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Protein

DNA-(apurinic or apyrimidinic site) lyase 1

Gene

APN1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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.

Miscellaneous

Present with 7250 molecules/cell in log phase SD medium.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

  • The C-O-P bond 3' to the apurinic or apyrimidinic site in DNA is broken by a beta-elimination reaction, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate. EC:4.2.99.18

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Zn2+Note: Binds 3 Zn2+ ions.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi83Zinc 1By similarity1
Metal bindingi123Zinc 1By similarity1
Metal bindingi158Zinc 1By similarity1
Metal bindingi158Zinc 2By similarity1
Metal bindingi192Zinc 2By similarity1
Metal bindingi195Zinc 3By similarity1
Metal bindingi229Zinc 2By similarity1
Metal bindingi242Zinc 3By similarity1
Metal bindingi244Zinc 3By similarity1
Metal bindingi274Zinc 2By similarity1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionLyase
Biological processDNA damage, DNA repair
LigandMetal-binding, Zinc

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
YEAST:G3O-31899-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
4.2.99.18 984

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
DNA-(apurinic or apyrimidinic site) lyase 1 (EC:4.2.99.18)
Alternative name(s):
Apurinic-apyrimidinic endonuclease 1
Short name:
AP endonuclease 1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:APN1
Ordered Locus Names:YKL114C
ORF Names:YKL513
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri559292 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002311 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome XI

Organism-specific databases

Saccharomyces Genome Database

More...
SGDi
S000001597 APN1

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Nucleus

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved1 Publication
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001908982 – 367DNA-(apurinic or apyrimidinic site) lyase 1Add BLAST366

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei356PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P22936

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P22936

PRoteomics IDEntifications database

More...
PRIDEi
P22936

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P22936

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Monomer.

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
34020, 109 interactors

Database of interacting proteins

More...
DIPi
DIP-4106N

Protein interaction database and analysis system

More...
IntActi
P22936, 2 interactors

Molecular INTeraction database

More...
MINTi
P22936

STRING: functional protein association networks

More...
STRINGi
4932.YKL114C

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P22936

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P22936

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the AP endonuclease 2 family.Curated

Phylogenomic databases

Ensembl GeneTree

More...
GeneTreei
ENSGT00390000013698

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000224893

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P22936

KEGG Orthology (KO)

More...
KOi
K10771

Identification of Orthologs from Complete Genome Data

More...
OMAi
HPGSHLK

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00019 AP2Ec, 1 hit

HAMAP database of protein families

More...
HAMAPi
MF_00152 Nfo, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR001719 AP_endonuc_2
IPR018246 AP_endonuc_F2_Zn_BS
IPR036237 Xyl_isomerase-like_sf
IPR013022 Xyl_isomerase-like_TIM-brl

The PANTHER Classification System

More...
PANTHERi
PTHR21445 PTHR21445, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01261 AP_endonuc_2, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00518 AP2Ec, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF51658 SSF51658, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR00587 nfo, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00729 AP_NUCLEASE_F2_1, 1 hit
PS00730 AP_NUCLEASE_F2_2, 1 hit
PS00731 AP_NUCLEASE_F2_3, 1 hit
PS51432 AP_NUCLEASE_F2_4, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P22936-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MPSTPSFVRS AVSKYKFGAH MSGAGGISNS VTNAFNTGCN SFAMFLKSPR
60 70 80 90 100
KWVSPQYTQE EIDKFKKNCA TYNYNPLTDV LPHGQYFINL ANPDREKAEK
110 120 130 140 150
SYESFMDDLN RCEQLGIGLY NLHPGSTLKG DHQLQLKQLA SYLNKAIKET
160 170 180 190 200
KFVKIVLENM AGTGNLVGSS LVDLKEVIGM IEDKSRIGVC IDTCHTFAAG
210 220 230 240 250
YDISTTETFN NFWKEFNDVI GFKYLSAVHL NDSKAPLGAN RDLHERLGQG
260 270 280 290 300
YLGIDVFRMI AHSEYLQGIP IVLETPYEND EGYGNEIKLM EWLESKSESE
310 320 330 340 350
LLEDKEYKEK NDTLQKLGAK SRKEQLDKFE VKQKKRAGGT KRKKATAEPS
360
DNDILSQMTK KRKTKKE
Length:367
Mass (Da):41,439
Last modified:January 23, 2007 - v4
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i76C14935B760A6D1
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti239A → S in AAA34429 (PubMed:1693433).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
M33667 Genomic DNA Translation: AAA34429.1
S93804 Genomic DNA Translation: AAB22003.1
Z28114 Genomic DNA Translation: CAA81954.1
BK006944 Genomic DNA Translation: DAA09044.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S29871

NCBI Reference Sequences

More...
RefSeqi
NP_012808.1, NM_001179680.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YKL114C_mRNA; YKL114C_mRNA; YKL114C

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
853746

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YKL114C

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M33667 Genomic DNA Translation: AAA34429.1
S93804 Genomic DNA Translation: AAB22003.1
Z28114 Genomic DNA Translation: CAA81954.1
BK006944 Genomic DNA Translation: DAA09044.1
PIRiS29871
RefSeqiNP_012808.1, NM_001179680.1

3D structure databases

ProteinModelPortaliP22936
SMRiP22936
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34020, 109 interactors
DIPiDIP-4106N
IntActiP22936, 2 interactors
MINTiP22936
STRINGi4932.YKL114C

PTM databases

iPTMnetiP22936

Proteomic databases

MaxQBiP22936
PaxDbiP22936
PRIDEiP22936

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYKL114C_mRNA; YKL114C_mRNA; YKL114C
GeneIDi853746
KEGGisce:YKL114C

Organism-specific databases

SGDiS000001597 APN1

Phylogenomic databases

GeneTreeiENSGT00390000013698
HOGENOMiHOG000224893
InParanoidiP22936
KOiK10771
OMAiHPGSHLK

Enzyme and pathway databases

BioCyciYEAST:G3O-31899-MONOMER
BRENDAi4.2.99.18 984

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P22936

Family and domain databases

CDDicd00019 AP2Ec, 1 hit
HAMAPiMF_00152 Nfo, 1 hit
InterProiView protein in InterPro
IPR001719 AP_endonuc_2
IPR018246 AP_endonuc_F2_Zn_BS
IPR036237 Xyl_isomerase-like_sf
IPR013022 Xyl_isomerase-like_TIM-brl
PANTHERiPTHR21445 PTHR21445, 1 hit
PfamiView protein in Pfam
PF01261 AP_endonuc_2, 1 hit
SMARTiView protein in SMART
SM00518 AP2Ec, 1 hit
SUPFAMiSSF51658 SSF51658, 1 hit
TIGRFAMsiTIGR00587 nfo, 1 hit
PROSITEiView protein in PROSITE
PS00729 AP_NUCLEASE_F2_1, 1 hit
PS00730 AP_NUCLEASE_F2_2, 1 hit
PS00731 AP_NUCLEASE_F2_3, 1 hit
PS51432 AP_NUCLEASE_F2_4, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiAPN1_YEAST
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P22936
Secondary accession number(s): D6VXH4
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: January 23, 2007
Last modified: January 16, 2019
This is version 168 of the entry and version 4 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome XI
    Yeast (Saccharomyces cerevisiae) chromosome XI: entries and gene names
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