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Reviewed, UniProtKB/Swiss-Prot Q68G58 (APEX2_MOUSE)

Last modified February 9, 2010. Version 50. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    DNA-(apurinic or apyrimidinic site) lyase 2
    EC=4.2.99.18
Alternative name(s):
    Apurinic-apyrimidinic endonuclease 2
      Short name=AP endonuclease 2
    APEX nuclease 2
Gene names
Name: Apex2
Synonyms: Ape2
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

Protein attributes

Sequence length516 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

May participate in both nuclear and mitochondrial post-replicative base excision repair (BER). In the nucleus functions in the PCNA-dependent BER pathway. Ref.1

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

Interacts with PCNA. This interaction is increased by misincorporation of uracil in nuclear DNA By similarity. Ref.1

Subcellular location

Nucleus Probable. Mitochondrion Probable. Note: Colocalized partly with PCNA in nuclear foci. Ref.1

Tissue specificity

Highly expressed in the thymus and weakly expressed in the bone marrow, spleen, eye, kidney, lung, brain and uterus. Ref.1

Sequence similarities

Belongs to the DNA repair enzymes AP/exoA family.

Ontologies

Keywords
   Biological processDNA damage
DNA repair
   Cellular componentMitochondrion
Nucleus
   Coding sequence diversityAlternative splicing
   Molecular functionLyase
Gene Ontology (GO)
   Biological processDNA repair

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentmitochondrial inner membrane Ref.1

Inferred from direct assay. Source: MGI

nucleus Ref.1

Inferred from direct assay. Source: MGI

   Molecular functionDNA binding

Inferred from electronic annotation. Source: InterPro

DNA-(apurinic or apyrimidinic site) lyase activity

Inferred from electronic annotation. Source: EC

endonuclease activity

Inferred from electronic annotation. Source: InterPro

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q68G58-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q68G58-2)

The sequence of this isoform differs from the canonical sequence as follows:
     79-79: S → SECSCPSP
Note: No experimental confirmation available.
Isoform 3 (identifier: Q68G58-3)

The sequence of this isoform differs from the canonical sequence as follows:
     213-246: ECFEEDPGRKWMDGLLSNPGDEAGPHIGLFMDSY → VRFPLNHRPQFCSVHPASQNWEFGTRGSFFYGKK
     247-516: Missing.
Note: No experimental confirmation available.
Isoform 4 (identifier: Q68G58-4)

The sequence of this isoform differs from the canonical sequence as follows:
     213-266: ECFEEDPGRK...FTCWSVVSGA → LPVAACGHTN...HTASLLRPSY
     267-516: Missing.
Note: No experimental confirmation available.
Isoform 5 (identifier: Q68G58-5)

The sequence of this isoform differs from the canonical sequence as follows:
     213-260: ECFEEDPGRK...PKQQRAFTCW → LPVAACGHTN...PLKFTESPCL
     261-516: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 516516DNA-(apurinic or apyrimidinic site) lyase 2
PRO_0000200015

Natural variations

Alternative sequence791S → SECSCPSP in isoform 2.
VSP_015346
Alternative sequence213 – 26654ECFEE…VVSGA → LPVAACGHTNLVPEWEAGPV WERTMREIMEGFCDLLHSVR IFHHHTASLLRPSY in isoform 4.
VSP_015347
Alternative sequence213 – 26048ECFEE…AFTCW → LPVAACGHTNLVPEWEAGPV WERTMREIMEVKTRFCSRPL KFTESPCL in isoform 5.
VSP_015348
Alternative sequence213 – 24634ECFEE…FMDSY → VRFPLNHRPQFCSVHPASQN WEFGTRGSFFYGKK in isoform 3.
VSP_015349
Alternative sequence247 – 516270Missing in isoform 3.
VSP_015350
Alternative sequence261 – 516256Missing in isoform 5.
VSP_015351
Alternative sequence267 – 516250Missing in isoform 4.
VSP_015352

Experimental info

Sequence conflict1101G → S in BAC38077. Ref.2
Sequence conflict1831A → P in BAB32346. Ref.2
Sequence conflict3721C → F in AAH78633. Ref.3
Sequence conflict4331V → M in AAH78633. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: ED32A88D9CEABB85

FASTA51657,340
        10         20         30         40         50         60 
MLRVVSWNIN GIRSPLQGLA CQEPSSCPTA LRRVLDELDA DIVCLQETKV TRDVLTEPLA 

        70         80         90        100        110        120 
IVEGYNSYFS FSRSRSGYSG VATFCKDSAT PVAAEEGLSG VFATLNGDIG CYGNMDEFTQ 

       130        140        150        160        170        180 
EELRVLDSEG RALLTQHKIR TLEGKEKTLT LINVYCPHAD PGKPERLTFK MRFYRLLQMR 

       190        200        210        220        230        240 
AEALLAAGSH VIILGDLNTA HRPIDHCDAS SLECFEEDPG RKWMDGLLSN PGDEAGPHIG 

       250        260        270        280        290        300 
LFMDSYRYLH PKQQRAFTCW SVVSGARHLN YGSRLDYVLG DRALVIDTFQ ASFLLPEVMG 

       310        320        330        340        350        360 
SDHCPVGAVL NVSCVPAKQC PALCTRFLPE FAGTQLKILR FLVPLEQEPV REQQVLQPSH 

       370        380        390        400        410        420 
QIQAQRQPRK ACMHSTRLRK SQGGPKRKQK NLMSYFQPSS SLSQTSGVEL PTLPLVGPLT 

       430        440        450        460        470        480 
TPKTAEEVAT ATVLEEKNKV PESKDEKGER TAFWKSMLSG PSPMPLCGGH REPCVMRTVK 

       490        500        510 
KTGPNFGRQF YMCARPRGPP SDPSSRCNFF LWSRPS 

« Hide

Isoform 2.

Checksum: 50712632B2D818F7
Show »

FASTA52358,043
Isoform 3.

Checksum: 194A612EF3CB1D8F
Show »

FASTA24627,389
Isoform 4.

Checksum: 7EBE161284108FD5
Show »

FASTA26629,575
Isoform 5.

Checksum: 0186A39DE091BA93
Show »

FASTA26028,880

References

« Hide 'large scale' references
[1]"Characterization of the genomic structure and expression of the mouse Apex2 gene."
Ide Y., Tsuchimoto D., Tominaga Y., Iwamoto Y., Nakabeppu Y.
Genomics 81:47-57(2003) [PubMed: 12573260] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH PCNA, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
Strain: 129/Sv and C57BL/6.
Tissue: B-cell.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1/2/4/5).
Strain: NOD.
Tissue: Adipose tissue, Head and Thymus.
[3]"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] (ISOFORMS 1 AND 3).
Strain: FVB/N-3.
Tissue: Mammary tumor.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB072498 mRNA. Translation: BAB88654.1.
AB085235 Genomic DNA. Translation: BAC11807.1.
AK021248 mRNA. Translation: BAB32346.1.
AK040145 mRNA. Translation: BAC30522.1.
AK050858 mRNA. Translation: BAC34436.1.
AK080916 mRNA. Translation: BAC38077.1.
AK081677 mRNA. Translation: BAC38287.1.
AK088918 mRNA. Translation: BAC40652.1.
BC026769 mRNA. Translation: AAH26769.1.
BC078633 mRNA. Translation: AAH78633.1.
IPIIPI00225176.
IPI00473955.
IPI00473962.
IPI00474999.
IPI00828973.
RefSeqNP_084219.1.
UniGeneMm.440275

3D structure databases

SMRQ68G58. Positions 1-311.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ68G58.

PTM databases

PhosphoSiteQ68G58.

Proteomic databases

PRIDEQ68G58.

Genome annotation databases

EnsemblENSMUST00000026303; ENSMUSP00000026303; ENSMUSG00000025269; Mus musculus. [Genome view]
ENSMUST00000112720; ENSMUSP00000108340; ENSMUSG00000025269; Mus musculus. [Genome view]
ENSMUST00000112721; ENSMUSP00000108341; ENSMUSG00000025269; Mus musculus. [Genome view]
ENSMUST00000112727; ENSMUSP00000108347; ENSMUSG00000025269; Mus musculus. [Genome view]
GeneID77622.
KEGGmmu:77622.
UCSCuc009uoi.1. mouse.
uc009uom.1. mouse.
uc009uon.1. mouse.

Organism-specific databases

CTD77622.
MGIMGI:1924872. Apex2.

Phylogenomic databases

HOVERGENQ68G58.
PhylomeDBQ68G58.

Enzyme and pathway databases

BRENDA4.2.99.18. 244.

Gene expression databases

ArrayExpressQ68G58.
BgeeQ68G58.
CleanExMM_APEX2.
GenevestigatorQ68G58.
GermOnlineENSMUSG00000025269. Mus musculus.

Family and domain databases

InterProIPR020847. AP_endonuclease_F1_BS.
IPR005135. Endo/exonuclease/phosphatase.
IPR004808. exoDNase_III.
[Graphical view]
PANTHERPTHR22748. ExoIII_xth. 1 hit.
PfamPF03372. Exo_endo_phos. 1 hit.
[Graphical view]
TIGRFAMsTIGR00633. xth. 1 hit.
PROSITEPS00726. AP_NUCLEASE_F1_1. 1 hit.
PS00727. AP_NUCLEASE_F1_2. False negative.
PS00728. AP_NUCLEASE_F1_3. False negative.
PS51435. AP_NUCLEASE_F1_4. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio347242.
SOURCESearch...

Entry information

Entry nameAPEX2_MOUSE
AccessionPrimary (citable) accession number: Q68G58
Secondary accession number(s): Q8BJP7 expand/collapse secondary AC list , Q8BTR7, Q8BUZ2, Q8BYE9, Q8R018, Q8R328, Q9CS12
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: October 11, 2004
Last modified: February 9, 2010
This is version 50 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents