SCHPO:RAD50

Species (Taxon ID)	Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast). (284812)
Gene Name(s)	rad50
Protein Name(s)	DNA repair protein rad50
External Links
UniProt	Q9UTJ8
EMBL	CU329670
PIR	T50080
RefSeq	XP_001713090.2
SMR	Q9UTJ8
BioGrid	278131
DIP	DIP-52389N
IntAct	Q9UTJ8
STRING	4896.SPAC1556.01c.1
iPTMnet	Q9UTJ8
MaxQB	Q9UTJ8
PaxDb	Q9UTJ8
PRIDE	Q9UTJ8
EnsemblFungi	SPAC1556.01c.1
EuPathDB	FungiDB:SPAC1556.01c
PomBase	SPAC1556.01c
HOGENOM	HOG000192269
InParanoid	Q9UTJ8
OMA	GNRSYNY
PhylomeDB	Q9UTJ8
Reactome	R-SPO-2559586 R-SPO-5693548 R-SPO-5693565
PRO	PR:Q9UTJ8
Proteomes	UP000002485
GO	GO:0000794 GO:0030870 GO:0000790 GO:0000784 GO:0035861 GO:0004017 GO:0005524 GO:0004003 GO:0045027 GO:0003691 GO:0051880 GO:0046872 GO:0043047 GO:0070192 GO:0042769 GO:0032508 GO:0110025 GO:1990918 GO:0000724 GO:0006303 GO:0031292 GO:0031573 GO:1990898 GO:0042138 GO:1903211 GO:1990426 GO:0010520 GO:0072422 GO:0016233 GO:0000723 GO:0000722 GO:0007004
InterPro	IPR027417 IPR038729 IPR004584 IPR013134
Pfam	PF13476
SUPFAM	SSF52540
TIGRFAMs	TIGR00606
PROSITE	PS51131

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		Rad50 is part of the Mre11-Rad50-Nbs1 complex which plays a role in DNA repair processes including DNA damage checkpoint and recruitment of telomerase. Rad50 is responsible for stimulating ATP dependent DNA unwinding. Fig. 4. Efficient NHEJ requires Ku70, DNA ligase 4 and MRN. (Mre11-Rad50-Nbs1=MRN)	complete CACAO 12784
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:1990426	mitotic recombination-dependent replication fork processing	PMID:23093942^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	happens_during:(GO:0000084)	Seeded From UniProt	complete
involved_in	GO:1903211	mitotic recombination involved in replication fork processing	PMID:29215009^[6]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0110025	DNA strand resection involved in replication fork processing	PMID:29215009^[6]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		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:30104346^[8]	ECO:0000269	experimental evidence used in manual assertion		F	happens_during:(GO:1990414)	Seeded From UniProt	complete
enables	GO:0043047	single-stranded telomeric DNA binding	GO_REF:0000024	ECO:0000266	sequence orthology evidence used in manual assertion	SGD:S000005194	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
involved_in	GO:0042138	meiotic DNA double-strand break formation	PMID:12019258^[10]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		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
involved_in	GO:0031292	gene conversion at mating-type locus, DNA double-strand break processing	PMID:30104346^[8]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0030870	Mre11 complex	PMID:30104346^[8]	ECO:0000353	physical interaction evidence used in manual assertion	PomBase:SPAC13C5.07	C		Seeded From UniProt	complete
involved_in	GO:0010520	regulation of reciprocal meiotic recombination	PMID:11726502^[11]	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:12944482^[7]	ECO:0000305	curator inference used in manual assertion	GO:0030870	P		Seeded From UniProt	complete
enables	GO:0005524	ATP binding	GO_REF:0000050	ECO:0000255	match to sequence model evidence used in manual assertion	InterPro:IPR003439	F		Seeded From UniProt	complete
enables	GO:0004003	ATP-dependent DNA helicase activity	GO_REF:0000024	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:Q92878	F		Seeded From UniProt	complete
enables	GO:0003691	double-stranded telomeric DNA binding	GO_REF:0000024	ECO:0000266	sequence orthology evidence used in manual assertion	SGD:S000005194	F		Seeded From UniProt	complete
part_of	GO:0000790	nuclear chromatin	GO_REF:0000111	ECO:0000305	curator inference used in manual assertion	GO:0030870	C		Seeded From UniProt	complete
involved_in	GO:0000724	double-strand break repair via homologous recombination	PMID:12944482^[7]	ECO:0000305	curator inference used in manual assertion	GO:0030870	P		Seeded From UniProt	complete
involved_in	GO:0000723	telomere maintenance	PMID:12861005^[12]	ECO:0000316	genetic interaction evidence used in manual assertion	PomBase:SPAC16A10.07c	P		Seeded From UniProt	complete
involved_in	GO:0000722	telomere maintenance via recombination	PMID:18160711^[13]	ECO:0000316	genetic interaction evidence used in manual assertion	PomBase:SPAC16A10.07c PomBase:SPBC29A3.14c	P		Seeded From UniProt	complete
involved_in	GO:0070192	chromosome organization involved in meiotic cell cycle	PMID:21873635^[14]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:109292 PANTHER:PTN000429848	P		Seeded From UniProt	complete
enables	GO:0051880	G-quadruplex DNA binding	PMID:21873635^[14]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000429848 SGD:S000005194	F		Seeded From UniProt	complete
enables	GO:0043047	single-stranded telomeric DNA binding	PMID:21873635^[14]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000429848 SGD:S000005194	F		Seeded From UniProt	complete
part_of	GO:0035861	site of double-strand break	PMID:21873635^[14]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000429848 UniProtKB:Q92878	C		Seeded From UniProt	complete
involved_in	GO:0032508	DNA duplex unwinding	PMID:21873635^[14]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000429848 UniProtKB:Q92878	P		Seeded From UniProt	complete
part_of	GO:0030870	Mre11 complex	PMID:21873635^[14]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000429848 UniProtKB:Q92878	C		Seeded From UniProt	complete
involved_in	GO:0016233	telomere capping	PMID:21873635^[14]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0034728 PANTHER:PTN000429848 TAIR:locus:2045437	P		Seeded From UniProt	complete
contributes_to	GO:0008408	3'-5' exonuclease activity	PMID:21873635^[14]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000429848 UniProtKB:Q92878	F		Seeded From UniProt	complete
involved_in	GO:0007004	telomere maintenance via telomerase	PMID:21873635^[14]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000429848 UniProtKB:Q92878	P		Seeded From UniProt	complete
enables	GO:0004017	adenylate kinase activity	PMID:21873635^[14]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000429848 SGD:S000005194	F		Seeded From UniProt	complete
contributes_to	GO:0004003	ATP-dependent DNA helicase activity	PMID:21873635^[14]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000429848 UniProtKB:Q92878	F		Seeded From UniProt	complete
enables	GO:0003691	double-stranded telomeric DNA binding	PMID:21873635^[14]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000429848 SGD:S000005194	F		Seeded From UniProt	complete
part_of	GO:0000794	condensed nuclear chromosome	PMID:21873635^[14]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000429848 RGD:621542	C		Seeded From UniProt	complete
part_of	GO:0000790	nuclear chromatin	PMID:21873635^[14]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000429848 RGD:621542	C		Seeded From UniProt	complete
part_of	GO:0000784	nuclear chromosome, telomeric region	PMID:21873635^[14]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000429848 UniProtKB:Q92878	C		Seeded From UniProt	complete
involved_in	GO:0000722	telomere maintenance via recombination	PMID:21873635^[14]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0034728 PANTHER:PTN000429848 PomBase:SPAC1556.01c SGD:S000005194	P		Seeded From UniProt	complete
contributes_to	GO:0000014	single-stranded DNA endodeoxyribonuclease activity	PMID:21873635^[14]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000429848 UniProtKB:Q92878	F		Seeded From UniProt	complete
involved_in	GO:0046940	nucleoside monophosphate phosphorylation	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0004017	P		Seeded From UniProt	complete
involved_in	GO:0000723	telomere maintenance	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR004584	P		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR004584	C		Seeded From UniProt	complete
involved_in	GO:0006281	DNA repair	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR004584	P		Seeded From UniProt	complete
enables	GO:0016887	ATPase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR004584	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:IPR004584	C		Seeded From UniProt	complete
enables	GO:0005524	ATP binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0067	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
enables	GO:0000166	nucleotide binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0547	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
enables	GO:0046872	metal ion binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0479	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
part_of	GO:0005694	chromosome	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0158 UniProtKB-SubCell:SL-0468	C		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
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
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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
↑ Iraqui, I et al. (2012) Recovery of arrested replication forks by homologous recombination is error-prone. PLoS Genet. 8 e1002976 PubMed GONUTS page
↑ ^6.0 ^6.1 Teixeira-Silva, A et al. (2017) The end-joining factor Ku acts in the end-resection of double strand break-free arrested replication forks. Nat Commun 8 1982 PubMed GONUTS page
↑ ^7.0 ^7.1 ^7.2 ^7.3 ^7.4 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 ^8.2 Zhu, M et al. (2018) Mre11 complex links sister chromatids to promote repair of a collapsed replication fork. Proc. Natl. Acad. Sci. U.S.A. 115 8793-8798 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
↑ Farah, JA et al. (2002) A 160-bp palindrome is a Rad50.Rad32-dependent mitotic recombination hotspot in Schizosaccharomyces pombe. Genetics 161 461-8 PubMed GONUTS page
↑ Hartsuiker, E et al. (2001) Fission yeast Rad50 stimulates sister chromatid recombination and links cohesion with repair. EMBO J. 20 6660-71 PubMed GONUTS page
↑ 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
↑ Subramanian, L et al. (2008) Recombination-based telomere maintenance is dependent on Tel1-MRN and Rap1 and inhibited by telomerase, Taz1, and Ku in fission yeast. Mol. Cell. Biol. 28 1443-55 PubMed GONUTS page
↑ ^14.00 ^14.01 ^14.02 ^14.03 ^14.04 ^14.05 ^14.06 ^14.07 ^14.08 ^14.09 ^14.10 ^14.11 ^14.12 ^14.13 ^14.14 ^14.15 ^14.16 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:23093942-5] Iraqui, I et al. (2012) Recovery of arrested replication forks by homologous recombination is error-prone. PLoS Genet. 8 e1002976 PubMed GONUTS page

[PMID:29215009-6] 6.0 ^6.1 Teixeira-Silva, A et al. (2017) The end-joining factor Ku acts in the end-resection of double strand break-free arrested replication forks. Nat Commun 8 1982 PubMed GONUTS page

[PMID:12944482-7] 7.0 ^7.1 ^7.2 ^7.3 ^7.4 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:30104346-8] 8.0 ^8.1 ^8.2 Zhu, M et al. (2018) Mre11 complex links sister chromatids to promote repair of a collapsed replication fork. Proc. Natl. Acad. Sci. U.S.A. 115 8793-8798 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:12019258-10] Farah, JA et al. (2002) A 160-bp palindrome is a Rad50.Rad32-dependent mitotic recombination hotspot in Schizosaccharomyces pombe. Genetics 161 461-8 PubMed GONUTS page

[PMID:11726502-11] Hartsuiker, E et al. (2001) Fission yeast Rad50 stimulates sister chromatid recombination and links cohesion with repair. EMBO J. 20 6660-71 PubMed GONUTS page

[PMID:12861005-12] 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:18160711-13] Subramanian, L et al. (2008) Recombination-based telomere maintenance is dependent on Tel1-MRN and Rap1 and inhibited by telomerase, Taz1, and Ku in fission yeast. Mol. Cell. Biol. 28 1443-55 PubMed GONUTS page

[PMID:21873635-14] 14.00 ^14.01 ^14.02 ^14.03 ^14.04 ^14.05 ^14.06 ^14.07 ^14.08 ^14.09 ^14.10 ^14.11 ^14.12 ^14.13 ^14.14 ^14.15 ^14.16 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:RAD50

Contents

Annotations

Notes

References

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