P25774 (CATS_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cathepsin S
EC=3.4.22.27

Gene names

Name:

CTSS

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	331 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Thiol protease. Key protease responsible for the removal of the invariant chain from MHC class II molecules. The bond-specificity of this proteinase is in part similar to the specificities of cathepsin L and cathepsin N.
Catalytic activity	Similar to cathepsin L, but with much less activity on Z-Phe-Arg-|-NHMec, and more activity on the Z-Val-Val-Arg-|-Xaa compound.
Subunit structure	Monomer.
Subcellular location	Lysosome.
Sequence similarities	Belongs to the peptidase C1 family.

Ontologies

Keywords
Cellular component	Lysosome
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Signal
Molecular function	Hydrolase Protease Thiol protease
PTM	Disulfide bond Glycoprotein Zymogen
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	adaptive immune response Inferred from expression pattern PubMed 15196205. Source: UniProtKB antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-independent Traceable author statement. Source: Reactome antigen processing and presentation of exogenous peptide antigen via MHC class II Traceable author statement. Source: Reactome cellular response to thyroid hormone stimulus Inferred from expression pattern PubMed 21217776. Source: UniProtKB innate immune response Traceable author statement. Source: Reactome proteolysis Traceable author statement Ref.1. Source: ProtInc toll-like receptor signaling pathway Traceable author statement. Source: Reactome
Cellular_component	endolysosome lumen Traceable author statement. Source: Reactome extracellular region Non-traceable author statement PubMed 14718574. Source: UniProtKB membrane Inferred from electronic annotation. Source: Compara
Molecular_function	cysteine-type endopeptidase activity Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Alternative products

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

Isoform 1 (identifier: P25774-1)

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: P25774-2)

The sequence of this isoform differs from the canonical sequence as follows:
     84-133: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 16

16

Potential

Propeptide

17 – 114

98

Activation peptide

PRO_0000026313

Chain

115 – 331

217

Cathepsin S

PRO_0000026314

Sites

Active site

139

1

By similarity

Active site

278

1

By similarity

Active site

298

1

By similarity

Amino acid modifications

Glycosylation

104

1

N-linked (GlcNAc...) Potential

Disulfide bond

126 ↔ 224

Ref.13

Disulfide bond

136 ↔ 180

Ref.13

Disulfide bond

170 ↔ 213

Ref.13

Disulfide bond

272 ↔ 320

Ref.13

Natural variations

Alternative sequence

84 – 133

50

Missing in isoform 2.

VSP_042712

Natural variant

113

1

R → W. Ref.5 Ref.6 Ref.9
Corresponds to variant rs2230061 [ dbSNP | Ensembl ].

VAR_025385

Natural variant

161

1

S → T. Ref.1 Ref.4
Corresponds to variant rs1059604 [ dbSNP | Ensembl ].

VAR_025386

Experimental info

Sequence conflict

92

1

M → T Ref.1

Sequence conflict

92

1

M → T Ref.4

Secondary structure

1

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331

Helix Strand Turn

Details...

Helix

22 – 24

3

Helix

25 – 35

11

Helix

44 – 67

24

Beta strand

72 – 75

4

Helix

79 – 82

4

Helix

85 – 91

7

Helix

100 – 102

3

Helix

121 – 124

4

Beta strand

135 – 137

3

Helix

139 – 156

18

Helix

164 – 170

7

Helix

173 – 175

3

Helix

179 – 181

3

Helix

185 – 195

11

Beta strand

198 – 200

3

Turn

201 – 203

3

Helix

217 – 219

3

Beta strand

220 – 222

3

Beta strand

226 – 229

4

Helix

235 – 244

10

Beta strand

248 – 252

5

Helix

257 – 261

5

Beta strand

264 – 267

4

Beta strand

278 – 288

11

Beta strand

291 – 297

7

Turn

301 – 303

3

Beta strand

309 – 313

5

Beta strand

315 – 318

4

Helix

319 – 321

3

Turn

322 – 324

3

Beta strand

327 – 330

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified February 21, 2006. Version 3. Checksum: 86093619DB6F0269	FASTA	331	37,496
	10 20 30 40 50 60 MKRLVCVLLV CSSAVAQLHK DPTLDHHWHL WKKTYGKQYK EKNEEAVRRL IWEKNLKFVM 70 80 90 100 110 120 LHNLEHSMGM HSYDLGMNHL GDMTSEEVMS LMSSLRVPSQ WQRNITYKSN PNRILPDSVD 130 140 150 160 170 180 WREKGCVTEV KYQGSCGACW AFSAVGALEA QLKLKTGKLV SLSAQNLVDC STEKYGNKGC 190 200 210 220 230 240 NGGFMTTAFQ YIIDNKGIDS DASYPYKAMD QKCQYDSKYR AATCSKYTEL PYGREDVLKE 250 260 270 280 290 300 AVANKGPVSV GVDARHPSFF LYRSGVYYEP SCTQNVNHGV LVVGYGDLNG KEYWLVKNSW 310 320 330 GHNFGEEGYI RMARNKGNHC GIASFPSYPE I
	Isoform 2 [UniParc]. Checksum: C0445894FAD89713	FASTA	281	31,626
	10 20 30 40 50 60 MKRLVCVLLV CSSAVAQLHK DPTLDHHWHL WKKTYGKQYK EKNEEAVRRL IWEKNLKFVM 70 80 90 100 110 120 LHNLEHSMGM HSYDLGMNHL GDMGSCGACW AFSAVGALEA QLKLKTGKLV SLSAQNLVDC 130 140 150 160 170 180 STEKYGNKGC NGGFMTTAFQ YIIDNKGIDS DASYPYKAMD QKCQYDSKYR AATCSKYTEL 190 200 210 220 230 240 PYGREDVLKE AVANKGPVSV GVDARHPSFF LYRSGVYYEP SCTQNVNHGV LVVGYGDLNG 250 260 270 280 KEYWLVKNSW GHNFGEEGYI RMARNKGNHC GIASFPSYPE I

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and expression of human alveolar macrophage cathepsin S, an elastinolytic cysteine protease." Shi G.-P., Munger J.S., Meara J.P., Rich D.H., Chapman H.A. J. Biol. Chem. 267:7258-7262(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT THR-161. Tissue: Alveolar macrophage.
[2]	"Phylogenetic conservation of cysteine proteinases. Cloning and expression of a cDNA coding for human cathepsin S." Wiederanders B., Broemme D., Kirschke H., von Figura K., Schmidt B., Peters C. J. Biol. Chem. 267:13708-13713(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Testis.
[3]	Wiederanders B., Broemme D., Kirschke H., von Figura K., Schmidt B., Peters C. Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION TO 211.
[4]	"Human cathepsin S: chromosomal localization, gene structure, and tissue distribution." Shi G.-P., Webb A.C., Foster K.E., Knoll J.H.M., Lemere C.A., Munger J.S., Chapman H.A. J. Biol. Chem. 269:11530-11536(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT THR-161.
[5]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT TRP-113.
[6]	"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 AND 2), VARIANT TRP-113. Tissue: Placenta and Synovium.
[7]	"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].
[8]	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].
[9]	"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), VARIANT TRP-113. Tissue: Pancreas.
[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]	"Three-dimensional structures of the cysteine proteases cathepsins K and S deduced by knowledge-based modelling and active site characteristics." Fengler A., Brandt W. Protein Eng. 11:1007-1013(1998) [PubMed] [Europe PMC] [Abstract] Cited for: 3D-STRUCTURE MODELING OF 115-331.
[12]	"Structure of a Cys25-->Ser mutant of human cathepsin S." Turkenburg J.P., Lamers M.B., Brzozowski A.M., Wright L.M., Hubbard R.E., Sturt S.L., Williams D.H. Acta Crystallogr. D 58:451-455(2002) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 115-331.
[13]	"Characterization and optimization of selective, nonpeptidic inhibitors of cathepsin S with an unprecedented binding mode." Inagaki H., Tsuruoka H., Hornsby M., Lesley S.A., Spraggon G., Ellman J.A. J. Med. Chem. 50:2693-2699(2007) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 112-331 IN COMPLEX WITH INHIBITOR, DISULFIDE BONDS.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

S93414 mRNA. Translation: AAB22005.1.
M86553 mRNA. Translation: AAA35655.1.
M90696 mRNA. Translation: AAC37592.1.
U07374 , U07370, U07371, U07372, U07373 Genomic DNA. Translation: AAB60643.2.
CR541676 mRNA. Translation: CAG46477.1.
AK301472 mRNA. Translation: BAG62991.1.
AK314482 mRNA. Translation: BAG37086.1.
AL356292 Genomic DNA. Translation: CAI13657.1.
CH471121 Genomic DNA. Translation: EAW53518.1.
CH471121 Genomic DNA. Translation: EAW53519.1.
BC002642 mRNA. Translation: AAH02642.1.

IPI

IPI00299150.
IPI00910216.

PIR

A42482.

RefSeq

NP_001186668.1. NM_001199739.1.
NP_004070.3. NM_004079.4.

UniGene

Hs.181301.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BXF	model	-	A	115-331	[»]
1GLO	X-ray	2.20	A	115-331	[»]
1MS6	X-ray	1.90	A	115-331	[»]
1NPZ	X-ray	2.00	A/B	115-331	[»]
1NQC	X-ray	1.80	A	115-331	[»]
2C0Y	X-ray	2.10	A	17-331	[»]
2F1G	X-ray	1.90	A/B	112-331	[»]
2FQ9	X-ray	1.65	A/B	114-331	[»]
2FRA	X-ray	1.90	A/B	114-330	[»]
2FRQ	X-ray	1.60	A/B	115-331	[»]
2FT2	X-ray	1.70	A/B	114-331	[»]
2FUD	X-ray	1.95	A/B	115-331	[»]
2FYE	X-ray	2.20	A	115-331	[»]
2G6D	X-ray	2.50	A	115-331	[»]
2G7Y	X-ray	2.00	A/B	114-330	[»]
2H7J	X-ray	1.50	A/B	112-331	[»]
2HH5	X-ray	1.80	A/B	112-331	[»]
2HHN	X-ray	1.55	A/B	112-331	[»]
2HXZ	X-ray	1.90	A/B/C	112-331	[»]
2OP3	X-ray	1.60	A/B	112-331	[»]
2R9M	X-ray	1.97	A/B	115-331	[»]
2R9N	X-ray	2.00	A/B	115-331	[»]
2R9O	X-ray	2.00	A/B	115-331	[»]
3IEJ	X-ray	2.18	A/B	115-331	[»]
3KWN	X-ray	2.10	A/B	115-331	[»]
3MPE	X-ray	2.25	A/B	114-331	[»]
3MPF	X-ray	1.80	A/B	115-331	[»]
3N3G	X-ray	1.60	A/B	115-331	[»]
3N4C	X-ray	1.90	A/B	115-331	[»]
3OVX	X-ray	1.49	A/B	114-331	[»]

ProteinModelPortal

P25774.

ModBase

Search...

Protein-protein interaction databases

IntAct

P25774. 2 interactions.

STRING

9606.ENSP00000357981.

Protein family/group databases

MEROPS

I29.004.

PTM databases

PhosphoSite

P25774.

Polymorphism databases

DMDM

88984046.

Proteomic databases

PaxDb

P25774.

PeptideAtlas

P25774.

PRIDE

P25774.

Protocols and materials databases

DNASU

1520.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000368985; ENSP00000357981; ENSG00000163131.
ENST00000448301; ENSP00000408414; ENSG00000163131.

GeneID

1520.

KEGG

hsa:1520.

UCSC

uc001evn.3. human.
uc010pcj.2. human.

Organism-specific databases

CTD

1520.

GeneCards

GC01M150702.

HGNC

HGNC:2545. CTSS.

HPA

CAB000460.
HPA002988.

MIM

116845. gene.

neXtProt

NX_P25774.

PharmGKB

PA27041.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG4870.

HOGENOM

HOG000230774.

HOVERGEN

HBG011513.

InParanoid

P25774.

KO

K01368.

OMA

KAMDQKC.

OrthoDB

EOG4JM7Q2.

PhylomeDB

P25774.

Enzyme and pathway databases

BRENDA

3.4.22.27. 2681.

Reactome

REACT_118779. Extracellular matrix organization.
REACT_6900. Immune System.

Gene expression databases

Bgee

P25774.

CleanEx

HS_CTSS.

Genevestigator

P25774.

GermOnline

ENSG00000163131. Homo sapiens.

Family and domain databases

InterPro

IPR025661. Pept_asp_AS.
IPR000169. Pept_cys_AS.
IPR025660. Pept_his_AS.
IPR013128. Peptidase_C1A.
IPR000668. Peptidase_C1A_C.
IPR013201. Prot_inhib_I29.
[Graphical view]

PANTHER

PTHR12411. PTHR12411. 1 hit.

Pfam

PF08246. Inhibitor_I29. 1 hit.
PF00112. Peptidase_C1. 1 hit.
[Graphical view]

PRINTS

PR00705. PAPAIN.

SMART

SM00848. Inhibitor_I29. 1 hit.
SM00645. Pept_C1. 1 hit.
[Graphical view]

PROSITE

PS00640. THIOL_PROTEASE_ASN. 1 hit.
PS00139. THIOL_PROTEASE_CYS. 1 hit.
PS00639. THIOL_PROTEASE_HIS. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P25774.

ChEMBL

CHEMBL2954.

ChiTaRS

CTSS. human.

EvolutionaryTrace

P25774.

GenomeRNAi

1520.

NextBio

6291.

PMAP-CutDB

P25774.

SOURCE

Search...

Entry information

Entry name

CATS_HUMAN

Accession

Primary (citable) accession number: P25774
Secondary accession number(s): B4DWC9 , D3DV05, Q5T5I0, Q6FHS5, Q9BUG3

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1992
Last sequence update:	February 21, 2006
Last modified:	May 29, 2013
This is version 142 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.