Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
The new UniProt website is here! Take me to UniProt BETA

UniProtKB - P46946 (COM1_YEAST)

Entry version 156 (25 May 2022)
Sequence version 1 (01 Nov 1995)
Previous versions | rss
Add a publicationFeedback
Protein

DNA endonuclease SAE2

Gene

SAE2

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

Endonuclease that cooperates with the MRX complex in processing meiotic and mitotic double-strand breaks by allowing the endonucleolytic removal of SPO11 from the break sites and ensuring both resection and intrachromosomal association of the broken ends. Required for proper recovery from checkpoint-mediated cell cycle arrest after DNA damage. MRX complex and SAE2 remove a small oligonucleotide(s) from the DNA ends to form an early intermediate which is rapidly processed by EXO1 and/or SGS1 to generate extensive tracts of single-stranded DNA that serve as substrate for RAD51. Plays a transitional role in the dissociation of MRE11 from, and the recruitment of RAD52 to, repair foci. Ensures that both ends of a DSB participate in a recombination event and impairs the formation of palindromic structures in the genome. With TEL1, promotes microhomology-mediated end joining (MMEJ) but inhibits non-homologous end joining (NHEJ), likely by regulating MRE11-dependent ssDNA accumulation at DNA break. SAE2 and MRX are particularly important for removal of hairpins, bulky adducts and other irregular end structures. Facilitates telomere length reequilibration and subsequent checkpoint switch off. Involved in homing efficiency of VMA1 intein VDE and in repair of transposon excision sites.

25 Publications

Miscellaneous

Present with 1030 molecules/cell in log phase SD medium.1 Publication

<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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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 functionDNA-binding, Endonuclease, Hydrolase, Nuclease
Biological processDNA damage, DNA repair, Meiosis

<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%5Fand%5Ftaxonomy%5Fsection">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 endonuclease SAE2 (EC:3.1.-.-)
Alternative name(s):
Completion of meiotic recombination protein 1
Sporulation in the absence of SPO11 protein 2
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:SAE2
Synonyms:COM1
Ordered Locus Names:YGL175C
ORF Names:G1639
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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 lineageiEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fmanual">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 VII

Organism-specific databases

Saccharomyces Genome Database

More...SGDi		S000003143, SAE2

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		FungiDB:YGL175C

<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

Keywords - Cellular componenti

Cytoplasm, Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi72S → A: Reduces DNA damage-induced phosphorylation; when associated with A-73, A-75, A-76 and A-90. 1 Publication1
Mutagenesisi73S → A: Reduces DNA damage-induced phosphorylation; when associated with A-73, A-75, A-76 and A-90. Abolishes DNA damage-induced phosphorylation and function in DNA repair; when associated with A-90, A-249, A-279 and A-289. 3 Publications1
Mutagenesisi75T → A: Reduces DNA damage-induced phosphorylation; when associated with A-72, A-75, A-76 and A-90. 1 Publication1
Mutagenesisi76S → A: Reduces DNA damage-induced phosphorylation; when associated with A-72, A-73, A-75 and A-90. 1 Publication1
Mutagenesisi90T → A: Reduces DNA damage-induced phosphorylation; when associated with A-72, A-73, A-75 and A-76. Abolishes DNA damage-induced phosphorylation and function in DNA repair; when associated with A-73, A-249, A-279 and A-289. 3 Publications1
Mutagenesisi223R → A: Leads to camptothecin hypersensitivity and loss of function; when associated with A-225. 1 Publication1
Mutagenesisi225L → A: Leads to camptothecin hypersensitivity and loss of function; when associated with A-223. 1 Publication1
Mutagenesisi249S → A: Reduces DNA damage-induced phosphorylation; when associated with A-278, A-279, and A-289. Abolishes DNA damage-induced phosphorylation and function in DNA repair; when associated with A-73, A-90, A-279 and A-289. 3 Publications1
Mutagenesisi267S → A: Leads to camptothecin hypersensitivity and loss of function. 2 Publications1
Mutagenesisi267S → E: Leads to constitutive activation of the DNA repair function. 2 Publications1
Mutagenesisi270G → D: Abolishes DNA-binding and endonuclease activity. 1 Publication1
Mutagenesisi278S → A: Reduces DNA damage-induced phosphorylation; when associated with A-249, A-279, and A-289. 1 Publication1
Mutagenesisi279T → A: Reduces DNA damage-induced phosphorylation; when associated with A-249, A-278, and A-289. Abolishes DNA damage-induced phosphorylation and function in DNA repair; when associated with A-73, A-90, A-249 and A-289. 3 Publications1
Mutagenesisi289S → A: Reduces DNA damage-induced phosphorylation; when associated with A-249, A-278, and A-279. Abolishes DNA damage-induced phosphorylation and function in DNA repair; when associated with A-73, A-90, A-249 and A-279. 3 Publications1

<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 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000975651 – 345DNA endonuclease SAE2Add BLAST345

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 residuei143PhosphoserineCombined sources1
Modified residuei267Phosphoserine; by CDC282 Publications1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Phosphorylated forms accumulate periodically during the unperturbed cell cycle and in response to DNA damage in G2. Phosphorylated by MEC1 and TEL1. Mutagenesis experiments showed that several of the 5 residues located in canonical (S/T)Q motifs, which are favored for phosphorylation by ATM/ATR kinases (Ser-73, Thr-90, Ser-249, Thr-279 and Ser-289) may be phosphorylated. Phosphorylated at Ser-267 by CDC28 which is required to initiate meiotic DSB resection by allowing SPO11 removal from DSB ends.6 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQB - The MaxQuant DataBase

More...MaxQBi		P46946

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

More...PaxDbi		P46946

PRoteomics IDEntifications database

More...PRIDEi		P46946

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P46946

<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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Dimer or multimer.

Interacts with MRE11.

1 Publication

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		33078, 178 interactors

Database of interacting proteins

More...DIPi		DIP-1603N

Protein interaction database and analysis system

More...IntActi		P46946, 8 interactors

Molecular INTeraction database

More...MINTi		P46946

STRING: functional protein association networks

More...STRINGi		4932.YGL175C

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		P46946, protein

<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

AlphaFold Protein Structure Database

More...AlphaFoldDBi		P46946

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

More...SMRi		P46946

Database of comparative protein structure models

More...ModBasei		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

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni21 – 172DNA-bindingAdd BLAST152
Regioni265 – 290DisorderedSequence analysisAdd BLAST26

<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 COM1/SAE2/CtIP family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		ENOG502S084, Eukaryota

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_064983_0_0_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P46946

Identification of Orthologs from Complete Genome Data

More...OMAi		PPYEREY

<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%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

P46946-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MVTGEENVYL KSSLSILKEL SLDELLNVQY DVTTLIAKRV QALQNRNKCV 
        60         70         80         90        100
LEEPNSKLAE ILCHEKNAPQ QSSQTSAGPG EQDSEDFILT QFDEDIKKES 
       110        120        130        140        150
AEVHYRNENK HTVQLPLVTM PPNRHKRKIS EFSSPLNGLN NLSDLEDCSD 
       160        170        180        190        200
TVIHEKDNDK ENKTRKLLGI ELENPESTSP NLYKNVKDNF LFDFNTNPLT 
       210        220        230        240        250
KRAWILEDFR PNEDIAPVKR GRRKLERFYA QVGKPEDSKH RSLSVVIESQ 
       260        270        280        290        300
NSDYEFAFDN LRNRSKSPPG FGRLDFPSTQ EGNEDKKKSQ EIIRRKTKYR 
       310        320        330        340 
FLMASNNKIP PYEREYVFKR EQLNQIVDDG CFFWSDKLLQ IYARC
Length:345
Mass (Da):40,097
Last modified:November 1, 1995 - v1
<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:i284D57A3C11DD92B
GO

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
U49447 Genomic DNA Translation: AAB96338.1
X84705 Genomic DNA Translation: CAA59178.1
Z72697 Genomic DNA Translation: CAA96887.1
BK006941 Genomic DNA Translation: DAA07938.1

Protein sequence database of the Protein Information Resource

More...PIRi		S59236

NCBI Reference Sequences

More...RefSeqi		NP_011340.1, NM_001181040.1

Genome annotation databases

Ensembl fungal genome annotation project

More...EnsemblFungii		YGL175C_mRNA; YGL175C; YGL175C

Database of genes from NCBI RefSeq genomes

More...GeneIDi		852700

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		sce:YGL175C

<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
U49447 Genomic DNA Translation: AAB96338.1
X84705 Genomic DNA Translation: CAA59178.1
Z72697 Genomic DNA Translation: CAA96887.1
BK006941 Genomic DNA Translation: DAA07938.1
PIRiS59236
RefSeqiNP_011340.1, NM_001181040.1

3D structure databases

AlphaFoldDBiP46946
SMRiP46946
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi33078, 178 interactors
DIPiDIP-1603N
IntActiP46946, 8 interactors
MINTiP46946
STRINGi4932.YGL175C

PTM databases

iPTMnetiP46946

Proteomic databases

MaxQBiP46946
PaxDbiP46946
PRIDEiP46946

Genome annotation databases

EnsemblFungiiYGL175C_mRNA; YGL175C; YGL175C
GeneIDi852700
KEGGisce:YGL175C

Organism-specific databases

SGDiS000003143, SAE2
VEuPathDBiFungiDB:YGL175C

Phylogenomic databases

eggNOGiENOG502S084, Eukaryota
HOGENOMiCLU_064983_0_0_1
InParanoidiP46946
OMAiPPYEREY

Miscellaneous databases

Protein Ontology

More...PROi		PR:P46946
RNActiP46946, protein

Family and domain databases

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		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 nameiCOM1_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: P46946
Secondary accession number(s): D6VTX7
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: May 25, 2022
This is version 156 of the entry and version 1 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

Reference proteome

Documents

  1. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  2. Yeast chromosome VII
    Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names
  3. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again