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YEAST:APN1

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Species (Taxon ID) Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). (559292)
Gene Name(s) APN1
Protein Name(s) DNA-(apurinic or apyrimidinic site) lyase 1

Apurinic-apyrimidinic endonuclease 1 AP endonuclease 1

External Links
UniProt P22936
EMBL M33667
S93804
Z28114
BK006944
PIR S29871
RefSeq NP_012808.1
ProteinModelPortal P22936
SMR P22936
BioGrid 34020
DIP DIP-4106N
IntAct P22936
MINT MINT-537191
STRING 4932.YKL114C
MaxQB P22936
PaxDb P22936
PeptideAtlas P22936
EnsemblFungi [example_ID YKL114C]
GeneID 853746
KEGG sce:YKL114C
SGD S000001597
eggNOG COG0648
GeneTree ENSGT00390000013698
HOGENOM HOG000224893
InParanoid P22936
KO K10771
OMA ENWWKAV
OrthoDB EOG71VT48
BioCyc YEAST:G3O-31899-MONOMER
BRENDA 4.2.99.18
NextBio 974804
PRO PR:P22936
Proteomes UP000002311
Genevestigator P22936
GO GO:0005739
GO:0005634
GO:0017005
GO:0003677
GO:0003906
GO:0008311
GO:0008081
GO:0008270
GO:0006284
GO:0000737
GO:0000738
Gene3D 3.20.20.150
HAMAP MF_00152
InterPro IPR001719
IPR018246
IPR013022
PANTHER PTHR21445
Pfam PF01261
SMART SM00518
SUPFAM SSF51658
TIGRFAMs TIGR00587
PROSITE PS00729
PS00730
PS00731
PS51432

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0006285

base-excision repair, AP site formation

PMID:22819077[1]

ECO:0000314

P

Fig.10. Incision activities of purified APN-1 on AP site and oxidized base lesions

complete
CACAO 8801

GO:0005634

nucleus

PMID:12767225[2]

ECO:0000314

C

Figure 3

complete
CACAO 9123

GO:0008296

3'-5'-exodeoxyribonuclease activity

PMID:12767225[2]

ECO:0000314

F

Figure 6

complete
CACAO 9124

GO:0003906

DNA-(apurinic or apyrimidinic site) lyase activity

PMID:12767225[2]

ECO:0000314

F

Figure 6A

complete
CACAO 9125

GO:0004520

endodeoxyribonuclease activity

PMID:1715020[3]

ECO:0000314

F

Figure 7

complete
CACAO 9126

GO:0017005

3'-tyrosyl-DNA phosphodiesterase activity

PMID:12767225[2]

ECO:0000314

F

Figure 6

complete
CACAO 9131

enables

GO:0017005

3'-tyrosyl-DNA phosphodiesterase activity

PMID:12767225[2]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0003906

DNA-(apurinic or apyrimidinic site) endonuclease activity

PMID:12767225[2]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0008296

3'-5'-exodeoxyribonuclease activity

PMID:12767225[2]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:0005634

nucleus

PMID:12767225[2]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0017005

3'-tyrosyl-DNA phosphodiesterase activity

PMID:12397185[4]

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:16024777[5]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0008081

phosphoric diester hydrolase activity

PMID:3056935[6]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0006284

base-excision repair

PMID:9295360[7]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005739

mitochondrion

PMID:11238901[8]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005634

nucleus

PMID:7690756[9]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0003906

DNA-(apurinic or apyrimidinic site) endonuclease activity

PMID:1693433[10]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0003906

DNA-(apurinic or apyrimidinic site) endonuclease activity

PMID:12767225[2]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0003906

DNA-(apurinic or apyrimidinic site) endonuclease activity

PMID:1693433[10]

ECO:0000250

sequence similarity evidence used in manual assertion

F

Seeded From UniProt

Missing: with/from

enables

GO:0008081

phosphoric diester hydrolase activity

PMID:21873635[11]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000485019
SGD:S000001597
WB:WBGene00000151

F

Seeded From UniProt

complete

involved_in

GO:0006284

base-excision repair

PMID:21873635[11]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000485019
SGD:S000001597
WB:WBGene00000151

P

Seeded From UniProt

complete

part_of

GO:0005739

mitochondrion

PMID:21873635[11]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000485021
SGD:S000001597

C

Seeded From UniProt

complete

part_of

GO:0005634

nucleus

PMID:21873635[11]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000485021
SGD:S000001597

C

Seeded From UniProt

complete

enables

GO:0003906

DNA-(apurinic or apyrimidinic site) endonuclease activity

PMID:21873635[11]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000485019
SGD:S000001597
WB:WBGene00000151

F

Seeded From UniProt

complete

involved_in

GO:0090305

nucleic acid phosphodiester bond hydrolysis

GO_REF:0000108

ECO:0000364

evidence based on logical inference from manual annotation used in automatic assertion

GO:0008296

P

Seeded From UniProt

complete

involved_in

GO:0090305

nucleic acid phosphodiester bond hydrolysis

GO_REF:0000108

ECO:0000364

evidence based on logical inference from manual annotation used in automatic assertion

GO:0008311

P

Seeded From UniProt

complete

enables

GO:0003677

DNA binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001719

F

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:IPR001719

P

Seeded From UniProt

complete

enables

GO:0008270

zinc ion binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001719
InterPro:IPR018246

F

Seeded From UniProt

complete

enables

GO:0140078

class I DNA-(apurinic or apyrimidinic site) endonuclease activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:4.2.99.18

F

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

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

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:0016829

lyase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0456

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

Notes

References

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

  1. Yang, X et al. (2012) Functional characterization of the Caenorhabditis elegans DNA repair enzyme APN-1. DNA Repair (Amst.) 11 811-22 PubMed GONUTS page
  2. 2.0 2.1 2.2 2.3 2.4 2.5 2.6 2.7 2.8 Jilani, A et al. (2003) Characterization of two independent amino acid substitutions that disrupt the DNA repair functions of the yeast Apn1. Biochemistry 42 6436-45 PubMed GONUTS page
  3. Ramotar, D et al. (1991) Cellular role of yeast Apn1 apurinic endonuclease/3'-diesterase: repair of oxidative and alkylation DNA damage and control of spontaneous mutation. Mol. Cell. Biol. 11 4537-44 PubMed GONUTS page
  4. Liu, C et al. (2002) Repair of topoisomerase I covalent complexes in the absence of the tyrosyl-DNA phosphodiesterase Tdp1. Proc. Natl. Acad. Sci. U.S.A. 99 14970-5 PubMed GONUTS page
  5. Ishchenko, AA et al. (2005) The 3'->5' exonuclease of Apn1 provides an alternative pathway to repair 7,8-dihydro-8-oxodeoxyguanosine in Saccharomyces cerevisiae. Mol. Cell. Biol. 25 6380-90 PubMed GONUTS page
  6. Johnson, AW & Demple, B (1988) Yeast DNA diesterase for 3'-fragments of deoxyribose: purification and physical properties of a repair enzyme for oxidative DNA damage. J. Biol. Chem. 263 18009-16 PubMed GONUTS page
  7. Wang, Z et al. (1997) Molecular mechanism of base excision repair of uracil-containing DNA in yeast cell-free extracts. J. Biol. Chem. 272 24064-71 PubMed GONUTS page
  8. Vongsamphanh, R et al. (2001) Pir1p mediates translocation of the yeast Apn1p endonuclease into the mitochondria to maintain genomic stability. Mol. Cell. Biol. 21 1647-55 PubMed GONUTS page
  9. Ramotar, D et al. (1993) Intracellular localization of the Apn1 DNA repair enzyme of Saccharomyces cerevisiae. Nuclear transport signals and biological role. J. Biol. Chem. 268 20533-9 PubMed GONUTS page
  10. 10.0 10.1 Popoff, SC et al. (1990) Yeast structural gene (APN1) for the major apurinic endonuclease: homology to Escherichia coli endonuclease IV. Proc. Natl. Acad. Sci. U.S.A. 87 4193-7 PubMed GONUTS page
  11. 11.0 11.1 11.2 11.3 11.4 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page