CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005128
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 DNA-(apurinic or apyrimidinic site) lyase 1 
Protein Synonyms/Alias
 Apurinic-apyrimidinic endonuclease 1; AP endonuclease 1 
Gene Name
 APN1 
Gene Synonyms/Alias
 YKL114C; YKL513 
Created Date
 July 27, 2013 
Organism
 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 
NCBI Taxa ID
 559292 
Lysine Modification
Position
Peptide
Type
References
316EKNDTLQKLGAKSRKacetylation[1]
328SRKEQLDKFEVKQKKacetylation[1]
Reference
 [1] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae.
 Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C.
 Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [PMID: 22865919
Functional Description
 DNA repair enzyme that cleaves apurinic/apyrimidinic (AP) sites and removes 3'-blocking groups present at single strand breaks of damaged DNA. APN1 accounts for > 97% of both apurinic/ apyrimidinic (AP) lyase and DNA 3'-repair diesterase activities. 
Sequence Annotation
 METAL 83 83 Zinc 1 (By similarity).
 METAL 123 123 Zinc 1 (By similarity).
 METAL 158 158 Zinc 1 (By similarity).
 METAL 158 158 Zinc 2 (By similarity).
 METAL 192 192 Zinc 2 (By similarity).
 METAL 195 195 Zinc 3 (By similarity).
 METAL 229 229 Zinc 2 (By similarity).
 METAL 242 242 Zinc 3 (By similarity).
 METAL 244 244 Zinc 3 (By similarity).
 METAL 274 274 Zinc 2 (By similarity).
 MOD_RES 356 356 Phosphoserine.  
Keyword
 Complete proteome; Direct protein sequencing; DNA damage; DNA repair; Lyase; Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 367 AA 
Protein Sequence
MPSTPSFVRS AVSKYKFGAH MSGAGGISNS VTNAFNTGCN SFAMFLKSPR KWVSPQYTQE 60
EIDKFKKNCA TYNYNPLTDV LPHGQYFINL ANPDREKAEK SYESFMDDLN RCEQLGIGLY 120
NLHPGSTLKG DHQLQLKQLA SYLNKAIKET KFVKIVLENM AGTGNLVGSS LVDLKEVIGM 180
IEDKSRIGVC IDTCHTFAAG YDISTTETFN NFWKEFNDVI GFKYLSAVHL NDSKAPLGAN 240
RDLHERLGQG YLGIDVFRMI AHSEYLQGIP IVLETPYEND EGYGNEIKLM EWLESKSESE 300
LLEDKEYKEK NDTLQKLGAK SRKEQLDKFE VKQKKRAGGT KRKKATAEPS DNDILSQMTK 360
KRKTKKE 367 
Gene Ontology
 GO:0005739; C:mitochondrion; IDA:SGD.
 GO:0005634; C:nucleus; IDA:SGD.
 GO:0017005; F:3'-tyrosyl-DNA phosphodiesterase activity; IDA:SGD.
 GO:0003677; F:DNA binding; IEA:InterPro.
 GO:0003906; F:DNA-(apurinic or apyrimidinic site) lyase activity; IDA:SGD.
 GO:0008311; F:double-stranded DNA specific 3'-5' exodeoxyribonuclease activity; IDA:SGD.
 GO:0004519; F:endonuclease activity; IEA:InterPro.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0006284; P:base-excision repair; IDA:SGD. 
Interpro
 IPR018246; AP_endonuc_F2_Zn_BS.
 IPR001719; Endodeoxyribonuclease_IV.
 IPR013022; Xyl_isomerase-like_TIM-brl. 
Pfam
 PF01261; AP_endonuc_2 
SMART
 SM00518; AP2Ec 
PROSITE
 PS00729; AP_NUCLEASE_F2_1
 PS00730; AP_NUCLEASE_F2_2
 PS00731; AP_NUCLEASE_F2_3
 PS51432; AP_NUCLEASE_F2_4 
PRINTS