

Alternative name(s):
ASC-1 complex subunit p100
Trip4 complex subunit p100

Gene names

Name:	ASCC2
Synonyms:	ASC1P100

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

General annotation (Comments)

Function	Enhances NF-kappa-B, SRF and AP1 transactivation.
Subunit structure	Part of TRIP4 complex, that contains ASCC1, ASCC2 and ASCC3. The TRIP4 complex interacts with ALKHB3. Ref.1 Ref.8
Tissue specificity	Ubiquitous.
Sequence similarities	Belongs to the ASCC2 family. Contains 1 CUE domain.
Sequence caution	The sequence BAB15089.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Coding sequence diversity	Alternative splicing Polymorphism
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

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

Isoform 1 (identifier: Q9H1I8-1)

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: Q9H1I8-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-114: Missing.
     483-484: GE → EK
     485-757: Missing.

Note: No experimental confirmation available.

Isoform 3 (identifier: Q9H1I8-3)

The sequence of this isoform differs from the canonical sequence as follows:
     28-80: Missing.
     137-159: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 757

757

Activating signal cointegrator 1 complex subunit 2

PRO_0000064689

Regions

Domain

467 – 510

44

CUE

Amino acid modifications

Modified residue

713

1

Phosphoserine Ref.5 Ref.6

Natural variations

Alternative sequence

1 – 114

114

Missing in isoform 2.

VSP_011009

Alternative sequence

28 – 80

53

Missing in isoform 3.

VSP_045878

Alternative sequence

137 – 159

23

Missing in isoform 3.

VSP_045879

Alternative sequence

483 – 484

2

GE → EK in isoform 2.

VSP_011010

Alternative sequence

485 – 757

273

Missing in isoform 2.

VSP_011011

Natural variant

96

1

R → C.
Corresponds to variant rs1894473 [ dbSNP | Ensembl ].

VAR_050675

Natural variant

123

1

V → I.
Corresponds to variant rs11549795 [ dbSNP | Ensembl ].

VAR_050676

Natural variant

407

1

D → H.
Corresponds to variant rs28265 [ dbSNP | Ensembl ].

VAR_025512

Natural variant

423

1

P → S.
Corresponds to variant rs36571 [ dbSNP | Ensembl ].

VAR_025513

Natural variant

509

1

R → Q. Ref.1
Corresponds to variant rs4823054 [ dbSNP | Ensembl ].

VAR_019464

Natural variant

546

1

D → G.
Corresponds to variant rs34833047 [ dbSNP | Ensembl ].

VAR_050677

Natural variant

588

1

E → K.
Corresponds to variant rs34062345 [ dbSNP | Ensembl ].

VAR_050678

Natural variant

639

1

R → L.
Corresponds to variant rs6006259 [ dbSNP | Ensembl ].

VAR_025514

Experimental info

Sequence conflict

344

1

Q → H in BAB15089. Ref.2

Sequence conflict

526

1

K → N in BAB15089. Ref.2

Sequence conflict

586

1

R → C in BAB15089. Ref.2

Sequence conflict

639

1

R → G in BAH13926. Ref.2

Sequence conflict

645

1

P → L in AAG45475. Ref.1

Sequence conflict

653

1

P → L in AAG45475. Ref.1

Sequence conflict

661

1

D → G in BAH13926. Ref.2

Sequence conflict

744

1

T → I in BAH13926. Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

757

Helix Strand Turn

Details...

Helix

466 – 478

13

Helix

484 – 493

10

Turn

494 – 496

3

Helix

498 – 506

9

Turn

512 – 516

5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 7, 2006. Version 3. Checksum: BB1DCE21E3068E64	FASTA	757	86,360
	10 20 30 40 50 60 MPALPLDQLQ ITHKDPKTGK LRTSPALHPE QKADRYFVLY KPPPKDNIPA LVEEYLERAT 70 80 90 100 110 120 FVANDLDWLL ALPHDKFWCQ VIFDETLQKC LDSYLRYVPR KFDEGVASAP EVVDMQKRLH 130 140 150 160 170 180 RSVFLTFLRM STHKESKDHF ISPSAFGEIL YNNFLFDIPK ILDLCVLFGK GNSPLLQKMI 190 200 210 220 230 240 GNIFTQQPSY YSDLDETLPT ILQVFSNILQ HCGLQGDGAN TTPQKLEERG RLTPSDMPLL 250 260 270 280 290 300 ELKDIVLYLC DTCTTLWAFL DIFPLACQTF QKHDFCYRLA SFYEAAIPEM ESAIKKRRLE 310 320 330 340 350 360 DSKLLGDLWQ RLSHSRKKLM EIFHIILNQI CLLPILESSC DNIQGFIEEF LQIFSSLLQE 370 380 390 400 410 420 KRFLRDYDAL FPVAEDISLL QQASSVLDET RTAYILQAVE SAWEGVDRRK ATDAKDPSVI 430 440 450 460 470 480 EEPNGEPNGV TVTAEAVSQA SSHPENSEEE ECMGAAAAVG PAMCGVELDS LISQVKDLLP 490 500 510 520 530 540 DLGEGFILAC LEYYHYDPEQ VINNILEERL APTLSQLDRN LDREMKPDPT PLLTSRHNVF 550 560 570 580 590 600 QNDEFDVFSR DSVDLSRVHK GKSTRKEENT RSLLNDKRAV AAQRQRYEQY SVVVEEVPLQ 610 620 630 640 650 660 PGESLPYHSV YYEDEYDDTY DGNQVGANDA DSDDELISRR PFTIPQVLRT KVPREGQEED 670 680 690 700 710 720 DDDEEDDADE EAPKPDHFVQ DPAVLREKAE ARRMAFLAKK GYRHDSSTAV AGSPRGHGQS 730 740 750 RETTQERRKK EANKATRANH NRRTMADRKR SKGMIPS
	Isoform 2 [UniParc]. Checksum: A89920B986C9E9B7	FASTA	370	41,794
	10 20 30 40 50 60 MQKRLHRSVF LTFLRMSTHK ESKDHFISPS AFGEILYNNF LFDIPKILDL CVLFGKGNSP 70 80 90 100 110 120 LLQKMIGNIF TQQPSYYSDL DETLPTILQV FSNILQHCGL QGDGANTTPQ KLEERGRLTP 130 140 150 160 170 180 SDMPLLELKD IVLYLCDTCT TLWAFLDIFP LACQTFQKHD FCYRLASFYE AAIPEMESAI 190 200 210 220 230 240 KKRRLEDSKL LGDLWQRLSH SRKKLMEIFH IILNQICLLP ILESSCDNIQ GFIEEFLQIF 250 260 270 280 290 300 SSLLQEKRFL RDYDALFPVA EDISLLQQAS SVLDETRTAY ILQAVESAWE GVDRRKATDA 310 320 330 340 350 360 KDPSVIEEPN GEPNGVTVTA EAVSQASSHP ENSEEEECMG AAAAVGPAMC GVELDSLISQ 370 VKDLLPDLEK
	Isoform 3 [UniParc]. Checksum: B2D69EB5D82C311E	FASTA	681	77,369
	10 20 30 40 50 60 MPALPLDQLQ ITHKDPKTGK LRTSPALVIF DETLQKCLDS YLRYVPRKFD EGVASAPEVV 70 80 90 100 110 120 DMQKRLHRSV FLTFLRMSTH KESKILDLCV LFGKGNSPLL QKMIGNIFTQ QPSYYSDLDE 130 140 150 160 170 180 TLPTILQVFS NILQHCGLQG DGANTTPQKL EERGRLTPSD MPLLELKDIV LYLCDTCTTL 190 200 210 220 230 240 WAFLDIFPLA CQTFQKHDFC YRLASFYEAA IPEMESAIKK RRLEDSKLLG DLWQRLSHSR 250 260 270 280 290 300 KKLMEIFHII LNQICLLPIL ESSCDNIQGF IEEFLQIFSS LLQEKRFLRD YDALFPVAED 310 320 330 340 350 360 ISLLQQASSV LDETRTAYIL QAVESAWEGV DRRKATDAKD PSVIEEPNGE PNGVTVTAEA 370 380 390 400 410 420 VSQASSHPEN SEEEECMGAA AAVGPAMCGV ELDSLISQVK DLLPDLGEGF ILACLEYYHY 430 440 450 460 470 480 DPEQVINNIL EERLAPTLSQ LDRNLDREMK PDPTPLLTSR HNVFQNDEFD VFSRDSVDLS 490 500 510 520 530 540 RVHKGKSTRK EENTRSLLND KRAVAAQRQR YEQYSVVVEE VPLQPGESLP YHSVYYEDEY 550 560 570 580 590 600 DDTYDGNQVG ANDADSDDEL ISRRPFTIPQ VLRTKVPREG QEEDDDDEED DADEEAPKPD 610 620 630 640 650 660 HFVQDPAVLR EKAEARRMAF LAKKGYRHDS STAVAGSPRG HGQSRETTQE RRKKEANKAT 670 680 RANHNRRTMA DRKRSKGMIP S

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Novel transcription coactivator complex containing activating signal cointegrator 1." Jung D.-J., Sung H.-S., Goo Y.-W., Lee H.M., Park O.K., Jung S.-Y., Lim J., Kim H.-J., Lee S.-K., Kim T.S., Lee J.W., Lee Y.C. Mol. Cell. Biol. 22:5203-5211(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, VARIANT GLN-509, INTERACTION WITH ASCC1 AND ASCC3. Tissue: Cervix carcinoma.
[2]	"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] (ISOFORMS 1; 2 AND 3). Tissue: Colon, Teratocarcinoma and Thymus.
[3]	"The DNA sequence of human chromosome 22." Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M. , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H. Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"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: Skin.
[5]	"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra." Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D. J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-713, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[6]	"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-713, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[7]	"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].
[8]	"DNA unwinding by ASCC3 helicase is coupled to ALKBH3-dependent DNA alkylation repair and cancer cell proliferation." Dango S., Mosammaparast N., Sowa M.E., Xiong L.J., Wu F., Park K., Rubin M., Gygi S., Harper J.W., Shi Y. Mol. Cell 44:373-384(2011) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ALKHB3.
[9]	"Solution structure of the CUE domain in the human activating signal cointegrator 1 complex subunit 2 (ASCC2)." RIKEN structural genomics initiative (RSGI) Submitted (SEP-2006) to the PDB data bank Cited for: STRUCTURE BY NMR OF 463-525.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AY013289 mRNA. Translation: AAG45475.1.
AK022886 mRNA. Translation: BAB14293.1.
AK025241 mRNA. Translation: BAB15089.1. Different initiation.
AK303257 mRNA. Translation: BAH13926.1.
Z82171, AC004882 Genomic DNA. Translation: CAI95602.1.
BC025368 mRNA. Translation: AAH25368.1.

IPI

IPI00452803.
IPI00549736.
IPI01015732.

RefSeq

NP_001229835.1. NM_001242906.1.
NP_115580.2. NM_032204.4.

UniGene

Hs.731754.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2DI0	NMR	-	A	463-525	[»]

ProteinModelPortal

Q9H1I8.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9H1I8. 33 interactions.

MINT

MINT-1182192.

STRING

9606.ENSP00000305502.

PTM databases

PhosphoSite

Q9H1I8.

Polymorphism databases

DMDM

92090990.

Proteomic databases

PaxDb

Q9H1I8.

PeptideAtlas

Q9H1I8.

PRIDE

Q9H1I8.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000307790; ENSP00000305502; ENSG00000100325.
ENST00000397771; ENSP00000380877; ENSG00000100325.
ENST00000542393; ENSP00000437570; ENSG00000100325.

GeneID

84164.

KEGG

hsa:84164.

UCSC

uc003agr.3. human.

Organism-specific databases

CTD

84164.

GeneCards

GC22M030184.

HGNC

HGNC:24103. ASCC2.

HPA

HPA001439.

MIM

614216. gene.

neXtProt

NX_Q9H1I8.

PharmGKB

PA134916940.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG245009.

HOGENOM

HOG000234347.

HOVERGEN

HBG050589.

InParanoid

Q9H1I8.

OMA

NDLDETM.

OrthoDB

EOG4F7NJF.

PhylomeDB

Q9H1I8.

Gene expression databases

ArrayExpress

Q9H1I8.

Bgee

Q9H1I8.

CleanEx

HS_ASCC2.

Genevestigator

Q9H1I8.

GermOnline

ENSG00000100325. Homo sapiens.

Family and domain databases

InterPro

IPR003892. CUE.
IPR009060. UBA-like.
[Graphical view]

Pfam

PF02845. CUE. 1 hit.
[Graphical view]

SMART

SM00546. CUE. 1 hit.
[Graphical view]

SUPFAM

SSF46934. UBA_like. 1 hit.

PROSITE

PS51140. CUE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

ASCC2. human.

EvolutionaryTrace

Q9H1I8.

GenomeRNAi

84164.

NextBio

73512.

SOURCE

Search...

Entry information

Entry name

ASCC2_HUMAN

Accession

Primary (citable) accession number: Q9H1I8
Secondary accession number(s): B7Z8E0 , F5H6J9, Q4TT54, Q8TAZ0, Q9H711, Q9H9D6

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2004
Last sequence update:	March 7, 2006
Last modified:	May 1, 2013
This is version 95 of the entry and version 3 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.