Reviewed, UniProtKB/Swiss-Prot Q15075 (EEA1_HUMAN)

Names and origin

Protein names

Recommended name:
    Early endosome antigen 1
Alternative name(s):
    Endosome-associated protein p162
    Zinc finger FYVE domain-containing protein 2

Gene names

Name:	EEA1
Synonyms:	ZFYVE2

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	1411 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Binds phospholipid vesicles containing phosphatidylinositol 3-phosphate and participates in endosomal trafficking.
Subunit structure	Homodimer. Binds STX6. Binds RAB5A, RAB5B, RAB5C and RAB22A that have been activated by GTP-binding. Ref.8 Ref.11 Ref.13
Subcellular location	Cytoplasm. Early endosome membrane; Peripheral membrane protein. Ref.1 Ref.7 Ref.9
Domain	The FYVE-type zinc finger domain mediates interactions with phosphatidylinositol 3-phosphate.
Involvement in disease	Antibodies against EEA1 are found in sera from patients with subacute cutaneous lupus erythematosus and other autoimmune diseases.
Sequence similarities	Contains 1 C2H2-type zinc finger. Contains 1 FYVE-type zinc finger.

Ontologies

Keywords
Cellular component	Cytoplasm Endosome Membrane
Coding sequence diversity	Polymorphism
Domain	Coiled coil Zinc-finger
Ligand	Metal-binding Zinc
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	early endosome to late endosome transport Ref.1 Non-traceable author statement. Source: UniProtKB synaptic vesicle to endosome fusion Ref.13 Traceable author statement. Source: UniProtKB vesicle fusion Ref.5 Inferred from mutant phenotype. Source: UniProtKB
Cellular component	cytosol Ref.1 Inferred from direct assay. Source: UniProtKB early endosome Ref.1 Ref.13 Inferred from direct assay. Source: UniProtKB extrinsic to plasma membrane Ref.1 Inferred from direct assay. Source: UniProtKB membrane fraction Ref.1 Traceable author statement. Source: ProtInc
Molecular function	GTP-dependent protein binding Ref.6 Inferred from direct assay. Source: UniProtKB calmodulin binding Ref.13 Non-traceable author statement. Source: UniProtKB phosphatidylinositol binding Ref.5 Inferred from direct assay. Source: UniProtKB protein homodimerization activity Ref.13 Inferred from direct assay. Source: UniProtKB zinc ion binding Ref.13 Traceable author statement. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
RAB22A	Q9UL26	1	EBI-298113,EBI-399456
RAB5A	P20339	3	EBI-298113,EBI-399437
RAB5B	P61020	1	EBI-298113,EBI-399401
Stx6	Q63635	2	EBI-298113,EBI-398854	From a different organism.
TOM1	O60784	1	EBI-298113,EBI-74634
ZFYVE16	Q7Z3T8	1	EBI-298113,EBI-298055

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1411

1411

Early endosome antigen 1

PRO_0000098706

Regions

Zinc finger

41 – 64

24

C2H2-type

Zinc finger

1352 – 1410

59

FYVE-type

Coiled coil

74 – 1348

1275

Potential

Compositional bias

397 – 758

362

Gln/Glu/Lys-rich

Compositional bias

937 – 1032

96

Gln/Glu/Lys-rich

Compositional bias

1093 – 1231

139

Glu/Lys-rich

Natural variations

Natural variant

810

1

K → Q: dbSNP rs10745623. Ref.1 Ref.2

VAR_052980

Experimental info

Mutagenesis

39

1

E → A: Strongly reduces interaction with RAB5C. Ref.11

Mutagenesis

41

1

F → A: Strongly reduces interaction with RAB5C. Ref.11

Mutagenesis

42

1

I → A: Strongly reduces interaction with RAB5C. Ref.11

Mutagenesis

44

1

P → A: Strongly reduces interaction with RAB5C. Ref.11

Mutagenesis

47

1

M → A: Strongly reduces interaction with RAB5C. Ref.11

Mutagenesis

60

1

Y → A: Strongly reduces interaction with RAB5C. Ref.11

Mutagenesis

1349

1

W → A: Reduces phosphatidylinositol 3-phosphate binding and endosomal location. Ref.9

Mutagenesis

1352

1

D → V: Reduces phosphatidylinositol 3-phosphate binding and endosomal location. Ref.8

Mutagenesis

1357

1

N → D: Reduces phosphatidylinositol 3-phosphate binding and endosomal location. Ref.8

Mutagenesis

1358

1

C → S: Abolishes phosphatidylinositol 3-phosphate binding and endosomal location. Ref.9

Mutagenesis

1365

1

F → A: Strongly reduces phosphatidylinositol 3-phosphate binding and endosomal location. Ref.9

Mutagenesis

1367 – 1368

2

VT → EE or GG: Abolishes phosphatidylinositol 3-phosphate binding and endosomal location.

Mutagenesis

1370

1

R → A: Abolishes endosomal location. Ref.9

Mutagenesis

1371

1

R → A: Abolishes phosphatidylinositol 3-phosphate binding and endosomal location. Ref.9

Mutagenesis

1372

1

H → A: Abolishes endosomal location. Ref.9

Mutagenesis

1373

1

H → A: Abolishes phosphatidylinositol 3-phosphate binding and endosomal location. Ref.9

Mutagenesis

1374

1

C → A: Abolishes phosphatidylinositol 3-phosphate binding and endosomal location. Ref.9

Mutagenesis

1375

1

R → G: Abolishes phosphatidylinositol 3-phosphate binding and endosomal location. Ref.8 Ref.9

Mutagenesis

1377

1

C → A: Abolishes phosphatidylinositol 3-phosphate binding and endosomal location. Ref.9

Mutagenesis

1378

1

G → A: Abolishes phosphatidylinositol 3-phosphate binding and endosomal location. Ref.9

Mutagenesis

1385

1

C → A: Abolishes phosphatidylinositol 3-phosphate binding and endosomal location. Ref.9

Mutagenesis

1400

1

R → G: Strongly reduces phosphatidylinositol 3-phosphate binding and abolishes endosomal location. Ref.8 Ref.9

Mutagenesis

1405

1

C → S: Abolishes phosphatidylinositol 3-phosphate binding and endosomal location. Ref.9

Sequence conflict

255

1

C → S in AAA79121. Ref.1

Sequence conflict

258 – 259

2

LQ → FE in AAA79121. Ref.1

Sequence conflict

277

1

A → S in AAA79121. Ref.1

Sequence conflict

284

1

A → R in AAA79121. Ref.1

Sequence conflict

520

1

D → E in AAA79121. Ref.1

Sequence conflict

575 – 576

2

EQ → DE in AAA79121. Ref.1

Sequence conflict

583 – 584

2

KL → NV in AAA79121. Ref.1

Sequence conflict

680

1

Q → H in AAA79121. Ref.1

Sequence conflict

1325

1

Missing in AAA79121. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

1411

Helix Strand Turn

Details...

Helix

1290 – 1346

57

Helix

1352 – 1354

3

Turn

1359 – 1361

3

Beta strand

1367 – 1369

3

Turn

1375 – 1377

3

Helix

1383 – 1385

3

Beta strand

1388 – 1390

3

Beta strand

1399 – 1401

3

Helix

1403 – 1408

6

Sequences

	Sequence		Length	Mass (Da)
	Q15075-1 [UniParc]. Last modified May 5, 2009. Version 2. Checksum: 51BA418F561E3411	FASTA	1,411	162,466
	10 20 30 40 50 60 MLRRILQRTP GRVGSQGSDL DSSATPINTV DVNNESSSEG FICPQCMKSL GSADELFKHY 70 80 90 100 110 120 EAVHDAGNDS GHGGESNLAL KRDDVTLLRQ EVQDLQASLK EEKWYSEELK KELEKYQGLQ 130 140 150 160 170 180 QQEAKPDGLV TDSSAELQSL EQQLEEAQTE NFNIKQMKDL FEQKAAQLAT EIADIKSKYD 190 200 210 220 230 240 EERSLREAAE QKVTRLTEEL NKEATVIQDL KTELLQRPGI EDVAVLKKEL VQVQTLMDNM 250 260 270 280 290 300 TLERERESEK LKDECKKLQS QYASSEATIS QLRSELAKGP QEVAVYVQEL QKLKSSVNEL 310 320 330 340 350 360 TQKNQTLTEN LLKKEQDYTK LEEKHNEESV SKKNIQATLH QKDLDCQQLQ SRLSASETSL 370 380 390 400 410 420 HRIHVELSEK GEATQKLKEE LSEVETKYQH LKAEFKQLQQ QREEKEQHGL QLQSEINQLH 430 440 450 460 470 480 SKLLETERQL GEAHGRLKEQ RQLSSEKLMD KEQQVADLQL KLSRLEEQLK EKVTNSTELQ 490 500 510 520 530 540 HQLDKTKQQH QEQQALQQST TAKLREAQND LEQVLRQIGD KDQKIQNLEA LLQKSKENIS 550 560 570 580 590 600 LLEKEREDLY AKIQAGEGET AVLNQLQEKN HTLQEQVTQL TEKLKNQSES HKQAQENLHD 610 620 630 640 650 660 QVQEQKAHLR AAQDRVLSLE TSVNELNSQL NESKEKVSQL DIQIKAKTEL LLSAEAAKTA 670 680 690 700 710 720 QRADLQNHLD TAQNALQDKQ QELNKITTQL DQVTAKLQDK QEHCSQLESH LKEYKEKYLS 730 740 750 760 770 780 LEQKTEELEG QIKKLEADSL EVKASKEQAL QDLQQQRQLN TDLELRATEL SKQLEMEKEI 790 800 810 820 830 840 VSSTRLDLQK KSEALESIKQ KLTKQEEEKK ILKQDFETLS QETKIQHEEL NNRIQTTVTE 850 860 870 880 890 900 LQKVKMEKEA LMTELSTVKD KLSKVSDSLK NSKSEFEKEN QKGKAAILDL EKTCKELKHQ 910 920 930 940 950 960 LQVQMENTLK EQKELKKSLE KEKEASHQLK LELNSMQEQL IQAQNTLKQN EKEEQQLQGN 970 980 990 1000 1010 1020 INELKQSSEQ KKKQIEALQG ELKIAVLQKT ELENKLQQQL TQAAQELAAE KEKISVLQNN 1030 1040 1050 1060 1070 1080 YEKSQETFKQ LQSDFYGRES ELLATRQDLK SVEEKLSLAQ EDLISNRNQI GNQNKLIQEL 1090 1100 1110 1120 1130 1140 KTAKATLEQD SAKKEQQLQE RCKALQDIQK EKSLKEKELV NEKSKLAEIE EIKCRQEKEI 1150 1160 1170 1180 1190 1200 TKLNEELKSH KLESIKEITN LKDAKQLLIQ QKLELQGKAD SLKAAVEQEK RNQQILKDQV 1210 1220 1230 1240 1250 1260 KKEEEELKKE FIEKEAKLHS EIKEKEVGMK KHEENEAKLT MQITALNENL GTVKKEWQSS 1270 1280 1290 1300 1310 1320 QRRVSELEKQ TDDLRGEIAV LEATVQNNQD ERRALLERCL KGEGEIEKLQ TKVLELQRKL 1330 1340 1350 1360 1370 1380 DNTTAAVQEL GRENQSLQIK HTQALNRKWA EDNEVQNCMA CGKGFSVTVR RHHCRQCGNI 1390 1400 1410 FCAECSAKNA LTPSSKKPVR VCDACFNDLQ G

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"EEA1, an early endosome-associated protein. EEA1 is a conserved alpha-helical peripheral membrane protein flanked by cysteine 'fingers' and contains a calmodulin-binding IQ motif." Mu F.-T., Callaghan J.M., Steele-Mortimer O., Stenmark H., Parton R.G., Campbell P.L., McCluskey J., Yeo J.-P., Tock E.P.C., Toh B.-H. J. Biol. Chem. 270:13503-13511(1995) [PubMed: 7768953] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, VARIANT GLN-810. Tissue: Cervix carcinoma.
[2]	Seelig H.P. Submitted (APR-1994) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT GLN-810.
[3]	"The finished DNA sequence of human chromosome 12." Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A. Nature 440:346-351(2006) [PubMed: 16541075] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	Lubec G., Chen W.-Q., Sun Y. Submitted (DEC-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 996-1011 AND 1319-1332, MASS SPECTROMETRY. Tissue: Fetal brain cortex.
[5]	"EEA1 links PI(3)K function to Rab5 regulation of endosome fusion." Simonsen A., Lippe R., Christoforidis S., Gaullier J.-M., Brech A., Callaghan J.M., Toh B.-H., Murphy C., Zerial M., Stenmark H. Nature 394:494-498(1998) [PubMed: 9697774] [Abstract] Cited for: INTERACTION WITH RAB5A.
[6]	"Direct interaction of EEA1 with Rab5b." Callaghan J.M., Nixon S., Bucci C., Toh B.-H., Stenmark H. Eur. J. Biochem. 265:361-366(1999) [PubMed: 10491193] [Abstract] Cited for: INTERACTION WITH RAB5A AND RAB5B.
[7]	"The Rab5 effector EEA1 interacts directly with syntaxin-6." Simonsen A., Gaullier J.-M., D'Arrigo A., Stenmark H. J. Biol. Chem. 274:28857-28860(1999) [PubMed: 10506127] [Abstract] Cited for: INTERACTION WITH STX6, SUBCELLULAR LOCATION.
[8]	"Phosphatidylinositol 3-phosphate recognition by the FYVE domain." Kutateladze T.G., Ogburn K.D., Watson W.T., de Beer T., Emr S.D., Burd C.G., Overduin M. Mol. Cell 3:805-811(1999) [PubMed: 10394369] [Abstract] Cited for: MUTAGENESIS OF ASP-1352; ASN-1357; 1367-VAL-THR-1368; ARG-1375 AND ARG-1400, HOMODIMERIZATION, INTERACTION WITH PHOSPHATIDYLINOSITOL 3-PHOSPHATE.
[9]	"Interaction of the EEA1 FYVE finger with phosphatidylinositol 3-phosphate and early endosomes. Role of conserved residues." Gaullier J.-M., Roenning E., Gillooly D.J., Stenmark H. J. Biol. Chem. 275:24595-24600(2000) [PubMed: 10807926] [Abstract] Cited for: MUTAGENESIS OF TRP-1349; CYS-1358; PHE-1365; ARG-1370; ARG-1371; HIS-1372; HIS-1373; CYS-1374; ARG-1375; CYS-1377; GLY-1378; CYS-1385; ARG-1400 AND CYS-1405, SUBCELLULAR LOCATION, INTERACTION WITH PHOSPHATIDYLINOSITOL 3-PHOSPHATE.
[10]	"The small GTPase Rab22 interacts with EEA1 and controls endosomal membrane trafficking." Kauppi M., Simonsen A., Bremnes B., Vieira A., Callaghan J.M., Stenmark H., Olkkonen V.M. J. Cell Sci. 115:899-911(2002) [PubMed: 11870209] [Abstract] Cited for: INTERACTION WITH RAB22A.
[11]	"Determinants of Rab5 interaction with the N-terminus of early endosome antigen 1." Merithew E., Stone C., Eathiraj S., Lambright D.G. J. Biol. Chem. 278:8494-8500(2003) [PubMed: 12493736] [Abstract] Cited for: MUTAGENESIS OF GLU-39; PHE-41; ILE-42; PRO-44; MET-47 AND TYR-60, HOMODIMERIZATION, INTERACTION WITH RAB5C.
[12]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[13]	"Multivalent endosome targeting by homodimeric EEA1." Dumas J.J., Merithew E., Sudharshan E., Rajamani D., Hayes S., Lawe D., Corvera S., Lambright D.G. Mol. Cell 8:947-958(2001) [PubMed: 11741531] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1289-1411 IN COMPLEX WITH PHOSPHATIDYLINOSITOL 3-PHOSPHATE, HOMODIMERIZATION.
[14]	"Structural mechanism of endosome docking by the FYVE domain." Kutateladze T.G., Overduin M. Science 291:1793-1796(2001) [PubMed: 11230696] [Abstract] Cited for: STRUCTURE BY NMR OF 1346-1410 ALONE AND IN COMPLEX WITH PHOSPHATIDYLINOSITOL 3-PHOSPHATE.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

L40157 mRNA. Translation: AAA79121.1.
X78998 mRNA. Translation: CAA55632.1.
AC016136 Genomic DNA. No translation available.
AC021646 Genomic DNA. No translation available.
AC026111 Genomic DNA. No translation available.

IPI

IPI00329536.

PIR

A57013.

RefSeq

NP_003557.2.

UniGene

Hs.567367

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1HYI	NMR	-	A	1347-1411	[»]
1HYJ	NMR	-	A	1347-1411	[»]
1JOC	X-ray	2.20	A/B	1287-1411	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

Q15075. 11 interactions.

STRING

Q15075.

PTM databases

PhosphoSite

Q15075.

Proteomic databases

PRIDE

Q15075.

Genome annotation databases

Ensembl

ENST00000322349; ENSP00000317955; ENSG00000102189; Homo sapiens. [Genome view]
ENST00000418984; ENSP00000394312; ENSG00000102189; Homo sapiens. [Genome view]

GeneID

8411.

KEGG

hsa:8411.

UCSC

uc001tck.1. human.

Organism-specific databases

CTD

8411.

GeneCards

GC12M091668.

H-InvDB

HIX0026379.

HGNC

HGNC:3185. EEA1.

HPA

CAB005861.
CAB018782.

MIM

605070. gene.

PharmGKB

PA27621.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

Q15075.

HOVERGEN

Q15075.

Gene expression databases

ArrayExpress

Q15075.

Bgee

Q15075.

CleanEx

HS_EEA1.

Genevestigator

Q15075.

GermOnline

ENSG00000102189. Homo sapiens.

Family and domain databases

InterPro

IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR000306. Znf_FYVE.
IPR017455. Znf_FYVE-rel.
[Graphical view]

Pfam

PF01363. FYVE. 1 hit.
[Graphical view]

SMART

SM00064. FYVE. 1 hit.
SM00355. ZnF_C2H2. 1 hit.
[Graphical view]

PROSITE

PS50178. ZF_FYVE. 1 hit.
PS00028. ZINC_FINGER_C2H2_1. 1 hit.
PS50157. ZINC_FINGER_C2H2_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

31490.

PMAP-CutDB

Q15075.

SOURCE

Search...

Entry information

Entry name

EEA1_HUMAN

Accession

Primary (citable) accession number: Q15075
Secondary accession number(s): Q14221

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 22, 2003
Last sequence update:	May 5, 2009
Last modified:	October 13, 2009
This is version 81 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.