SCHPO:RAD32

Species (Taxon ID)	Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast). (284812)
Gene Name(s)	rad32
Protein Name(s)	DNA repair protein rad32
External Links
UniProt	Q09683
EMBL	X82322 CU329670
PIR	S58097
RefSeq	NP_592935.1
PDB	4FBK 4FBQ 4FBW 4FCX
PDBsum	4FBK 4FBQ 4FBW 4FCX
ProteinModelPortal	Q09683
SMR	Q09683
BioGrid	279207
DIP	DIP-52388N
IntAct	Q09683
STRING	4896.SPAC13C5.07.1
MaxQB	Q09683
PaxDb	Q09683
PRIDE	Q09683
EnsemblFungi	SPAC13C5.07.1
GeneID	2542757
KEGG	spo:SPAC13C5.07
EuPathDB	FungiDB:SPAC13C5.07
PomBase	SPAC13C5.07
HOGENOM	HOG000216581
InParanoid	Q09683
KO	K10865
OMA	RMFVNKQ
PhylomeDB	Q09683
Reactome	R-SPO-1834949 R-SPO-2559586 R-SPO-5693548 R-SPO-5693565
PRO	PR:Q09683
Proteomes	UP000002485
GO	GO:0030870 GO:0000784 GO:0035861 GO:1990421 GO:0008408 GO:0008296 GO:0045027 GO:0008311 GO:0030145 GO:0004518 GO:0008310 GO:0000014 GO:0000403 GO:0042769 GO:0000729 GO:0006302 GO:1990918 GO:0000724 GO:0006303 GO:0031573 GO:1990898 GO:0042138 GO:0097552 GO:0007095 GO:0007131 GO:0072422 GO:0000723
Gene3D	3.30.110.110 3.60.21.10
InterPro	IPR004843 IPR029052 IPR003701 IPR007281 IPR038487
Pfam	PF00149 PF04152
PIRSF	PIRSF000882
SMART	SM01347
TIGRFAMs	TIGR00583

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
	GO:0006303	double-strand break repair via nonhomologous end joining	PMID:28292918^[1]	ECO:0000315			P		Mre11, a protein required for double stranded break repair via non homologous end joining, forms a dimer to bridge the gap between the two broken ends of the double-stranded DNA. Figure 6 proves how dimerization of mre11 ( or rad32 in S. pombe) needs to occur for efficient non homologous end joining since the introduced mutations in the Mre11 dimerization domain, but not the nuclease domain, reduce NHEJ. This data is represented by the drastic decrease in PCR products since the bands for PCR products would indicate successful repair by non homologous end-joining. Therefore, mre11 dimerization is essential for NHEJ since there were no excision products from PCR.	complete CACAO 12476
involved_in	GO:1990918	double-strand break repair involved in meiotic recombination	PMID:15238514^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:1990898	meiotic DNA double-strand break clipping	PMID:19911044^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:1990898	meiotic DNA double-strand break clipping	PMID:19752195^[4]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:1990898	meiotic DNA double-strand break clipping	PMID:19139281^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:1990421	subtelomeric heterochromatin	PMID:12196391^[6]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0072422	signal transduction involved in DNA damage checkpoint	PMID:12944482^[7]	ECO:0000305	curator inference used in manual assertion	GO:0030870	P		Seeded From UniProt	complete
enables	GO:0045027	DNA end binding	PMID:18854158^[8]	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:Q8U1N9	F		Seeded From UniProt	complete
involved_in	GO:0042769	DNA damage response, detection of DNA damage	PMID:12944482^[7]	ECO:0000305	curator inference used in manual assertion	GO:0030870	P		Seeded From UniProt	complete
involved_in	GO:0042138	meiotic DNA double-strand break formation	PMID:15654094^[9]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0035861	site of double-strand break	PMID:23080121^[10]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0035861	site of double-strand break	PMID:21931565^[11]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0035861	site of double-strand break	PMID:19804755^[12]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0035861	site of double-strand break	PMID:17936710^[13]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0031573	intra-S DNA damage checkpoint	PMID:12944482^[7]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0030870	Mre11 complex	PMID:22705791^[14]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0030145	manganese ion binding	PMID:22705791^[14]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0008311	double-stranded DNA 3'-5' exodeoxyribonuclease activity	PMID:9651580^[15]	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:P49959	F		Seeded From UniProt	complete
enables	GO:0008310	single-stranded DNA 3'-5' exodeoxyribonuclease activity	PMID:9651580^[15]	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:P49959	F		Seeded From UniProt	complete
involved_in	GO:0007131	reciprocal meiotic recombination	PMID:7885834^[16]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006303	double-strand break repair via nonhomologous end joining	PMID:10373582^[17]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006302	double-strand break repair	PMID:7885834^[16]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0004518	nuclease activity	PMID:22705791^[14]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0000784	nuclear chromosome, telomeric region	PMID:12861005^[18]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0000729	DNA double-strand break processing	PMID:23080121^[10]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0000729	DNA double-strand break processing	PMID:21931565^[11]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	part_of:(GO:0000724)	Seeded From UniProt	complete
involved_in	GO:0000724	double-strand break repair via homologous recombination	PMID:12628934^[19]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0000723	telomere maintenance	PMID:12861005^[18]	ECO:0000316	genetic interaction evidence used in manual assertion	PomBase:SPAC16A10.07c	P		Seeded From UniProt	complete
enables	GO:0000403	Y-form DNA binding	PMID:18854158^[8]	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:Q8U1N9	F		Seeded From UniProt	complete
enables	GO:0000014	single-stranded DNA endodeoxyribonuclease activity	PMID:9651580^[15]	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:P49959	F		Seeded From UniProt	complete
involved_in	GO:0097552	mitochondrial double-strand break repair via homologous recombination	PMID:21873635^[20]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000015644 SGD:S000004837	P		Seeded From UniProt	complete
involved_in	GO:0042138	meiotic DNA double-strand break formation	PMID:21873635^[20]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000015644 PomBase:SPAC13C5.07	P		Seeded From UniProt	complete
involved_in	GO:0031573	intra-S DNA damage checkpoint	PMID:21873635^[20]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:1100512 PANTHER:PTN000015646 PomBase:SPAC13C5.07	P		Seeded From UniProt	complete
enables	GO:0008408	3'-5' exonuclease activity	PMID:21873635^[20]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN002228124 SGD:S000004837 UniProtKB:P49959	F		Seeded From UniProt	complete
enables	GO:0008296	3'-5'-exodeoxyribonuclease activity	PMID:21873635^[20]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN002228124 SGD:S000004837	F		Seeded From UniProt	complete
involved_in	GO:0007095	mitotic G2 DNA damage checkpoint	PMID:21873635^[20]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0020270 MGI:MGI:1100512 PANTHER:PTN000015644	P		Seeded From UniProt	complete
involved_in	GO:0006303	double-strand break repair via nonhomologous end joining	PMID:21873635^[20]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000015644 PomBase:SPAC13C5.07 SGD:S000004837 UniProtKB:P49959	P		Seeded From UniProt	complete
colocalizes_with	GO:0000784	nuclear chromosome, telomeric region	PMID:21873635^[20]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:1100512 PANTHER:PTN000015644 PomBase:SPAC13C5.07 UniProtKB:P49959	C		Seeded From UniProt	complete
involved_in	GO:0000724	double-strand break repair via homologous recombination	PMID:21873635^[20]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000015644 PomBase:SPAC13C5.07 SGD:S000004837 UniProtKB:P49959	P		Seeded From UniProt	complete
involved_in	GO:0000723	telomere maintenance	PMID:21873635^[20]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0020270 PANTHER:PTN000015644 PomBase:SPAC13C5.07 SGD:S000004837 UniProtKB:P49959	P		Seeded From UniProt	complete
enables	GO:0004519	endonuclease activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR003701 InterPro:IPR007281	F		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR007281	C		Seeded From UniProt	complete
involved_in	GO:0006302	double-strand break repair	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR003701 InterPro:IPR007281	P		Seeded From UniProt	complete
enables	GO:0008408	3'-5' exonuclease activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR003701	F		Seeded From UniProt	complete
enables	GO:0016787	hydrolase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR004843	F		Seeded From UniProt	complete
enables	GO:0030145	manganese ion binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR007281	F		Seeded From UniProt	complete
part_of	GO:0030870	Mre11 complex	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR003701	C		Seeded From UniProt	complete
enables	GO:0004518	nuclease activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0540	F		Seeded From UniProt	complete
enables	GO:0004527	exonuclease activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0269	F		Seeded From UniProt	complete
enables	GO:0016787	hydrolase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0378	F		Seeded From UniProt	complete
involved_in	GO:0006281	DNA repair	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0234	P		Seeded From UniProt	complete
involved_in	GO:0006974	cellular response to DNA damage stimulus	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0227	P		Seeded From UniProt	complete
involved_in	GO:0051321	meiotic cell cycle	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0469	P		Seeded From UniProt	complete
enables	GO:0004519	endonuclease activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0255	F		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0539 UniProtKB-SubCell:SL-0191	C		Seeded From UniProt	complete
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Notes

References

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

↑ Li, Y et al. (2017) Non-Homologous End-Joining with Minimal Sequence Loss Is Promoted by the Mre11-Rad50-Nbs1-Ctp1 Complex in Schizosaccharomyces pombe. Genetics PubMed GONUTS page
↑ Young, JA et al. (2004) Conserved and nonconserved proteins for meiotic DNA breakage and repair in yeasts. Genetics 167 593-605 PubMed GONUTS page
↑ Rothenberg, M et al. (2009) Ctp1 and the MRN-complex are required for endonucleolytic Rec12 removal with release of a single class of oligonucleotides in fission yeast. PLoS Genet. 5 e1000722 PubMed GONUTS page
↑ Milman, N et al. (2009) Meiotic DNA double-strand break repair requires two nucleases, MRN and Ctp1, to produce a single size class of Rec12 (Spo11)-oligonucleotide complexes. Mol. Cell. Biol. 29 5998-6005 PubMed GONUTS page
↑ Hartsuiker, E et al. (2009) Ctp1CtIP and Rad32Mre11 nuclease activity are required for Rec12Spo11 removal, but Rec12Spo11 removal is dispensable for other MRN-dependent meiotic functions. Mol. Cell. Biol. 29 1671-81 PubMed GONUTS page
↑ Nakamura, TM et al. (2002) Telomere binding of checkpoint sensor and DNA repair proteins contributes to maintenance of functional fission yeast telomeres. Genetics 161 1437-52 PubMed GONUTS page
↑ ^7.0 ^7.1 ^7.2 Chahwan, C et al. (2003) The fission yeast Rad32 (Mre11)-Rad50-Nbs1 complex is required for the S-phase DNA damage checkpoint. Mol. Cell. Biol. 23 6564-73 PubMed GONUTS page
↑ ^8.0 ^8.1 Williams, RS et al. (2008) Mre11 dimers coordinate DNA end bridging and nuclease processing in double-strand-break repair. Cell 135 97-109 PubMed GONUTS page
↑ Farah, JA et al. (2005) A novel recombination pathway initiated by the Mre11/Rad50/Nbs1 complex eliminates palindromes during meiosis in Schizosaccharomyces pombe. Genetics 169 1261-74 PubMed GONUTS page
↑ ^10.0 ^10.1 Limbo, O et al. (2012) Mre11 ATLD17/18 mutation retains Tel1/ATM activity but blocks DNA double-strand break repair. Nucleic Acids Res. 40 11435-49 PubMed GONUTS page
↑ ^11.0 ^11.1 Langerak, P et al. (2011) Release of Ku and MRN from DNA ends by Mre11 nuclease activity and Ctp1 is required for homologous recombination repair of double-strand breaks. PLoS Genet. 7 e1002271 PubMed GONUTS page
↑ Williams, RS et al. (2009) Nbs1 flexibly tethers Ctp1 and Mre11-Rad50 to coordinate DNA double-strand break processing and repair. Cell 139 87-99 PubMed GONUTS page
↑ Limbo, O et al. (2007) Ctp1 is a cell-cycle-regulated protein that functions with Mre11 complex to control double-strand break repair by homologous recombination. Mol. Cell 28 134-46 PubMed GONUTS page
↑ ^14.0 ^14.1 ^14.2 Schiller, CB et al. (2012) Structure of Mre11-Nbs1 complex yields insights into ataxia-telangiectasia-like disease mutations and DNA damage signaling. Nat. Struct. Mol. Biol. 19 693-700 PubMed GONUTS page
↑ ^15.0 ^15.1 ^15.2 Paull, TT & Gellert, M (1998) The 3' to 5' exonuclease activity of Mre 11 facilitates repair of DNA double-strand breaks. Mol. Cell 1 969-79 PubMed GONUTS page
↑ ^16.0 ^16.1 Tavassoli, M et al. (1995) Cloning and characterisation of the Schizosaccharomyces pombe rad32 gene: a gene required for repair of double strand breaks and recombination. Nucleic Acids Res. 23 383-8 PubMed GONUTS page
↑ Wilson, S et al. (1999) The role of Schizosaccharomyces pombe Rad32, the Mre11 homologue, and other DNA damage response proteins in non-homologous end joining and telomere length maintenance. Nucleic Acids Res. 27 2655-61 PubMed GONUTS page
↑ ^18.0 ^18.1 Tomita, K et al. (2003) Competition between the Rad50 complex and the Ku heterodimer reveals a role for Exo1 in processing double-strand breaks but not telomeres. Mol. Cell. Biol. 23 5186-97 PubMed GONUTS page
↑ Prudden, J et al. (2003) Pathway utilization in response to a site-specific DNA double-strand break in fission yeast. EMBO J. 22 1419-30 PubMed GONUTS page
↑ ^20.0 ^20.1 ^20.2 ^20.3 ^20.4 ^20.5 ^20.6 ^20.7 ^20.8 ^20.9 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:28292918-1] Li, Y et al. (2017) Non-Homologous End-Joining with Minimal Sequence Loss Is Promoted by the Mre11-Rad50-Nbs1-Ctp1 Complex in Schizosaccharomyces pombe. Genetics PubMed GONUTS page

[PMID:15238514-2] Young, JA et al. (2004) Conserved and nonconserved proteins for meiotic DNA breakage and repair in yeasts. Genetics 167 593-605 PubMed GONUTS page

[PMID:19911044-3] Rothenberg, M et al. (2009) Ctp1 and the MRN-complex are required for endonucleolytic Rec12 removal with release of a single class of oligonucleotides in fission yeast. PLoS Genet. 5 e1000722 PubMed GONUTS page

[PMID:19752195-4] Milman, N et al. (2009) Meiotic DNA double-strand break repair requires two nucleases, MRN and Ctp1, to produce a single size class of Rec12 (Spo11)-oligonucleotide complexes. Mol. Cell. Biol. 29 5998-6005 PubMed GONUTS page

[PMID:19139281-5] Hartsuiker, E et al. (2009) Ctp1CtIP and Rad32Mre11 nuclease activity are required for Rec12Spo11 removal, but Rec12Spo11 removal is dispensable for other MRN-dependent meiotic functions. Mol. Cell. Biol. 29 1671-81 PubMed GONUTS page

[PMID:12196391-6] Nakamura, TM et al. (2002) Telomere binding of checkpoint sensor and DNA repair proteins contributes to maintenance of functional fission yeast telomeres. Genetics 161 1437-52 PubMed GONUTS page

[PMID:12944482-7] 7.0 ^7.1 ^7.2 Chahwan, C et al. (2003) The fission yeast Rad32 (Mre11)-Rad50-Nbs1 complex is required for the S-phase DNA damage checkpoint. Mol. Cell. Biol. 23 6564-73 PubMed GONUTS page

[PMID:18854158-8] 8.0 ^8.1 Williams, RS et al. (2008) Mre11 dimers coordinate DNA end bridging and nuclease processing in double-strand-break repair. Cell 135 97-109 PubMed GONUTS page

[PMID:15654094-9] Farah, JA et al. (2005) A novel recombination pathway initiated by the Mre11/Rad50/Nbs1 complex eliminates palindromes during meiosis in Schizosaccharomyces pombe. Genetics 169 1261-74 PubMed GONUTS page

[PMID:23080121-10] 10.0 ^10.1 Limbo, O et al. (2012) Mre11 ATLD17/18 mutation retains Tel1/ATM activity but blocks DNA double-strand break repair. Nucleic Acids Res. 40 11435-49 PubMed GONUTS page

[PMID:21931565-11] 11.0 ^11.1 Langerak, P et al. (2011) Release of Ku and MRN from DNA ends by Mre11 nuclease activity and Ctp1 is required for homologous recombination repair of double-strand breaks. PLoS Genet. 7 e1002271 PubMed GONUTS page

[PMID:19804755-12] Williams, RS et al. (2009) Nbs1 flexibly tethers Ctp1 and Mre11-Rad50 to coordinate DNA double-strand break processing and repair. Cell 139 87-99 PubMed GONUTS page

[PMID:17936710-13] Limbo, O et al. (2007) Ctp1 is a cell-cycle-regulated protein that functions with Mre11 complex to control double-strand break repair by homologous recombination. Mol. Cell 28 134-46 PubMed GONUTS page

[PMID:22705791-14] 14.0 ^14.1 ^14.2 Schiller, CB et al. (2012) Structure of Mre11-Nbs1 complex yields insights into ataxia-telangiectasia-like disease mutations and DNA damage signaling. Nat. Struct. Mol. Biol. 19 693-700 PubMed GONUTS page

[PMID:9651580-15] 15.0 ^15.1 ^15.2 Paull, TT & Gellert, M (1998) The 3' to 5' exonuclease activity of Mre 11 facilitates repair of DNA double-strand breaks. Mol. Cell 1 969-79 PubMed GONUTS page

[PMID:7885834-16] 16.0 ^16.1 Tavassoli, M et al. (1995) Cloning and characterisation of the Schizosaccharomyces pombe rad32 gene: a gene required for repair of double strand breaks and recombination. Nucleic Acids Res. 23 383-8 PubMed GONUTS page

[PMID:10373582-17] Wilson, S et al. (1999) The role of Schizosaccharomyces pombe Rad32, the Mre11 homologue, and other DNA damage response proteins in non-homologous end joining and telomere length maintenance. Nucleic Acids Res. 27 2655-61 PubMed GONUTS page

[PMID:12861005-18] 18.0 ^18.1 Tomita, K et al. (2003) Competition between the Rad50 complex and the Ku heterodimer reveals a role for Exo1 in processing double-strand breaks but not telomeres. Mol. Cell. Biol. 23 5186-97 PubMed GONUTS page

[PMID:12628934-19] Prudden, J et al. (2003) Pathway utilization in response to a site-specific DNA double-strand break in fission yeast. EMBO J. 22 1419-30 PubMed GONUTS page

[PMID:21873635-20] 20.0 ^20.1 ^20.2 ^20.3 ^20.4 ^20.5 ^20.6 ^20.7 ^20.8 ^20.9 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

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SCHPO:RAD32

Contents

Annotations

Notes

References

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