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Description:
DNA-(apurinic or apyrimidinic site) lyase 2 (EC 4.2.99.18) (APendonuclease 2) (Apurinic-apyrimidinic endonuclease 2).
Molecular weight: 59445
View which proteins in this organism that is involved with DNA Repair;
classified after biological processes (using data from the GOA project):
DNA repair( GO:0006281 )
Important dates:
01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
01-OCT-1994, sequence version 1.
07-MAR-2006, entry version 45.
Phylogenetic order:
Eukaryota Fungi Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces.
To calculate the pI (Isoelectric point - the pH where a protein has a neutral charge),
go to this page and enter the protein ID (e.g 3MG_ECOLI): http://us.expasy.org/tools/pi_tool.html
Links to references in other databases for protein APN2_YEAST:
| Database | Pointer | Add. info#1 | Add. info#2 |
| EMBL | Z35780 | CAA84838.1 | - |
| PIR | S45753 | S45753. | |
| HSSP | P27695 | 1E9N | |
| GermOnline | 138454 | -.1 | |
| Ensembl | YBL019W | Saccharomyces cerevisiae.1 | |
| GenomeReviews | Y13134_GR | YBL019W.1 | |
| SGD | S000000115 | APN2. | |
| BioCyc | SCER-S28-01:SCER-S28-01-000157-MONOMER | -.1 | |
| LinkHub | P38207 | -.1 | |
| GO | GO:0005634 | C:nucleus | IC. |
| GO | GO:0008311 | F:double-stranded DNA specific 3'-5' exodeoxy... | IDA. |
| GO | GO:0004528 | F:phosphodiesterase I activity | IDA. |
| GO | GO:0006281 | P:DNA repair | IMP. |
| InterPro | IPR000097 | APendonclse1. | |
| InterPro | IPR005135 | Exo_endo_phos. | |
| InterPro | IPR010666 | Znf_GRF. | |
| Pfam | PF03372 | Exo_endo_phos | 1. |
| Pfam | PF06839 | zf-GRF | 1. |
| PROSITE | PS00726 | AP_NUCLEASE_F1_1 | FALSE_NEG. |
| PROSITE | PS00727 | AP_NUCLEASE_F1_2 | FALSE_NEG. |
| PROSITE | PS00728 | AP_NUCLEASE_F1_3 | 1. |
Keywords:
Complete proteome; DNA damage; DNA repair; Lyase; Nuclear protein.
References:
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S288c;
RX MEDLINE=95112788; PubMed=7813418;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J.,
RA Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C.,
RA Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M.,
RA Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L.,
RA Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J.,
RA Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T.,
RA Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A.,
RA Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B.,
RA Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I.,
RA Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M.,
RA Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A.,
RA van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I.,
RA Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H.,
RA Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [2]
RP CHARACTERIZATION.
RX MEDLINE=98438458; PubMed=9765213;
RA Johnson R.E., Torres-Ramos C.A., Izumi T., Mitra S., Prakash S.,
RA Prakash L.;
RT "Identification of APN2, the Saccharomyces cerevisiae homolog of the
RT major human AP endonuclease HAP1, and its role in the repair of abasic
RT sites.";
RL Genes Dev. 12:3137-3143(1998).
RN [3]
RP CHARACTERIZATION.
RX MEDLINE=20357371; PubMed=10806210; DOI=10.1074/jbc.M002845200;
RA Unk I., Haracska L., Johnson R.E., Prakash S., Prakash L.;
RT "Apurinic endonuclease activity of yeast Apn2 protein.";
RL J. Biol. Chem. 275:22427-22434(2000).
RN [4]
RP LEVEL OF PROTEIN EXPRESSION.
RX MEDLINE=22923965; PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
RA Dephoure N., O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
Feature:
CHAIN 1 520 DNA-(apurinic or apyrimidinic site) lyase
2.
/FTId=PRO_0000200020.
Comments:
-!- FUNCTION: DNA repair enzyme that cleaves apurinic/apyrimidinic
(AP) sites and removes 3'-blocking groups present at single strand
breaks of damaged DNA.
-!- 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.
-!- SUBCELLULAR LOCATION: Nucleus.
-!- MISCELLANEOUS: Present with 414 molecules/cell.
-!- SIMILARITY: Belongs to the DNA repair enzymes AP/exoA family.
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Sequence length: 520
MSSSENTLLD GKSENTIRFL TFNVNGIRTF FHYQPFSQMN QSLRSVFDFF RADIITFQEL
KTEKLSISKW GRVDGFYSFI SIPQTRKGYS GVGCWIRIPE KNHPLYHALQ VVKAEEGITG
YLTIKNGKHS AISYRNDVNQ GIGGYDSLDP DLDEKSALEL DSEGRCVMVE LACGIVIISV
YCPANSNSSE EGEMFRLRFL KVLLRRVRNL DKIGKKIVLM GDVNVCRDLI DSADTLEQFS
IPITDPMGGT KLEAQYRDKA IQFIINPDTP HRRIFNQILA DSLLPDASKR GILIDTTRLI
QTRNRLKMYT VWNMLKNLRP SNYGSRIDFI LVSLKLERCI KAADILPDIL GSDHCPVYSD
LDILDDRIEP GTTQVPIPKF EARYKYNLRN HNVLEMFAKK DTNKESNKQK YCVSKVMNTK
KNSNIKNKSL DSFFQKVNGE KDDRIKESSE IPQQAKKRIS TPKLNFKDVF GKPPLCRHGE
ESMLKTSKTS ANPGRKFWIC KRSRGDSNNT ESSCGFFQWV