Reviewed, UniProtKB/Swiss-Prot Q9UBZ4 (APEX2_HUMAN)

Names and origin

Protein names

Recommended 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
    APEX nuclease-like 2
    AP endonuclease XTH2

Gene names

Name:	APEX2
Synonyms:	APE2, APEXL2, XTH2

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	518 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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. Ref.1
Subcellular location	Nucleus Probable. Mitochondrion Probable. Note: Colocalized partly with PCNA in nuclear foci.
Tissue specificity	Highly expressed in cells, adult brain and kidney. Weakly expressed in the fetal brain. Ref.1
Sequence similarities	Belongs to the DNA repair enzymes AP/exoA family.

Ontologies

Keywords
Biological process	DNA damage DNA repair
Cellular component	Mitochondrion Nucleus
Coding sequence diversity	Polymorphism
Molecular function	Lyase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	DNA repair Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrion Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	DNA 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...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 518	518	DNA-(apurinic or apyrimidinic site) lyase 2		PRO_0000200014
Natural variations
	Natural variant	141	1	R → C: dbSNP rs2301416. Ref.5		VAR_023390
	Natural variant	141	1	R → W: dbSNP rs2301416.		VAR_048261
Experimental info
	Sequence conflict	399	1	P → S in AAD43041. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Q9UBZ4-1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 08464806153F8832	FASTA	518	57,401
	10 20 30 40 50 60 MLRVVSWNIN GIRRPLQGVA NQEPSNCAAV AVGRILDELD ADIVCLQETK VTRDALTEPL 70 80 90 100 110 120 AIVEGYNSYF SFSRNRSGYS GVATFCKDNA TPVAAEEGLS GLFATQNGDV GCYGNMDEFT 130 140 150 160 170 180 QEELRALDSE GRALLTQHKI RTWEGKEKTL TLINVYCPHA DPGRPERLVF KMRFYRLLQI 190 200 210 220 230 240 RAEALLAAGS HVIILGDLNT AHRPIDHWDA VNLECFEEDP GRKWMDSLLS NLGCQSASHV 250 260 270 280 290 300 GPFIDSYRCF QPKQEGAFTC WSAVTGARHL NYGSRLDYVL GDRTLVIDTF QASFLLPEVM 310 320 330 340 350 360 GSDHCPVGAV LSVSSVPAKQ CPPLCTRFLP EFAGTQLKIL RFLVPLEQSP VLEQSTLQHN 370 380 390 400 410 420 NQTRVQTCQN KAQVRSTRPQ PSQVGSSRGQ KNLKSYFQPS PSCPQASPDI ELPSLPLMSA 430 440 450 460 470 480 LMTPKTPEEK AVAKVVKGQA KTSEAKDEKE LRTSFWKSVL AGPLRTPLCG GHREPCVMRT 490 500 510 VKKPGPNLGR RFYMCARPRG PPTDPSSRCN FFLWSRPS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Human APE2 protein is mostly localized in the nuclei and to some extent in the mitochondria, while nuclear APE2 is partly associated with proliferating cell nuclear antigen." Tsuchimoto D., Sakai Y., Sakumi K., Nishioka K., Sasaki M., Fujiwara T., Nakabeppu Y. Nucleic Acids Res. 29:2349-2360(2001) [PubMed: 11376153] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH PCNA, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[2]	"Putative human AP endonuclease XTH2." Luna L., Rognes T., Henriksen A.C., Bjoras M., Seeberg E. Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Lung tumor.
[3]	"cDNA cloning and characterization of human APEX nuclease-like 2 (APEXL2) protein." Akiyama K., Sarker A.H., Yao M., Tsutsui K., Seki S. Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Bone marrow.
[4]	Hadi M.Z., Erzberger J.P., Ramirez M.H., Thelen M.P., Wilson D.M. III Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Lung tumor.
[5]	NIEHS SNPs program Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT CYS-141.
[6]	"The DNA sequence of the human X chromosome." Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R. Nature 434:325-337(2005) [PubMed: 15772651] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"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]. Tissue: Lung.
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

Cross-references

Sequence databases
EMBLGenBankDDBJ	AB049211 mRNA. Translation: BAB13764.1. AJ011311 mRNA. Translation: CAB45242.1. AB021260 mRNA. Translation: BAA78422.1. AF119046 mRNA. Translation: AAD43041.1. AY884244 Genomic DNA. Translation: AAW56941.1. AL020991 Genomic DNA. Translation: CAI43126.1. BC002959 mRNA. Translation: AAH02959.1.
IPI	IPI00083281.
RefSeq	NP_055296.2.
UniGene	Hs.659558
3D structure databases
HSSP	HSSP built from PDB template 1AKO based on UniProtKB P09030.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9UBZ4. 7 interactions.
STRING	Q9UBZ4.
PTM databases
PhosphoSite	Q9UBZ4.
Proteomic databases
PeptideAtlas	Q9UBZ4.
PRIDE	Q9UBZ4.
Genome annotation databases
Ensembl	ENST00000374987; ENSP00000364126; ENSG00000169188; Homo sapiens. [Genome view]
GeneID	27301.
KEGG	hsa:27301.
UCSC	uc004dtz.1. human.
Organism-specific databases
CTD	27301.
GeneCards	GC0XP055043.
H-InvDB	HIX0016825.
HGNC	HGNC:17889. APEX2.
PharmGKB	PA38474.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	Q9UBZ4.
HOVERGEN	Q9UBZ4.
OMA	RLDYVLG.
Enzyme and pathway databases
BRENDA	4.2.99.18. 247.
Gene expression databases
ArrayExpress	Q9UBZ4.
Bgee	Q9UBZ4.
CleanEx	HS_APEX2.
Genevestigator	Q9UBZ4.
GermOnline	ENSG00000169188. Homo sapiens.
Family and domain databases
InterPro	IPR000097. AP_endonuclease_F1. IPR005135. Endo/exonuclease/phosphatase. IPR004808. exoDNase_III. IPR010666. Znf_GRF. [Graphical view]
PANTHER	PTHR22748. ExoIII_xth. 1 hit.
Pfam	PF03372. Exo_endo_phos. 1 hit. PF06839. zf-GRF. 1 hit. [Graphical view]
TIGRFAMs	TIGR00633. xth. 1 hit.
PROSITE	PS00726. 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]
ProtoNet	Search...
Other Resources
NextBio	50285.

Entry information

Entry name

APEX2_HUMAN

Accession

Primary (citable) accession number: Q9UBZ4
Secondary accession number(s): Q9Y5X7

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 30, 2005
Last sequence update:	May 1, 2000
Last modified:	November 3, 2009
This is version 71 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.