HUMAN:TNNT2

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	TNNT2
Protein Name(s)	Troponin T, cardiac muscle TnTc Cardiac muscle troponin T cTnT
External Links
UniProt	P45379
EMBL	S64668 X74819 L40162 X79855 X79856 X79857 X79858 AF004422 AF004409 AF004410 AF004411 AF004412 AF004413 AF004414 AF004415 AF004416 AF004417 AF004418 AF004419 AF004420 AF004421 AY044273 AK290621 EF179183 AC119427 BC002653 Y09626 Y09627 Y09628 S71126 S71127 S71128
CCDS	CCDS30968.1 CCDS30969.1 CCDS60390.1 CCDS73003.1
PIR	A54671
RefSeq	NP_000355.2 NP_001001430.1 NP_001001431.1 NP_001001432.1 NP_001263274.1 NP_001263275.1 NP_001263276.1 XP_006711571.1 XP_006711575.1 XP_006711576.1
UniGene	Hs.533613
PDB	1J1D 1J1E
PDBsum	1J1D 1J1E
ProteinModelPortal	P45379
SMR	P45379
BioGrid	112993
IntAct	P45379
MINT	MINT-3015968
STRING	9606.ENSP00000350511
ChEMBL	CHEMBL2095202
PhosphoSite	P45379
DMDM	21264536
UCD-2DPAGE	P45379
PaxDb	P45379
PRIDE	P45379
DNASU	7139
Ensembl	ENST00000236918 ENST00000360372 ENST00000367318 ENST00000367320 ENST00000367322 ENST00000509001
GeneID	7139
KEGG	hsa:7139
UCSC	uc001gwf.4 uc001gwg.4 uc001gwi.4 uc009wzt.2
CTD	7139
GeneCards	GC01M201328
GeneReviews	TNNT2
HGNC	HGNC:11949
HPA	CAB015371 HPA015774 HPA017888
MIM	115195 191045 601494 612422
neXtProt	NX_P45379
Orphanet	154 155 75249 54260
PharmGKB	PA36638
eggNOG	NOG299534
GeneTree	ENSGT00390000013611
HOGENOM	HOG000231049
HOVERGEN	HBG052790
InParanoid	P45379
KO	K12045
OrthoDB	EOG7W155J
PhylomeDB	P45379
TreeFam	TF313321
Reactome	REACT_16969
ChiTaRS	TNNT2
EvolutionaryTrace	P45379
GeneWiki	TNNT2
GenomeRNAi	7139
NextBio	27933
PRO	PR:P45379
Proteomes	UP000005640
Bgee	P45379
CleanEx	HS_TNNT2
ExpressionAtlas	P45379
Genevestigator	P45379
GO	GO:0005829 GO:0030017 GO:0005865 GO:0005861 GO:0003779 GO:0005523 GO:0030172 GO:0031013 GO:0006200 GO:0030049 GO:0032780 GO:0032781 GO:0008016 GO:0006937 GO:0051592 GO:0055010
InterPro	IPR027707 IPR001978
PANTHER	PTHR11521
Pfam	PF00992

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Notes	Status
	GO:0005861	troponin complex	PMID:7898523^[1]	ECO:0000315			C	Figure 3 shows compared with patients with β cardiac myosin heavy-chain mutations, patients with cardiac troponin T mutations had a higher incidence of death before the age of 30 years. Table 3 shows each cardiac troponin T mutation produced an increase in the maximal thickness of the left ventricular wall.	complete CACAO 3839
	GO:0031014	troponin T binding	PMID:25646632^[2]	ECO:0000314			F	high sensitivity for emergency situations	complete CACAO 10658
involved_in	GO:0060048	cardiac muscle contraction	PMID:25771144^[3]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0097512	cardiac myofibril	PMID:25771144^[3]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:1990584	cardiac Troponin complex	PMID:25771144^[3]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:0055010	ventricular cardiac muscle tissue morphogenesis	PMID:16754800^[4]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0051592	response to calcium ion	PMID:8205619^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0032781	positive regulation of ATPase activity	PMID:10850966^[6]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0032781	positive regulation of ATPase activity	PMID:12186860^[7]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0032780	negative regulation of ATPase activity	PMID:10850966^[6]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0031013	troponin I binding	PMID:15542288^[8]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P19429	F	Seeded From UniProt	complete
enables	GO:0030172	troponin C binding	PMID:15542288^[8]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P63316	F	Seeded From UniProt	complete
enables	GO:0030172	troponin C binding	PMID:8205619^[5]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P63316	F	Seeded From UniProt	complete
involved_in	GO:0030049	muscle filament sliding	PMID:15923195^[9]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0030049	muscle filament sliding	PMID:12186860^[7]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0008016	regulation of heart contraction	PMID:15542288^[8]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0005865	striated muscle thin filament	PMID:12186860^[7]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005861	troponin complex	PMID:12186860^[7]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0005523	tropomyosin binding	PMID:10850966^[6]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0003779	actin binding	PMID:8205619^[5]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0060048	cardiac muscle contraction	PMID:21873635^[10]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000162487 RGD:3882 UniProtKB:P45379	P	Seeded From UniProt	complete
involved_in	GO:0045214	sarcomere organization	PMID:21873635^[10]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0004169 MGI:MGI:104597 PANTHER:PTN000162487 WB:WBGene00003495 ZFIN:ZDB-GENE-030520-1	P	Seeded From UniProt	complete
enables	GO:0031013	troponin I binding	PMID:21873635^[10]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000162544 RGD:3882 UniProtKB:P45379	F	Seeded From UniProt	complete
contributes_to	GO:0030899	calcium-dependent ATPase activity	PMID:21873635^[10]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000162487 UniProtKB:P45378	F	Seeded From UniProt	complete
enables	GO:0030172	troponin C binding	PMID:21873635^[10]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000162544 UniProtKB:P45379	F	Seeded From UniProt	complete
involved_in	GO:0006936	muscle contraction	PMID:21873635^[10]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:104597 PANTHER:PTN000162487 RGD:3882 WB:WBGene00006589	P	Seeded From UniProt	complete
part_of	GO:0005861	troponin complex	PMID:21873635^[10]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:104597 PANTHER:PTN000162487 RGD:3882 RGD:3883 RGD:621852 UniProtKB:P13805 UniProtKB:P45378 UniProtKB:P45379	C	Seeded From UniProt	complete
contributes_to	GO:0005523	tropomyosin binding	PMID:21873635^[10]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000162487 UniProtKB:P13805 UniProtKB:P45378 UniProtKB:P45379	F	Seeded From UniProt	complete
enables	GO:0005509	calcium ion binding	PMID:21873635^[10]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0004169 PANTHER:PTN000162487	F	Seeded From UniProt	complete
involved_in	GO:0003009	skeletal muscle contraction	PMID:21873635^[10]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000162487 UniProtKB:P13805 UniProtKB:P45378	P	Seeded From UniProt	complete
involved_in	GO:0060048	cardiac muscle contraction	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P50753 ensembl:ENSRNOP00000069434	P	Seeded From UniProt	complete
involved_in	GO:0051764	actin crosslink formation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P50753 ensembl:ENSRNOP00000069434	P	Seeded From UniProt	complete
involved_in	GO:0051291	protein heterooligomerization	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P50753 ensembl:ENSRNOP00000069434	P	Seeded From UniProt	complete
involved_in	GO:0032972	regulation of muscle filament sliding speed	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P50753 ensembl:ENSRNOP00000069434	P	Seeded From UniProt	complete
enables	GO:0031013	troponin I binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P50753 ensembl:ENSRNOP00000069434	F	Seeded From UniProt	complete
enables	GO:0030674	protein binding, bridging	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P50753 ensembl:ENSRNOP00000069434	F	Seeded From UniProt	complete
part_of	GO:0030016	myofibril	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P50753 ensembl:ENSRNOP00000069434	C	Seeded From UniProt	complete
involved_in	GO:0006937	regulation of muscle contraction	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P50753 ensembl:ENSRNOP00000069434	P	Seeded From UniProt	complete
involved_in	GO:0006936	muscle contraction	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P50753 ensembl:ENSRNOP00000069434	P	Seeded From UniProt	complete
part_of	GO:0005861	troponin complex	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P50753 ensembl:ENSRNOP00000069434	C	Seeded From UniProt	complete
part_of	GO:0005861	troponin complex	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001978 InterPro:IPR027707	C	Seeded From UniProt	complete
involved_in	GO:0006937	regulation of muscle contraction	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR027707	P	Seeded From UniProt	complete
involved_in	GO:0051592	response to calcium ion	PMID:2530435^[11]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0032780	negative regulation of ATPase activity	PMID:12093807^[12]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
contributes_to	GO:0016887	ATPase activity	PMID:2530435^[11]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
contributes_to	GO:0016887	ATPase activity	PMID:12093807^[12]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
part_of	GO:0005861	troponin complex	PMID:2530435^[11]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005861	troponin complex	PMID:12093807^[12]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:0051592	response to calcium ion	PMID:2530435^[11]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0032780	negative regulation of ATPase activity	PMID:12093807^[12]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
contributes_to	GO:0016887	ATPase activity	PMID:2530435^[11]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
contributes_to	GO:0016887	ATPase activity	PMID:12093807^[12]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
part_of	GO:0005861	troponin complex	PMID:2530435^[11]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005861	troponin complex	PMID:12093807^[12]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:0051592	response to calcium ion	PMID:2530435^[11]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0032780	negative regulation of ATPase activity	PMID:12093807^[12]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
contributes_to	GO:0016887	ATPase activity	PMID:2530435^[11]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
contributes_to	GO:0016887	ATPase activity	PMID:12093807^[12]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
part_of	GO:0005861	troponin complex	PMID:2530435^[11]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005861	troponin complex	PMID:12093807^[12]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:0051592	response to calcium ion	PMID:2530435^[11]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0032780	negative regulation of ATPase activity	PMID:12093807^[12]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
contributes_to	GO:0016887	ATPase activity	PMID:2530435^[11]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
contributes_to	GO:0016887	ATPase activity	PMID:12093807^[12]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
part_of	GO:0005861	troponin complex	PMID:2530435^[11]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005861	troponin complex	PMID:12093807^[12]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0030017	sarcomere	PMID:16754800^[4]	ECO:0000304	author statement supported by traceable reference used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:0030049	muscle filament sliding	Reactome:R-HSA-390522	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0005829	cytosol	Reactome:R-HSA-390598 Reactome:R-HSA-390597 Reactome:R-HSA-390595 Reactome:R-HSA-390593	ECO:0000304	author statement supported by traceable reference used in manual assertion		C	Seeded From UniProt	complete
edit table

Notes

References

See Help:References for how to manage references in GONUTS.

↑ Watkins, H et al. (1995) Mutations in the genes for cardiac troponin T and alpha-tropomyosin in hypertrophic cardiomyopathy. N. Engl. J. Med. 332 1058-64 PubMed GONUTS page
↑ Zhelev, Z et al. (2015) Diagnostic accuracy of single baseline measurement of Elecsys Troponin T high-sensitive assay for diagnosis of acute myocardial infarction in emergency department: systematic review and meta-analysis. BMJ 350 h15 PubMed GONUTS page
↑ ^3.0 ^3.1 ^3.2 Wijnker, PJ et al. (2015) A novel phosphorylation site, Serine 199, in the C-terminus of cardiac troponin I regulates calcium sensitivity and susceptibility to calpain-induced proteolysis. J. Mol. Cell. Cardiol. 82 93-103 PubMed GONUTS page
↑ ^4.0 ^4.1 Morita, H et al. (2006) Single-gene mutations and increased left ventricular wall thickness in the community: the Framingham Heart Study. Circulation 113 2697-705 PubMed GONUTS page
↑ ^5.0 ^5.1 ^5.2 Thierfelder, L et al. (1994) Alpha-tropomyosin and cardiac troponin T mutations cause familial hypertrophic cardiomyopathy: a disease of the sarcomere. Cell 77 701-12 PubMed GONUTS page
↑ ^6.0 ^6.1 ^6.2 Redwood, C et al. (2000) Investigation of a truncated cardiac troponin T that causes familial hypertrophic cardiomyopathy: Ca(2+) regulatory properties of reconstituted thin filaments depend on the ratio of mutant to wild-type protein. Circ. Res. 86 1146-52 PubMed GONUTS page
↑ ^7.0 ^7.1 ^7.2 ^7.3 Robinson, P et al. (2002) Alterations in thin filament regulation induced by a human cardiac troponin T mutant that causes dilated cardiomyopathy are distinct from those induced by troponin T mutants that cause hypertrophic cardiomyopathy. J. Biol. Chem. 277 40710-6 PubMed GONUTS page
↑ ^8.0 ^8.1 ^8.2 Mogensen, J et al. (2004) Severe disease expression of cardiac troponin C and T mutations in patients with idiopathic dilated cardiomyopathy. J. Am. Coll. Cardiol. 44 2033-40 PubMed GONUTS page
↑ Mirza, M et al. (2005) Dilated cardiomyopathy mutations in three thin filament regulatory proteins result in a common functional phenotype. J. Biol. Chem. 280 28498-506 PubMed GONUTS page
↑ ^10.0 ^10.1 ^10.2 ^10.3 ^10.4 ^10.5 ^10.6 ^10.7 ^10.8 ^10.9 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ ^11.00 ^11.01 ^11.02 ^11.03 ^11.04 ^11.05 ^11.06 ^11.07 ^11.08 ^11.09 ^11.10 ^11.11 Solaro, RJ et al. (1989) Ca2+, pH and the regulation of cardiac myofilament force and ATPase activity. Mol. Cell. Biochem. 89 163-7 PubMed GONUTS page
↑ ^12.00 ^12.01 ^12.02 ^12.03 ^12.04 ^12.05 ^12.06 ^12.07 ^12.08 ^12.09 ^12.10 ^12.11 Gomes, AV et al. (2002) Cardiac troponin T isoforms affect the Ca2+ sensitivity and inhibition of force development. Insights into the role of troponin T isoforms in the heart. J. Biol. Chem. 277 35341-9 PubMed GONUTS page

[PMID:7898523-1] Watkins, H et al. (1995) Mutations in the genes for cardiac troponin T and alpha-tropomyosin in hypertrophic cardiomyopathy. N. Engl. J. Med. 332 1058-64 PubMed GONUTS page

[PMID:25646632-2] Zhelev, Z et al. (2015) Diagnostic accuracy of single baseline measurement of Elecsys Troponin T high-sensitive assay for diagnosis of acute myocardial infarction in emergency department: systematic review and meta-analysis. BMJ 350 h15 PubMed GONUTS page

[PMID:25771144-3] 3.0 ^3.1 ^3.2 Wijnker, PJ et al. (2015) A novel phosphorylation site, Serine 199, in the C-terminus of cardiac troponin I regulates calcium sensitivity and susceptibility to calpain-induced proteolysis. J. Mol. Cell. Cardiol. 82 93-103 PubMed GONUTS page

[PMID:16754800-4] 4.0 ^4.1 Morita, H et al. (2006) Single-gene mutations and increased left ventricular wall thickness in the community: the Framingham Heart Study. Circulation 113 2697-705 PubMed GONUTS page

[PMID:8205619-5] 5.0 ^5.1 ^5.2 Thierfelder, L et al. (1994) Alpha-tropomyosin and cardiac troponin T mutations cause familial hypertrophic cardiomyopathy: a disease of the sarcomere. Cell 77 701-12 PubMed GONUTS page

[PMID:10850966-6] 6.0 ^6.1 ^6.2 Redwood, C et al. (2000) Investigation of a truncated cardiac troponin T that causes familial hypertrophic cardiomyopathy: Ca(2+) regulatory properties of reconstituted thin filaments depend on the ratio of mutant to wild-type protein. Circ. Res. 86 1146-52 PubMed GONUTS page

[PMID:12186860-7] 7.0 ^7.1 ^7.2 ^7.3 Robinson, P et al. (2002) Alterations in thin filament regulation induced by a human cardiac troponin T mutant that causes dilated cardiomyopathy are distinct from those induced by troponin T mutants that cause hypertrophic cardiomyopathy. J. Biol. Chem. 277 40710-6 PubMed GONUTS page

[PMID:15542288-8] 8.0 ^8.1 ^8.2 Mogensen, J et al. (2004) Severe disease expression of cardiac troponin C and T mutations in patients with idiopathic dilated cardiomyopathy. J. Am. Coll. Cardiol. 44 2033-40 PubMed GONUTS page

[PMID:15923195-9] Mirza, M et al. (2005) Dilated cardiomyopathy mutations in three thin filament regulatory proteins result in a common functional phenotype. J. Biol. Chem. 280 28498-506 PubMed GONUTS page

[PMID:21873635-10] 10.0 ^10.1 ^10.2 ^10.3 ^10.4 ^10.5 ^10.6 ^10.7 ^10.8 ^10.9 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

[PMID:2530435-11] 11.00 ^11.01 ^11.02 ^11.03 ^11.04 ^11.05 ^11.06 ^11.07 ^11.08 ^11.09 ^11.10 ^11.11 Solaro, RJ et al. (1989) Ca2+, pH and the regulation of cardiac myofilament force and ATPase activity. Mol. Cell. Biochem. 89 163-7 PubMed GONUTS page

[PMID:12093807-12] 12.00 ^12.01 ^12.02 ^12.03 ^12.04 ^12.05 ^12.06 ^12.07 ^12.08 ^12.09 ^12.10 ^12.11 Gomes, AV et al. (2002) Cardiac troponin T isoforms affect the Ca2+ sensitivity and inhibition of force development. Insights into the role of troponin T isoforms in the heart. J. Biol. Chem. 277 35341-9 PubMed GONUTS page

[1]

[2]

[3]

[4]

[5]

[6]

[7]

[8]

[9]

[10]

[11]

[12]

HUMAN:TNNT2

Contents

Annotations

Notes

References

a

c

e

h

m

n

p

r

s

t

v

Navigation menu

Personal tools

Namespaces

Variants

Views

More

Search

Navigation

Cacao

Links

Tools