GenomeNet

Database: UniProt
Entry: RAD14_SCHPO
LinkDB: RAD14_SCHPO
Original site: RAD14_SCHPO 
ID   RAD14_SCHPO             Reviewed;         289 AA.
AC   O59753;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   29-OCT-2014, entry version 84.
DE   RecName: Full=DNA repair protein rad14;
DE   AltName: Full=XP-A family homolog rhp14;
GN   Name=rhp14 {ECO:0000312|EMBL:CAA19045.1}; Synonyms=rad14;
GN   ORFNames=SPBC649.03;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales;
OC   Schizosaccharomycetaceae; Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1] {ECO:0000312|EMBL:CAA19045.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   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   [2] {ECO:0000305}
RP   FUNCTION.
RX   PubMed=10080187; DOI=10.1038/6838;
RA   Fleck O., Lehmann E., Schaer P., Kohli J.;
RT   "Involvement of nucleotide-excision repair in msh2 pms1-independent
RT   mismatch repair.";
RL   Nat. Genet. 21:314-317(1999).
RN   [3] {ECO:0000305}
RP   FUNCTION.
RX   PubMed=11408483; DOI=10.1074/jbc.M104039200;
RA   Hohl M., Christensen O., Kunz C., Naegeli H., Fleck O.;
RT   "Binding and repair of mismatched DNA mediated by Rhp14, the fission
RT   yeast homologue of human XPA.";
RL   J. Biol. Chem. 276:30766-30772(2001).
CC   -!- FUNCTION: Involved in nucleotide excision repair (NER). Functional
CC       in repair of ultraviolet radiation induced damages and in mitotic
CC       mutation avoidance. Binds damaged DNA. Binds specifically to base-
CC       base mismatches or small insertion/deletion loops with unpaired
CC       nucleotides. Maintains GT repeat stability. Functions as a part of
CC       the short-patch excision repair system.
CC       {ECO:0000269|PubMed:10080187, ECO:0000269|PubMed:11408483}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P28519}.
CC   -!- SIMILARITY: Belongs to the XPA family. {ECO:0000255}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CU329671; CAA19045.1; -; Genomic_DNA.
DR   PIR; T40596; T40596.
DR   RefSeq; NP_595222.1; NM_001021128.2.
DR   ProteinModelPortal; O59753; -.
DR   BioGrid; 277635; 96.
DR   STRING; 4896.SPBC649.03-1; -.
DR   MaxQB; O59753; -.
DR   EnsemblFungi; SPBC649.03.1; SPBC649.03.1:pep; SPBC649.03.
DR   GeneID; 2541120; -.
DR   KEGG; spo:SPBC649.03; -.
DR   PomBase; SPBC649.03; -.
DR   eggNOG; COG5145; -.
DR   HOGENOM; HOG000161510; -.
DR   InParanoid; O59753; -.
DR   KO; K10847; -.
DR   OMA; KDYIEYD; -.
DR   OrthoDB; EOG7H79F8; -.
DR   PhylomeDB; O59753; -.
DR   Reactome; REACT_207825; Dual incision reaction in GG-NER.
DR   Reactome; REACT_225144; Formation of incision complex in GG-NER.
DR   NextBio; 20802233; -.
DR   PRO; PR:O59753; -.
DR   GO; GO:0000109; C:nucleotide-excision repair complex; ISO:PomBase.
DR   GO; GO:0003684; F:damaged DNA binding; ISO:PomBase.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006289; P:nucleotide-excision repair; IGI:PomBase.
DR   GO; GO:1901255; P:nucleotide-excision repair involved in interstrand cross-link repair; IMP:PomBase.
DR   GO; GO:0000715; P:nucleotide-excision repair, DNA damage recognition; ISO:PomBase.
DR   GO; GO:0070914; P:UV-damage excision repair; IMP:PomBase.
DR   Gene3D; 3.90.530.10; -; 1.
DR   InterPro; IPR009061; DNA-bd_dom_put.
DR   InterPro; IPR000465; XPA.
DR   InterPro; IPR022656; XPA_C.
DR   InterPro; IPR022652; Znf_XPA_CS.
DR   PANTHER; PTHR10142; PTHR10142; 1.
DR   Pfam; PF05181; XPA_C; 1.
DR   Pfam; PF01286; XPA_N; 1.
DR   SUPFAM; SSF46955; SSF46955; 1.
DR   TIGRFAMs; TIGR00598; rad14; 1.
PE   3: Inferred from homology;
KW   Complete proteome; DNA damage; DNA repair; DNA-binding; Metal-binding;
KW   Nucleus; Reference proteome; Zinc; Zinc-finger.
FT   CHAIN         1    289       DNA repair protein rad14.
FT                                /FTId=PRO_0000274248.
FT   ZN_FING     116    140       {ECO:0000250|UniProtKB:P28519}.
SQ   SEQUENCE   289 AA;  34663 MW;  F9C2D8B582D30D6F CRC64;
     MENSSIVKSP NPTIEEQRNE IEKLKNLTGI EEVHVDGAKV NKRKRTFDEQ SEITKDYIEY
     DFSKIEDTKG GYLLEEKKVE DLREKPAERE LREQEERQKK LRLAPLNLDP ETAPKCFECD
     SIELDTKYFD IFHCRVCHTC REKYPDKYSL LTKTECKLDY LLTEPELQDQ ELLPRLLKAN
     PHQQGWSNMM LYLRYQVEEF AKKKWGSMEA LDAEFERREV QKKEMKEKKF EKQLLELRKR
     TRTSNYSRMS IREKRKHVHS YDEEFEKPNE PGVIVQRCKC GLEIEQLEI
//
DBGET integrated database retrieval system