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Description:
Protein aprataxin-like.
Molecular weight: 76477
View which proteins in this organism that is involved with DNA Repair;
classified after biological processes (using data from the GOA project):
single strand break repair( GO:0000012 ) DNA repair( GO:0006281 )
Important dates:
07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
07-JUN-2004, sequence version 2.
07-MAR-2006, entry version 22.
Phylogenetic order:
Eukaryota Metazoa Arthropoda Hexapoda Insecta Pterygota Neoptera Endopterygota Diptera Brachycera Muscomorpha Ephydroidea Drosophilidae Drosophila.
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 APTX_DROME:
| Database | Pointer | Add. info#1 | Add. info#2 |
| EMBL | AE003726 | AAF55666.2.1 | - |
| EMBL | AE003726 | AAF55667.1 | ALT_SEQ |
| EMBL | AY118832 | AAM50692.1 | - |
| EMBL | BT011192 | AAR88553.1 | ALT_TERM |
| EMBL | BT012473 | AAS93744.1 | - |
| Ensembl | CG5316 | Drosophila melanogaster.1 | |
| FlyBase | FBgn0038704 | CG5316. | |
| BioCyc | DMEL-XXX-02:DMEL-XXX-02-012355-MONOMER | -.1 | |
| BioCyc | DMEL-XXX-02:DMEL-XXX-02-012357-MONOMER | -.1 | |
| GO | GO:0005634 | C:nucleus | ISS. |
| GO | GO:0003684 | F:damaged DNA binding | ISS. |
| GO | GO:0000012 | P:single strand break repair | ISS. |
| InterPro | IPR001310 | HIT. | |
| InterPro | IPR007087 | Znf_C2H2. | |
| Pfam | PF01230 | HIT | 1. |
| SMART | SM00355 | ZnF_C2H2 | 2. |
| PROSITE | PS00892 | HIT_1 | 1. |
| PROSITE | PS51084 | HIT_2 | 1. |
| PROSITE | PS00028 | ZINC_FINGER_C2H2_1 | FALSE_NEG. |
| PROSITE | PS50157 | ZINC_FINGER_C2H2_2 | FALSE_NEG. |
Keywords:
Alternative splicing; Complete proteome; DNA damage; DNA repair; Metal-binding; Nuclear protein; Zinc; Zinc-finger.
References:
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX MEDLINE=20196006; PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z.,
RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O.,
RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION.
RX MEDLINE=22426069; PubMed=12537572;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
RA Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a
RT systematic review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=Berkeley; TISSUE=Ovary;
RX MEDLINE=22426066; PubMed=12537569;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
RA Rubin G.M., Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE (ISOFORM 2), AND NUCLEOTIDE SEQUENCE OF 1-632
RP (ISOFORM 3).
RC STRAIN=Berkeley; TISSUE=Larva, and Pupae;
RA Stapleton M., Carlson J., Chavez C., Frise E., George R., Pacleb J.,
RA Park S., Wan K., Yu C., Rubin G.M., Celniker S.E.;
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
Feature:
CHAIN 1 662 Protein aprataxin-like.
/FTId=PRO_0000109849.
DOMAIN 4 108 HIT.
ZN_FING 381 403 C2H2-type.
COMPBIAS 538 647 Gln-rich.
VARSPLIC 1 219 Missing (in isoform 3).
/FTId=VSP_010546.
VARSPLIC 1 90 Missing (in isoform 2).
/FTId=VSP_010547.
CONFLICT 44 44 A -> D (in Ref. 3).
CONFLICT 106 106 T -> K (in Ref. 3).
CONFLICT 109 109 K -> E (in Ref. 4; AAS93744).
CONFLICT 194 194 F -> I (in Ref. 3).
CONFLICT 300 300 K -> T (in Ref. 3).
CONFLICT 410 410 E -> K (in Ref. 3).
CONFLICT 440 440 N -> P (in Ref. 3).
CONFLICT 451 452 AA -> GSG (in Ref. 3).
Comments:
-!- FUNCTION: May be involved in the DNA repair (By similarity).
-!- SUBCELLULAR LOCATION: Nucleus (Potential).
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q8MSG8-1; Sequence=Displayed;
Name=2;
IsoId=Q8MSG8-2; Sequence=VSP_010547;
Note=No experimental confirmation available;
Name=3;
IsoId=Q8MSG8-3; Sequence=VSP_010546;
Note=No experimental confirmation available;
-!- SIMILARITY: Contains 1 C2H2-type zinc finger.
-!- SIMILARITY: Contains 1 FHA-like domain.
-!- SIMILARITY: Contains 1 HIT domain.
-!- CAUTION: Ref.1 (AAF55667) sequence differs from that shown due to
erroneous gene model prediction.
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Sequence length: 662
MSWSSALIKD ISKPENLIIS SEIAVVIADK FPKAQHHYLV LPLADIPSIF HLNRSHLSLL
EELHLLARNV VEVKGVRWQD FNVGFHAEPS MQRLHLHVIS KDFVSTSLKT KKHWNSFNTE
LFVPYTKLYA QLEKENSISR LPKSLKDELL AKPLICNQCE FVARNLPSLK GHLVGHLQDP
KSVCQRVRLG NQFFPTAGYR TSELAYCFDF VDFYEYKKQM EVDKLAYIRD ELQRKLNDKR
NFLIESDRAV VMKADYPKSQ YHFRVVAKEE FRDITQLTEA QLPLLDHMMD LANQIIEKQK
HLESRNFLIG FKVNTFWNRL NLHVISNDFY SMAMKRISHW NSFNTELFMP FQIAYMMLSV
QGSIESISEE TYNNLQEKTP LRCNQCEFVT NMLLDLKAHL YQHWQRKEDE RDQKKKVDKI
IQMISETKLD EAEAKPKLLN EEEPIQAQPV AAIAQYPNEH LGKPLTPQQQ PGKQQAQNVY
DKNINGPSVN MMNQNNPNNP FRNTPHLNRQ SQKPPHPRSG PRGPMAPWTG PRFPCHQQQN
RFRPPGFNAC RQPYPPYHSG HQQFPNASSV GGGQTGLPGQ GQGPRPKWNS NKIFNQQNRQ
NTVQAQPQAQ NQQTNQQQIQ NSNKNQTPKK KPWKNRLQPV GKVQNQGGAN RDPAPPSNSK
PS