RAD14_YEAST
ID RAD14_YEAST Reviewed; 371 AA.
AC P28519; D6W026;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=DNA repair protein RAD14;
GN Name=RAD14; OrderedLocusNames=YMR201C; ORFNames=YM8325.02C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTANT RAD14-2.
RX PubMed=9046084;
RX DOI=10.1002/(sici)1097-0061(199701)13:1<31::aid-yea60>3.0.co;2-4;
RA Jones G.W., Reed S.H., Waters R.;
RT "Characterization of the rad14-2 mutant of Saccharomyces cerevisiae:
RT implications for the recognition of UV photoproducts by the Rad14
RT protein.";
RL Yeast 13:31-36(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 125-371.
RX PubMed=1741034; DOI=10.1038/355555a0;
RA Bankmann M., Prakash L., Prakash S.;
RT "Yeast RAD14 and human Xeroderma pigmentosum group A DNA-repair genes
RT encode homologous proteins.";
RL Nature 355:555-558(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP CHARACTERIZATION.
RX PubMed=8516285; DOI=10.1073/pnas.90.12.5433;
RA Guzder S.N., Sung P., Prakash L., Prakash S.;
RT "Yeast DNA-repair gene RAD14 encodes a zinc metalloprotein with affinity
RT for ultraviolet-damaged DNA.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:5433-5437(1993).
RN [6]
RP IDENTIFICATION IN THE NEF1 COMPLEX.
RX PubMed=8621533; DOI=10.1074/jbc.271.15.8903;
RA Guzder S.N., Sung P., Prakash L., Prakash S.;
RT "Nucleotide excision repair in yeast is mediated by sequential assembly of
RT repair factors and not by a pre-assembled repairosome.";
RL J. Biol. Chem. 271:8903-8910(1996).
RN [7]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Involved in nucleotide excision repair. Binds specifically to
CC damaged DNA. Required for the incision step.
CC -!- SUBUNIT: Component of the nucleotide excision repair factor 1 (NEF1)
CC complex consisting of RAD1, RAD10 and RAD14.
CC {ECO:0000269|PubMed:8621533}.
CC -!- INTERACTION:
CC P28519; P06777: RAD1; NbExp=4; IntAct=EBI-14641, EBI-14752;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- MISCELLANEOUS: Present with 1030 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the XPA family. {ECO:0000305}.
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DR EMBL; X64064; CAA45420.1; -; Genomic_DNA.
DR EMBL; Z48755; CAA88642.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA10100.1; -; Genomic_DNA.
DR PIR; S59442; S59442.
DR RefSeq; NP_013928.1; NM_001182708.1.
DR PDB; 5A39; X-ray; 2.80 A; A/B=188-302.
DR PDB; 5A3D; X-ray; 1.80 A; A/B=188-302.
DR PDB; 5G32; X-ray; 2.20 A; A/B=188-306.
DR PDB; 5G33; X-ray; 2.40 A; A/B=188-306.
DR PDB; 5G34; X-ray; 1.90 A; A/B=188-306.
DR PDB; 5G35; X-ray; 2.00 A; A/B=188-306.
DR PDB; 5LCL; X-ray; 2.20 A; A=188-306, B=1-371.
DR PDB; 5LCM; X-ray; 1.90 A; A/B=188-306.
DR PDBsum; 5A39; -.
DR PDBsum; 5A3D; -.
DR PDBsum; 5G32; -.
DR PDBsum; 5G33; -.
DR PDBsum; 5G34; -.
DR PDBsum; 5G35; -.
DR PDBsum; 5LCL; -.
DR PDBsum; 5LCM; -.
DR AlphaFoldDB; P28519; -.
DR SMR; P28519; -.
DR BioGRID; 35379; 396.
DR ComplexPortal; CPX-1708; Nucleotide-excision repair factor 1 complex.
DR DIP; DIP-1896N; -.
DR ELM; P28519; -.
DR IntAct; P28519; 10.
DR MINT; P28519; -.
DR STRING; 4932.YMR201C; -.
DR iPTMnet; P28519; -.
DR MaxQB; P28519; -.
DR PaxDb; P28519; -.
DR PRIDE; P28519; -.
DR EnsemblFungi; YMR201C_mRNA; YMR201C; YMR201C.
DR GeneID; 855241; -.
DR KEGG; sce:YMR201C; -.
DR SGD; S000004814; RAD14.
DR VEuPathDB; FungiDB:YMR201C; -.
DR eggNOG; KOG4017; Eukaryota.
DR GeneTree; ENSGT00390000002721; -.
DR HOGENOM; CLU_053731_0_1_1; -.
DR InParanoid; P28519; -.
DR OMA; MMLFLRF; -.
DR BioCyc; YEAST:G3O-32888-MON; -.
DR Reactome; R-SCE-5696395; Formation of Incision Complex in GG-NER.
DR Reactome; R-SCE-6781823; Formation of TC-NER Pre-Incision Complex.
DR Reactome; R-SCE-6782135; Dual incision in TC-NER.
DR PRO; PR:P28519; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P28519; protein.
DR GO; GO:0000110; C:nucleotide-excision repair factor 1 complex; IPI:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0003684; F:damaged DNA binding; IDA:SGD.
DR GO; GO:0008270; F:zinc ion binding; IDA:SGD.
DR GO; GO:0006284; P:base-excision repair; IBA:GO_Central.
DR GO; GO:1901255; P:nucleotide-excision repair involved in interstrand cross-link repair; IBA:GO_Central.
DR GO; GO:0000715; P:nucleotide-excision repair, DNA damage recognition; IDA:SGD.
DR GO; GO:0033683; P:nucleotide-excision repair, DNA incision; IBA:GO_Central.
DR GO; GO:0070914; P:UV-damage excision repair; IBA:GO_Central.
DR Gene3D; 3.90.530.10; -; 1.
DR InterPro; IPR009061; DNA-bd_dom_put_sf.
DR InterPro; IPR000465; XPA.
DR InterPro; IPR022656; XPA_C.
DR InterPro; IPR022658; XPA_CS.
DR InterPro; IPR037129; XPA_sf.
DR InterPro; IPR022652; Znf_XPA_CS.
DR PANTHER; PTHR10142; PTHR10142; 1.
DR Pfam; PF05181; XPA_C; 1.
DR SUPFAM; SSF46955; SSF46955; 1.
DR TIGRFAMs; TIGR00598; rad14; 1.
DR PROSITE; PS00752; XPA_1; 1.
DR PROSITE; PS00753; XPA_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA damage; DNA repair; DNA-binding; Metal-binding; Nucleus;
KW Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..371
FT /note="DNA repair protein RAD14"
FT /id="PRO_0000208654"
FT ZN_FING 191..216
FT REGION 26..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 207
FT /note="V->M: In RAD14-2; loss of recognition of cyclobutane
FT pyrimidine dimers."
FT MUTAGEN 216
FT /note="C->Y: In RAD14-2; loss of recognition of cyclobutane
FT pyrimidine dimers."
FT TURN 192..194
FT /evidence="ECO:0007829|PDB:5A3D"
FT HELIX 202..206
FT /evidence="ECO:0007829|PDB:5A3D"
FT HELIX 214..219
FT /evidence="ECO:0007829|PDB:5A3D"
FT HELIX 221..224
FT /evidence="ECO:0007829|PDB:5A3D"
FT STRAND 226..228
FT /evidence="ECO:0007829|PDB:5A3D"
FT HELIX 229..236
FT /evidence="ECO:0007829|PDB:5A3D"
FT HELIX 240..243
FT /evidence="ECO:0007829|PDB:5A3D"
FT TURN 246..248
FT /evidence="ECO:0007829|PDB:5A3D"
FT STRAND 252..254
FT /evidence="ECO:0007829|PDB:5A3D"
FT STRAND 265..269
FT /evidence="ECO:0007829|PDB:5A3D"
FT HELIX 270..281
FT /evidence="ECO:0007829|PDB:5A3D"
FT HELIX 283..300
FT /evidence="ECO:0007829|PDB:5A3D"
SQ SEQUENCE 371 AA; 43038 MW; A90FA9CAA6F3EA52 CRC64;
MTPEQKAKLE ANRKLAIERL RKRGILSSDQ LNRIESRNEP LKTRPLAVTS GSNRDDNAAA
AVHVPNHNGQ PSALANTNTN TTSLYGSGVV DGSKRDASVL DKRPTDRIRP SIRKQDYIEY
DFATMQNLNG GYINPKDKLP NSDFTDDQEF ESEFGSKKQK TLQDWKKEQL ERKMLYENAP
PPEHISKAPK CIECHINIEM DPVLHDVFKL QVCKQCSKEH PEKYALLTKT ECKEDYFLTD
PELNDEDLFH RLEKPNPHSG TFARMQLFVR CEVEAFAFKK WGGEEGLDEE WQRREEGKAH
RREKKYEKKI KEMRLKTRAQ EYTNRLREKK HGKAHIHHFS DPVDGGIDED GYQIQRRRCT
DCGLETEEID I
