Q9ULT8 (HECD1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
E3 ubiquitin-protein ligase HECTD1
EC=6.3.2.-

Alternative name(s):
E3 ligase for inhibin receptor
EULIR
HECT domain-containing protein 1

Gene names

Name:	HECTD1
Synonyms:	KIAA1131

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	2610 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Probable E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. May be required for development of the head mesenchyme and neural tube closure By similarity.
Pathway	Protein modification; protein ubiquitination.
Subunit structure	Interacts with IGSF1. Ref.7
Sequence similarities	Belongs to the UPL family. K-HECT subfamily. Contains 4 ANK repeats. Contains 1 HECT (E6AP-type E3 ubiquitin-protein ligase) domain. Contains 1 MIB/HERC2 domain.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Coding sequence diversity	Polymorphism
Domain	ANK repeat Repeat
Molecular function	Ligase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	neural tube closure Inferred from electronic annotation. Source: Compara protein ubiquitination involved in ubiquitin-dependent protein catabolic process Inferred from Biological aspect of Ancestor. Source: RefGenome
Cellular_component	cytoplasm Inferred from Biological aspect of Ancestor. Source: RefGenome nucleus Inferred from Biological aspect of Ancestor. Source: RefGenome
Molecular_function	metal ion binding Inferred from electronic annotation. Source: InterPro ubiquitin-protein ligase activity Inferred from Biological aspect of Ancestor. Source: RefGenome
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 2610

2610

E3 ubiquitin-protein ligase HECTD1

PRO_0000083945

Regions

Repeat

395 – 424

30

ANK 1

Repeat

426 – 455

30

ANK 2

Repeat

459 – 491

33

ANK 3

Repeat

579 – 612

34

ANK 4

Domain

1266 – 1338

73

MIB/HERC2

Domain

2151 – 2610

460

HECT

Region

2029 – 2103

75

K-box

Compositional bias

1350 – 1649

300

Ser-rich

Sites

Active site

2579

1

Glycyl thioester intermediate By similarity

Amino acid modifications

Modified residue

631

1

Phosphoserine Ref.11

Modified residue

1390

1

Phosphoserine By similarity

Modified residue

1488

1

Phosphoserine Ref.8

Natural variations

Natural variant

656

1

Q → H.
Corresponds to variant rs11620816 [ dbSNP | Ensembl ].

VAR_059666

Natural variant

2027

1

L → P. Ref.3 Ref.4 Ref.5
Corresponds to variant rs1315794 [ dbSNP | Ensembl ].

VAR_067707

Experimental info

Sequence conflict

561

1

K → Q in AAP13073. Ref.1

Sequence conflict

603

1

L → I in AAP13073. Ref.1

Sequence conflict

611 – 613

3

FLD → YKH in AAP13073. Ref.1

Sequence conflict

653

1

K → Q in AAP13073. Ref.1

Sequence conflict

894

1

E → K in AAP13073. Ref.1

Sequence conflict

927 – 944

18

SMDLD…VERIN → VSIFRATKQKQNEVPKVILS in AAP13073. Ref.1

Sequence conflict

951

1

S → T in AAP13073. Ref.1

Sequence conflict

1281

1

I → T in BAA86445. Ref.2

Secondary structure

1

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2610

Helix Strand Turn

Details...

Helix

1270 – 1272

3

Beta strand

1279 – 1282

4

Turn

1289 – 1292

4

Beta strand

1299 – 1301

3

Beta strand

1309 – 1314

6

Turn

1315 – 1317

3

Beta strand

1319 – 1325

7

Helix

1326 – 1328

3

Beta strand

1332 – 1334

3

Helix

1883 – 1886

4

Helix

1896 – 1902

7

Beta strand

1905 – 1908

4

Helix

1910 – 1920

11

Helix

1923 – 1928

6

Helix

1935 – 1941

7

Helix

1944 – 1957

14

Turn

1960 – 1962

3

Sequences

	Sequence		Length	Mass (Da)
	Q9ULT8 [UniParc]. Last modified November 30, 2010. Version 3. Checksum: 27E56401E07E158C	FASTA	2,610	289,384
	10 20 30 40 50 60 MADVDPDTLL EWLQMGQGDE RDMQLIALEQ LCMLLLMSDN VDRCFETCPP RTFLPALCKI 70 80 90 100 110 120 FLDESAPDNV LEVTARAITY YLDVSAECTR RIVGVDGAIK ALCNRLVVVE LNNRTSRDLA 130 140 150 160 170 180 EQCVKVLELI CTRESGAVFE AGGLNCVLTF IRDSGHLVHK DTLHSAMAVV SRLCGKMEPQ 190 200 210 220 230 240 DSSLEICVES LSSLLKHEDH QVSDGALRCF ASLADRFTRR GVDPAPLAKH GLTEELLSRM 250 260 270 280 290 300 AAAGGTVSGP SSACKPGRST TGAPSTTADS KLSNQVSTIV SLLSTLCRGS PVVTHDLLRS 310 320 330 340 350 360 ELPDSIESAL QGDERCVLDT MRLVDLLLVL LFEGRKALPK SSAGSTGRIP GLRRLDSSGE 370 380 390 400 410 420 RSHRQLIDCI RSKDTDALID AIDTGAFEVN FMDDVGQTLL NWASAFGTQE MVEFLCERGA 430 440 450 460 470 480 DVNRGQRSSS LHYAACFGRP QVAKTLLRHG ANPDLRDEDG KTPLDKARER GHSEVVAILQ 490 500 510 520 530 540 SPGDWMCPVN KGDDKKKKDT NKDEEECNEP KGDPEMAPIY LKRLLPVFAQ TFQQTMLPSI 550 560 570 580 590 600 RKASLALIRK MIHFCSEALL KEVCDSDVGH NLPTILVEIT ATVLDQEDDD DGHLLALQII 610 620 630 640 650 660 RDLVDKGGDI FLDQLARLGV ISKVSTLAGP SSDDENEEES KPEKEDEPQE DAKELQQGKP 670 680 690 700 710 720 YHWRDWSIIR GRDCLYIWSD AAALELSNGS NGWFRFILDG KLATMYSSGS PEGGSDSSES 730 740 750 760 770 780 RSEFLEKLQR ARGQVKPSTS SQPILSAPGP TKLTVGNWSL TCLKEGEIAI HNSDGQQATI 790 800 810 820 830 840 LKEDLPGFVF ESNRGTKHSF TAETSLGSEF VTGWTGKRGR KLKSKLEKTK QKVRTMARDL 850 860 870 880 890 900 YDDHFKAVES MPRGVVVTLR NIATQLESSW ELHTNRQCIE SENTWRDLMK TALENLIVLL 910 920 930 940 950 960 KDENTISPYE MCSSGLVQAL LTVLNNSMDL DMKQDCSQLV ERINVFKTAF SENEDDESRP 970 980 990 1000 1010 1020 AVALIRKLIA VLESIERLPL HLYDTPGSTY NLQILTRRLR FRLERAPGET ALIDRTGRML 1030 1040 1050 1060 1070 1080 KMEPLATVES LEQYLLKMVA KQWYDFDRSS FVFVRKLREG QNFIFRHQHD FDENGIIYWI 1090 1100 1110 1120 1130 1140 GTNAKTAYEW VNPAAYGLVV VTSSEGRNLP YGRLEDILSR DNSALNCHSN DDKNAWFAID 1150 1160 1170 1180 1190 1200 LGLWVIPSAY TLRHARGYGR SALRNWVFQV SKDGQNWTSL YTHVDDCSLN EPGSTATWPL 1210 1220 1230 1240 1250 1260 DPPKDEKQGW RHVRIKQMGK NASGQTHYLS LSGFELYGTV NGVCEDQLGK AAKEAEANLR 1270 1280 1290 1300 1310 1320 RQRRLVRSQV LKYMVPGARV IRGLDWKWRD QDGSPQGEGT VTGELHNGWI DVTWDAGGSN 1330 1340 1350 1360 1370 1380 SYRMGAEGKF DLKLAPGYDP DTVASPKPVS STVSGTTQSW SSLVKNNCPD KTSAAAGSSS 1390 1400 1410 1420 1430 1440 RKGSSSSVCS VASSSDISLG STKTERRSEI VMEHSIVSGA DVHEPIVVLS SAENVPQTEV 1450 1460 1470 1480 1490 1500 GSSSSASTST LTAETGSENA ERKLGPDSSV RTPGESSAIS MGIVSVSSPD VSSVSELTNK 1510 1520 1530 1540 1550 1560 EAASQRPLSS SASNRLSVSS LLAAGAPMSS SASVPNLSSR ETSSLESFVR RVANIARTNA 1570 1580 1590 1600 1610 1620 TNNMNLSRSS SDNNTNTLGR NVMSTATSPL MGAQSFPNLT TPGTTSTVTM STSSVTSSSN 1630 1640 1650 1660 1670 1680 VATATTVLSV GQSLSNTLTT SLTSTSSESD TGQEAEYSLY DFLDSCRAST LLAELDDDED 1690 1700 1710 1720 1730 1740 LPEPDEEDDE NEDDNQEDQE YEEVMILRRP SLQRRAGSRS DVTHHAVTSQ LPQVPAGAGS 1750 1760 1770 1780 1790 1800 RPIGEQEEEE YETKGGRRRT WDDDYVLKRQ FSALVPAFDP RPGRTNVQQT TDLEIPPPGT 1810 1820 1830 1840 1850 1860 PHSELLEEVE CTPSPRLALT LKVTGLGTTR EVELPLTNFR STIFYYVQKL LQLSCNGNVK 1870 1880 1890 1900 1910 1920 SDKLRRIWEP TYTIMYREMK DSDKEKENGK MGCWSIEHVE QYLGTDELPK NDLITYLQKN 1930 1940 1950 1960 1970 1980 ADAAFLRHWK LTGTNKSIRK NRNCSQLIAA YKDFCEHGTK SGLNQGAIST LQSSDILNLT 1990 2000 2010 2020 2030 2040 KEQPQAKAGN GQNSCGVEDV LQLLRILYIV ASDPYSRISQ EDGDEQLQFT FPPDEFTSKK 2050 2060 2070 2080 2090 2100 ITTKILQQIE EPLALASGAL PDWCEQLTSK CPFLIPFETR QLYFTCTAFG ASRAIVWLQN 2110 2120 2130 2140 2150 2160 RREATVERTR TTSSVRRDDP GEFRVGRLKH ERVKVPRGES LMEWAENVMQ IHADRKSVLE 2170 2180 2190 2200 2210 2220 VEFLGEEGTG LGPTLEFYAL VAAEFQRTDL GAWLCDDNFP DDESRHVDLG GGLKPPGYYV 2230 2240 2250 2260 2270 2280 QRSCGLFTAP FPQDSDELER ITKLFHFLGI FLAKCIQDNR LVDLPISKPF FKLMCMGDIK 2290 2300 2310 2320 2330 2340 SNMSKLIYES RGDRDLHCTE SQSEASTEEG HDSLSVGSFE EDSKSEFILD PPKPKPPAWF 2350 2360 2370 2380 2390 2400 NGILTWEDFE LVNPHRARFL KEIKDLAIKR RQILSNKGLS EDEKNTKLQE LVLKNPSGSG 2410 2420 2430 2440 2450 2460 PPLSIEDLGL NFQFCPSSRI YGFTAVDLKP SGEDEMITMD NAEEYVDLMF DFCMHTGIQK 2470 2480 2490 2500 2510 2520 QMEAFRDGFN KVFPMEKLSS FSHEEVQMIL CGNQSPSWAA EDIINYTEPK LGYTRDSPGF 2530 2540 2550 2560 2570 2580 LRFVRVLCGM SSDERKAFLQ FTTGCSTLPP GGLANLHPRL TVVRKVDATD ASYPSVNTCV 2590 2600 2610 HYLKLPEYSS EEIMRERLLA ATMEKGFHLN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"EULIR is an E3 ubiquitin ligase for inhibin receptor." Zhang H. Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"The DNA sequence and analysis of human chromosome 14." Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H. , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J. Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	Mural R.J., Istrail S., Sutton 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT PRO-2027.
[4]	"Characterization of cDNA clones selected by the GeneMark analysis from size-fractionated cDNA libraries from human brain." Hirosawa M., Nagase T., Ishikawa K., Kikuno R., Nomura N., Ohara O. DNA Res. 6:329-336(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 443-2610, VARIANT PRO-2027. Tissue: Brain.
[5]	"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] OF 1652-2610, VARIANT PRO-2027. Tissue: Testis.
[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] OF 2091-2610. Tissue: Muscle and Urinary bladder.
[7]	"Protein-protein interactions between large proteins: two-hybrid screening using a functionally classified library composed of long cDNAs." Nakayama M., Kikuno R., Ohara O. Genome Res. 12:1773-1784(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH IGSF1.
[8]	"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-1488, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[10]	"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].
[11]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-631, MASS SPECTROMETRY.
[12]	"Solution structure of MIB-HERC2 domain in HECT domain containing protein 1." RIKEN structural genomics initiative (RSGI) Submitted (OCT-2006) to the PDB data bank Cited for: STRUCTURE BY NMR OF 1266-1338.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AY254380 mRNA. Translation: AAP13073.1.
AL121808 Genomic DNA. No translation available.
AL136418 Genomic DNA. No translation available.
CH471078 Genomic DNA. Translation: EAW65950.1.
CH471078 Genomic DNA. Translation: EAW65952.1.
AB032957 mRNA. Translation: BAA86445.2.
AL110222 mRNA. Translation: CAB53681.1.
BC011658 mRNA. Translation: AAH11658.2.
BC063686 mRNA. Translation: AAH63686.1.

IPI

IPI00328911.

PIR

T14761.

RefSeq

NP_056197.2. NM_015382.2.

UniGene

Hs.708017.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2DK3	NMR	-	A	1268-1338	[»]
2LC3	NMR	-	A	1879-1966	[»]
3DKM	X-ray	1.60	A	1271-1341	[»]

ProteinModelPortal

Q9ULT8.

SMR

Q9ULT8. Positions 1266-1338, 1879-1966.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-31669N.

IntAct

Q9ULT8. 6 interactions.

MINT

MINT-6783566.

STRING

9606.ENSP00000382269.

PTM databases

PhosphoSite

Q9ULT8.

Polymorphism databases

DMDM

85682779.

Proteomic databases

PaxDb

Q9ULT8.

PeptideAtlas

Q9ULT8.

PRIDE

Q9ULT8.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000399332; ENSP00000382269; ENSG00000092148.
ENST00000553700; ENSP00000450697; ENSG00000092148.

GeneID

25831.

KEGG

hsa:25831.

UCSC

uc001wrc.1. human.

Organism-specific databases

CTD

25831.

GeneCards

GC14M031569.

HGNC

HGNC:20157. HECTD1.

HPA

HPA002929.

neXtProt

NX_Q9ULT8.

PharmGKB

PA134989284.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5021.

HOGENOM

HOG000018061.

HOVERGEN

HBG067533.

InParanoid

Q9ULT8.

KO

K12231.

Enzyme and pathway databases

UniPathway

UPA00143.

Gene expression databases

ArrayExpress

Q9ULT8.

Bgee

Q9ULT8.

CleanEx

HS_HECTD1.

Genevestigator

Q9ULT8.

GermOnline

ENSG00000092148. Homo sapiens.

Family and domain databases

Gene3D

1.25.10.10. 2 hits.
1.25.40.20. 1 hit.
2.60.120.260. 1 hit.

InterPro

IPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR008979. Galactose-bd-like.
IPR000569. HECT.
IPR010606. Mib_Herc2.
IPR012919. Sad1_UNC_C.
[Graphical view]

Pfam

PF12796. Ank_2. 1 hit.
PF00632. HECT. 1 hit.
PF06701. MIB_HERC2. 1 hit.
PF07738. Sad1_UNC. 1 hit.
[Graphical view]

SMART

SM00248. ANK. 3 hits.
SM00119. HECTc. 1 hit.
[Graphical view]

SUPFAM

SSF48403. ANK. 1 hit.
SSF48371. ARM-type_fold. 1 hit.
SSF49785. Gal_bind_like. 1 hit.
SSF56204. HECT. 1 hit.

PROSITE

PS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 2 hits.
PS50237. HECT. 1 hit.
PS51416. MIB_HERC2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

HECTD1. human.

EvolutionaryTrace

Q9ULT8.

GenomeRNAi

25831.

NextBio

47125.

Entry information

Entry name

HECD1_HUMAN

Accession

Primary (citable) accession number: Q9ULT8
Secondary accession number(s): D3DS86 , Q6P445, Q86VJ1, Q96F34, Q9UFZ7

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 12, 2003
Last sequence update:	November 30, 2010
Last modified:	May 29, 2013
This is version 119 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.