Reviewed, UniProtKB/Swiss-Prot P28352 (APEX1_MOUSE)

Names and origin

Protein names

Recommended name:
    DNA-(apurinic or apyrimidinic site) lyase
    EC=4.2.99.18
Alternative name(s):
    Apurinic-apyrimidinic endonuclease 1
      Short name=AP endonuclease 1
    APEX nuclease
      Short name=APEN

Gene names

Name:	Apex1
Synonyms:	Ape, Apex

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	317 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Repairs oxidative DNA damages in vitro. May have a role in protection against cell lethality and suppression of mutations. Removes the blocking groups from the 3'-termini of the DNA strand breaks generated by ionizing radiations and bleomycin.
Catalytic activity	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.
Subunit structure	Monomer. Component of the SET complex, which also contains SET, ANP32A, HMGB2 and NME1 By similarity.
Subcellular location	Nucleus.
Sequence similarities	Belongs to the DNA repair enzymes AP/exoA family.

Ontologies

Keywords
Biological process	DNA damage DNA repair
Cellular component	Nucleus
Ligand	Magnesium Metal-binding
Molecular function	Lyase
PTM	Acetylation Phosphoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	DNA repair Inferred from electronic annotation. Source: UniProtKB-KW cell redox homeostasis Inferred from direct assay. Source: MGI
Cellular component	nucleus Inferred from sequence or structural similarity. Source: UniProtKB perinuclear region of cytoplasm Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	DNA binding Inferred from sequence or structural similarity. Source: UniProtKB DNA-(apurinic or apyrimidinic site) lyase activity Inferred from electronic annotation. Source: EC endonuclease activity Inferred from electronic annotation. Source: InterPro magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW oxidoreductase activity Inferred from sequence or structural similarity. Source: UniProtKB transcription coactivator activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.5
	Chain	2 – 317	316	DNA-(apurinic or apyrimidinic site) lyase		PRO_0000200011
Sites
	Active site	308	1	Proton acceptor By similarity
	Metal binding	67	1	Magnesium or manganese By similarity
	Metal binding	95	1	Magnesium or manganese By similarity
	Metal binding	209	1	Magnesium or manganese By similarity
	Metal binding	211	1	Magnesium or manganese By similarity
	Metal binding	307	1	Magnesium or manganese By similarity
	Metal binding	308	1	Magnesium or manganese By similarity
	Site	211	1	Important for substrate recognition By similarity
Amino acid modifications
	Modified residue	196	1	N6-acetyllysine By similarity
	Modified residue	261	1	Phosphotyrosine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P28352-1 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: CF086691FAC89C4A	FASTA	317	35,490
	10 20 30 40 50 60 MPKRGKKAAA DDGEEPKSEP ETKKSKGAAK KTEKEAAGEG PVLYEDPPDQ KTSPSGKSAT 70 80 90 100 110 120 LKICSWNVDG LRAWIKKKGL DWVKEEAPDI LCLQETKCSE NKLPAELQEL PGLTHQYWSA 130 140 150 160 170 180 PSDKEGYSGV GLLSRQCPLK VSYGIGEEEH DQEGRVIVAE FESFVLVTAY VPNAGRGLVR 190 200 210 220 230 240 LEYRQRWDEA FRKFLKDLAS RKPLVLCGDL NVAHEEIDLR NPKGNKKNAG FTPQERQGFG 250 260 270 280 290 300 ELLQAVPLAD SFRHLYPNTA YAYTFWTYMM NARSKNVGWR LDYFLLSHSL LPALCDSKIR 310 SKALGSDHCP ITLYLAL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"cDNA and deduced amino acid sequence of a mouse DNA repair enzyme (APEX nuclease) with significant homology to Escherichia coli exonuclease III." Seki S., Akiyama K., Watanabe S., Hatsushika M., Ikeda S., Tsutsui K. J. Biol. Chem. 266:20797-20802(1991) [PubMed: 1939131] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Genomic structure of the mouse apurinic/apyrimidinic endonuclease gene." Takiguchi Y., Chen D.J. Mamm. Genome 5:717-722(1994) [PubMed: 7533013] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 129. Tissue: Embryo.
[3]	"Cloning, sequence analysis, and chromosomal assignment of the mouse Apex gene." Akiyama K., Nagao K., Oshida T., Tsutsui K., Yoshida M.C., Seki S. Genomics 26:63-69(1995) [PubMed: 7782087] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: BALB/c. Tissue: Blood.
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6. Tissue: Brain.
[5]	"A mouse DNA repair enzyme (APEX nuclease) having exonuclease and apurinic/apyrimidinic endonuclease activities: purification and characterization." Seki S., Ikeda S., Watanabe S., Hatsushika M., Tsutsui K., Akiyama K., Zhang B. Biochim. Biophys. Acta 1079:57-64(1991) [PubMed: 1716153] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE OF 2-22, CHARACTERIZATION. Tissue: Ascites.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	D90374 mRNA. Translation: BAA14382.1. U12273 Genomic DNA. Translation: AAC13769.1. D38077 Genomic DNA. Translation: BAA07270.1. BC052401 mRNA. Translation: AAH52401.1.
IPI	IPI00224152.
PIR	A39500.
RefSeq	NP_033817.1.
UniGene	Mm.203
3D structure databases
HSSP	HSSP built from PDB template 1BIX based on UniProtKB P27695.
SMR	P28352. Positions 39-317.
ModBase	Search...
Protein-protein interaction databases
STRING	P28352.
PTM databases
PhosphoSite	P28352.
Proteomic databases
PRIDE	P28352.
Genome annotation databases
Ensembl	ENSMUST00000049411; ENSMUSP00000042602; ENSMUSG00000035960; Mus musculus. [Genome view]
GeneID	11792.
KEGG	mmu:11792.
UCSC	uc007tly.1. mouse.
Organism-specific databases
CTD	11792.
MGI	MGI:88042. Apex1.
Phylogenomic databases
HOGENOM	P28352.
HOVERGEN	P28352.
OMA	YTWWSYM.
Enzyme and pathway databases
BRENDA	4.2.99.18. 244.
Gene expression databases
ArrayExpress	P28352.
Bgee	P28352.
CleanEx	MM_APEX1.
Genevestigator	P28352.
GermOnline	ENSMUSG00000035960. Mus musculus.
Family and domain databases
InterPro	IPR000097. AP_endonuclease_F1. IPR005135. Endo/exonuclease/phosphatase. IPR004808. exoDNase_III. [Graphical view]
PANTHER	PTHR22748. ExoIII_xth. 1 hit.
Pfam	PF03372. Exo_endo_phos. 1 hit. [Graphical view]
TIGRFAMs	TIGR00195. exoDNase_III. 1 hit. TIGR00633. xth. 1 hit.
PROSITE	PS00726. AP_NUCLEASE_F1_1. 1 hit. PS00727. AP_NUCLEASE_F1_2. 1 hit. PS00728. AP_NUCLEASE_F1_3. 1 hit. PS51435. AP_NUCLEASE_F1_4. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	279621.
SOURCE	Search...

Entry information

Entry name

APEX1_MOUSE

Accession

Primary (citable) accession number: P28352

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 1992
Last sequence update:	January 23, 2007
Last modified:	November 3, 2009
This is version 99 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)