Q13424 (SNTA1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Alpha-1-syntrophin

Alternative name(s):
59 kDa dystrophin-associated protein A1 acidic component 1
Pro-TGF-alpha cytoplasmic domain-interacting protein 1
Short name=TACIP1
Syntrophin-1

Gene names

Name:	SNTA1
Synonyms:	SNT1

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 › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	505 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Adapter protein that binds to and probably organizes the subcellular localization of a variety of membrane proteins. May link various receptors to the actin cytoskeleton and the extracellular matrix via the dystrophin glycoprotein complex. Plays an important role in synapse formation and in the organization of UTRN and acetylcholine receptors at the neuromuscular synapse. Binds to phosphatidylinositol 4,5-bisphosphate By similarity.
Subunit structure	Monomer and homodimer. Interacts with the other members of the syntrophin family SNTB1 and SNTB2; SGCG and SGCA of the dystrophin glycoprotein complex; NOS1; GRB2; the sodium channel proteins SCN4A and SCN5A; F-actin and calmodulin By similarity. Interacts with dystrophin protein DMD and related proteins DTNA and UTRN and with MAPK12, TGFA and GA. Interacts with MYOC; regulates muscle hypertrophy By similarity. Ref.1 Ref.2 Ref.3 Ref.8 Ref.9
Subcellular location	Cell membrane › sarcolemma; Peripheral membrane protein; Cytoplasmic side By similarity. Cell junction By similarity. Cytoplasm › cytoskeleton By similarity. Note: In skeletal muscle, it localizes at the cytoplasmic side of the sarcolemmal membrane and at neuromuscular junctions By similarity.
Tissue specificity	High expression in skeletal muscle and heart. Low expression in brain, pancreas, liver, kidney and lung. Not detected in placenta.
Domain	The PH 1 domain mediates the oligomerization in a calcium dependent manner, and the association with the phosphatidylinositol 4,5-bisphosphate By similarity. The PDZ domain binds to the last three or four amino acids of ion channels and receptor proteins. The association with dystrophin or related proteins probably leaves the PDZ domain available to recruit proteins to the membrane By similarity. The SU domain binds calmodulin in a calcium-dependent manner By similarity.
Post-translational modification	Phosphorylated by CaM-kinase II. Phosphorylation may inhibit the interaction with DMD By similarity.
Involvement in disease	Long QT syndrome 12 (LQT12) [MIM:612955]: A heart disorder characterized by a prolonged QT interval on the ECG and polymorphic ventricular arrhythmias. They cause syncope and sudden death in response to exercise or emotional stress, and can present with a sentinel event of sudden cardiac death in infancy. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.14 Ref.15
Sequence similarities	Belongs to the syntrophin family. Contains 1 PDZ (DHR) domain. Contains 2 PH domains. Contains 1 SU (syntrophin unique) domain.

Ontologies

Keywords
Cellular component	Cell junction Cell membrane Cytoplasm Cytoskeleton Membrane
Coding sequence diversity	Polymorphism
Disease	Disease mutation Long QT syndrome
Domain	Repeat
Ligand	Actin-binding Calcium Calmodulin-binding
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	muscle contraction Traceable author statement Ref.1. Source: ProtInc negative regulation of peptidyl-cysteine S-nitrosylation Inferred from mutant phenotype Ref.15. Source: BHF-UCL neuromuscular junction development Inferred from electronic annotation. Source: Ensembl regulation of heart rate Inferred from mutant phenotype Ref.15. Source: BHF-UCL regulation of sodium ion transmembrane transport Inferred from mutant phenotype Ref.15. Source: BHF-UCL regulation of vasoconstriction by circulating norepinephrine Inferred from electronic annotation. Source: Ensembl regulation of ventricular cardiac muscle cell membrane repolarization Inferred from mutant phenotype Ref.15. Source: BHF-UCL ventricular cardiac muscle cell action potential Inferred from mutant phenotype Ref.15. Source: BHF-UCL
Cellular_component	cell junction Inferred from electronic annotation. Source: UniProtKB-SubCell cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW cytoskeleton Inferred from electronic annotation. Source: UniProtKB-SubCell intracellular Inferred from direct assay PubMed 17628813. Source: UniProtKB neuromuscular junction Inferred from electronic annotation. Source: Ensembl postsynaptic membrane Inferred from electronic annotation. Source: Ensembl protein complex Inferred from direct assay Ref.15. Source: BHF-UCL sarcolemma Inferred from electronic annotation. Source: UniProtKB-SubCell syntrophin complex Traceable author statement PubMed 21164104. Source: BHF-UCL
Molecular_function	ATPase binding Inferred from physical interaction Ref.15. Source: BHF-UCL ion channel binding Inferred from physical interaction Ref.15. Source: BHF-UCL nitric-oxide synthase binding Inferred from physical interaction Ref.15. Source: BHF-UCL protein binding Inferred from physical interaction PubMed 19931615. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ABCA1	O95477	2	EBI-717191,EBI-784112
Mapk12	Q63538	5	EBI-717191,EBI-783937	From a different organism.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 505	505	Alpha-1-syntrophin		PRO_0000184006
Regions
	Domain	6 – 269	264	PH 1
	Domain	87 – 170	84	PDZ
	Domain	293 – 401	109	PH 2
	Domain	449 – 505	57	SU
	Region	483 – 505	23	Calmodulin-binding By similarity
Amino acid modifications
	Modified residue	189	1	Phosphoserine Ref.10 Ref.11 Ref.13
	Modified residue	193	1	Phosphoserine Ref.10 Ref.11
Natural variations
	Natural variant	257	1	A → G in LQT12; leads to a gain of function of the voltage dependent sodium channel. Ref.14 Corresponds to variant rs56157422 [ dbSNP | Ensembl ].		VAR_062399
	Natural variant	364	1	L → F. Corresponds to variant rs1046815 [ dbSNP | Ensembl ].		VAR_014075
	Natural variant	390	1	A → V in LQT12; results in released inhibition of nNOS, S-nitrosylation of SCN5A and increased late sodium current. Ref.15		VAR_062400
Experimental info
	Sequence conflict	6	1	R → P in AAB36398. Ref.2
	Sequence conflict	25	1	G → A in AAB36398. Ref.2
	Sequence conflict	32 – 33	2	LL → PV in AAB36398. Ref.2
	Sequence conflict	66	1	G → D in AAB36398. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q13424 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: C07DA5F21C775CF8	FASTA	505	53,895
	10 20 30 40 50 60 MASGRRAPRT GLLELRAGAG SGAGGERWQR VLLSLAEDVL TVSPADGDPG PEPGAPREQE 70 80 90 100 110 120 PAQLNGAAEP GAGPPQLPEA LLLQRRRVTV RKADAGGLGI SIKGGRENKM PILISKIFKG 130 140 150 160 170 180 LAADQTEALF VGDAILSVNG EDLSSATHDE AVQVLKKTGK EVVLEVKYMK DVSPYFKNST 190 200 210 220 230 240 GGTSVGWDSP PASPLQRQPS SPGPTPRNFS EAKHMSLKMA YVSKRCTPND PEPRYLEICS 250 260 270 280 290 300 ADGQDTLFLR AKDEASARSW ATAIQAQVNT LTPRVKDELQ ALLAATSTAG SQDIKQIGWL 310 320 330 340 350 360 TEQLPSGGTA PTLALLTEKE LLLYLSLPET REALSRPART APLIATRLVH SGPSKGSVPY 370 380 390 400 410 420 DAELSFALRT GTRHGVDTHL FSVESPQELA AWTRQLVDGC HRAAEGVQEV STACTWNGRP 430 440 450 460 470 480 CSLSVHIDKG FTLWAAEPGA ARAVLLRQPF EKLQMSSDDG ASLLFLDFGG AEGEIQLDLH 490 500 SCPKTIVFII HSFLSAKVTR LGLLA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The three human syntrophin genes are expressed in diverse tissues, have distinct chromosomal locations, and each bind to dystrophin and its relatives." Ahn A.H., Feener C.A., Gussoni E., Yoshida M., Ozawa E., Kunkel L.M. J. Biol. Chem. 271:2724-2730(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH DMD; DTNA AND UTRN. Tissue: Muscle.
[2]	"Characterization of the dystrophin-syntrophin interaction using the two-hybrid system in yeast." Castello A., Brocheriou V., Chafey P., Kahn A., Gilgenkrantz H. FEBS Lett. 383:124-128(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH DMD. Tissue: Heart.
[3]	"Stress-activated protein kinase-3 interacts with the PDZ domain of alpha1-syntrophin. A mechanism for specific substrate recognition." Hasegawa M., Cuenda A., Spillantini M.G., Thomas G.M., Buee-Scherrer V., Cohen P., Goedert M. J. Biol. Chem. 274:12626-12631(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH MAPK12.
[4]	"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]. Tissue: Small intestine.
[5]	"The DNA sequence and comparative analysis of human chromosome 20." Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J. Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	Mural R.J., Istrail S., Sutton G.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].
[7]	"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]. Tissue: Liver.
[8]	"A role for a PDZ protein in the early secretory pathway for the targeting of proTGF-alpha to the cell surface." Fernandez-Larrea J., Merlos-Suarez A., Urena J.M., Baselga J., Arribas J. Mol. Cell 3:423-433(1999) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TGFA.
[9]	"The C-terminus of human glutaminase L mediates association with PDZ domain-containing proteins." Olalla L., Aledo J.C., Bannenberg G., Marquez J. FEBS Lett. 488:116-122(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH GA.
[10]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-189 AND SER-193, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[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 SER-189 AND SER-193, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[12]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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 SER-189, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[14]	"alpha-1-syntrophin mutation and the long-QT syndrome: a disease of sodium channel disruption." Wu G., Ai T., Kim J.J., Mohapatra B., Xi Y., Li Z., Abbasi S., Purevjav E., Samani K., Ackerman M.J., Qi M., Moss A.J., Shimizu W., Towbin J.A., Cheng J., Vatta M. Circ. Arrhythm. Electrophysiol. 1:193-201(2008) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT LQT12 GLY-257, CHARACTERIZATION OF VARIANT LQT12 GLY-257.
[15]	"Syntrophin mutation associated with long QT syndrome through activation of the nNOS-SCN5A macromolecular complex." Ueda K., Valdivia C., Medeiros-Domingo A., Tester D.J., Vatta M., Farrugia G., Ackerman M.J., Makielski J.C. Proc. Natl. Acad. Sci. U.S.A. 105:9355-9360(2008) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT LQT12 VAL-390, CHARACTERIZATION OF VARIANT LQT12 VAL-390.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U40571 mRNA. Translation: AAC50448.1. S81737 mRNA. Translation: AAB36398.1. AL355392 Genomic DNA. Translation: CAC15884.1. AK291994 mRNA. Translation: BAF84683.1. CH471077 Genomic DNA. Translation: EAW76316.1. CH471077 Genomic DNA. Translation: EAW76317.1. BC026215 mRNA. Translation: AAH26215.1.
CCDS	CCDS13220.1.
PIR	S62894.
RefSeq	NP_003089.1. NM_003098.2.
UniGene	Hs.31121.
3D structure databases
ProteinModelPortal	Q13424.
SMR	Q13424. Positions 2-270.
ModBase	Search...
MobiDB	Search...
Protein-protein interaction databases
BioGrid	112523. 78 interactions.
DIP	DIP-966N.
IntAct	Q13424. 5 interactions.
MINT	MINT-90249.
STRING	9606.ENSP00000217381.
PTM databases
PhosphoSite	Q13424.
Polymorphism databases
DMDM	23822157.
Proteomic databases
MaxQB	Q13424.
PaxDb	Q13424.
PRIDE	Q13424.
Protocols and materials databases
DNASU	6640.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000217381; ENSP00000217381; ENSG00000101400.
GeneID	6640.
KEGG	hsa:6640.
UCSC	uc002wzd.1. human.
Organism-specific databases
CTD	6640.
GeneCards	GC20M031995.
GeneReviews	SNTA1.
HGNC	HGNC:11167. SNTA1.
HPA	CAB037059.
MIM	601017. gene. 612955. phenotype.
neXtProt	NX_Q13424.
Orphanet	101016. Romano-Ward syndrome.
PharmGKB	PA36007.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG318350.
HOGENOM	HOG000231596.
HOVERGEN	HBG054204.
InParanoid	Q13424.
OMA	TGTRHGV.
OrthoDB	EOG7R56VZ.
PhylomeDB	Q13424.
TreeFam	TF317932.
Gene expression databases
ArrayExpress	Q13424.
Bgee	Q13424.
CleanEx	HS_SNTA1.
Genevestigator	Q13424.
Family and domain databases
Gene3D	2.30.42.10. 1 hit.
InterPro	IPR001478. PDZ. IPR001849. Pleckstrin_homology. IPR028552. SNTA1. IPR015482. Syntrophin. [Graphical view]
PANTHER	PTHR10554. PTHR10554. 1 hit. PTHR10554:SF6. PTHR10554:SF6. 1 hit.
Pfam	PF00595. PDZ. 1 hit. [Graphical view]
SMART	SM00228. PDZ. 1 hit. SM00233. PH. 2 hits. [Graphical view]
SUPFAM	SSF50156. SSF50156. 1 hit.
PROSITE	PS50106. PDZ. 1 hit. PS50003. PH_DOMAIN. 2 hits. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	SNTA1. human.
GeneWiki	Syntrophin,_alpha_1.
GenomeRNAi	6640.
NextBio	25873.
PRO	Q13424.
SOURCE	Search...

Entry information

Entry name

SNTA1_HUMAN

Accession

Primary (citable) accession number: Q13424
Secondary accession number(s): A8K7H9, E1P5N1, Q16438

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 10, 2002
Last sequence update:	November 1, 1996
Last modified:	July 9, 2014
This is version 135 of the entry and version 1 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.