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Protein data for APN1_SCHPO:

Description:
DNA-(apurinic or apyrimidinic site) lyase 1 (EC 4.2.99.18) (APendonuclease 1) (Apurinic-apyrimidinic endonuclease 1).

Molecular weight: 38657

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-1996, integrated into UniProtKB/Swiss-Prot.
07-JUN-2004, sequence version 3.
07-FEB-2006, entry version 42.

Phylogenetic order:
Eukaryota Fungi Ascomycota Schizosaccharomycetes Schizosaccharomycetales Schizosaccharomycetaceae Schizosaccharomyces.

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 APN1_SCHPO:

DatabasePointerAdd. info#1Add. info#2
EMBLAY483157AAR83751.1-
EMBLAL033127CAB61503.4.1-
EMBLU33625AAC28163.1ALT_SEQ
PIRT52563T52563.
HSSPP126381QTW
GeneDB_SpombeSPCC622.17-.1
GOGO:0005739C:mitochondrionTAS.
InterProIPR001719AP_endnuclease2.
InterProIPR012307Xylisom_TIMbarrl.
PfamPF01261AP_endonuc_21.
SMARTSM00518AP2Ec1.
TIGRFAMsTIGR00587nfo1.
PROSITEPS00729AP_NUCLEASE_F2_11.
PROSITEPS00730AP_NUCLEASE_F2_21.
PROSITEPS00731AP_NUCLEASE_F2_31.

General information about the databases mentioned above

Keywords:
Complete proteome; DNA damage; DNA repair; Lyase; Metal-binding; Nuclear protein; Zinc.

References:
RN [1]
RP NUCLEOTIDE SEQUENCE, AND FUNCTION.
RX PubMed=14704348; DOI=10.1093/nar/gkh151;
RA Ribar B., Izumi T., Mitra S.;
RT "The major role of human AP-endonuclease homolog Apn2 in repair of
RT abasic sites in Schizosaccharomyces pombe.";
RL Nucleic Acids Res. 32:115-126(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972;
RX MEDLINE=21848401; PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M.,
RA Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A.,
RA Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G.,
RA Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K.,
RA James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J.,
RA Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C.,
RA Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E.,
RA Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S.,
RA Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K.,
RA Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S.,
RA Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B.,
RA Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S.,
RA Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D.,
RA Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R.,
RA Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B.,
RA Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S.,
RA Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M.,
RA Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G.,
RA Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J.,
RA Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L.,
RA Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J.,
RA Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP SEQUENCE REVISION.
RA Seeger K., Harris D., Lyne M., Rajandream M.A., Barrell B.G.;
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE OF 1-319.
RX MEDLINE=98193122; PubMed=9524207; DOI=10.1016/S0167-4781(97)00160-7;
RA Ramotar D., Vadnais J., Masson J.Y., Tremblay S.;
RT "Schizosaccharomyces pombe apn1 encodes a homologue of the Escherichia
RT coli endonuclease IV family of DNA repair proteins.";
RL Biochim. Biophys. Acta 1396:15-20(1998).

Feature:
CHAIN 1 342 DNA-(apurinic or apyrimidinic site) lyase
1.
/FTId=PRO_0000190897.
METAL 61 61 Zinc 1 (By similarity).
METAL 136 136 Zinc 1 (By similarity).
METAL 136 136 Zinc 2 (By similarity).
METAL 170 170 Zinc 2 (By similarity).
METAL 173 173 Zinc 3 (By similarity).
METAL 207 207 Zinc 2 (By similarity).
METAL 220 220 Zinc 3 (By similarity).
METAL 222 222 Zinc 3 (By similarity).
METAL 252 252 Zinc 2 (By similarity).

Comments:
-!- FUNCTION: DNA repair enzyme that cleaves apurinic/apyrimidinic
(AP) sites and removes 3'-blocking groups present at single strand
breaks of damaged DNA. Provides back-up AP endonuclease (APE)
activity to apn2 together with uve1.
-!- 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.
-!- COFACTOR: Binds 3 zinc ions (By similarity).
-!- SUBCELLULAR LOCATION: Nucleus (By similarity).
-!- SIMILARITY: Belongs to the AP endonuclease 2 family.
-!- CAUTION: Ref.4 sequence differs from that shown due to a
frameshift in position 298.
-!- CAUTION: Ref.4 sequence differs from that shown due to erroneous
intron retention.
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Sequence length: 342

     MCAINKAYLL TKFYISANSC AFFVKSQRKW TSPDLSEDVA QKFLETASEM KFDASKQVLV
     HGSYLINMAN ADEQKREQAF NCFVDDLKRC ERLGVGLYNF HPGSTASCTK EEGINNLAEC
     INRAHEETKS VIIVTENMAG QGNCLGGTFD DFAALKSKIK NLDRWRVCLD TCHTFAAGYD
     IRTEESYKKV IDEFDEKVGA KYVSGWHLND SKAPLGSNRD LHENIGLGFL GLEPFRLIMN
     DSRWDGIPLV LETPAKSPEQ WKKEVELLRF MVGKSSDDVE LMKESARLSN LGAASRKEHL
     NKFEKKEAKK DRKKKSKDGD QTTLLLRKKQ KLGNAEVKSL DE

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